data_4PPH
# 
_entry.id   4PPH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4PPH         
RCSB  RCSB085059   
WWPDB D_1000085059 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3AUP 
'Crystal structure of basic 7S globulin, a xyloglucan-specific endo-1,4-glucanase inhibitor protein-like protein from soybean' 
unspecified 
PDB 3VLB 'Structural basis for inhibition of xyloglucan-specific endo-1,4-glucanase (XEG) by XEG-protein inhibitor' unspecified 
PDB 3VLA 'Structural basis for inhibition of xyloglucan-specific endo-1,4-glucanase (XEG) by XEG-protein inhibitor' unspecified 
PDB 3HD8 'Crystal structure of the Triticum aestivum xylanase inhibitor-II' unspecified 
PDB 1T6E 'Structural basis for inhibition of Aspergillus niger xylanase by triticum aestivum xylanase inhibitor-I' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4PPH 
_pdbx_database_status.recvd_initial_deposition_date   2014-02-27 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Czubinski, J.'       1 ? 
'Barciszewski, J.'    2 ? 
'Gilski, M.'          3 ? 
'Lampart-Szczapa, E.' 4 ? 
'Jaskolski, M.'       5 ? 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Structure of gamma-conglutin: insight into the quaternary structure of 7S basic globulins from legumes.' 
'Acta Crystallogr.,Sect.D'  71  224  238  2015 ABCRE6 DK 0907-4449 0766 ? 25664733 10.1107/S1399004714025073        
1       'Characterisation of different digestion susceptibility of lupin seed globulins.' 'Food Chem'                 143 418  426 
2014 ?      ?  ?         ?    ? 24054261 10.1016/j.foodchem.2013.08.015   
2       'Release of flavonoids from lupin globulin proteins during digestion in a model system.' 'J.Agric.Food Chem.'        60  
1830 1836 2012 ?      US 0021-8561 ?    ? 22264085 10.1021/jf2042592                
3       
;Crystal structure of basic 7S globulin, a xyloglucan-specific endo-beta-1,4-glucanase inhibitor protein-like protein from soybean lacking inhibitory activity against endo-beta-glucanase.
;
'Febs J.'                   278 1944 1954 2011 ?      UK 1742-464X ?    ? 21457461 10.1111/j.1742-4658.2011.08111.x 
4       
'Internalisation and multiple phosphorylation of gamma-Conglutin, the lupin seed glycaemia-lowering protein, in HepG2 cells.' 
Biochem.Biophys.Res.Commun. 437 648  652  2013 BBRCA9 US 0006-291X 0146 ? 23872149 10.1016/j.bbrc.2013.07.026       
5       'Lupin seed gamma-conglutin lowers blood glucose in hyperglycaemic rats and increases glucose consumption of HepG2 cells.' 
'Br. J. Nutr.'              107 67   73   2012 ?      ?  ?         ?    ? 21733318 10.1017/S0007114511002601        
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Czubinski, J.'       1  
primary 'Barciszewski, J.'    2  
primary 'Gilski, M.'          3  
primary 'Szpotkowski, K.'     4  
primary 'Debski, J.'          5  
primary 'Lampart-Szczapa, E.' 6  
primary 'Jaskolski, M.'       7  
1       'Czubinski, J.'       8  
1       'Dwiecki, K.'         9  
1       'Siger, A.'           10 
1       'Neunert, G.'         11 
1       'Lampart-Szczapa, E.' 12 
2       'Czubinski, J.'       13 
2       'Dwiecki, K.'         14 
2       'Siger, A.'           15 
2       'Kachlicki, P.'       16 
2       'Neunert, G.'         17 
2       'Lampart-Szczapa, E.' 18 
2       'Nogala-Kalucka, M.'  19 
3       'Yoshizawa, T.'       20 
3       'Shimizu, T.'         21 
3       'Yamabe, M.'          22 
3       'Taichi, M.'          23 
3       'Nishiuchi, Y.'       24 
3       'Shichijo, N.'        25 
3       'Unzai, S.'           26 
3       'Hirano, H.'          27 
3       'Sato, M.'            28 
3       'Hashimoto, H.'       29 
4       'Capraro, J.'         30 
4       'Magni, C.'           31 
4       'Faoro, F.'           32 
4       'Maffi, D.'           33 
4       'Scarafoni, A.'       34 
4       'Tedeschi, G.'        35 
4       'Maffioli, E.'        36 
4       'Parolari, A.'        37 
4       'Manzoni, C.'         38 
4       'Lovati, M.R.'        39 
4       'Duranti, M.'         40 
5       'Lovati, M.R.'        41 
5       'Manzoni, C.'         42 
5       'Castiglioni, S.'     43 
5       'Parolari, A.'        44 
5       'Magni, C.'           45 
5       'Duranti, M.'         46 
# 
_cell.entry_id           4PPH 
_cell.length_a           121.990 
_cell.length_b           121.990 
_cell.length_c           188.490 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              18 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4PPH 
_symmetry.space_group_name_H-M             'P 31' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                144 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'Conglutin gamma'      45411.059 6   ? ? 'Lupinus angustifolius Conglutin gamma,UNP residues 33-449' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   7   ? ? ?                                                           ? 
3 non-polymer man ALPHA-L-FUCOSE         164.156   1   ? ? ?                                                           ? 
4 non-polymer syn 1,2-ETHANEDIOL         62.068    32  ? ? ?                                                           ? 
5 water       nat water                  18.015    794 ? ? ?                                                           ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Conglutin gamma 1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;LYHNSQPTSSKPNLLVLPVQEDASTGLHWANIHKRTPLMQVPLLLDLNGKHLWVTCSQHYSSSTYQAPFCHSTQCSRANT
HQCFTCTDSTTTRPGCHNNTCGLLSSNPVTQESGLGELAQDVLAIHSTHGSKLGPMVKVPQFLFSCAPSFLAQKGLPNNV
QGALGLGQAPISLQNQLFSHFGLKRQFSVCLSRYSTSNGAILFGDINDPNNNNYIHNSLDVLHDLVYTPLTISKQGEYFI
QVNAIRVNKHLVIPTKNPFISPSSTSYHGSGEIGGALITTTHPYTVLSHSIFEVFTQVFANNMPKQAQVKAVGPFGLCYD
SRKISGGAPSVDLILDKNDAVWRISSENFMVQAQDGVSCLGFVDGGVHARAGIALGAHHLEENLVVFDLERSRVGFNSNS
LKSYGKTCSNLFDLNNP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LYHNSQPTSSKPNLLVLPVQEDASTGLHWANIHKRTPLMQVPLLLDLNGKHLWVTCSQHYSSSTYQAPFCHSTQCSRANT
HQCFTCTDSTTTRPGCHNNTCGLLSSNPVTQESGLGELAQDVLAIHSTHGSKLGPMVKVPQFLFSCAPSFLAQKGLPNNV
QGALGLGQAPISLQNQLFSHFGLKRQFSVCLSRYSTSNGAILFGDINDPNNNNYIHNSLDVLHDLVYTPLTISKQGEYFI
QVNAIRVNKHLVIPTKNPFISPSSTSYHGSGEIGGALITTTHPYTVLSHSIFEVFTQVFANNMPKQAQVKAVGPFGLCYD
SRKISGGAPSVDLILDKNDAVWRISSENFMVQAQDGVSCLGFVDGGVHARAGIALGAHHLEENLVVFDLERSRVGFNSNS
LKSYGKTCSNLFDLNNP
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LEU n 
1 2   TYR n 
1 3   HIS n 
1 4   ASN n 
1 5   SER n 
1 6   GLN n 
1 7   PRO n 
1 8   THR n 
1 9   SER n 
1 10  SER n 
1 11  LYS n 
1 12  PRO n 
1 13  ASN n 
1 14  LEU n 
1 15  LEU n 
1 16  VAL n 
1 17  LEU n 
1 18  PRO n 
1 19  VAL n 
1 20  GLN n 
1 21  GLU n 
1 22  ASP n 
1 23  ALA n 
1 24  SER n 
1 25  THR n 
1 26  GLY n 
1 27  LEU n 
1 28  HIS n 
1 29  TRP n 
1 30  ALA n 
1 31  ASN n 
1 32  ILE n 
1 33  HIS n 
1 34  LYS n 
1 35  ARG n 
1 36  THR n 
1 37  PRO n 
1 38  LEU n 
1 39  MET n 
1 40  GLN n 
1 41  VAL n 
1 42  PRO n 
1 43  LEU n 
1 44  LEU n 
1 45  LEU n 
1 46  ASP n 
1 47  LEU n 
1 48  ASN n 
1 49  GLY n 
1 50  LYS n 
1 51  HIS n 
1 52  LEU n 
1 53  TRP n 
1 54  VAL n 
1 55  THR n 
1 56  CYS n 
1 57  SER n 
1 58  GLN n 
1 59  HIS n 
1 60  TYR n 
1 61  SER n 
1 62  SER n 
1 63  SER n 
1 64  THR n 
1 65  TYR n 
1 66  GLN n 
1 67  ALA n 
1 68  PRO n 
1 69  PHE n 
1 70  CYS n 
1 71  HIS n 
1 72  SER n 
1 73  THR n 
1 74  GLN n 
1 75  CYS n 
1 76  SER n 
1 77  ARG n 
1 78  ALA n 
1 79  ASN n 
1 80  THR n 
1 81  HIS n 
1 82  GLN n 
1 83  CYS n 
1 84  PHE n 
1 85  THR n 
1 86  CYS n 
1 87  THR n 
1 88  ASP n 
1 89  SER n 
1 90  THR n 
1 91  THR n 
1 92  THR n 
1 93  ARG n 
1 94  PRO n 
1 95  GLY n 
1 96  CYS n 
1 97  HIS n 
1 98  ASN n 
1 99  ASN n 
1 100 THR n 
1 101 CYS n 
1 102 GLY n 
1 103 LEU n 
1 104 LEU n 
1 105 SER n 
1 106 SER n 
1 107 ASN n 
1 108 PRO n 
1 109 VAL n 
1 110 THR n 
1 111 GLN n 
1 112 GLU n 
1 113 SER n 
1 114 GLY n 
1 115 LEU n 
1 116 GLY n 
1 117 GLU n 
1 118 LEU n 
1 119 ALA n 
1 120 GLN n 
1 121 ASP n 
1 122 VAL n 
1 123 LEU n 
1 124 ALA n 
1 125 ILE n 
1 126 HIS n 
1 127 SER n 
1 128 THR n 
1 129 HIS n 
1 130 GLY n 
1 131 SER n 
1 132 LYS n 
1 133 LEU n 
1 134 GLY n 
1 135 PRO n 
1 136 MET n 
1 137 VAL n 
1 138 LYS n 
1 139 VAL n 
1 140 PRO n 
1 141 GLN n 
1 142 PHE n 
1 143 LEU n 
1 144 PHE n 
1 145 SER n 
1 146 CYS n 
1 147 ALA n 
1 148 PRO n 
1 149 SER n 
1 150 PHE n 
1 151 LEU n 
1 152 ALA n 
1 153 GLN n 
1 154 LYS n 
1 155 GLY n 
1 156 LEU n 
1 157 PRO n 
1 158 ASN n 
1 159 ASN n 
1 160 VAL n 
1 161 GLN n 
1 162 GLY n 
1 163 ALA n 
1 164 LEU n 
1 165 GLY n 
1 166 LEU n 
1 167 GLY n 
1 168 GLN n 
1 169 ALA n 
1 170 PRO n 
1 171 ILE n 
1 172 SER n 
1 173 LEU n 
1 174 GLN n 
1 175 ASN n 
1 176 GLN n 
1 177 LEU n 
1 178 PHE n 
1 179 SER n 
1 180 HIS n 
1 181 PHE n 
1 182 GLY n 
1 183 LEU n 
1 184 LYS n 
1 185 ARG n 
1 186 GLN n 
1 187 PHE n 
1 188 SER n 
1 189 VAL n 
1 190 CYS n 
1 191 LEU n 
1 192 SER n 
1 193 ARG n 
1 194 TYR n 
1 195 SER n 
1 196 THR n 
1 197 SER n 
1 198 ASN n 
1 199 GLY n 
1 200 ALA n 
1 201 ILE n 
1 202 LEU n 
1 203 PHE n 
1 204 GLY n 
1 205 ASP n 
1 206 ILE n 
1 207 ASN n 
1 208 ASP n 
1 209 PRO n 
1 210 ASN n 
1 211 ASN n 
1 212 ASN n 
1 213 ASN n 
1 214 TYR n 
1 215 ILE n 
1 216 HIS n 
1 217 ASN n 
1 218 SER n 
1 219 LEU n 
1 220 ASP n 
1 221 VAL n 
1 222 LEU n 
1 223 HIS n 
1 224 ASP n 
1 225 LEU n 
1 226 VAL n 
1 227 TYR n 
1 228 THR n 
1 229 PRO n 
1 230 LEU n 
1 231 THR n 
1 232 ILE n 
1 233 SER n 
1 234 LYS n 
1 235 GLN n 
1 236 GLY n 
1 237 GLU n 
1 238 TYR n 
1 239 PHE n 
1 240 ILE n 
1 241 GLN n 
1 242 VAL n 
1 243 ASN n 
1 244 ALA n 
1 245 ILE n 
1 246 ARG n 
1 247 VAL n 
1 248 ASN n 
1 249 LYS n 
1 250 HIS n 
1 251 LEU n 
1 252 VAL n 
1 253 ILE n 
1 254 PRO n 
1 255 THR n 
1 256 LYS n 
1 257 ASN n 
1 258 PRO n 
1 259 PHE n 
1 260 ILE n 
1 261 SER n 
1 262 PRO n 
1 263 SER n 
1 264 SER n 
1 265 THR n 
1 266 SER n 
1 267 TYR n 
1 268 HIS n 
1 269 GLY n 
1 270 SER n 
1 271 GLY n 
1 272 GLU n 
1 273 ILE n 
1 274 GLY n 
1 275 GLY n 
1 276 ALA n 
1 277 LEU n 
1 278 ILE n 
1 279 THR n 
1 280 THR n 
1 281 THR n 
1 282 HIS n 
1 283 PRO n 
1 284 TYR n 
1 285 THR n 
1 286 VAL n 
1 287 LEU n 
1 288 SER n 
1 289 HIS n 
1 290 SER n 
1 291 ILE n 
1 292 PHE n 
1 293 GLU n 
1 294 VAL n 
1 295 PHE n 
1 296 THR n 
1 297 GLN n 
1 298 VAL n 
1 299 PHE n 
1 300 ALA n 
1 301 ASN n 
1 302 ASN n 
1 303 MET n 
1 304 PRO n 
1 305 LYS n 
1 306 GLN n 
1 307 ALA n 
1 308 GLN n 
1 309 VAL n 
1 310 LYS n 
1 311 ALA n 
1 312 VAL n 
1 313 GLY n 
1 314 PRO n 
1 315 PHE n 
1 316 GLY n 
1 317 LEU n 
1 318 CYS n 
1 319 TYR n 
1 320 ASP n 
1 321 SER n 
1 322 ARG n 
1 323 LYS n 
1 324 ILE n 
1 325 SER n 
1 326 GLY n 
1 327 GLY n 
1 328 ALA n 
1 329 PRO n 
1 330 SER n 
1 331 VAL n 
1 332 ASP n 
1 333 LEU n 
1 334 ILE n 
1 335 LEU n 
1 336 ASP n 
1 337 LYS n 
1 338 ASN n 
1 339 ASP n 
1 340 ALA n 
1 341 VAL n 
1 342 TRP n 
1 343 ARG n 
1 344 ILE n 
1 345 SER n 
1 346 SER n 
1 347 GLU n 
1 348 ASN n 
1 349 PHE n 
1 350 MET n 
1 351 VAL n 
1 352 GLN n 
1 353 ALA n 
1 354 GLN n 
1 355 ASP n 
1 356 GLY n 
1 357 VAL n 
1 358 SER n 
1 359 CYS n 
1 360 LEU n 
1 361 GLY n 
1 362 PHE n 
1 363 VAL n 
1 364 ASP n 
1 365 GLY n 
1 366 GLY n 
1 367 VAL n 
1 368 HIS n 
1 369 ALA n 
1 370 ARG n 
1 371 ALA n 
1 372 GLY n 
1 373 ILE n 
1 374 ALA n 
1 375 LEU n 
1 376 GLY n 
1 377 ALA n 
1 378 HIS n 
1 379 HIS n 
1 380 LEU n 
1 381 GLU n 
1 382 GLU n 
1 383 ASN n 
1 384 LEU n 
1 385 VAL n 
1 386 VAL n 
1 387 PHE n 
1 388 ASP n 
1 389 LEU n 
1 390 GLU n 
1 391 ARG n 
1 392 SER n 
1 393 ARG n 
1 394 VAL n 
1 395 GLY n 
1 396 PHE n 
1 397 ASN n 
1 398 SER n 
1 399 ASN n 
1 400 SER n 
1 401 LEU n 
1 402 LYS n 
1 403 SER n 
1 404 TYR n 
1 405 GLY n 
1 406 LYS n 
1 407 THR n 
1 408 CYS n 
1 409 SER n 
1 410 ASN n 
1 411 LEU n 
1 412 PHE n 
1 413 ASP n 
1 414 LEU n 
1 415 ASN n 
1 416 ASN n 
1 417 PRO n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                'Narrow-leaved blue lupin' 
_entity_src_nat.pdbx_organism_scientific   'Lupinus angustifolius' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      3871 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q42369_LUPAN 
_struct_ref.pdbx_db_accession          Q42369 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LYHNSQPTSSKPNLLVLPVQEDASTGLHWANIHKRTPLMQVPLLLDLNGKHLWVTCSQHYSSSTYQAPFCHSTQCSRANT
HQCFTCTDSTTTRPGCHNNTCGLLSSNPVTQESGLGELAQDVLAIHSTHGSKLGPMVKVPQFLFSCAPSFLAQKGLPNNV
QGALGLGQAPISLQNQLFSHFGLKRQFSVCLSRYSTSNGAILFGDINDPNNNNYIHNSLDVLHDLVYTPLTISKQGEYFI
QVNAIRVNKHLVIPTKNPFISPSSTSYHGSGEIGGALITTTHPYTVLSHSIFEVFTQVFANNMPKQAQVKAVGPFGLCYD
SRKISGGAPSVDLILDKNDAVWRISSENFMVQAQDGVSCLGFVDGGVHARAGIALGAHHLEENLVVFDLERSRVGFNSNS
LKSYGKTCSNLFDLNNP
;
_struct_ref.pdbx_align_begin           33 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 4PPH A 1 ? 417 ? Q42369 33 ? 449 ? 1 417 
2 1 4PPH B 1 ? 417 ? Q42369 33 ? 449 ? 1 417 
3 1 4PPH C 1 ? 417 ? Q42369 33 ? 449 ? 1 417 
4 1 4PPH D 1 ? 417 ? Q42369 33 ? 449 ? 1 417 
5 1 4PPH E 1 ? 417 ? Q42369 33 ? 449 ? 1 417 
6 1 4PPH F 1 ? 417 ? Q42369 33 ? 449 ? 1 417 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE               ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL         'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
FUC saccharide          . ALPHA-L-FUCOSE         ?                 'C6 H12 O5'      164.156 
GLN 'L-peptide linking' y GLUTAMINE              ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ?                 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ?                 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ?                 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4PPH 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.97 
_exptl_crystal.density_percent_sol   58.61 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '7% PEG 6000, 0.1M HEPES pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'RAYONIX MX-225' 
_diffrn_detector.pdbx_collection_date   2013-07-07 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Double Crystal Monochromator, Si-111 crystal' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.91841 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'BESSY BEAMLINE 14.2' 
_diffrn_source.pdbx_synchrotron_site       BESSY 
_diffrn_source.pdbx_synchrotron_beamline   14.2 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.91841 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4PPH 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             43.76 
_reflns.d_resolution_high            2.00 
_reflns.number_obs                   208256 
_reflns.number_all                   208256 
_reflns.percent_possible_obs         99.70 
_reflns.pdbx_Rmerge_I_obs            0.068 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.22 
_reflns.B_iso_Wilson_estimate        42.37 
_reflns.pdbx_redundancy              3.86 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.00 
_reflns_shell.d_res_low              2.12 
_reflns_shell.percent_possible_all   99.3 
_reflns_shell.Rmerge_I_obs           0.755 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.98 
_reflns_shell.pdbx_redundancy        3.86 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4PPH 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     208256 
_refine.ls_number_reflns_all                     208256 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.97 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             43.764 
_refine.ls_d_res_high                            2.009 
_refine.ls_percent_reflns_obs                    99.54 
_refine.ls_R_factor_obs                          0.1457 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1446 
_refine.ls_R_factor_R_free                       0.1740 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 0.48 
_refine.ls_number_reflns_R_free                  999 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               45.18 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  'HYDROGEN ATOMS WERE ADDED AT RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB ENTRY 3AUP, chain A' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       TWIN_LSQ_F 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            . 
_refine.pdbx_overall_phase_error                 27.18 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        17982 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         236 
_refine_hist.number_atoms_solvent             794 
_refine_hist.number_atoms_total               19012 
_refine_hist.d_res_high                       2.009 
_refine_hist.d_res_low                        43.764 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.011  ? ? 18741 'X-RAY DIFFRACTION' ? 
f_angle_d          1.425  ? ? 25374 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 14.071 ? ? 6654  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.061  ? ? 2906  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.007  ? ? 3294  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 2.0097 2.1157  29380 0.2434 99.00 0.2504 . . 142 . . . . 
'X-RAY DIFFRACTION' . 2.1157 2.2482  29717 0.2196 99.00 0.2516 . . 143 . . . . 
'X-RAY DIFFRACTION' . 2.2482 2.4218  29648 0.1945 99.00 0.2256 . . 143 . . . . 
'X-RAY DIFFRACTION' . 2.4218 2.6655  29676 0.1787 99.00 0.2240 . . 142 . . . . 
'X-RAY DIFFRACTION' . 2.6655 3.0511  29705 0.1646 99.00 0.1804 . . 144 . . . . 
'X-RAY DIFFRACTION' . 3.0511 3.8437  29607 0.1384 99.00 0.1656 . . 143 . . . . 
'X-RAY DIFFRACTION' . 3.8437 43.7745 29486 0.1024 99.00 0.1342 . . 142 . . . . 
# 
_struct.entry_id                  4PPH 
_struct.title                     'Crystal structure of conglutin gamma, a unique basic 7S globulin from lupine seeds' 
_struct.pdbx_descriptor           'Conglutin gamma' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4PPH 
_struct_keywords.pdbx_keywords   'PLANT PROTEIN' 
_struct_keywords.text            
;plant protein, lupine cotyledons, non-storage role, 7S basic globulin, glycoside-hydrolase-inhibitor-like protein, apigenin glycosides, N-linked glycosylation, insulin
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 2 ? 
H  N N 2 ? 
I  N N 3 ? 
J  N N 4 ? 
K  N N 4 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 2 ? 
Q  N N 4 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 4 ? 
V  N N 2 ? 
W  N N 4 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 2 ? 
CA N N 4 ? 
DA N N 4 ? 
EA N N 4 ? 
FA N N 4 ? 
GA N N 4 ? 
HA N N 4 ? 
IA N N 4 ? 
JA N N 4 ? 
KA N N 4 ? 
LA N N 4 ? 
MA N N 2 ? 
NA N N 2 ? 
OA N N 4 ? 
PA N N 4 ? 
QA N N 4 ? 
RA N N 4 ? 
SA N N 4 ? 
TA N N 4 ? 
UA N N 5 ? 
VA N N 5 ? 
WA N N 5 ? 
XA N N 5 ? 
YA N N 5 ? 
ZA N N 5 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  SER A 72  ? ALA A 78  ? SER A 72  ALA A 78  1 ? 7  
HELX_P HELX_P2  2  PRO A 148 ? GLN A 153 ? PRO A 148 GLN A 153 5 ? 6  
HELX_P HELX_P3  3  SER A 172 ? GLY A 182 ? SER A 172 GLY A 182 1 ? 11 
HELX_P HELX_P4  4  ASP A 208 ? ASN A 210 ? ASP A 208 ASN A 210 5 ? 3  
HELX_P HELX_P5  5  ASN A 211 ? HIS A 216 ? ASN A 211 HIS A 216 1 ? 6  
HELX_P HELX_P6  6  SER A 218 ? ASP A 224 ? SER A 218 ASP A 224 1 ? 7  
HELX_P HELX_P7  7  SER A 288 ? ASN A 302 ? SER A 288 ASN A 302 1 ? 15 
HELX_P HELX_P8  8  ARG A 322 ? GLY A 327 ? ARG A 322 GLY A 327 5 ? 6  
HELX_P HELX_P9  9  LYS A 337 ? ASP A 339 ? LYS A 337 ASP A 339 5 ? 3  
HELX_P HELX_P10 10 SER A 345 ? PHE A 349 ? SER A 345 PHE A 349 1 ? 5  
HELX_P HELX_P11 11 GLY A 376 ? GLU A 381 ? GLY A 376 GLU A 381 1 ? 6  
HELX_P HELX_P12 12 SER A 400 ? GLY A 405 ? SER A 400 GLY A 405 5 ? 6  
HELX_P HELX_P13 13 SER B 72  ? ALA B 78  ? SER B 72  ALA B 78  1 ? 7  
HELX_P HELX_P14 14 PRO B 148 ? GLN B 153 ? PRO B 148 GLN B 153 5 ? 6  
HELX_P HELX_P15 15 SER B 172 ? GLY B 182 ? SER B 172 GLY B 182 1 ? 11 
HELX_P HELX_P16 16 ASP B 208 ? ASN B 212 ? ASP B 208 ASN B 212 5 ? 5  
HELX_P HELX_P17 17 ILE B 215 ? ASN B 217 ? ILE B 215 ASN B 217 5 ? 3  
HELX_P HELX_P18 18 SER B 218 ? ASP B 224 ? SER B 218 ASP B 224 1 ? 7  
HELX_P HELX_P19 19 SER B 288 ? ASN B 302 ? SER B 288 ASN B 302 1 ? 15 
HELX_P HELX_P20 20 MET B 303 ? GLN B 308 ? MET B 303 GLN B 308 5 ? 6  
HELX_P HELX_P21 21 LYS B 337 ? ASP B 339 ? LYS B 337 ASP B 339 5 ? 3  
HELX_P HELX_P22 22 SER B 345 ? PHE B 349 ? SER B 345 PHE B 349 1 ? 5  
HELX_P HELX_P23 23 GLY B 376 ? GLU B 381 ? GLY B 376 GLU B 381 1 ? 6  
HELX_P HELX_P24 24 SER B 400 ? GLY B 405 ? SER B 400 GLY B 405 5 ? 6  
HELX_P HELX_P25 25 SER C 72  ? ASN C 79  ? SER C 72  ASN C 79  1 ? 8  
HELX_P HELX_P26 26 PRO C 148 ? GLN C 153 ? PRO C 148 GLN C 153 5 ? 6  
HELX_P HELX_P27 27 SER C 172 ? GLY C 182 ? SER C 172 GLY C 182 1 ? 11 
HELX_P HELX_P28 28 ASP C 208 ? ASN C 210 ? ASP C 208 ASN C 210 5 ? 3  
HELX_P HELX_P29 29 ASN C 211 ? HIS C 216 ? ASN C 211 HIS C 216 1 ? 6  
HELX_P HELX_P30 30 SER C 218 ? ASP C 224 ? SER C 218 ASP C 224 1 ? 7  
HELX_P HELX_P31 31 SER C 288 ? ASN C 301 ? SER C 288 ASN C 301 1 ? 14 
HELX_P HELX_P32 32 ASN C 302 ? MET C 303 ? ASN C 302 MET C 303 5 ? 2  
HELX_P HELX_P33 33 PRO C 304 ? GLN C 306 ? PRO C 304 GLN C 306 5 ? 3  
HELX_P HELX_P34 34 SER C 345 ? PHE C 349 ? SER C 345 PHE C 349 1 ? 5  
HELX_P HELX_P35 35 GLY C 376 ? GLU C 381 ? GLY C 376 GLU C 381 1 ? 6  
HELX_P HELX_P36 36 LEU C 401 ? GLY C 405 ? LEU C 401 GLY C 405 5 ? 5  
HELX_P HELX_P37 37 SER D 72  ? ALA D 78  ? SER D 72  ALA D 78  1 ? 7  
HELX_P HELX_P38 38 PRO D 148 ? GLN D 153 ? PRO D 148 GLN D 153 5 ? 6  
HELX_P HELX_P39 39 SER D 172 ? GLY D 182 ? SER D 172 GLY D 182 1 ? 11 
HELX_P HELX_P40 40 ASP D 208 ? ASN D 212 ? ASP D 208 ASN D 212 5 ? 5  
HELX_P HELX_P41 41 ILE D 215 ? ASN D 217 ? ILE D 215 ASN D 217 5 ? 3  
HELX_P HELX_P42 42 SER D 218 ? ASP D 224 ? SER D 218 ASP D 224 1 ? 7  
HELX_P HELX_P43 43 HIS D 289 ? ASN D 302 ? HIS D 289 ASN D 302 1 ? 14 
HELX_P HELX_P44 44 MET D 303 ? GLN D 306 ? MET D 303 GLN D 306 5 ? 4  
HELX_P HELX_P45 45 SER D 321 ? SER D 325 ? SER D 321 SER D 325 1 ? 5  
HELX_P HELX_P46 46 LYS D 337 ? ASP D 339 ? LYS D 337 ASP D 339 5 ? 3  
HELX_P HELX_P47 47 SER D 345 ? PHE D 349 ? SER D 345 PHE D 349 1 ? 5  
HELX_P HELX_P48 48 GLY D 376 ? GLU D 381 ? GLY D 376 GLU D 381 1 ? 6  
HELX_P HELX_P49 49 LEU D 401 ? GLY D 405 ? LEU D 401 GLY D 405 5 ? 5  
HELX_P HELX_P50 50 SER E 72  ? ALA E 78  ? SER E 72  ALA E 78  1 ? 7  
HELX_P HELX_P51 51 PRO E 148 ? GLN E 153 ? PRO E 148 GLN E 153 5 ? 6  
HELX_P HELX_P52 52 SER E 172 ? GLY E 182 ? SER E 172 GLY E 182 1 ? 11 
HELX_P HELX_P53 53 ASP E 208 ? ASN E 212 ? ASP E 208 ASN E 212 5 ? 5  
HELX_P HELX_P54 54 ILE E 215 ? ASN E 217 ? ILE E 215 ASN E 217 5 ? 3  
HELX_P HELX_P55 55 SER E 218 ? ASP E 224 ? SER E 218 ASP E 224 1 ? 7  
HELX_P HELX_P56 56 SER E 288 ? ASN E 302 ? SER E 288 ASN E 302 1 ? 15 
HELX_P HELX_P57 57 MET E 303 ? GLN E 306 ? MET E 303 GLN E 306 5 ? 4  
HELX_P HELX_P58 58 LYS E 337 ? ASP E 339 ? LYS E 337 ASP E 339 5 ? 3  
HELX_P HELX_P59 59 GLY E 376 ? GLU E 381 ? GLY E 376 GLU E 381 1 ? 6  
HELX_P HELX_P60 60 SER E 400 ? GLY E 405 ? SER E 400 GLY E 405 5 ? 6  
HELX_P HELX_P61 61 SER F 72  ? ALA F 78  ? SER F 72  ALA F 78  1 ? 7  
HELX_P HELX_P62 62 PRO F 148 ? GLN F 153 ? PRO F 148 GLN F 153 5 ? 6  
HELX_P HELX_P63 63 SER F 172 ? GLY F 182 ? SER F 172 GLY F 182 1 ? 11 
HELX_P HELX_P64 64 ASP F 208 ? ASN F 212 ? ASP F 208 ASN F 212 5 ? 5  
HELX_P HELX_P65 65 ILE F 215 ? ASN F 217 ? ILE F 215 ASN F 217 5 ? 3  
HELX_P HELX_P66 66 SER F 218 ? ASP F 224 ? SER F 218 ASP F 224 1 ? 7  
HELX_P HELX_P67 67 SER F 288 ? ASN F 302 ? SER F 288 ASN F 302 1 ? 15 
HELX_P HELX_P68 68 MET F 303 ? GLN F 306 ? MET F 303 GLN F 306 5 ? 4  
HELX_P HELX_P69 69 LYS F 337 ? ASP F 339 ? LYS F 337 ASP F 339 5 ? 3  
HELX_P HELX_P70 70 SER F 345 ? PHE F 349 ? SER F 345 PHE F 349 1 ? 5  
HELX_P HELX_P71 71 GLY F 376 ? GLU F 381 ? GLY F 376 GLU F 381 1 ? 6  
HELX_P HELX_P72 72 LEU F 401 ? GLY F 405 ? LEU F 401 GLY F 405 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A  CYS 56  SG  ? ? ? 1_555 A  CYS 146 SG ? ? A CYS 56  A CYS 146 1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf2  disulf ? ? A  CYS 70  SG  ? ? ? 1_555 A  CYS 83  SG ? ? A CYS 70  A CYS 83  1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf3  disulf ? ? A  CYS 75  SG  ? ? ? 1_555 A  CYS 101 SG B ? A CYS 75  A CYS 101 1_555 ? ? ? ? ? ? ? 2.005 ? 
disulf4  disulf ? ? A  CYS 75  SG  ? ? ? 1_555 A  CYS 101 SG A ? A CYS 75  A CYS 101 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf5  disulf ? ? A  CYS 86  SG  ? ? ? 1_555 A  CYS 96  SG ? ? A CYS 86  A CYS 96  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf6  disulf ? ? A  CYS 190 SG  ? ? ? 1_555 A  CYS 408 SG ? ? A CYS 190 A CYS 408 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf7  disulf ? ? A  CYS 318 SG  ? ? ? 1_555 A  CYS 359 SG ? ? A CYS 318 A CYS 359 1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf8  disulf ? ? B  CYS 56  SG  ? ? ? 1_555 B  CYS 146 SG ? ? B CYS 56  B CYS 146 1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf9  disulf ? ? B  CYS 70  SG  ? ? ? 1_555 B  CYS 83  SG ? ? B CYS 70  B CYS 83  1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf10 disulf ? ? B  CYS 75  SG  ? ? ? 1_555 B  CYS 101 SG B ? B CYS 75  B CYS 101 1_555 ? ? ? ? ? ? ? 1.993 ? 
disulf11 disulf ? ? B  CYS 75  SG  ? ? ? 1_555 B  CYS 101 SG A ? B CYS 75  B CYS 101 1_555 ? ? ? ? ? ? ? 2.012 ? 
disulf12 disulf ? ? B  CYS 86  SG  ? ? ? 1_555 B  CYS 96  SG ? ? B CYS 86  B CYS 96  1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf13 disulf ? ? B  CYS 190 SG  ? ? ? 1_555 B  CYS 408 SG ? ? B CYS 190 B CYS 408 1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf14 disulf ? ? B  CYS 318 SG  ? ? ? 1_555 B  CYS 359 SG ? ? B CYS 318 B CYS 359 1_555 ? ? ? ? ? ? ? 2.024 ? 
disulf15 disulf ? ? C  CYS 56  SG  ? ? ? 1_555 C  CYS 146 SG ? ? C CYS 56  C CYS 146 1_555 ? ? ? ? ? ? ? 2.022 ? 
disulf16 disulf ? ? C  CYS 70  SG  ? ? ? 1_555 C  CYS 83  SG ? ? C CYS 70  C CYS 83  1_555 ? ? ? ? ? ? ? 2.022 ? 
disulf17 disulf ? ? C  CYS 75  SG  ? ? ? 1_555 C  CYS 101 SG B ? C CYS 75  C CYS 101 1_555 ? ? ? ? ? ? ? 2.001 ? 
disulf18 disulf ? ? C  CYS 75  SG  ? ? ? 1_555 C  CYS 101 SG A ? C CYS 75  C CYS 101 1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf19 disulf ? ? C  CYS 86  SG  ? ? ? 1_555 C  CYS 96  SG ? ? C CYS 86  C CYS 96  1_555 ? ? ? ? ? ? ? 1.959 ? 
disulf20 disulf ? ? C  CYS 190 SG  ? ? ? 1_555 C  CYS 408 SG ? ? C CYS 190 C CYS 408 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf21 disulf ? ? C  CYS 318 SG  ? ? ? 1_555 C  CYS 359 SG ? ? C CYS 318 C CYS 359 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf22 disulf ? ? D  CYS 56  SG  ? ? ? 1_555 D  CYS 146 SG ? ? D CYS 56  D CYS 146 1_555 ? ? ? ? ? ? ? 2.015 ? 
disulf23 disulf ? ? D  CYS 70  SG  ? ? ? 1_555 D  CYS 83  SG ? ? D CYS 70  D CYS 83  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf24 disulf ? ? D  CYS 75  SG  ? ? ? 1_555 D  CYS 101 SG ? ? D CYS 75  D CYS 101 1_555 ? ? ? ? ? ? ? 2.007 ? 
disulf25 disulf ? ? D  CYS 86  SG  ? ? ? 1_555 D  CYS 96  SG ? ? D CYS 86  D CYS 96  1_555 ? ? ? ? ? ? ? 2.015 ? 
disulf26 disulf ? ? D  CYS 190 SG  ? ? ? 1_555 D  CYS 408 SG ? ? D CYS 190 D CYS 408 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf27 disulf ? ? D  CYS 318 SG  ? ? ? 1_555 D  CYS 359 SG ? ? D CYS 318 D CYS 359 1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf28 disulf ? ? E  CYS 56  SG  ? ? ? 1_555 E  CYS 146 SG ? ? E CYS 56  E CYS 146 1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf29 disulf ? ? E  CYS 70  SG  ? ? ? 1_555 E  CYS 83  SG ? ? E CYS 70  E CYS 83  1_555 ? ? ? ? ? ? ? 2.010 ? 
disulf30 disulf ? ? E  CYS 75  SG  ? ? ? 1_555 E  CYS 101 SG ? ? E CYS 75  E CYS 101 1_555 ? ? ? ? ? ? ? 2.018 ? 
disulf31 disulf ? ? E  CYS 86  SG  ? ? ? 1_555 E  CYS 96  SG ? ? E CYS 86  E CYS 96  1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf32 disulf ? ? E  CYS 190 SG  ? ? ? 1_555 E  CYS 408 SG ? ? E CYS 190 E CYS 408 1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf33 disulf ? ? E  CYS 318 SG  ? ? ? 1_555 E  CYS 359 SG ? ? E CYS 318 E CYS 359 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf34 disulf ? ? F  CYS 56  SG  ? ? ? 1_555 F  CYS 146 SG ? ? F CYS 56  F CYS 146 1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf35 disulf ? ? F  CYS 70  SG  ? ? ? 1_555 F  CYS 83  SG ? ? F CYS 70  F CYS 83  1_555 ? ? ? ? ? ? ? 2.010 ? 
disulf36 disulf ? ? F  CYS 75  SG  ? ? ? 1_555 F  CYS 101 SG A ? F CYS 75  F CYS 101 1_555 ? ? ? ? ? ? ? 1.981 ? 
disulf37 disulf ? ? F  CYS 75  SG  ? ? ? 1_555 F  CYS 101 SG B ? F CYS 75  F CYS 101 1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf38 disulf ? ? F  CYS 86  SG  ? ? ? 1_555 F  CYS 96  SG ? ? F CYS 86  F CYS 96  1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf39 disulf ? ? F  CYS 190 SG  ? ? ? 1_555 F  CYS 408 SG ? ? F CYS 190 F CYS 408 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf40 disulf ? ? F  CYS 318 SG  ? ? ? 1_555 F  CYS 359 SG ? ? F CYS 318 F CYS 359 1_555 ? ? ? ? ? ? ? 2.047 ? 
covale1  covale ? ? MA NAG .   O4  ? ? ? 1_555 NA NAG .   C1 ? ? F NAG 501 F NAG 502 1_555 ? ? ? ? ? ? ? 1.465 ? 
covale2  covale ? ? C  ASN 98  ND2 ? ? ? 1_555 V  NAG .   C1 ? ? C ASN 98  C NAG 501 1_555 ? ? ? ? ? ? ? 1.468 ? 
covale3  covale ? ? G  NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? A NAG 501 A NAG 502 1_555 ? ? ? ? ? ? ? 1.477 ? 
covale4  covale ? ? G  NAG .   O3  ? ? ? 1_555 I  FUC .   C1 ? ? A NAG 501 A FUC 503 1_555 ? ? ? ? ? ? ? 1.479 ? 
covale5  covale ? ? A  ASN 98  ND2 ? ? ? 1_555 G  NAG .   C1 ? ? A ASN 98  A NAG 501 1_555 ? ? ? ? ? ? ? 1.480 ? 
covale6  covale ? ? F  ASN 98  ND2 ? ? ? 1_555 MA NAG .   C1 ? ? F ASN 98  F NAG 501 1_555 ? ? ? ? ? ? ? 1.485 ? 
covale7  covale ? ? B  ASN 98  ND2 ? ? ? 1_555 P  NAG .   C1 ? ? B ASN 98  B NAG 501 1_555 ? ? ? ? ? ? ? 1.502 ? 
covale8  covale ? ? D  ASN 98  ND2 ? ? ? 1_555 BA NAG .   C1 ? ? D ASN 98  D NAG 501 1_555 ? ? ? ? ? ? ? 1.508 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 THR 36  A . ? THR 36  A PRO 37  A ? PRO 37  A 1 2.31 
2 THR 36  B . ? THR 36  B PRO 37  B ? PRO 37  B 1 1.03 
3 THR 36  C . ? THR 36  C PRO 37  C ? PRO 37  C 1 1.04 
4 GLY 326 C . ? GLY 326 C GLY 327 C ? GLY 327 C 1 2.26 
5 THR 36  D . ? THR 36  D PRO 37  D ? PRO 37  D 1 2.45 
6 THR 36  E . ? THR 36  E PRO 37  E ? PRO 37  E 1 2.69 
7 THR 36  F . ? THR 36  F PRO 37  F ? PRO 37  F 1 1.52 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A  ? 9 ? 
B  ? 9 ? 
C  ? 6 ? 
D  ? 8 ? 
E  ? 4 ? 
F  ? 9 ? 
G  ? 9 ? 
H  ? 6 ? 
I  ? 3 ? 
J  ? 9 ? 
K  ? 9 ? 
L  ? 6 ? 
M  ? 8 ? 
N  ? 4 ? 
O  ? 9 ? 
P  ? 9 ? 
Q  ? 6 ? 
R  ? 4 ? 
S  ? 9 ? 
T  ? 9 ? 
U  ? 6 ? 
V  ? 8 ? 
W  ? 4 ? 
X  ? 9 ? 
Y  ? 9 ? 
Z  ? 6 ? 
AA ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A  1 2 ? anti-parallel 
A  2 3 ? anti-parallel 
A  3 4 ? anti-parallel 
A  4 5 ? anti-parallel 
A  5 6 ? anti-parallel 
A  6 7 ? anti-parallel 
A  7 8 ? anti-parallel 
A  8 9 ? anti-parallel 
B  1 2 ? anti-parallel 
B  2 3 ? anti-parallel 
B  3 4 ? anti-parallel 
B  4 5 ? anti-parallel 
B  5 6 ? parallel      
B  6 7 ? anti-parallel 
B  7 8 ? parallel      
B  8 9 ? anti-parallel 
C  1 2 ? anti-parallel 
C  2 3 ? anti-parallel 
C  3 4 ? parallel      
C  4 5 ? anti-parallel 
C  5 6 ? parallel      
D  1 2 ? anti-parallel 
D  2 3 ? anti-parallel 
D  3 4 ? anti-parallel 
D  4 5 ? parallel      
D  5 6 ? anti-parallel 
D  6 7 ? anti-parallel 
D  7 8 ? anti-parallel 
E  1 2 ? anti-parallel 
E  2 3 ? anti-parallel 
E  3 4 ? anti-parallel 
F  1 2 ? anti-parallel 
F  2 3 ? anti-parallel 
F  3 4 ? anti-parallel 
F  4 5 ? anti-parallel 
F  5 6 ? anti-parallel 
F  6 7 ? anti-parallel 
F  7 8 ? anti-parallel 
F  8 9 ? anti-parallel 
G  1 2 ? anti-parallel 
G  2 3 ? anti-parallel 
G  3 4 ? anti-parallel 
G  4 5 ? anti-parallel 
G  5 6 ? parallel      
G  6 7 ? anti-parallel 
G  7 8 ? parallel      
G  8 9 ? anti-parallel 
H  1 2 ? anti-parallel 
H  2 3 ? anti-parallel 
H  3 4 ? parallel      
H  4 5 ? anti-parallel 
H  5 6 ? parallel      
I  1 2 ? anti-parallel 
I  2 3 ? anti-parallel 
J  1 2 ? anti-parallel 
J  2 3 ? anti-parallel 
J  3 4 ? anti-parallel 
J  4 5 ? anti-parallel 
J  5 6 ? anti-parallel 
J  6 7 ? anti-parallel 
J  7 8 ? anti-parallel 
J  8 9 ? anti-parallel 
K  1 2 ? anti-parallel 
K  2 3 ? anti-parallel 
K  3 4 ? anti-parallel 
K  4 5 ? anti-parallel 
K  5 6 ? parallel      
K  6 7 ? anti-parallel 
K  7 8 ? parallel      
K  8 9 ? anti-parallel 
L  1 2 ? anti-parallel 
L  2 3 ? anti-parallel 
L  3 4 ? parallel      
L  4 5 ? anti-parallel 
L  5 6 ? parallel      
M  1 2 ? anti-parallel 
M  2 3 ? anti-parallel 
M  3 4 ? anti-parallel 
M  4 5 ? parallel      
M  5 6 ? anti-parallel 
M  6 7 ? anti-parallel 
M  7 8 ? anti-parallel 
N  1 2 ? anti-parallel 
N  2 3 ? anti-parallel 
N  3 4 ? anti-parallel 
O  1 2 ? anti-parallel 
O  2 3 ? anti-parallel 
O  3 4 ? anti-parallel 
O  4 5 ? anti-parallel 
O  5 6 ? anti-parallel 
O  6 7 ? anti-parallel 
O  7 8 ? anti-parallel 
O  8 9 ? anti-parallel 
P  1 2 ? anti-parallel 
P  2 3 ? anti-parallel 
P  3 4 ? anti-parallel 
P  4 5 ? anti-parallel 
P  5 6 ? parallel      
P  6 7 ? anti-parallel 
P  7 8 ? parallel      
P  8 9 ? anti-parallel 
Q  1 2 ? anti-parallel 
Q  2 3 ? anti-parallel 
Q  3 4 ? parallel      
Q  4 5 ? anti-parallel 
Q  5 6 ? parallel      
R  1 2 ? anti-parallel 
R  2 3 ? anti-parallel 
R  3 4 ? anti-parallel 
S  1 2 ? anti-parallel 
S  2 3 ? anti-parallel 
S  3 4 ? anti-parallel 
S  4 5 ? anti-parallel 
S  5 6 ? anti-parallel 
S  6 7 ? anti-parallel 
S  7 8 ? anti-parallel 
S  8 9 ? anti-parallel 
T  1 2 ? anti-parallel 
T  2 3 ? anti-parallel 
T  3 4 ? anti-parallel 
T  4 5 ? anti-parallel 
T  5 6 ? parallel      
T  6 7 ? anti-parallel 
T  7 8 ? parallel      
T  8 9 ? anti-parallel 
U  1 2 ? anti-parallel 
U  2 3 ? anti-parallel 
U  3 4 ? parallel      
U  4 5 ? anti-parallel 
U  5 6 ? parallel      
V  1 2 ? anti-parallel 
V  2 3 ? anti-parallel 
V  3 4 ? anti-parallel 
V  4 5 ? parallel      
V  5 6 ? anti-parallel 
V  6 7 ? anti-parallel 
V  7 8 ? anti-parallel 
W  1 2 ? anti-parallel 
W  2 3 ? anti-parallel 
W  3 4 ? anti-parallel 
X  1 2 ? anti-parallel 
X  2 3 ? anti-parallel 
X  3 4 ? anti-parallel 
X  4 5 ? anti-parallel 
X  5 6 ? anti-parallel 
X  6 7 ? anti-parallel 
X  7 8 ? anti-parallel 
X  8 9 ? anti-parallel 
Y  1 2 ? anti-parallel 
Y  2 3 ? anti-parallel 
Y  3 4 ? anti-parallel 
Y  4 5 ? anti-parallel 
Y  5 6 ? parallel      
Y  6 7 ? anti-parallel 
Y  7 8 ? parallel      
Y  8 9 ? anti-parallel 
Z  1 2 ? anti-parallel 
Z  2 3 ? anti-parallel 
Z  3 4 ? parallel      
Z  4 5 ? anti-parallel 
Z  5 6 ? parallel      
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A  1 CYS A 83  ? PHE A 84  ? CYS A 83  PHE A 84  
A  2 THR A 100 ? SER A 106 ? THR A 100 SER A 106 
A  3 SER A 113 ? HIS A 129 ? SER A 113 HIS A 129 
A  4 LEU A 15  ? GLU A 21  ? LEU A 15  GLU A 21  
A  5 GLY A 199 ? PHE A 203 ? GLY A 199 PHE A 203 
A  6 GLN A 186 ? CYS A 190 ? GLN A 186 CYS A 190 
A  7 VAL A 385 ? ASP A 388 ? VAL A 385 ASP A 388 
A  8 ARG A 393 ? PHE A 396 ? ARG A 393 PHE A 396 
A  9 VAL A 226 ? PRO A 229 ? VAL A 226 PRO A 229 
B  1 CYS A 83  ? PHE A 84  ? CYS A 83  PHE A 84  
B  2 THR A 100 ? SER A 106 ? THR A 100 SER A 106 
B  3 SER A 113 ? HIS A 129 ? SER A 113 HIS A 129 
B  4 HIS A 28  ? LYS A 34  ? HIS A 28  LYS A 34  
B  5 MET A 39  ? ASP A 46  ? MET A 39  ASP A 46  
B  6 GLY A 162 ? GLY A 165 ? GLY A 162 GLY A 165 
B  7 TRP A 53  ? THR A 55  ? TRP A 53  THR A 55  
B  8 LYS A 132 ? ALA A 147 ? LYS A 132 ALA A 147 
B  9 SER A 113 ? HIS A 129 ? SER A 113 HIS A 129 
C  1 THR A 231 ? ILE A 232 ? THR A 231 ILE A 232 
C  2 TYR A 238 ? ILE A 240 ? TYR A 238 ILE A 240 
C  3 ALA A 276 ? ILE A 278 ? ALA A 276 ILE A 278 
C  4 ILE A 373 ? LEU A 375 ? ILE A 373 LEU A 375 
C  5 THR A 285 ? LEU A 287 ? THR A 285 LEU A 287 
C  6 PHE A 362 ? ASP A 364 ? PHE A 362 ASP A 364 
D  1 VAL A 341 ? ILE A 344 ? VAL A 341 ILE A 344 
D  2 VAL A 331 ? LEU A 335 ? VAL A 331 LEU A 335 
D  3 VAL A 242 ? VAL A 247 ? VAL A 242 VAL A 247 
D  4 HIS A 250 ? ILE A 253 ? HIS A 250 ILE A 253 
D  5 HIS B 250 ? PRO B 254 ? HIS B 250 PRO B 254 
D  6 VAL B 242 ? VAL B 247 ? VAL B 242 VAL B 247 
D  7 VAL B 331 ? LEU B 335 ? VAL B 331 LEU B 335 
D  8 VAL B 341 ? ILE B 344 ? VAL B 341 ILE B 344 
E  1 GLN A 308 ? VAL A 309 ? GLN A 308 VAL A 309 
E  2 CYS A 318 ? ASP A 320 ? CYS A 318 ASP A 320 
E  3 VAL A 357 ? LEU A 360 ? VAL A 357 LEU A 360 
E  4 MET A 350 ? GLN A 354 ? MET A 350 GLN A 354 
F  1 CYS B 83  ? PHE B 84  ? CYS B 83  PHE B 84  
F  2 THR B 100 ? SER B 106 ? THR B 100 SER B 106 
F  3 SER B 113 ? HIS B 129 ? SER B 113 HIS B 129 
F  4 LEU B 15  ? GLU B 21  ? LEU B 15  GLU B 21  
F  5 GLY B 199 ? PHE B 203 ? GLY B 199 PHE B 203 
F  6 GLN B 186 ? CYS B 190 ? GLN B 186 CYS B 190 
F  7 VAL B 385 ? ASP B 388 ? VAL B 385 ASP B 388 
F  8 ARG B 393 ? ASN B 397 ? ARG B 393 ASN B 397 
F  9 LEU B 225 ? PRO B 229 ? LEU B 225 PRO B 229 
G  1 CYS B 83  ? PHE B 84  ? CYS B 83  PHE B 84  
G  2 THR B 100 ? SER B 106 ? THR B 100 SER B 106 
G  3 SER B 113 ? HIS B 129 ? SER B 113 HIS B 129 
G  4 HIS B 28  ? LYS B 34  ? HIS B 28  LYS B 34  
G  5 MET B 39  ? ASP B 46  ? MET B 39  ASP B 46  
G  6 GLY B 162 ? GLY B 165 ? GLY B 162 GLY B 165 
G  7 TRP B 53  ? THR B 55  ? TRP B 53  THR B 55  
G  8 LYS B 132 ? ALA B 147 ? LYS B 132 ALA B 147 
G  9 SER B 113 ? HIS B 129 ? SER B 113 HIS B 129 
H  1 THR B 231 ? ILE B 232 ? THR B 231 ILE B 232 
H  2 TYR B 238 ? ILE B 240 ? TYR B 238 ILE B 240 
H  3 ALA B 276 ? ILE B 278 ? ALA B 276 ILE B 278 
H  4 ILE B 373 ? LEU B 375 ? ILE B 373 LEU B 375 
H  5 THR B 285 ? LEU B 287 ? THR B 285 LEU B 287 
H  6 PHE B 362 ? ASP B 364 ? PHE B 362 ASP B 364 
I  1 CYS B 318 ? ASP B 320 ? CYS B 318 ASP B 320 
I  2 VAL B 357 ? LEU B 360 ? VAL B 357 LEU B 360 
I  3 MET B 350 ? GLN B 354 ? MET B 350 GLN B 354 
J  1 CYS C 83  ? THR C 85  ? CYS C 83  THR C 85  
J  2 ASN C 98  ? SER C 106 ? ASN C 98  SER C 106 
J  3 SER C 113 ? HIS C 129 ? SER C 113 HIS C 129 
J  4 LEU C 15  ? GLU C 21  ? LEU C 15  GLU C 21  
J  5 GLY C 199 ? PHE C 203 ? GLY C 199 PHE C 203 
J  6 GLN C 186 ? CYS C 190 ? GLN C 186 CYS C 190 
J  7 VAL C 385 ? ASP C 388 ? VAL C 385 ASP C 388 
J  8 ARG C 393 ? ASN C 397 ? ARG C 393 ASN C 397 
J  9 LEU C 225 ? PRO C 229 ? LEU C 225 PRO C 229 
K  1 CYS C 83  ? THR C 85  ? CYS C 83  THR C 85  
K  2 ASN C 98  ? SER C 106 ? ASN C 98  SER C 106 
K  3 SER C 113 ? HIS C 129 ? SER C 113 HIS C 129 
K  4 HIS C 28  ? LYS C 34  ? HIS C 28  LYS C 34  
K  5 MET C 39  ? ASP C 46  ? MET C 39  ASP C 46  
K  6 GLY C 162 ? GLY C 165 ? GLY C 162 GLY C 165 
K  7 TRP C 53  ? THR C 55  ? TRP C 53  THR C 55  
K  8 LYS C 132 ? ALA C 147 ? LYS C 132 ALA C 147 
K  9 SER C 113 ? HIS C 129 ? SER C 113 HIS C 129 
L  1 THR C 231 ? ILE C 232 ? THR C 231 ILE C 232 
L  2 TYR C 238 ? ILE C 240 ? TYR C 238 ILE C 240 
L  3 ALA C 276 ? ILE C 278 ? ALA C 276 ILE C 278 
L  4 ILE C 373 ? LEU C 375 ? ILE C 373 LEU C 375 
L  5 THR C 285 ? LEU C 287 ? THR C 285 LEU C 287 
L  6 PHE C 362 ? ASP C 364 ? PHE C 362 ASP C 364 
M  1 VAL C 341 ? ILE C 344 ? VAL C 341 ILE C 344 
M  2 VAL C 331 ? LEU C 335 ? VAL C 331 LEU C 335 
M  3 VAL C 242 ? VAL C 247 ? VAL C 242 VAL C 247 
M  4 HIS C 250 ? ILE C 253 ? HIS C 250 ILE C 253 
M  5 HIS D 250 ? PRO D 254 ? HIS D 250 PRO D 254 
M  6 VAL D 242 ? VAL D 247 ? VAL D 242 VAL D 247 
M  7 VAL D 331 ? LEU D 335 ? VAL D 331 LEU D 335 
M  8 VAL D 341 ? ILE D 344 ? VAL D 341 ILE D 344 
N  1 GLN C 308 ? VAL C 309 ? GLN C 308 VAL C 309 
N  2 CYS C 318 ? ASP C 320 ? CYS C 318 ASP C 320 
N  3 VAL C 357 ? LEU C 360 ? VAL C 357 LEU C 360 
N  4 MET C 350 ? GLN C 354 ? MET C 350 GLN C 354 
O  1 CYS D 83  ? THR D 85  ? CYS D 83  THR D 85  
O  2 ASN D 98  ? SER D 106 ? ASN D 98  SER D 106 
O  3 SER D 113 ? HIS D 129 ? SER D 113 HIS D 129 
O  4 LEU D 14  ? GLU D 21  ? LEU D 14  GLU D 21  
O  5 GLY D 199 ? GLY D 204 ? GLY D 199 GLY D 204 
O  6 GLN D 186 ? CYS D 190 ? GLN D 186 CYS D 190 
O  7 VAL D 385 ? ASP D 388 ? VAL D 385 ASP D 388 
O  8 ARG D 393 ? ASN D 397 ? ARG D 393 ASN D 397 
O  9 LEU D 225 ? PRO D 229 ? LEU D 225 PRO D 229 
P  1 CYS D 83  ? THR D 85  ? CYS D 83  THR D 85  
P  2 ASN D 98  ? SER D 106 ? ASN D 98  SER D 106 
P  3 SER D 113 ? HIS D 129 ? SER D 113 HIS D 129 
P  4 HIS D 28  ? LYS D 34  ? HIS D 28  LYS D 34  
P  5 MET D 39  ? ASP D 46  ? MET D 39  ASP D 46  
P  6 GLY D 162 ? GLY D 165 ? GLY D 162 GLY D 165 
P  7 TRP D 53  ? THR D 55  ? TRP D 53  THR D 55  
P  8 LYS D 132 ? ALA D 147 ? LYS D 132 ALA D 147 
P  9 SER D 113 ? HIS D 129 ? SER D 113 HIS D 129 
Q  1 THR D 231 ? ILE D 232 ? THR D 231 ILE D 232 
Q  2 TYR D 238 ? ILE D 240 ? TYR D 238 ILE D 240 
Q  3 ALA D 276 ? ILE D 278 ? ALA D 276 ILE D 278 
Q  4 ILE D 373 ? LEU D 375 ? ILE D 373 LEU D 375 
Q  5 THR D 285 ? SER D 288 ? THR D 285 SER D 288 
Q  6 PHE D 362 ? GLY D 366 ? PHE D 362 GLY D 366 
R  1 GLN D 308 ? VAL D 309 ? GLN D 308 VAL D 309 
R  2 CYS D 318 ? ASP D 320 ? CYS D 318 ASP D 320 
R  3 VAL D 357 ? LEU D 360 ? VAL D 357 LEU D 360 
R  4 MET D 350 ? GLN D 352 ? MET D 350 GLN D 352 
S  1 CYS E 83  ? PHE E 84  ? CYS E 83  PHE E 84  
S  2 THR E 100 ? SER E 106 ? THR E 100 SER E 106 
S  3 SER E 113 ? HIS E 129 ? SER E 113 HIS E 129 
S  4 LEU E 14  ? GLU E 21  ? LEU E 14  GLU E 21  
S  5 GLY E 199 ? GLY E 204 ? GLY E 199 GLY E 204 
S  6 GLN E 186 ? CYS E 190 ? GLN E 186 CYS E 190 
S  7 LEU E 384 ? ASP E 388 ? LEU E 384 ASP E 388 
S  8 ARG E 393 ? PHE E 396 ? ARG E 393 PHE E 396 
S  9 VAL E 226 ? PRO E 229 ? VAL E 226 PRO E 229 
T  1 CYS E 83  ? PHE E 84  ? CYS E 83  PHE E 84  
T  2 THR E 100 ? SER E 106 ? THR E 100 SER E 106 
T  3 SER E 113 ? HIS E 129 ? SER E 113 HIS E 129 
T  4 HIS E 28  ? LYS E 34  ? HIS E 28  LYS E 34  
T  5 MET E 39  ? ASP E 46  ? MET E 39  ASP E 46  
T  6 GLY E 162 ? GLY E 165 ? GLY E 162 GLY E 165 
T  7 TRP E 53  ? THR E 55  ? TRP E 53  THR E 55  
T  8 LYS E 132 ? ALA E 147 ? LYS E 132 ALA E 147 
T  9 SER E 113 ? HIS E 129 ? SER E 113 HIS E 129 
U  1 THR E 231 ? ILE E 232 ? THR E 231 ILE E 232 
U  2 TYR E 238 ? ILE E 240 ? TYR E 238 ILE E 240 
U  3 ALA E 276 ? ILE E 278 ? ALA E 276 ILE E 278 
U  4 ILE E 373 ? LEU E 375 ? ILE E 373 LEU E 375 
U  5 THR E 285 ? LEU E 287 ? THR E 285 LEU E 287 
U  6 PHE E 362 ? ASP E 364 ? PHE E 362 ASP E 364 
V  1 VAL E 341 ? ILE E 344 ? VAL E 341 ILE E 344 
V  2 VAL E 331 ? LEU E 335 ? VAL E 331 LEU E 335 
V  3 VAL E 242 ? VAL E 247 ? VAL E 242 VAL E 247 
V  4 HIS E 250 ? ILE E 253 ? HIS E 250 ILE E 253 
V  5 HIS F 250 ? PRO F 254 ? HIS F 250 PRO F 254 
V  6 VAL F 242 ? VAL F 247 ? VAL F 242 VAL F 247 
V  7 VAL F 331 ? LEU F 335 ? VAL F 331 LEU F 335 
V  8 VAL F 341 ? ILE F 344 ? VAL F 341 ILE F 344 
W  1 GLN E 308 ? VAL E 309 ? GLN E 308 VAL E 309 
W  2 CYS E 318 ? TYR E 319 ? CYS E 318 TYR E 319 
W  3 SER E 358 ? LEU E 360 ? SER E 358 LEU E 360 
W  4 MET E 350 ? VAL E 351 ? MET E 350 VAL E 351 
X  1 CYS F 83  ? PHE F 84  ? CYS F 83  PHE F 84  
X  2 THR F 100 ? SER F 106 ? THR F 100 SER F 106 
X  3 SER F 113 ? HIS F 129 ? SER F 113 HIS F 129 
X  4 LEU F 14  ? GLU F 21  ? LEU F 14  GLU F 21  
X  5 GLY F 199 ? GLY F 204 ? GLY F 199 GLY F 204 
X  6 GLN F 186 ? CYS F 190 ? GLN F 186 CYS F 190 
X  7 LEU F 384 ? ASP F 388 ? LEU F 384 ASP F 388 
X  8 ARG F 393 ? ASN F 397 ? ARG F 393 ASN F 397 
X  9 LEU F 225 ? PRO F 229 ? LEU F 225 PRO F 229 
Y  1 CYS F 83  ? PHE F 84  ? CYS F 83  PHE F 84  
Y  2 THR F 100 ? SER F 106 ? THR F 100 SER F 106 
Y  3 SER F 113 ? HIS F 129 ? SER F 113 HIS F 129 
Y  4 HIS F 28  ? LYS F 34  ? HIS F 28  LYS F 34  
Y  5 MET F 39  ? ASP F 46  ? MET F 39  ASP F 46  
Y  6 GLY F 162 ? GLY F 165 ? GLY F 162 GLY F 165 
Y  7 TRP F 53  ? THR F 55  ? TRP F 53  THR F 55  
Y  8 LYS F 132 ? ALA F 147 ? LYS F 132 ALA F 147 
Y  9 SER F 113 ? HIS F 129 ? SER F 113 HIS F 129 
Z  1 THR F 231 ? ILE F 232 ? THR F 231 ILE F 232 
Z  2 TYR F 238 ? ILE F 240 ? TYR F 238 ILE F 240 
Z  3 ALA F 276 ? ILE F 278 ? ALA F 276 ILE F 278 
Z  4 ILE F 373 ? LEU F 375 ? ILE F 373 LEU F 375 
Z  5 THR F 285 ? LEU F 287 ? THR F 285 LEU F 287 
Z  6 PHE F 362 ? ASP F 364 ? PHE F 362 ASP F 364 
AA 1 GLN F 308 ? VAL F 309 ? GLN F 308 VAL F 309 
AA 2 CYS F 318 ? ASP F 320 ? CYS F 318 ASP F 320 
AA 3 VAL F 357 ? LEU F 360 ? VAL F 357 LEU F 360 
AA 4 MET F 350 ? GLN F 354 ? MET F 350 GLN F 354 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A  1 2 N PHE A 84  ? N PHE A 84  O THR A 100 ? O THR A 100 
A  2 3 N LEU A 103 ? N LEU A 103 O GLY A 116 ? O GLY A 116 
A  3 4 O HIS A 126 ? O HIS A 126 N VAL A 16  ? N VAL A 16  
A  4 5 N VAL A 19  ? N VAL A 19  O GLY A 199 ? O GLY A 199 
A  5 6 O ALA A 200 ? O ALA A 200 N CYS A 190 ? N CYS A 190 
A  6 7 N PHE A 187 ? N PHE A 187 O PHE A 387 ? O PHE A 387 
A  7 8 N VAL A 386 ? N VAL A 386 O GLY A 395 ? O GLY A 395 
A  8 9 O VAL A 394 ? O VAL A 394 N THR A 228 ? N THR A 228 
B  1 2 N PHE A 84  ? N PHE A 84  O THR A 100 ? O THR A 100 
B  2 3 N LEU A 103 ? N LEU A 103 O GLY A 116 ? O GLY A 116 
B  3 4 O ALA A 124 ? O ALA A 124 N HIS A 33  ? N HIS A 33  
B  4 5 N ALA A 30  ? N ALA A 30  O LEU A 43  ? O LEU A 43  
B  5 6 N LEU A 44  ? N LEU A 44  O GLY A 162 ? O GLY A 162 
B  6 7 O ALA A 163 ? O ALA A 163 N TRP A 53  ? N TRP A 53  
B  7 8 N VAL A 54  ? N VAL A 54  O ALA A 147 ? O ALA A 147 
B  8 9 O VAL A 137 ? O VAL A 137 N ILE A 125 ? N ILE A 125 
C  1 2 N THR A 231 ? N THR A 231 O PHE A 239 ? O PHE A 239 
C  2 3 N ILE A 240 ? N ILE A 240 O ALA A 276 ? O ALA A 276 
C  3 4 N LEU A 277 ? N LEU A 277 O LEU A 375 ? O LEU A 375 
C  4 5 O ALA A 374 ? O ALA A 374 N VAL A 286 ? N VAL A 286 
C  5 6 N THR A 285 ? N THR A 285 O VAL A 363 ? O VAL A 363 
D  1 2 O TRP A 342 ? O TRP A 342 N LEU A 333 ? N LEU A 333 
D  2 3 O ASP A 332 ? O ASP A 332 N ARG A 246 ? N ARG A 246 
D  3 4 N ILE A 245 ? N ILE A 245 O VAL A 252 ? O VAL A 252 
D  4 5 N LEU A 251 ? N LEU A 251 O ILE B 253 ? O ILE B 253 
D  5 6 O VAL B 252 ? O VAL B 252 N ILE B 245 ? N ILE B 245 
D  6 7 N ARG B 246 ? N ARG B 246 O ASP B 332 ? O ASP B 332 
D  7 8 N VAL B 331 ? N VAL B 331 O ILE B 344 ? O ILE B 344 
E  1 2 N VAL A 309 ? N VAL A 309 O CYS A 318 ? O CYS A 318 
E  2 3 N TYR A 319 ? N TYR A 319 O SER A 358 ? O SER A 358 
E  3 4 O CYS A 359 ? O CYS A 359 N VAL A 351 ? N VAL A 351 
F  1 2 N PHE B 84  ? N PHE B 84  O THR B 100 ? O THR B 100 
F  2 3 N LEU B 103 ? N LEU B 103 O GLY B 116 ? O GLY B 116 
F  3 4 O HIS B 126 ? O HIS B 126 N VAL B 16  ? N VAL B 16  
F  4 5 N LEU B 17  ? N LEU B 17  O ILE B 201 ? O ILE B 201 
F  5 6 O ALA B 200 ? O ALA B 200 N CYS B 190 ? N CYS B 190 
F  6 7 N PHE B 187 ? N PHE B 187 O PHE B 387 ? O PHE B 387 
F  7 8 N VAL B 386 ? N VAL B 386 O GLY B 395 ? O GLY B 395 
F  8 9 O VAL B 394 ? O VAL B 394 N THR B 228 ? N THR B 228 
G  1 2 N PHE B 84  ? N PHE B 84  O THR B 100 ? O THR B 100 
G  2 3 N LEU B 103 ? N LEU B 103 O GLY B 116 ? O GLY B 116 
G  3 4 O ALA B 124 ? O ALA B 124 N HIS B 33  ? N HIS B 33  
G  4 5 N ILE B 32  ? N ILE B 32  O VAL B 41  ? O VAL B 41  
G  5 6 N LEU B 44  ? N LEU B 44  O LEU B 164 ? O LEU B 164 
G  6 7 O ALA B 163 ? O ALA B 163 N TRP B 53  ? N TRP B 53  
G  7 8 N VAL B 54  ? N VAL B 54  O ALA B 147 ? O ALA B 147 
G  8 9 O PHE B 144 ? O PHE B 144 N ALA B 119 ? N ALA B 119 
H  1 2 N THR B 231 ? N THR B 231 O PHE B 239 ? O PHE B 239 
H  2 3 N ILE B 240 ? N ILE B 240 O ALA B 276 ? O ALA B 276 
H  3 4 N LEU B 277 ? N LEU B 277 O LEU B 375 ? O LEU B 375 
H  4 5 O ALA B 374 ? O ALA B 374 N VAL B 286 ? N VAL B 286 
H  5 6 N LEU B 287 ? N LEU B 287 O VAL B 363 ? O VAL B 363 
I  1 2 N TYR B 319 ? N TYR B 319 O SER B 358 ? O SER B 358 
I  2 3 O CYS B 359 ? O CYS B 359 N VAL B 351 ? N VAL B 351 
J  1 2 N PHE C 84  ? N PHE C 84  O THR C 100 ? O THR C 100 
J  2 3 N LEU C 103 ? N LEU C 103 O GLY C 116 ? O GLY C 116 
J  3 4 O HIS C 126 ? O HIS C 126 N VAL C 16  ? N VAL C 16  
J  4 5 N LEU C 17  ? N LEU C 17  O ILE C 201 ? O ILE C 201 
J  5 6 O ALA C 200 ? O ALA C 200 N CYS C 190 ? N CYS C 190 
J  6 7 N PHE C 187 ? N PHE C 187 O PHE C 387 ? O PHE C 387 
J  7 8 N VAL C 386 ? N VAL C 386 O GLY C 395 ? O GLY C 395 
J  8 9 O VAL C 394 ? O VAL C 394 N THR C 228 ? N THR C 228 
K  1 2 N PHE C 84  ? N PHE C 84  O THR C 100 ? O THR C 100 
K  2 3 N LEU C 103 ? N LEU C 103 O GLY C 116 ? O GLY C 116 
K  3 4 O ALA C 124 ? O ALA C 124 N HIS C 33  ? N HIS C 33  
K  4 5 N ALA C 30  ? N ALA C 30  O LEU C 43  ? O LEU C 43  
K  5 6 N LEU C 44  ? N LEU C 44  O GLY C 162 ? O GLY C 162 
K  6 7 O ALA C 163 ? O ALA C 163 N TRP C 53  ? N TRP C 53  
K  7 8 N VAL C 54  ? N VAL C 54  O ALA C 147 ? O ALA C 147 
K  8 9 O VAL C 139 ? O VAL C 139 N LEU C 123 ? N LEU C 123 
L  1 2 N THR C 231 ? N THR C 231 O PHE C 239 ? O PHE C 239 
L  2 3 N TYR C 238 ? N TYR C 238 O ILE C 278 ? O ILE C 278 
L  3 4 N LEU C 277 ? N LEU C 277 O LEU C 375 ? O LEU C 375 
L  4 5 O ALA C 374 ? O ALA C 374 N VAL C 286 ? N VAL C 286 
L  5 6 N LEU C 287 ? N LEU C 287 O VAL C 363 ? O VAL C 363 
M  1 2 O ILE C 344 ? O ILE C 344 N VAL C 331 ? N VAL C 331 
M  2 3 O ASP C 332 ? O ASP C 332 N ARG C 246 ? N ARG C 246 
M  3 4 N ILE C 245 ? N ILE C 245 O VAL C 252 ? O VAL C 252 
M  4 5 N LEU C 251 ? N LEU C 251 O ILE D 253 ? O ILE D 253 
M  5 6 O HIS D 250 ? O HIS D 250 N VAL D 247 ? N VAL D 247 
M  6 7 N ALA D 244 ? N ALA D 244 O ILE D 334 ? O ILE D 334 
M  7 8 N LEU D 333 ? N LEU D 333 O TRP D 342 ? O TRP D 342 
N  1 2 N VAL C 309 ? N VAL C 309 O CYS C 318 ? O CYS C 318 
N  2 3 N TYR C 319 ? N TYR C 319 O SER C 358 ? O SER C 358 
N  3 4 O CYS C 359 ? O CYS C 359 N VAL C 351 ? N VAL C 351 
O  1 2 N PHE D 84  ? N PHE D 84  O THR D 100 ? O THR D 100 
O  2 3 N LEU D 103 ? N LEU D 103 O GLY D 116 ? O GLY D 116 
O  3 4 O HIS D 126 ? O HIS D 126 N VAL D 16  ? N VAL D 16  
O  4 5 N LEU D 17  ? N LEU D 17  O ILE D 201 ? O ILE D 201 
O  5 6 O GLY D 204 ? O GLY D 204 N GLN D 186 ? N GLN D 186 
O  6 7 N PHE D 187 ? N PHE D 187 O PHE D 387 ? O PHE D 387 
O  7 8 N VAL D 386 ? N VAL D 386 O GLY D 395 ? O GLY D 395 
O  8 9 O VAL D 394 ? O VAL D 394 N THR D 228 ? N THR D 228 
P  1 2 N PHE D 84  ? N PHE D 84  O THR D 100 ? O THR D 100 
P  2 3 N LEU D 103 ? N LEU D 103 O GLY D 116 ? O GLY D 116 
P  3 4 O ALA D 124 ? O ALA D 124 N HIS D 33  ? N HIS D 33  
P  4 5 N LYS D 34  ? N LYS D 34  O MET D 39  ? O MET D 39  
P  5 6 N LEU D 44  ? N LEU D 44  O GLY D 162 ? O GLY D 162 
P  6 7 O ALA D 163 ? O ALA D 163 N TRP D 53  ? N TRP D 53  
P  7 8 N VAL D 54  ? N VAL D 54  O SER D 145 ? O SER D 145 
P  8 9 O LYS D 132 ? O LYS D 132 N HIS D 129 ? N HIS D 129 
Q  1 2 N THR D 231 ? N THR D 231 O PHE D 239 ? O PHE D 239 
Q  2 3 N ILE D 240 ? N ILE D 240 O ALA D 276 ? O ALA D 276 
Q  3 4 N LEU D 277 ? N LEU D 277 O LEU D 375 ? O LEU D 375 
Q  4 5 O ALA D 374 ? O ALA D 374 N VAL D 286 ? N VAL D 286 
Q  5 6 N LEU D 287 ? N LEU D 287 O GLY D 365 ? O GLY D 365 
R  1 2 N VAL D 309 ? N VAL D 309 O CYS D 318 ? O CYS D 318 
R  2 3 N TYR D 319 ? N TYR D 319 O SER D 358 ? O SER D 358 
R  3 4 O CYS D 359 ? O CYS D 359 N VAL D 351 ? N VAL D 351 
S  1 2 N PHE E 84  ? N PHE E 84  O THR E 100 ? O THR E 100 
S  2 3 N LEU E 103 ? N LEU E 103 O GLY E 116 ? O GLY E 116 
S  3 4 O HIS E 126 ? O HIS E 126 N VAL E 16  ? N VAL E 16  
S  4 5 N VAL E 19  ? N VAL E 19  O GLY E 199 ? O GLY E 199 
S  5 6 O ALA E 200 ? O ALA E 200 N CYS E 190 ? N CYS E 190 
S  6 7 N PHE E 187 ? N PHE E 187 O PHE E 387 ? O PHE E 387 
S  7 8 N VAL E 386 ? N VAL E 386 O GLY E 395 ? O GLY E 395 
S  8 9 O PHE E 396 ? O PHE E 396 N VAL E 226 ? N VAL E 226 
T  1 2 N PHE E 84  ? N PHE E 84  O THR E 100 ? O THR E 100 
T  2 3 N LEU E 103 ? N LEU E 103 O GLY E 116 ? O GLY E 116 
T  3 4 O ALA E 124 ? O ALA E 124 N HIS E 33  ? N HIS E 33  
T  4 5 N ILE E 32  ? N ILE E 32  O VAL E 41  ? O VAL E 41  
T  5 6 N LEU E 44  ? N LEU E 44  O LEU E 164 ? O LEU E 164 
T  6 7 O ALA E 163 ? O ALA E 163 N TRP E 53  ? N TRP E 53  
T  7 8 N VAL E 54  ? N VAL E 54  O ALA E 147 ? O ALA E 147 
T  8 9 O GLY E 134 ? O GLY E 134 N SER E 127 ? N SER E 127 
U  1 2 N THR E 231 ? N THR E 231 O PHE E 239 ? O PHE E 239 
U  2 3 N ILE E 240 ? N ILE E 240 O ALA E 276 ? O ALA E 276 
U  3 4 N LEU E 277 ? N LEU E 277 O ILE E 373 ? O ILE E 373 
U  4 5 O ALA E 374 ? O ALA E 374 N VAL E 286 ? N VAL E 286 
U  5 6 N LEU E 287 ? N LEU E 287 O VAL E 363 ? O VAL E 363 
V  1 2 O ILE E 344 ? O ILE E 344 N VAL E 331 ? N VAL E 331 
V  2 3 O ASP E 332 ? O ASP E 332 N ARG E 246 ? N ARG E 246 
V  3 4 N VAL E 247 ? N VAL E 247 O HIS E 250 ? O HIS E 250 
V  4 5 N LEU E 251 ? N LEU E 251 O ILE F 253 ? O ILE F 253 
V  5 6 O HIS F 250 ? O HIS F 250 N VAL F 247 ? N VAL F 247 
V  6 7 N ARG F 246 ? N ARG F 246 O ASP F 332 ? O ASP F 332 
V  7 8 N VAL F 331 ? N VAL F 331 O ILE F 344 ? O ILE F 344 
W  1 2 N VAL E 309 ? N VAL E 309 O CYS E 318 ? O CYS E 318 
W  2 3 N TYR E 319 ? N TYR E 319 O SER E 358 ? O SER E 358 
W  3 4 O CYS E 359 ? O CYS E 359 N VAL E 351 ? N VAL E 351 
X  1 2 N PHE F 84  ? N PHE F 84  O THR F 100 ? O THR F 100 
X  2 3 N LEU F 103 ? N LEU F 103 O GLY F 116 ? O GLY F 116 
X  3 4 O HIS F 126 ? O HIS F 126 N VAL F 16  ? N VAL F 16  
X  4 5 N LEU F 17  ? N LEU F 17  O ILE F 201 ? O ILE F 201 
X  5 6 O GLY F 204 ? O GLY F 204 N GLN F 186 ? N GLN F 186 
X  6 7 N PHE F 187 ? N PHE F 187 O PHE F 387 ? O PHE F 387 
X  7 8 N VAL F 386 ? N VAL F 386 O GLY F 395 ? O GLY F 395 
X  8 9 O VAL F 394 ? O VAL F 394 N THR F 228 ? N THR F 228 
Y  1 2 N PHE F 84  ? N PHE F 84  O THR F 100 ? O THR F 100 
Y  2 3 N LEU F 103 ? N LEU F 103 O GLY F 116 ? O GLY F 116 
Y  3 4 O ALA F 124 ? O ALA F 124 N HIS F 33  ? N HIS F 33  
Y  4 5 N HIS F 28  ? N HIS F 28  O LEU F 45  ? O LEU F 45  
Y  5 6 N LEU F 44  ? N LEU F 44  O LEU F 164 ? O LEU F 164 
Y  6 7 O ALA F 163 ? O ALA F 163 N TRP F 53  ? N TRP F 53  
Y  7 8 N VAL F 54  ? N VAL F 54  O ALA F 147 ? O ALA F 147 
Y  8 9 O VAL F 139 ? O VAL F 139 N LEU F 123 ? N LEU F 123 
Z  1 2 N THR F 231 ? N THR F 231 O PHE F 239 ? O PHE F 239 
Z  2 3 N ILE F 240 ? N ILE F 240 O ALA F 276 ? O ALA F 276 
Z  3 4 N LEU F 277 ? N LEU F 277 O LEU F 375 ? O LEU F 375 
Z  4 5 O ALA F 374 ? O ALA F 374 N VAL F 286 ? N VAL F 286 
Z  5 6 N LEU F 287 ? N LEU F 287 O VAL F 363 ? O VAL F 363 
AA 1 2 N VAL F 309 ? N VAL F 309 O CYS F 318 ? O CYS F 318 
AA 2 3 N TYR F 319 ? N TYR F 319 O SER F 358 ? O SER F 358 
AA 3 4 O CYS F 359 ? O CYS F 359 N VAL F 351 ? N VAL F 351 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 501' 
AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 502' 
AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE FUC A 503' 
AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO A 504' 
AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO A 505' 
AC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE EDO A 506' 
AC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE EDO A 507' 
AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO A 508' 
AC9 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 509' 
BC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG B 501' 
BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO B 502' 
BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO B 503' 
BC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE EDO B 504' 
BC5 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO B 505' 
BC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO B 506' 
BC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG C 501' 
BC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO C 502' 
BC9 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO C 503' 
CC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO C 504' 
CC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO C 505' 
CC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE EDO C 506' 
CC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG D 501' 
CC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO D 502' 
CC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO D 503' 
CC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO D 504' 
CC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO D 505' 
CC9 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO D 506' 
DC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO D 507' 
DC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO D 508' 
DC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO D 509' 
DC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE EDO D 510' 
DC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO E 501' 
DC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG F 501' 
DC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG F 502' 
DC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO F 503' 
DC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO F 504' 
EC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE EDO F 505' 
EC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE EDO F 506' 
EC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO F 507' 
EC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO F 508' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 4 THR A  92  ? THR A 92  . ? 1_555 ? 
2   AC1 4 ASN A  98  ? ASN A 98  . ? 1_555 ? 
3   AC1 4 NAG H  .   ? NAG A 502 . ? 1_555 ? 
4   AC1 4 FUC I  .   ? FUC A 503 . ? 1_555 ? 
5   AC2 2 NAG G  .   ? NAG A 501 . ? 1_555 ? 
6   AC2 2 FUC I  .   ? FUC A 503 . ? 1_555 ? 
7   AC3 3 THR A  90  ? THR A 90  . ? 1_555 ? 
8   AC3 3 NAG G  .   ? NAG A 501 . ? 1_555 ? 
9   AC3 3 NAG H  .   ? NAG A 502 . ? 1_555 ? 
10  AC4 6 ARG A  185 ? ARG A 185 . ? 1_555 ? 
11  AC4 6 LEU A  389 ? LEU A 389 . ? 1_555 ? 
12  AC4 6 HOH UA .   ? HOH A 620 . ? 1_555 ? 
13  AC4 6 HOH UA .   ? HOH A 707 . ? 1_555 ? 
14  AC4 6 HOH UA .   ? HOH A 741 . ? 1_555 ? 
15  AC4 6 ARG F  77  ? ARG F 77  . ? 1_555 ? 
16  AC5 4 ASP A  224 ? ASP A 224 . ? 1_555 ? 
17  AC5 4 SER A  398 ? SER A 398 . ? 1_555 ? 
18  AC5 4 ASN A  399 ? ASN A 399 . ? 1_555 ? 
19  AC5 4 GLY D  130 ? GLY D 130 . ? 1_565 ? 
20  AC6 8 ASN A  399 ? ASN A 399 . ? 1_555 ? 
21  AC6 8 SER A  400 ? SER A 400 . ? 1_555 ? 
22  AC6 8 SER A  403 ? SER A 403 . ? 1_555 ? 
23  AC6 8 ASN D  210 ? ASN D 210 . ? 1_565 ? 
24  AC6 8 ASN D  211 ? ASN D 211 . ? 1_565 ? 
25  AC6 8 ASN D  212 ? ASN D 212 . ? 1_565 ? 
26  AC6 8 ASN D  213 ? ASN D 213 . ? 1_565 ? 
27  AC6 8 HOH XA .   ? HOH D 689 . ? 1_565 ? 
28  AC7 2 PRO A  18  ? PRO A 18  . ? 1_555 ? 
29  AC7 2 ASN A  31  ? ASN A 31  . ? 1_555 ? 
30  AC8 4 ASN A  48  ? ASN A 48  . ? 1_555 ? 
31  AC8 4 GLN A  235 ? GLN A 235 . ? 1_555 ? 
32  AC8 4 GLU A  237 ? GLU A 237 . ? 1_555 ? 
33  AC8 4 EDO O  .   ? EDO A 509 . ? 1_555 ? 
34  AC9 7 GLY A  49  ? GLY A 49  . ? 1_555 ? 
35  AC9 7 LYS A  50  ? LYS A 50  . ? 1_555 ? 
36  AC9 7 LEU A  104 ? LEU A 104 . ? 1_555 ? 
37  AC9 7 SER A  106 ? SER A 106 . ? 1_555 ? 
38  AC9 7 EDO N  .   ? EDO A 508 . ? 1_555 ? 
39  AC9 7 HOH UA .   ? HOH A 631 . ? 1_555 ? 
40  AC9 7 HOH UA .   ? HOH A 682 . ? 1_555 ? 
41  BC1 2 THR B  90  ? THR B 90  . ? 1_555 ? 
42  BC1 2 ASN B  98  ? ASN B 98  . ? 1_555 ? 
43  BC2 4 ARG B  185 ? ARG B 185 . ? 1_555 ? 
44  BC2 4 LEU B  389 ? LEU B 389 . ? 1_555 ? 
45  BC2 4 HOH VA .   ? HOH B 731 . ? 1_555 ? 
46  BC2 4 ARG C  77  ? ARG C 77  . ? 1_555 ? 
47  BC3 4 THR B  285 ? THR B 285 . ? 1_555 ? 
48  BC3 4 ASN B  348 ? ASN B 348 . ? 1_555 ? 
49  BC3 4 HIS B  379 ? HIS B 379 . ? 1_555 ? 
50  BC3 4 HOH VA .   ? HOH B 638 . ? 1_555 ? 
51  BC4 1 ASN B  158 ? ASN B 158 . ? 1_555 ? 
52  BC5 7 GLY B  49  ? GLY B 49  . ? 1_555 ? 
53  BC5 7 LYS B  50  ? LYS B 50  . ? 1_555 ? 
54  BC5 7 HIS B  51  ? HIS B 51  . ? 1_555 ? 
55  BC5 7 LEU B  104 ? LEU B 104 . ? 1_555 ? 
56  BC5 7 SER B  106 ? SER B 106 . ? 1_555 ? 
57  BC5 7 HOH VA .   ? HOH B 614 . ? 1_555 ? 
58  BC5 7 HOH VA .   ? HOH B 656 . ? 1_555 ? 
59  BC6 4 PRO B  18  ? PRO B 18  . ? 1_555 ? 
60  BC6 4 GLN B  20  ? GLN B 20  . ? 1_555 ? 
61  BC6 4 ALA B  30  ? ALA B 30  . ? 1_555 ? 
62  BC6 4 ASN B  31  ? ASN B 31  . ? 1_555 ? 
63  BC7 3 CYS C  86  ? CYS C 86  . ? 1_555 ? 
64  BC7 3 SER C  89  ? SER C 89  . ? 1_555 ? 
65  BC7 3 ASN C  98  ? ASN C 98  . ? 1_555 ? 
66  BC8 5 GLN B  74  ? GLN B 74  . ? 1_555 ? 
67  BC8 5 ARG B  77  ? ARG B 77  . ? 1_555 ? 
68  BC8 5 ARG C  185 ? ARG C 185 . ? 1_555 ? 
69  BC8 5 LEU C  389 ? LEU C 389 . ? 1_555 ? 
70  BC8 5 HOH WA .   ? HOH C 724 . ? 1_555 ? 
71  BC9 7 GLY C  49  ? GLY C 49  . ? 1_555 ? 
72  BC9 7 LYS C  50  ? LYS C 50  . ? 1_555 ? 
73  BC9 7 HIS C  51  ? HIS C 51  . ? 1_555 ? 
74  BC9 7 LEU C  104 ? LEU C 104 . ? 1_555 ? 
75  BC9 7 SER C  105 ? SER C 105 . ? 1_555 ? 
76  BC9 7 SER C  106 ? SER C 106 . ? 1_555 ? 
77  BC9 7 HOH WA .   ? HOH C 644 . ? 1_555 ? 
78  CC1 4 GLN C  241 ? GLN C 241 . ? 1_555 ? 
79  CC1 4 ASP C  336 ? ASP C 336 . ? 1_555 ? 
80  CC1 4 HOH WA .   ? HOH C 620 . ? 1_555 ? 
81  CC1 4 HOH WA .   ? HOH C 714 . ? 1_555 ? 
82  CC2 4 PRO C  18  ? PRO C 18  . ? 1_555 ? 
83  CC2 4 GLN C  20  ? GLN C 20  . ? 1_555 ? 
84  CC2 4 ALA C  30  ? ALA C 30  . ? 1_555 ? 
85  CC2 4 ASN C  31  ? ASN C 31  . ? 1_555 ? 
86  CC3 8 VAL C  16  ? VAL C 16  . ? 1_555 ? 
87  CC3 8 LEU C  17  ? LEU C 17  . ? 1_555 ? 
88  CC3 8 ASN C  31  ? ASN C 31  . ? 1_555 ? 
89  CC3 8 ILE C  32  ? ILE C 32  . ? 1_555 ? 
90  CC3 8 HIS C  33  ? HIS C 33  . ? 1_555 ? 
91  CC3 8 ALA C  124 ? ALA C 124 . ? 1_555 ? 
92  CC3 8 ILE C  125 ? ILE C 125 . ? 1_555 ? 
93  CC3 8 HIS C  126 ? HIS C 126 . ? 1_555 ? 
94  CC4 2 THR D  90  ? THR D 90  . ? 1_555 ? 
95  CC4 2 ASN D  98  ? ASN D 98  . ? 1_555 ? 
96  CC5 5 PRO D  18  ? PRO D 18  . ? 1_555 ? 
97  CC5 5 TRP D  29  ? TRP D 29  . ? 1_555 ? 
98  CC5 5 ALA D  30  ? ALA D 30  . ? 1_555 ? 
99  CC5 5 ASN D  31  ? ASN D 31  . ? 1_555 ? 
100 CC5 5 ASN D  198 ? ASN D 198 . ? 1_555 ? 
101 CC6 5 ARG D  185 ? ARG D 185 . ? 1_555 ? 
102 CC6 5 LEU D  389 ? LEU D 389 . ? 1_555 ? 
103 CC6 5 HOH XA .   ? HOH D 636 . ? 1_555 ? 
104 CC6 5 ARG E  77  ? ARG E 77  . ? 1_555 ? 
105 CC6 5 HOH YA .   ? HOH E 601 . ? 1_555 ? 
106 CC7 6 LYS D  50  ? LYS D 50  . ? 1_555 ? 
107 CC7 6 HIS D  51  ? HIS D 51  . ? 1_555 ? 
108 CC7 6 SER D  105 ? SER D 105 . ? 1_555 ? 
109 CC7 6 SER D  106 ? SER D 106 . ? 1_555 ? 
110 CC7 6 HOH XA .   ? HOH D 637 . ? 1_555 ? 
111 CC7 6 HOH XA .   ? HOH D 683 . ? 1_555 ? 
112 CC8 5 THR D  285 ? THR D 285 . ? 1_555 ? 
113 CC8 5 ASN D  348 ? ASN D 348 . ? 1_555 ? 
114 CC8 5 GLY D  361 ? GLY D 361 . ? 1_555 ? 
115 CC8 5 HIS D  378 ? HIS D 378 . ? 1_555 ? 
116 CC8 5 HIS D  379 ? HIS D 379 . ? 1_555 ? 
117 CC9 7 ALA D  152 ? ALA D 152 . ? 1_555 ? 
118 CC9 7 GLN D  153 ? GLN D 153 . ? 1_555 ? 
119 CC9 7 LYS D  154 ? LYS D 154 . ? 1_555 ? 
120 CC9 7 GLY D  155 ? GLY D 155 . ? 1_555 ? 
121 CC9 7 LEU D  156 ? LEU D 156 . ? 1_555 ? 
122 CC9 7 PRO D  157 ? PRO D 157 . ? 1_555 ? 
123 CC9 7 VAL D  160 ? VAL D 160 . ? 1_555 ? 
124 DC1 5 GLN D  66  ? GLN D 66  . ? 1_555 ? 
125 DC1 5 GLN D  74  ? GLN D 74  . ? 1_555 ? 
126 DC1 5 HOH XA .   ? HOH D 639 . ? 1_555 ? 
127 DC1 5 GLU E  390 ? GLU E 390 . ? 1_555 ? 
128 DC1 5 ARG E  391 ? ARG E 391 . ? 1_555 ? 
129 DC2 4 ARG C  246 ? ARG C 246 . ? 1_555 ? 
130 DC2 4 GLN D  297 ? GLN D 297 . ? 1_555 ? 
131 DC2 4 ASN D  301 ? ASN D 301 . ? 1_555 ? 
132 DC2 4 HOH XA .   ? HOH D 698 . ? 1_555 ? 
133 DC3 4 ALA D  340 ? ALA D 340 . ? 1_555 ? 
134 DC3 4 VAL D  341 ? VAL D 341 . ? 1_555 ? 
135 DC3 4 ARG D  343 ? ARG D 343 . ? 1_555 ? 
136 DC3 4 SER D  398 ? SER D 398 . ? 1_555 ? 
137 DC4 1 LYS D  138 ? LYS D 138 . ? 1_555 ? 
138 DC5 5 LYS E  50  ? LYS E 50  . ? 1_555 ? 
139 DC5 5 HIS E  51  ? HIS E 51  . ? 1_555 ? 
140 DC5 5 SER E  105 ? SER E 105 . ? 1_555 ? 
141 DC5 5 SER E  106 ? SER E 106 . ? 1_555 ? 
142 DC5 5 HOH YA .   ? HOH E 667 . ? 1_555 ? 
143 DC6 3 THR F  92  ? THR F 92  . ? 1_555 ? 
144 DC6 3 ASN F  98  ? ASN F 98  . ? 1_555 ? 
145 DC6 3 NAG NA .   ? NAG F 502 . ? 1_555 ? 
146 DC7 1 NAG MA .   ? NAG F 501 . ? 1_555 ? 
147 DC8 6 PRO F  18  ? PRO F 18  . ? 1_555 ? 
148 DC8 6 VAL F  19  ? VAL F 19  . ? 1_555 ? 
149 DC8 6 GLN F  20  ? GLN F 20  . ? 1_555 ? 
150 DC8 6 TRP F  29  ? TRP F 29  . ? 1_555 ? 
151 DC8 6 ALA F  30  ? ALA F 30  . ? 1_555 ? 
152 DC8 6 ASN F  31  ? ASN F 31  . ? 1_555 ? 
153 DC9 4 HIS F  282 ? HIS F 282 . ? 1_555 ? 
154 DC9 4 PRO F  283 ? PRO F 283 . ? 1_555 ? 
155 DC9 4 TYR F  284 ? TYR F 284 . ? 1_555 ? 
156 DC9 4 VAL F  286 ? VAL F 286 . ? 1_555 ? 
157 EC1 2 SER F  24  ? SER F 24  . ? 1_555 ? 
158 EC1 2 THR F  25  ? THR F 25  . ? 1_555 ? 
159 EC2 8 LYS F  50  ? LYS F 50  . ? 1_555 ? 
160 EC2 8 HIS F  51  ? HIS F 51  . ? 1_555 ? 
161 EC2 8 LEU F  104 ? LEU F 104 . ? 1_555 ? 
162 EC2 8 SER F  105 ? SER F 105 . ? 1_555 ? 
163 EC2 8 SER F  106 ? SER F 106 . ? 1_555 ? 
164 EC2 8 HOH ZA .   ? HOH F 617 . ? 1_555 ? 
165 EC2 8 HOH ZA .   ? HOH F 652 . ? 1_555 ? 
166 EC2 8 HOH ZA .   ? HOH F 686 . ? 1_555 ? 
167 EC3 4 ARG A  77  ? ARG A 77  . ? 1_555 ? 
168 EC3 4 ARG F  185 ? ARG F 185 . ? 1_555 ? 
169 EC3 4 LEU F  389 ? LEU F 389 . ? 1_555 ? 
170 EC3 4 HOH ZA .   ? HOH F 670 . ? 1_555 ? 
171 EC4 6 THR F  285 ? THR F 285 . ? 1_555 ? 
172 EC4 6 ILE F  344 ? ILE F 344 . ? 1_555 ? 
173 EC4 6 ASN F  348 ? ASN F 348 . ? 1_555 ? 
174 EC4 6 PHE F  349 ? PHE F 349 . ? 1_555 ? 
175 EC4 6 HIS F  379 ? HIS F 379 . ? 1_555 ? 
176 EC4 6 HOH ZA .   ? HOH F 748 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4PPH 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4PPH 
_atom_sites.fract_transf_matrix[1][1]   0.008197 
_atom_sites.fract_transf_matrix[1][2]   0.004733 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009466 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005305 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . LYS A  1 11  ? 120.864 95.737  0.398   1.00   71.89  ? 11  LYS A N   1 
ATOM   2     C CA  . LYS A  1 11  ? 120.529 94.454  1.033   1.00   70.62  ? 11  LYS A CA  1 
ATOM   3     C C   . LYS A  1 11  ? 119.008 94.349  1.244   1.00   67.29  ? 11  LYS A C   1 
ATOM   4     O O   . LYS A  1 11  ? 118.515 94.732  2.311   1.00   66.38  ? 11  LYS A O   1 
ATOM   5     C CB  . LYS A  1 11  ? 121.263 94.339  2.374   1.00   73.33  ? 11  LYS A CB  1 
ATOM   6     C CG  . LYS A  1 11  ? 122.685 93.759  2.297   1.00   75.42  ? 11  LYS A CG  1 
ATOM   7     C CD  . LYS A  1 11  ? 123.396 93.862  3.665   1.00   77.84  ? 11  LYS A CD  1 
ATOM   8     C CE  . LYS A  1 11  ? 124.890 93.483  3.609   1.00   77.96  ? 11  LYS A CE  1 
ATOM   9     N NZ  . LYS A  1 11  ? 125.436 92.827  4.844   1.00   77.16  ? 11  LYS A NZ  1 
ATOM   10    N N   . PRO A  1 12  ? 118.265 93.799  0.247   1.00   63.20  ? 12  PRO A N   1 
ATOM   11    C CA  . PRO A  1 12  ? 116.787 93.855  0.275   1.00   58.36  ? 12  PRO A CA  1 
ATOM   12    C C   . PRO A  1 12  ? 116.062 92.985  1.295   1.00   52.54  ? 12  PRO A C   1 
ATOM   13    O O   . PRO A  1 12  ? 116.505 91.872  1.601   1.00   48.12  ? 12  PRO A O   1 
ATOM   14    C CB  . PRO A  1 12  ? 116.391 93.410  -1.143  1.00   56.49  ? 12  PRO A CB  1 
ATOM   15    C CG  . PRO A  1 12  ? 117.485 92.560  -1.591  1.00   57.60  ? 12  PRO A CG  1 
ATOM   16    C CD  . PRO A  1 12  ? 118.753 93.125  -0.970  1.00   61.87  ? 12  PRO A CD  1 
ATOM   17    N N   . ASN A  1 13  ? 114.924 93.499  1.773   1.00   51.26  ? 13  ASN A N   1 
ATOM   18    C CA  . ASN A  1 13  ? 114.066 92.788  2.711   1.00   49.61  ? 13  ASN A CA  1 
ATOM   19    C C   . ASN A  1 13  ? 112.805 92.272  2.098   1.00   41.58  ? 13  ASN A C   1 
ATOM   20    O O   . ASN A  1 13  ? 112.069 91.572  2.769   1.00   41.55  ? 13  ASN A O   1 
ATOM   21    C CB  . ASN A  1 13  ? 113.630 93.648  3.894   1.00   59.89  ? 13  ASN A CB  1 
ATOM   22    C CG  . ASN A  1 13  ? 114.645 93.688  4.989   1.00   71.04  ? 13  ASN A CG  1 
ATOM   23    O OD1 . ASN A  1 13  ? 115.419 94.642  5.111   1.00   77.11  ? 13  ASN A OD1 1 
ATOM   24    N ND2 . ASN A  1 13  ? 114.692 92.617  5.779   1.00   74.01  ? 13  ASN A ND2 1 
ATOM   25    N N   . LEU A  1 14  ? 112.553 92.599  0.836   1.00   35.32  ? 14  LEU A N   1 
ATOM   26    C CA  . LEU A  1 14  ? 111.322 92.159  0.201   1.00   31.87  ? 14  LEU A CA  1 
ATOM   27    C C   . LEU A  1 14  ? 111.497 92.101  -1.290  1.00   33.20  ? 14  LEU A C   1 
ATOM   28    O O   . LEU A  1 14  ? 112.005 93.032  -1.897  1.00   37.35  ? 14  LEU A O   1 
ATOM   29    C CB  . LEU A  1 14  ? 110.169 93.097  0.564   1.00   31.31  ? 14  LEU A CB  1 
ATOM   30    C CG  . LEU A  1 14  ? 108.709 92.709  0.299   1.00   30.38  ? 14  LEU A CG  1 
ATOM   31    C CD1 . LEU A  1 14  ? 108.228 91.635  1.239   1.00   28.55  ? 14  LEU A CD1 1 
ATOM   32    C CD2 . LEU A  1 14  ? 107.842 93.935  0.470   1.00   32.26  ? 14  LEU A CD2 1 
ATOM   33    N N   . LEU A  1 15  ? 111.051 91.010  -1.877  1.00   31.06  ? 15  LEU A N   1 
ATOM   34    C CA  . LEU A  1 15  ? 111.156 90.830  -3.301  1.00   30.84  ? 15  LEU A CA  1 
ATOM   35    C C   . LEU A  1 15  ? 109.785 90.618  -3.897  1.00   29.99  ? 15  LEU A C   1 
ATOM   36    O O   . LEU A  1 15  ? 108.886 90.167  -3.218  1.00   30.17  ? 15  LEU A O   1 
ATOM   37    C CB  . LEU A  1 15  ? 112.076 89.659  -3.617  1.00   28.53  ? 15  LEU A CB  1 
ATOM   38    C CG  . LEU A  1 15  ? 113.451 89.664  -2.942  1.00   29.68  ? 15  LEU A CG  1 
ATOM   39    C CD1 . LEU A  1 15  ? 114.106 88.341  -3.191  1.00   28.16  ? 15  LEU A CD1 1 
ATOM   40    C CD2 . LEU A  1 15  ? 114.357 90.794  -3.440  1.00   28.51  ? 15  LEU A CD2 1 
ATOM   41    N N   . VAL A  1 16  ? 109.613 90.986  -5.157  1.00   29.99  ? 16  VAL A N   1 
ATOM   42    C CA  . VAL A  1 16  ? 108.298 90.914  -5.783  1.00   33.58  ? 16  VAL A CA  1 
ATOM   43    C C   . VAL A  1 16  ? 108.356 90.239  -7.154  1.00   35.80  ? 16  VAL A C   1 
ATOM   44    O O   . VAL A  1 16  ? 109.231 90.539  -7.977  1.00   34.14  ? 16  VAL A O   1 
ATOM   45    C CB  . VAL A  1 16  ? 107.648 92.329  -5.925  1.00   36.65  ? 16  VAL A CB  1 
ATOM   46    C CG1 . VAL A  1 16  ? 106.288 92.268  -6.612  1.00   31.59  ? 16  VAL A CG1 1 
ATOM   47    C CG2 . VAL A  1 16  ? 107.519 92.987  -4.579  1.00   35.10  ? 16  VAL A CG2 1 
ATOM   48    N N   . LEU A  1 17  ? 107.451 89.276  -7.352  1.00   36.67  ? 17  LEU A N   1 
ATOM   49    C CA  . LEU A  1 17  ? 107.285 88.600  -8.632  1.00   35.74  ? 17  LEU A CA  1 
ATOM   50    C C   . LEU A  1 17  ? 105.853 88.761  -9.133  1.00   36.28  ? 17  LEU A C   1 
ATOM   51    O O   . LEU A  1 17  ? 104.926 88.176  -8.580  1.00   34.84  ? 17  LEU A O   1 
ATOM   52    C CB  . LEU A  1 17  ? 107.631 87.127  -8.524  1.00   32.92  ? 17  LEU A CB  1 
ATOM   53    C CG  . LEU A  1 17  ? 107.433 86.368  -9.835  1.00   33.50  ? 17  LEU A CG  1 
ATOM   54    C CD1 . LEU A  1 17  ? 108.475 86.753  -10.881 1.00   36.30  ? 17  LEU A CD1 1 
ATOM   55    C CD2 . LEU A  1 17  ? 107.463 84.900  -9.560  1.00   30.36  ? 17  LEU A CD2 1 
ATOM   56    N N   . PRO A  1 18  ? 105.673 89.567  -10.183 1.00   38.94  ? 18  PRO A N   1 
ATOM   57    C CA  . PRO A  1 18  ? 104.369 89.769  -10.819 1.00   40.90  ? 18  PRO A CA  1 
ATOM   58    C C   . PRO A  1 18  ? 103.974 88.512  -11.549 1.00   41.70  ? 18  PRO A C   1 
ATOM   59    O O   . PRO A  1 18  ? 104.866 87.879  -12.144 1.00   38.56  ? 18  PRO A O   1 
ATOM   60    C CB  . PRO A  1 18  ? 104.620 90.917  -11.790 1.00   43.52  ? 18  PRO A CB  1 
ATOM   61    C CG  . PRO A  1 18  ? 105.873 91.577  -11.290 1.00   41.95  ? 18  PRO A CG  1 
ATOM   62    C CD  . PRO A  1 18  ? 106.697 90.446  -10.763 1.00   39.02  ? 18  PRO A CD  1 
ATOM   63    N N   . VAL A  1 19  ? 102.697 88.133  -11.459 1.00   40.32  ? 19  VAL A N   1 
ATOM   64    C CA  . VAL A  1 19  ? 102.215 86.903  -12.076 1.00   39.20  ? 19  VAL A CA  1 
ATOM   65    C C   . VAL A  1 19  ? 100.967 87.259  -12.874 1.00   37.69  ? 19  VAL A C   1 
ATOM   66    O O   . VAL A  1 19  ? 100.301 88.228  -12.567 1.00   37.02  ? 19  VAL A O   1 
ATOM   67    C CB  . VAL A  1 19  ? 101.930 85.769  -11.020 1.00   29.28  ? 19  VAL A CB  1 
ATOM   68    C CG1 . VAL A  1 19  ? 103.146 85.494  -10.197 1.00   27.71  ? 19  VAL A CG1 1 
ATOM   69    C CG2 . VAL A  1 19  ? 100.816 86.150  -10.110 1.00   35.38  ? 19  VAL A CG2 1 
ATOM   70    N N   . GLN A  1 20  ? 100.673 86.482  -13.908 1.00   37.81  ? 20  GLN A N   1 
ATOM   71    C CA  . GLN A  1 20  ? 99.543  86.744  -14.784 1.00   35.91  ? 20  GLN A CA  1 
ATOM   72    C C   . GLN A  1 20  ? 98.630  85.547  -14.987 1.00   44.39  ? 20  GLN A C   1 
ATOM   73    O O   . GLN A  1 20  ? 99.100  84.428  -15.128 1.00   44.09  ? 20  GLN A O   1 
ATOM   74    C CB  . GLN A  1 20  ? 100.022 87.177  -16.157 1.00   41.54  ? 20  GLN A CB  1 
ATOM   75    C CG  . GLN A  1 20  ? 98.855  87.642  -17.000 1.00   50.31  ? 20  GLN A CG  1 
ATOM   76    C CD  . GLN A  1 20  ? 99.260  88.206  -18.328 1.00   56.16  ? 20  GLN A CD  1 
ATOM   77    O OE1 . GLN A  1 20  ? 100.140 89.056  -18.407 1.00   55.91  ? 20  GLN A OE1 1 
ATOM   78    N NE2 . GLN A  1 20  ? 98.626  87.716  -19.397 1.00   59.54  ? 20  GLN A NE2 1 
ATOM   79    N N   . GLU A  1 21  ? 97.325  85.790  -15.047 1.00   45.88  ? 21  GLU A N   1 
ATOM   80    C CA  . GLU A  1 21  ? 96.353  84.742  -15.360 1.00   46.87  ? 21  GLU A CA  1 
ATOM   81    C C   . GLU A  1 21  ? 96.268  84.505  -16.873 1.00   45.15  ? 21  GLU A C   1 
ATOM   82    O O   . GLU A  1 21  ? 96.232  85.445  -17.669 1.00   44.27  ? 21  GLU A O   1 
ATOM   83    C CB  . GLU A  1 21  ? 94.967  85.108  -14.800 1.00   50.44  ? 21  GLU A CB  1 
ATOM   84    C CG  . GLU A  1 21  ? 93.982  83.949  -14.660 1.00   37.76  ? 21  GLU A CG  1 
ATOM   85    C CD  . GLU A  1 21  ? 92.969  83.918  -15.779 1.00   43.05  ? 21  GLU A CD  1 
ATOM   86    O OE1 . GLU A  1 21  ? 93.048  84.775  -16.673 1.00   46.07  ? 21  GLU A OE1 1 
ATOM   87    O OE2 . GLU A  1 21  ? 92.073  83.057  -15.766 1.00   45.73  ? 21  GLU A OE2 1 
ATOM   88    N N   . ASP A  1 22  ? 96.239  83.237  -17.263 1.00   44.08  ? 22  ASP A N   1 
ATOM   89    C CA  . ASP A  1 22  ? 96.046  82.897  -18.655 1.00   45.26  ? 22  ASP A CA  1 
ATOM   90    C C   . ASP A  1 22  ? 94.574  82.630  -18.844 1.00   47.05  ? 22  ASP A C   1 
ATOM   91    O O   . ASP A  1 22  ? 94.023  81.705  -18.248 1.00   47.84  ? 22  ASP A O   1 
ATOM   92    C CB  . ASP A  1 22  ? 96.878  81.680  -19.060 1.00   45.47  ? 22  ASP A CB  1 
ATOM   93    C CG  . ASP A  1 22  ? 96.627  81.257  -20.506 1.00   49.33  ? 22  ASP A CG  1 
ATOM   94    O OD1 . ASP A  1 22  ? 96.898  82.056  -21.423 1.00   51.37  ? 22  ASP A OD1 1 
ATOM   95    O OD2 . ASP A  1 22  ? 96.173  80.116  -20.732 1.00   50.33  1 22  ASP A OD2 1 
ATOM   96    N N   . ALA A  1 23  ? 93.941  83.456  -19.665 1.00   48.23  ? 23  ALA A N   1 
ATOM   97    C CA  . ALA A  1 23  ? 92.500  83.424  -19.825 1.00   52.12  ? 23  ALA A CA  1 
ATOM   98    C C   . ALA A  1 23  ? 92.076  82.059  -20.332 1.00   57.23  ? 23  ALA A C   1 
ATOM   99    O O   . ALA A  1 23  ? 91.103  81.491  -19.861 1.00   58.75  ? 23  ALA A O   1 
ATOM   100   C CB  . ALA A  1 23  ? 92.043  84.511  -20.780 1.00   52.27  ? 23  ALA A CB  1 
ATOM   101   N N   . SER A  1 24  ? 92.831  81.521  -21.278 1.00   59.33  ? 24  SER A N   1 
ATOM   102   C CA  . SER A  1 24  ? 92.477  80.250  -21.879 1.00   60.23  ? 24  SER A CA  1 
ATOM   103   C C   . SER A  1 24  ? 92.411  79.088  -20.877 1.00   55.70  ? 24  SER A C   1 
ATOM   104   O O   . SER A  1 24  ? 91.427  78.352  -20.841 1.00   55.85  ? 24  SER A O   1 
ATOM   105   C CB  . SER A  1 24  ? 93.470  79.925  -22.989 1.00   62.63  ? 24  SER A CB  1 
ATOM   106   O OG  . SER A  1 24  ? 93.220  78.638  -23.505 1.00   64.33  ? 24  SER A OG  1 
ATOM   107   N N   . THR A  1 25  ? 93.457  78.924  -20.072 1.00   51.60  ? 25  THR A N   1 
ATOM   108   C CA  . THR A  1 25  ? 93.564  77.770  -19.188 1.00   43.90  ? 25  THR A CA  1 
ATOM   109   C C   . THR A  1 25  ? 93.150  78.105  -17.766 1.00   45.76  ? 25  THR A C   1 
ATOM   110   O O   . THR A  1 25  ? 92.902  77.222  -16.957 1.00   45.68  ? 25  THR A O   1 
ATOM   111   C CB  . THR A  1 25  ? 94.988  77.221  -19.140 1.00   43.88  ? 25  THR A CB  1 
ATOM   112   O OG1 . THR A  1 25  ? 95.840  78.173  -18.500 1.00   43.19  ? 25  THR A OG1 1 
ATOM   113   C CG2 . THR A  1 25  ? 95.495  76.928  -20.531 1.00   44.60  ? 25  THR A CG2 1 
ATOM   114   N N   . GLY A  1 26  ? 93.137  79.382  -17.425 1.00   44.26  ? 26  GLY A N   1 
ATOM   115   C CA  . GLY A  1 26  ? 92.791  79.748  -16.070 1.00   42.83  ? 26  GLY A CA  1 
ATOM   116   C C   . GLY A  1 26  ? 93.937  79.578  -15.114 1.00   41.93  ? 26  GLY A C   1 
ATOM   117   O O   . GLY A  1 26  ? 93.776  79.734  -13.914 1.00   41.04  ? 26  GLY A O   1 
ATOM   118   N N   . LEU A  1 27  ? 95.111  79.272  -15.653 1.00   45.95  ? 27  LEU A N   1 
ATOM   119   C CA  . LEU A  1 27  ? 96.328  79.123  -14.856 1.00   41.74  ? 27  LEU A CA  1 
ATOM   120   C C   . LEU A  1 27  ? 97.151  80.411  -14.874 1.00   39.43  ? 27  LEU A C   1 
ATOM   121   O O   . LEU A  1 27  ? 96.922  81.287  -15.699 1.00   41.22  ? 27  LEU A O   1 
ATOM   122   C CB  . LEU A  1 27  ? 97.172  77.961  -15.375 1.00   43.75  ? 27  LEU A CB  1 
ATOM   123   C CG  . LEU A  1 27  ? 96.511  76.584  -15.384 1.00   45.34  ? 27  LEU A CG  1 
ATOM   124   C CD1 . LEU A  1 27  ? 97.410  75.574  -16.043 1.00   46.13  ? 27  LEU A CD1 1 
ATOM   125   C CD2 . LEU A  1 27  ? 96.189  76.158  -13.968 1.00   43.45  ? 27  LEU A CD2 1 
ATOM   126   N N   . HIS A  1 28  ? 98.128  80.498  -13.978 1.00   36.94  ? 28  HIS A N   1 
ATOM   127   C CA  . HIS A  1 28  ? 98.939  81.696  -13.833 1.00   35.22  ? 28  HIS A CA  1 
ATOM   128   C C   . HIS A  1 28  ? 100.379 81.405  -14.169 1.00   34.11  ? 28  HIS A C   1 
ATOM   129   O O   . HIS A  1 28  ? 100.848 80.298  -13.970 1.00   34.89  ? 28  HIS A O   1 
ATOM   130   C CB  . HIS A  1 28  ? 98.842  82.245  -12.412 1.00   33.07  ? 28  HIS A CB  1 
ATOM   131   C CG  . HIS A  1 28  ? 97.475  82.724  -12.050 1.00   34.40  ? 28  HIS A CG  1 
ATOM   132   N ND1 . HIS A  1 28  ? 97.177  84.055  -11.865 1.00   34.41  ? 28  HIS A ND1 1 
ATOM   133   C CD2 . HIS A  1 28  ? 96.317  82.046  -11.855 1.00   31.30  ? 28  HIS A CD2 1 
ATOM   134   C CE1 . HIS A  1 28  ? 95.895  84.176  -11.569 1.00   33.48  ? 28  HIS A CE1 1 
ATOM   135   N NE2 . HIS A  1 28  ? 95.354  82.970  -11.548 1.00   34.37  ? 28  HIS A NE2 1 
ATOM   136   N N   . TRP A  1 29  ? 101.072 82.403  -14.693 1.00   35.11  ? 29  TRP A N   1 
ATOM   137   C CA  . TRP A  1 29  ? 102.448 82.235  -15.115 1.00   34.62  ? 29  TRP A CA  1 
ATOM   138   C C   . TRP A  1 29  ? 103.226 83.509  -14.816 1.00   35.23  ? 29  TRP A C   1 
ATOM   139   O O   . TRP A  1 29  ? 102.629 84.540  -14.530 1.00   36.36  ? 29  TRP A O   1 
ATOM   140   C CB  . TRP A  1 29  ? 102.509 81.882  -16.605 1.00   36.92  ? 29  TRP A CB  1 
ATOM   141   C CG  . TRP A  1 29  ? 101.943 82.968  -17.447 1.00   41.16  ? 29  TRP A CG  1 
ATOM   142   C CD1 . TRP A  1 29  ? 100.623 83.177  -17.726 1.00   42.27  ? 29  TRP A CD1 1 
ATOM   143   C CD2 . TRP A  1 29  ? 102.662 84.031  -18.091 1.00   42.22  ? 29  TRP A CD2 1 
ATOM   144   N NE1 . TRP A  1 29  ? 100.477 84.292  -18.506 1.00   43.25  ? 29  TRP A NE1 1 
ATOM   145   C CE2 . TRP A  1 29  ? 101.711 84.836  -18.748 1.00   45.01  ? 29  TRP A CE2 1 
ATOM   146   C CE3 . TRP A  1 29  ? 104.017 84.369  -18.186 1.00   39.63  ? 29  TRP A CE3 1 
ATOM   147   C CZ2 . TRP A  1 29  ? 102.067 85.959  -19.484 1.00   47.43  ? 29  TRP A CZ2 1 
ATOM   148   C CZ3 . TRP A  1 29  ? 104.369 85.477  -18.903 1.00   41.11  ? 29  TRP A CZ3 1 
ATOM   149   C CH2 . TRP A  1 29  ? 103.399 86.262  -19.553 1.00   47.15  ? 29  TRP A CH2 1 
ATOM   150   N N   . ALA A  1 30  ? 104.555 83.414  -14.844 1.00   33.68  ? 30  ALA A N   1 
ATOM   151   C CA  . ALA A  1 30  ? 105.428 84.555  -14.631 1.00   33.56  ? 30  ALA A CA  1 
ATOM   152   C C   . ALA A  1 30  ? 106.620 84.529  -15.575 1.00   36.55  ? 30  ALA A C   1 
ATOM   153   O O   . ALA A  1 30  ? 107.105 83.466  -15.955 1.00   31.82  ? 30  ALA A O   1 
ATOM   154   C CB  . ALA A  1 30  ? 105.905 84.587  -13.209 1.00   32.62  ? 30  ALA A CB  1 
ATOM   155   N N   . ASN A  1 31  ? 107.077 85.712  -15.954 1.00   40.94  ? 31  ASN A N   1 
ATOM   156   C CA  . ASN A  1 31  ? 108.365 85.882  -16.613 1.00   44.29  ? 31  ASN A CA  1 
ATOM   157   C C   . ASN A  1 31  ? 109.470 85.911  -15.576 1.00   44.94  ? 31  ASN A C   1 
ATOM   158   O O   . ASN A  1 31  ? 109.528 86.807  -14.741 1.00   44.35  ? 31  ASN A O   1 
ATOM   159   C CB  . ASN A  1 31  ? 108.392 87.169  -17.412 1.00   36.85  ? 31  ASN A CB  1 
ATOM   160   C CG  . ASN A  1 31  ? 107.766 87.020  -18.757 1.00   43.30  ? 31  ASN A CG  1 
ATOM   161   O OD1 . ASN A  1 31  ? 107.996 86.044  -19.455 1.00   44.09  ? 31  ASN A OD1 1 
ATOM   162   N ND2 . ASN A  1 31  ? 106.966 87.998  -19.143 1.00   47.47  ? 31  ASN A ND2 1 
ATOM   163   N N   . ILE A  1 32  ? 110.352 84.931  -15.620 1.00   44.47  ? 32  ILE A N   1 
ATOM   164   C CA  . ILE A  1 32  ? 111.459 84.914  -14.693 1.00   43.34  ? 32  ILE A CA  1 
ATOM   165   C C   . ILE A  1 32  ? 112.681 85.384  -15.428 1.00   43.68  ? 32  ILE A C   1 
ATOM   166   O O   . ILE A  1 32  ? 112.918 84.963  -16.553 1.00   44.04  ? 32  ILE A O   1 
ATOM   167   C CB  . ILE A  1 32  ? 111.711 83.532  -14.141 1.00   42.88  ? 32  ILE A CB  1 
ATOM   168   C CG1 . ILE A  1 32  ? 110.412 82.950  -13.621 1.00   44.28  ? 32  ILE A CG1 1 
ATOM   169   C CG2 . ILE A  1 32  ? 112.734 83.598  -13.044 1.00   41.66  ? 32  ILE A CG2 1 
ATOM   170   C CD1 . ILE A  1 32  ? 109.941 83.641  -12.403 1.00   44.85  ? 32  ILE A CD1 1 
ATOM   171   N N   . HIS A  1 33  ? 113.455 86.257  -14.805 1.00   42.73  ? 33  HIS A N   1 
ATOM   172   C CA  . HIS A  1 33  ? 114.660 86.736  -15.436 1.00   42.87  ? 33  HIS A CA  1 
ATOM   173   C C   . HIS A  1 33  ? 115.803 85.836  -15.071 1.00   42.32  ? 33  HIS A C   1 
ATOM   174   O O   . HIS A  1 33  ? 116.053 85.609  -13.899 1.00   42.38  ? 33  HIS A O   1 
ATOM   175   C CB  . HIS A  1 33  ? 114.935 88.152  -15.010 1.00   45.03  ? 33  HIS A CB  1 
ATOM   176   C CG  . HIS A  1 33  ? 113.897 89.112  -15.480 1.00   49.74  ? 33  HIS A CG  1 
ATOM   177   N ND1 . HIS A  1 33  ? 112.612 89.119  -14.975 1.00   51.71  ? 33  HIS A ND1 1 
ATOM   178   C CD2 . HIS A  1 33  ? 113.944 90.094  -16.412 1.00   51.43  ? 33  HIS A CD2 1 
ATOM   179   C CE1 . HIS A  1 33  ? 111.914 90.063  -15.583 1.00   52.68  ? 33  HIS A CE1 1 
ATOM   180   N NE2 . HIS A  1 33  ? 112.700 90.671  -16.455 1.00   52.96  ? 33  HIS A NE2 1 
ATOM   181   N N   . LYS A  1 34  ? 116.465 85.279  -16.079 1.00   41.52  ? 34  LYS A N   1 
ATOM   182   C CA  . LYS A  1 34  ? 117.558 84.334  -15.868 1.00   39.53  ? 34  LYS A CA  1 
ATOM   183   C C   . LYS A  1 34  ? 118.704 84.505  -16.854 1.00   42.78  ? 34  LYS A C   1 
ATOM   184   O O   . LYS A  1 34  ? 118.546 85.159  -17.879 1.00   45.87  ? 34  LYS A O   1 
ATOM   185   C CB  . LYS A  1 34  ? 117.035 82.907  -15.942 1.00   36.87  ? 34  LYS A CB  1 
ATOM   186   C CG  . LYS A  1 34  ? 115.889 82.681  -15.013 1.00   35.67  ? 34  LYS A CG  1 
ATOM   187   C CD  . LYS A  1 34  ? 115.690 81.250  -14.713 1.00   35.43  ? 34  LYS A CD  1 
ATOM   188   C CE  . LYS A  1 34  ? 116.877 80.646  -14.045 1.00   33.53  ? 34  LYS A CE  1 
ATOM   189   N NZ  . LYS A  1 34  ? 116.800 79.224  -14.389 1.00   30.68  ? 34  LYS A NZ  1 
ATOM   190   N N   . ARG A  1 35  ? 119.855 83.920  -16.516 1.00   39.76  ? 35  ARG A N   1 
ATOM   191   C CA  . ARG A  1 35  ? 121.011 83.795  -17.412 1.00   38.47  ? 35  ARG A CA  1 
ATOM   192   C C   . ARG A  1 35  ? 121.812 85.076  -17.544 1.00   39.70  ? 35  ARG A C   1 
ATOM   193   O O   . ARG A  1 35  ? 121.412 86.122  -17.053 1.00   41.01  ? 35  ARG A O   1 
ATOM   194   C CB  . ARG A  1 35  ? 120.577 83.322  -18.805 1.00   37.90  ? 35  ARG A CB  1 
ATOM   195   C CG  . ARG A  1 35  ? 119.820 82.028  -18.746 1.00   37.43  ? 35  ARG A CG  1 
ATOM   196   C CD  . ARG A  1 35  ? 119.111 81.625  -20.033 1.00   39.46  ? 35  ARG A CD  1 
ATOM   197   N NE  . ARG A  1 35  ? 118.048 80.657  -19.719 1.00   40.51  ? 35  ARG A NE  1 
ATOM   198   C CZ  . ARG A  1 35  ? 117.319 79.993  -20.618 1.00   42.38  ? 35  ARG A CZ  1 
ATOM   199   N NH1 . ARG A  1 35  ? 117.554 80.145  -21.914 1.00   44.33  ? 35  ARG A NH1 1 
ATOM   200   N NH2 . ARG A  1 35  ? 116.377 79.141  -20.217 1.00   39.21  ? 35  ARG A NH2 1 
ATOM   201   N N   . THR A  1 36  ? 122.975 84.947  -18.176 1.00   41.20  ? 36  THR A N   1 
ATOM   202   C CA  . THR A  1 36  ? 123.813 86.064  -18.590 1.00   43.02  ? 36  THR A CA  1 
ATOM   203   C C   . THR A  1 36  ? 124.126 85.903  -20.078 1.00   42.01  ? 36  THR A C   1 
ATOM   204   O O   . THR A  1 36  ? 124.787 84.953  -20.477 1.00   44.57  ? 36  THR A O   1 
ATOM   205   C CB  . THR A  1 36  ? 125.113 86.157  -17.783 1.00   42.72  ? 36  THR A CB  1 
ATOM   206   O OG1 . THR A  1 36  ? 124.808 86.237  -16.383 1.00   42.96  ? 36  THR A OG1 1 
ATOM   207   C CG2 . THR A  1 36  ? 125.839 87.400  -18.163 1.00   45.28  ? 36  THR A CG2 1 
ATOM   208   N N   . PRO A  1 37  ? 123.635 86.828  -20.911 1.00   52.86  ? 37  PRO A N   1 
ATOM   209   C CA  . PRO A  1 37  ? 122.858 88.022  -20.551 1.00   52.67  ? 37  PRO A CA  1 
ATOM   210   C C   . PRO A  1 37  ? 121.450 87.692  -20.052 1.00   50.56  ? 37  PRO A C   1 
ATOM   211   O O   . PRO A  1 37  ? 120.892 86.666  -20.458 1.00   50.59  ? 37  PRO A O   1 
ATOM   212   C CB  . PRO A  1 37  ? 122.782 88.801  -21.871 1.00   53.58  ? 37  PRO A CB  1 
ATOM   213   C CG  . PRO A  1 37  ? 122.880 87.755  -22.919 1.00   53.98  ? 37  PRO A CG  1 
ATOM   214   C CD  . PRO A  1 37  ? 123.810 86.709  -22.371 1.00   54.60  ? 37  PRO A CD  1 
ATOM   215   N N   . LEU A  1 38  ? 120.899 88.557  -19.200 1.00   47.51  ? 38  LEU A N   1 
ATOM   216   C CA  . LEU A  1 38  ? 119.604 88.330  -18.570 1.00   45.58  ? 38  LEU A CA  1 
ATOM   217   C C   . LEU A  1 38  ? 118.473 88.337  -19.572 1.00   44.14  ? 38  LEU A C   1 
ATOM   218   O O   . LEU A  1 38  ? 118.369 89.233  -20.402 1.00   45.39  ? 38  LEU A O   1 
ATOM   219   C CB  . LEU A  1 38  ? 119.360 89.393  -17.506 1.00   48.76  ? 38  LEU A CB  1 
ATOM   220   C CG  . LEU A  1 38  ? 118.457 89.065  -16.321 1.00   49.33  ? 38  LEU A CG  1 
ATOM   221   C CD1 . LEU A  1 38  ? 118.966 87.896  -15.508 1.00   47.78  ? 38  LEU A CD1 1 
ATOM   222   C CD2 . LEU A  1 38  ? 118.400 90.304  -15.454 1.00   50.90  ? 38  LEU A CD2 1 
ATOM   223   N N   . MET A  1 39  ? 117.590 87.361  -19.457 1.00   43.22  ? 39  MET A N   1 
ATOM   224   C CA  . MET A  1 39  ? 116.451 87.302  -20.348 1.00   45.84  ? 39  MET A CA  1 
ATOM   225   C C   . MET A  1 39  ? 115.252 86.690  -19.656 1.00   43.60  ? 39  MET A C   1 
ATOM   226   O O   . MET A  1 39  ? 115.366 86.169  -18.550 1.00   41.09  ? 39  MET A O   1 
ATOM   227   C CB  . MET A  1 39  ? 116.830 86.531  -21.619 1.00   49.74  ? 39  MET A CB  1 
ATOM   228   C CG  . MET A  1 39  ? 117.553 85.212  -21.368 1.00   50.21  ? 39  MET A CG  1 
ATOM   229   S SD  . MET A  1 39  ? 116.467 83.840  -20.910 1.00   77.17  ? 39  MET A SD  1 
ATOM   230   C CE  . MET A  1 39  ? 115.661 83.491  -22.481 1.00   55.42  ? 39  MET A CE  1 
ATOM   231   N N   . GLN A  1 40  ? 114.098 86.752  -20.312 1.00   45.82  ? 40  GLN A N   1 
ATOM   232   C CA  . GLN A  1 40  ? 112.866 86.306  -19.690 1.00   49.44  ? 40  GLN A CA  1 
ATOM   233   C C   . GLN A  1 40  ? 112.395 84.953  -20.165 1.00   49.04  ? 40  GLN A C   1 
ATOM   234   O O   . GLN A  1 40  ? 112.372 84.653  -21.360 1.00   50.15  ? 40  GLN A O   1 
ATOM   235   C CB  . GLN A  1 40  ? 111.776 87.339  -19.905 1.00   54.14  ? 40  GLN A CB  1 
ATOM   236   C CG  . GLN A  1 40  ? 112.073 88.595  -19.152 1.00   57.70  ? 40  GLN A CG  1 
ATOM   237   C CD  . GLN A  1 40  ? 111.021 89.637  -19.346 1.00   62.99  ? 40  GLN A CD  1 
ATOM   238   O OE1 . GLN A  1 40  ? 109.893 89.481  -18.911 1.00   62.04  ? 40  GLN A OE1 1 
ATOM   239   N NE2 . GLN A  1 40  ? 111.382 90.714  -20.012 1.00   68.86  ? 40  GLN A NE2 1 
ATOM   240   N N   . VAL A  1 41  ? 112.048 84.142  -19.178 1.00   46.29  ? 41  VAL A N   1 
ATOM   241   C CA  . VAL A  1 41  ? 111.512 82.819  -19.379 1.00   48.06  ? 41  VAL A CA  1 
ATOM   242   C C   . VAL A  1 41  ? 110.116 82.736  -18.780 1.00   42.32  ? 41  VAL A C   1 
ATOM   243   O O   . VAL A  1 41  ? 109.948 82.871  -17.572 1.00   37.86  ? 41  VAL A O   1 
ATOM   244   C CB  . VAL A  1 41  ? 112.411 81.750  -18.709 1.00   52.02  ? 41  VAL A CB  1 
ATOM   245   C CG1 . VAL A  1 41  ? 112.017 80.347  -19.166 1.00   53.58  ? 41  VAL A CG1 1 
ATOM   246   C CG2 . VAL A  1 41  ? 113.866 82.025  -19.020 1.00   54.55  ? 41  VAL A CG2 1 
ATOM   247   N N   . PRO A  1 42  ? 109.110 82.515  -19.621 1.00   41.16  ? 42  PRO A N   1 
ATOM   248   C CA  . PRO A  1 42  ? 107.763 82.312  -19.088 1.00   42.83  ? 42  PRO A CA  1 
ATOM   249   C C   . PRO A  1 42  ? 107.586 80.927  -18.467 1.00   40.29  ? 42  PRO A C   1 
ATOM   250   O O   . PRO A  1 42  ? 107.779 79.926  -19.155 1.00   41.64  ? 42  PRO A O   1 
ATOM   251   C CB  . PRO A  1 42  ? 106.874 82.498  -20.317 1.00   46.76  ? 42  PRO A CB  1 
ATOM   252   C CG  . PRO A  1 42  ? 107.759 82.221  -21.486 1.00   45.83  ? 42  PRO A CG  1 
ATOM   253   C CD  . PRO A  1 42  ? 109.130 82.645  -21.083 1.00   42.92  ? 42  PRO A CD  1 
ATOM   254   N N   . LEU A  1 43  ? 107.209 80.879  -17.192 1.00   35.00  ? 43  LEU A N   1 
ATOM   255   C CA  . LEU A  1 43  ? 107.111 79.622  -16.447 1.00   35.37  ? 43  LEU A CA  1 
ATOM   256   C C   . LEU A  1 43  ? 105.773 79.538  -15.702 1.00   35.75  ? 43  LEU A C   1 
ATOM   257   O O   . LEU A  1 43  ? 105.274 80.549  -15.214 1.00   37.25  ? 43  LEU A O   1 
ATOM   258   C CB  . LEU A  1 43  ? 108.284 79.493  -15.447 1.00   34.23  ? 43  LEU A CB  1 
ATOM   259   C CG  . LEU A  1 43  ? 109.729 79.489  -15.977 1.00   35.68  ? 43  LEU A CG  1 
ATOM   260   C CD1 . LEU A  1 43  ? 110.751 79.530  -14.861 1.00   27.23  ? 43  LEU A CD1 1 
ATOM   261   C CD2 . LEU A  1 43  ? 109.987 78.293  -16.868 1.00   35.86  ? 43  LEU A CD2 1 
ATOM   262   N N   . LEU A  1 44  ? 105.202 78.337  -15.606 1.00   33.27  ? 44  LEU A N   1 
ATOM   263   C CA  . LEU A  1 44  ? 103.954 78.138  -14.881 1.00   32.28  ? 44  LEU A CA  1 
ATOM   264   C C   . LEU A  1 44  ? 104.138 78.323  -13.375 1.00   32.06  ? 44  LEU A C   1 
ATOM   265   O O   . LEU A  1 44  ? 105.100 77.850  -12.803 1.00   31.79  ? 44  LEU A O   1 
ATOM   266   C CB  . LEU A  1 44  ? 103.387 76.745  -15.143 1.00   30.71  ? 44  LEU A CB  1 
ATOM   267   C CG  . LEU A  1 44  ? 102.056 76.487  -14.436 1.00   29.36  ? 44  LEU A CG  1 
ATOM   268   C CD1 . LEU A  1 44  ? 100.980 77.112  -15.201 1.00   31.16  ? 44  LEU A CD1 1 
ATOM   269   C CD2 . LEU A  1 44  ? 101.762 75.019  -14.280 1.00   31.68  ? 44  LEU A CD2 1 
ATOM   270   N N   . LEU A  1 45  ? 103.202 79.005  -12.729 1.00   32.73  ? 45  LEU A N   1 
ATOM   271   C CA  . LEU A  1 45  ? 103.220 79.096  -11.273 1.00   30.06  ? 45  LEU A CA  1 
ATOM   272   C C   . LEU A  1 45  ? 102.664 77.805  -10.643 1.00   28.90  ? 45  LEU A C   1 
ATOM   273   O O   . LEU A  1 45  ? 101.479 77.484  -10.811 1.00   30.75  ? 45  LEU A O   1 
ATOM   274   C CB  . LEU A  1 45  ? 102.425 80.319  -10.822 1.00   30.82  ? 45  LEU A CB  1 
ATOM   275   C CG  . LEU A  1 45  ? 102.182 80.471  -9.324  1.00   32.40  ? 45  LEU A CG  1 
ATOM   276   C CD1 . LEU A  1 45  ? 103.487 80.665  -8.617  1.00   32.87  ? 45  LEU A CD1 1 
ATOM   277   C CD2 . LEU A  1 45  ? 101.240 81.647  -9.054  1.00   34.90  ? 45  LEU A CD2 1 
ATOM   278   N N   . ASP A  1 46  ? 103.531 77.064  -9.947  1.00   28.69  ? 46  ASP A N   1 
ATOM   279   C CA  . ASP A  1 46  ? 103.184 75.787  -9.302  1.00   26.46  ? 46  ASP A CA  1 
ATOM   280   C C   . ASP A  1 46  ? 103.468 75.877  -7.806  1.00   24.38  ? 46  ASP A C   1 
ATOM   281   O O   . ASP A  1 46  ? 104.600 75.724  -7.356  1.00   26.98  ? 46  ASP A O   1 
ATOM   282   C CB  . ASP A  1 46  ? 103.954 74.624  -9.925  1.00   29.03  ? 46  ASP A CB  1 
ATOM   283   C CG  . ASP A  1 46  ? 103.553 73.272  -9.345  1.00   32.26  ? 46  ASP A CG  1 
ATOM   284   O OD1 . ASP A  1 46  ? 102.596 73.215  -8.537  1.00   33.92  ? 46  ASP A OD1 1 
ATOM   285   O OD2 . ASP A  1 46  ? 104.174 72.257  -9.728  1.00   33.19  1 46  ASP A OD2 1 
ATOM   286   N N   . LEU A  1 47  ? 102.423 76.166  -7.045  1.00   23.76  ? 47  LEU A N   1 
ATOM   287   C CA  . LEU A  1 47  ? 102.564 76.422  -5.630  1.00   24.87  ? 47  LEU A CA  1 
ATOM   288   C C   . LEU A  1 47  ? 103.280 75.290  -4.907  1.00   25.11  ? 47  LEU A C   1 
ATOM   289   O O   . LEU A  1 47  ? 104.153 75.516  -4.089  1.00   28.64  ? 47  LEU A O   1 
ATOM   290   C CB  . LEU A  1 47  ? 101.186 76.660  -5.015  1.00   25.39  ? 47  LEU A CB  1 
ATOM   291   C CG  . LEU A  1 47  ? 101.202 76.875  -3.510  1.00   23.68  ? 47  LEU A CG  1 
ATOM   292   C CD1 . LEU A  1 47  ? 101.978 78.139  -3.172  1.00   23.11  ? 47  LEU A CD1 1 
ATOM   293   C CD2 . LEU A  1 47  ? 99.787  77.014  -3.078  1.00   23.18  ? 47  LEU A CD2 1 
ATOM   294   N N   . ASN A  1 48  ? 102.937 74.062  -5.248  1.00   25.85  ? 48  ASN A N   1 
ATOM   295   C CA  . ASN A  1 48  ? 103.476 72.911  -4.541  1.00   24.31  ? 48  ASN A CA  1 
ATOM   296   C C   . ASN A  1 48  ? 104.707 72.303  -5.216  1.00   26.67  ? 48  ASN A C   1 
ATOM   297   O O   . ASN A  1 48  ? 105.248 71.321  -4.740  1.00   29.52  ? 48  ASN A O   1 
ATOM   298   C CB  . ASN A  1 48  ? 102.363 71.869  -4.410  1.00   24.75  ? 48  ASN A CB  1 
ATOM   299   C CG  . ASN A  1 48  ? 101.247 72.328  -3.511  1.00   25.90  ? 48  ASN A CG  1 
ATOM   300   O OD1 . ASN A  1 48  ? 101.487 72.742  -2.386  1.00   27.86  ? 48  ASN A OD1 1 
ATOM   301   N ND2 . ASN A  1 48  ? 100.022 72.276  -4.004  1.00   25.21  ? 48  ASN A ND2 1 
ATOM   302   N N   . GLY A  1 49  ? 105.155 72.890  -6.321  1.00   26.08  ? 49  GLY A N   1 
ATOM   303   C CA  . GLY A  1 49  ? 106.269 72.332  -7.055  1.00   25.19  ? 49  GLY A CA  1 
ATOM   304   C C   . GLY A  1 49  ? 107.541 72.352  -6.234  1.00   29.35  ? 49  GLY A C   1 
ATOM   305   O O   . GLY A  1 49  ? 107.779 73.313  -5.506  1.00   32.14  ? 49  GLY A O   1 
ATOM   306   N N   . LYS A  1 50  ? 108.344 71.282  -6.340  1.00   29.69  ? 50  LYS A N   1 
ATOM   307   C CA  . LYS A  1 50  ? 109.551 71.078  -5.516  1.00   28.02  ? 50  LYS A CA  1 
ATOM   308   C C   . LYS A  1 50  ? 110.742 71.877  -5.968  1.00   27.79  ? 50  LYS A C   1 
ATOM   309   O O   . LYS A  1 50  ? 111.657 72.121  -5.182  1.00   26.81  ? 50  LYS A O   1 
ATOM   310   C CB  . LYS A  1 50  ? 109.963 69.615  -5.487  1.00   28.94  ? 50  LYS A CB  1 
ATOM   311   C CG  . LYS A  1 50  ? 109.064 68.706  -4.695  1.00   31.11  ? 50  LYS A CG  1 
ATOM   312   C CD  . LYS A  1 50  ? 109.639 67.287  -4.649  1.00   32.73  ? 50  LYS A CD  1 
ATOM   313   C CE  . LYS A  1 50  ? 108.615 66.345  -4.048  1.00   37.67  ? 50  LYS A CE  1 
ATOM   314   N NZ  . LYS A  1 50  ? 108.979 64.905  -4.071  1.00   41.77  ? 50  LYS A NZ  1 
ATOM   315   N N   . HIS A  1 51  ? 110.730 72.268  -7.236  1.00   26.46  ? 51  HIS A N   1 
ATOM   316   C CA  . HIS A  1 51  ? 111.805 73.089  -7.789  1.00   25.80  ? 51  HIS A CA  1 
ATOM   317   C C   . HIS A  1 51  ? 111.369 73.794  -9.070  1.00   26.48  ? 51  HIS A C   1 
ATOM   318   O O   . HIS A  1 51  ? 110.326 73.477  -9.643  1.00   26.63  ? 51  HIS A O   1 
ATOM   319   C CB  . HIS A  1 51  ? 113.043 72.220  -8.061  1.00   25.91  ? 51  HIS A CB  1 
ATOM   320   C CG  . HIS A  1 51  ? 112.808 71.133  -9.062  1.00   23.42  ? 51  HIS A CG  1 
ATOM   321   N ND1 . HIS A  1 51  ? 112.644 69.813  -8.700  1.00   25.83  ? 51  HIS A ND1 1 
ATOM   322   C CD2 . HIS A  1 51  ? 112.708 71.166  -10.410 1.00   22.45  ? 51  HIS A CD2 1 
ATOM   323   C CE1 . HIS A  1 51  ? 112.433 69.086  -9.783  1.00   24.16  ? 51  HIS A CE1 1 
ATOM   324   N NE2 . HIS A  1 51  ? 112.459 69.886  -10.833 1.00   23.37  ? 51  HIS A NE2 1 
ATOM   325   N N   . LEU A  1 52  ? 112.206 74.708  -9.544  1.00   24.54  ? 52  LEU A N   1 
ATOM   326   C CA  . LEU A  1 52  ? 112.006 75.349  -10.825 1.00   26.54  ? 52  LEU A CA  1 
ATOM   327   C C   . LEU A  1 52  ? 112.556 74.466  -11.929 1.00   28.34  ? 52  LEU A C   1 
ATOM   328   O O   . LEU A  1 52  ? 113.633 73.907  -11.804 1.00   30.01  ? 52  LEU A O   1 
ATOM   329   C CB  . LEU A  1 52  ? 112.695 76.731  -10.857 1.00   26.88  ? 52  LEU A CB  1 
ATOM   330   C CG  . LEU A  1 52  ? 112.512 77.613  -12.089 1.00   27.08  ? 52  LEU A CG  1 
ATOM   331   C CD1 . LEU A  1 52  ? 112.630 79.038  -11.678 1.00   27.21  ? 52  LEU A CD1 1 
ATOM   332   C CD2 . LEU A  1 52  ? 113.529 77.305  -13.192 1.00   25.92  ? 52  LEU A CD2 1 
ATOM   333   N N   . TRP A  1 53  ? 111.808 74.292  -13.004 1.00   28.38  ? 53  TRP A N   1 
ATOM   334   C CA  . TRP A  1 53  ? 112.387 73.593  -14.125 1.00   27.04  ? 53  TRP A CA  1 
ATOM   335   C C   . TRP A  1 53  ? 112.048 74.281  -15.417 1.00   29.52  ? 53  TRP A C   1 
ATOM   336   O O   . TRP A  1 53  ? 111.010 74.895  -15.540 1.00   32.80  ? 53  TRP A O   1 
ATOM   337   C CB  . TRP A  1 53  ? 111.946 72.138  -14.143 1.00   26.61  ? 53  TRP A CB  1 
ATOM   338   C CG  . TRP A  1 53  ? 110.506 71.935  -14.253 1.00   29.62  ? 53  TRP A CG  1 
ATOM   339   C CD1 . TRP A  1 53  ? 109.627 71.812  -13.228 1.00   30.56  ? 53  TRP A CD1 1 
ATOM   340   C CD2 . TRP A  1 53  ? 109.751 71.765  -15.459 1.00   33.80  ? 53  TRP A CD2 1 
ATOM   341   N NE1 . TRP A  1 53  ? 108.359 71.604  -13.714 1.00   34.69  ? 53  TRP A NE1 1 
ATOM   342   C CE2 . TRP A  1 53  ? 108.407 71.561  -15.082 1.00   36.46  ? 53  TRP A CE2 1 
ATOM   343   C CE3 . TRP A  1 53  ? 110.077 71.780  -16.822 1.00   35.06  ? 53  TRP A CE3 1 
ATOM   344   C CZ2 . TRP A  1 53  ? 107.381 71.376  -16.021 1.00   38.89  ? 53  TRP A CZ2 1 
ATOM   345   C CZ3 . TRP A  1 53  ? 109.063 71.587  -17.754 1.00   37.46  ? 53  TRP A CZ3 1 
ATOM   346   C CH2 . TRP A  1 53  ? 107.732 71.387  -17.348 1.00   39.90  ? 53  TRP A CH2 1 
ATOM   347   N N   . VAL A  1 54  ? 112.949 74.170  -16.377 1.00   31.20  ? 54  VAL A N   1 
ATOM   348   C CA  . VAL A  1 54  ? 112.810 74.805  -17.679 1.00   29.82  ? 54  VAL A CA  1 
ATOM   349   C C   . VAL A  1 54  ? 113.321 73.786  -18.678 1.00   38.46  ? 54  VAL A C   1 
ATOM   350   O O   . VAL A  1 54  ? 114.091 72.911  -18.313 1.00   36.38  ? 54  VAL A O   1 
ATOM   351   C CB  . VAL A  1 54  ? 113.604 76.142  -17.750 1.00   33.18  ? 54  VAL A CB  1 
ATOM   352   C CG1 . VAL A  1 54  ? 115.101 75.903  -17.664 1.00   30.83  ? 54  VAL A CG1 1 
ATOM   353   C CG2 . VAL A  1 54  ? 113.253 76.928  -19.018 1.00   37.44  ? 54  VAL A CG2 1 
ATOM   354   N N   . THR A  1 55  ? 112.861 73.841  -19.916 1.00   43.63  ? 55  THR A N   1 
ATOM   355   C CA  . THR A  1 55  ? 113.436 73.001  -20.966 1.00   49.95  ? 55  THR A CA  1 
ATOM   356   C C   . THR A  1 55  ? 114.805 73.526  -21.429 1.00   47.63  ? 55  THR A C   1 
ATOM   357   O O   . THR A  1 55  ? 114.977 74.732  -21.618 1.00   45.40  ? 55  THR A O   1 
ATOM   358   C CB  . THR A  1 55  ? 112.531 72.929  -22.190 1.00   59.84  ? 55  THR A CB  1 
ATOM   359   O OG1 . THR A  1 55  ? 112.342 74.250  -22.700 1.00   64.49  ? 55  THR A OG1 1 
ATOM   360   C CG2 . THR A  1 55  ? 111.168 72.269  -21.845 1.00   42.73  ? 55  THR A CG2 1 
ATOM   361   N N   . CYS A  1 56  ? 115.798 72.643  -21.509 1.00   47.60  ? 56  CYS A N   1 
ATOM   362   C CA  . CYS A  1 56  ? 117.124 73.020  -21.978 1.00   46.58  ? 56  CYS A CA  1 
ATOM   363   C C   . CYS A  1 56  ? 117.503 72.327  -23.287 1.00   49.65  ? 56  CYS A C   1 
ATOM   364   O O   . CYS A  1 56  ? 117.160 71.160  -23.483 1.00   52.23  ? 56  CYS A O   1 
ATOM   365   C CB  . CYS A  1 56  ? 118.150 72.707  -20.903 1.00   43.65  ? 56  CYS A CB  1 
ATOM   366   S SG  . CYS A  1 56  ? 117.902 73.722  -19.458 1.00   49.76  ? 56  CYS A SG  1 
ATOM   367   N N   . SER A  1 57  ? 118.214 73.038  -24.167 1.00   49.31  ? 57  SER A N   1 
ATOM   368   C CA  . SER A  1 57  ? 118.675 72.489  -25.447 1.00   50.04  ? 57  SER A CA  1 
ATOM   369   C C   . SER A  1 57  ? 120.044 73.074  -25.817 1.00   52.03  ? 57  SER A C   1 
ATOM   370   O O   . SER A  1 57  ? 120.614 73.849  -25.053 1.00   52.28  ? 57  SER A O   1 
ATOM   371   C CB  . SER A  1 57  ? 117.681 72.790  -26.546 1.00   52.18  ? 57  SER A CB  1 
ATOM   372   O OG  . SER A  1 57  ? 117.685 74.176  -26.808 1.00   52.81  ? 57  SER A OG  1 
ATOM   373   N N   . GLN A  1 58  ? 120.570 72.724  -26.989 1.00   52.20  ? 58  GLN A N   1 
ATOM   374   C CA  . GLN A  1 58  ? 121.774 73.376  -27.517 1.00   52.40  ? 58  GLN A CA  1 
ATOM   375   C C   . GLN A  1 58  ? 121.509 74.868  -27.796 1.00   52.36  ? 58  GLN A C   1 
ATOM   376   O O   . GLN A  1 58  ? 122.428 75.613  -28.126 1.00   50.97  ? 58  GLN A O   1 
ATOM   377   C CB  . GLN A  1 58  ? 122.300 72.695  -28.796 1.00   58.97  ? 58  GLN A CB  1 
ATOM   378   C CG  . GLN A  1 58  ? 121.367 72.696  -30.006 1.00   64.72  ? 58  GLN A CG  1 
ATOM   379   C CD  . GLN A  1 58  ? 120.282 71.653  -29.968 1.00   65.93  ? 58  GLN A CD  1 
ATOM   380   O OE1 . GLN A  1 58  ? 119.945 71.117  -28.914 1.00   64.27  ? 58  GLN A OE1 1 
ATOM   381   N NE2 . GLN A  1 58  ? 119.722 71.358  -31.133 1.00   69.72  ? 58  GLN A NE2 1 
ATOM   382   N N   . HIS A  1 59  ? 120.243 75.280  -27.751 1.00   49.70  ? 59  HIS A N   1 
ATOM   383   C CA  . HIS A  1 59  ? 119.881 76.671  -28.036 1.00   58.93  ? 59  HIS A CA  1 
ATOM   384   C C   . HIS A  1 59  ? 119.830 77.551  -26.784 1.00   55.88  ? 59  HIS A C   1 
ATOM   385   O O   . HIS A  1 59  ? 119.560 78.751  -26.863 1.00   55.98  ? 59  HIS A O   1 
ATOM   386   C CB  . HIS A  1 59  ? 118.529 76.738  -28.749 1.00   59.57  ? 59  HIS A CB  1 
ATOM   387   C CG  . HIS A  1 59  ? 118.466 75.929  -30.009 1.00   61.63  ? 59  HIS A CG  1 
ATOM   388   N ND1 . HIS A  1 59  ? 119.273 76.186  -31.097 1.00   63.78  ? 59  HIS A ND1 1 
ATOM   389   C CD2 . HIS A  1 59  ? 117.698 74.867  -30.350 1.00   60.85  ? 59  HIS A CD2 1 
ATOM   390   C CE1 . HIS A  1 59  ? 119.004 75.316  -32.054 1.00   65.47  ? 59  HIS A CE1 1 
ATOM   391   N NE2 . HIS A  1 59  ? 118.052 74.506  -31.627 1.00   63.90  ? 59  HIS A NE2 1 
ATOM   392   N N   . TYR A  1 60  ? 120.082 76.941  -25.636 1.00   52.41  ? 60  TYR A N   1 
ATOM   393   C CA  . TYR A  1 60  ? 120.273 77.645  -24.372 1.00   51.04  ? 60  TYR A CA  1 
ATOM   394   C C   . TYR A  1 60  ? 121.603 78.423  -24.348 1.00   54.80  ? 60  TYR A C   1 
ATOM   395   O O   . TYR A  1 60  ? 122.664 77.819  -24.460 1.00   58.23  ? 60  TYR A O   1 
ATOM   396   C CB  . TYR A  1 60  ? 120.233 76.628  -23.247 1.00   47.44  ? 60  TYR A CB  1 
ATOM   397   C CG  . TYR A  1 60  ? 120.259 77.154  -21.830 1.00   44.80  ? 60  TYR A CG  1 
ATOM   398   C CD1 . TYR A  1 60  ? 121.345 77.881  -21.343 1.00   42.03  ? 60  TYR A CD1 1 
ATOM   399   C CD2 . TYR A  1 60  ? 119.240 76.825  -20.940 1.00   44.02  ? 60  TYR A CD2 1 
ATOM   400   C CE1 . TYR A  1 60  ? 121.382 78.312  -20.031 1.00   38.63  ? 60  TYR A CE1 1 
ATOM   401   C CE2 . TYR A  1 60  ? 119.271 77.251  -19.622 1.00   39.89  ? 60  TYR A CE2 1 
ATOM   402   C CZ  . TYR A  1 60  ? 120.342 77.989  -19.172 1.00   37.98  ? 60  TYR A CZ  1 
ATOM   403   O OH  . TYR A  1 60  ? 120.367 78.405  -17.855 1.00   36.18  ? 60  TYR A OH  1 
ATOM   404   N N   . SER A  1 61  ? 121.559 79.751  -24.252 1.00   55.46  ? 61  SER A N   1 
ATOM   405   C CA  . SER A  1 61  ? 122.794 80.551  -24.220 1.00   57.40  ? 61  SER A CA  1 
ATOM   406   C C   . SER A  1 61  ? 122.956 81.370  -22.933 1.00   53.15  ? 61  SER A C   1 
ATOM   407   O O   . SER A  1 61  ? 122.123 82.207  -22.605 1.00   52.53  ? 61  SER A O   1 
ATOM   408   C CB  . SER A  1 61  ? 122.871 81.485  -25.422 1.00   64.74  ? 61  SER A CB  1 
ATOM   409   O OG  . SER A  1 61  ? 124.062 82.249  -25.361 1.00   68.16  ? 61  SER A OG  1 
ATOM   410   N N   . SER A  1 62  ? 124.045 81.128  -22.216 1.00   52.45  ? 62  SER A N   1 
ATOM   411   C CA  . SER A  1 62  ? 124.339 81.802  -20.956 1.00   49.23  ? 62  SER A CA  1 
ATOM   412   C C   . SER A  1 62  ? 125.804 81.656  -20.614 1.00   50.86  ? 62  SER A C   1 
ATOM   413   O O   . SER A  1 62  ? 126.375 80.569  -20.739 1.00   51.88  ? 62  SER A O   1 
ATOM   414   C CB  . SER A  1 62  ? 123.505 81.239  -19.821 1.00   43.34  ? 62  SER A CB  1 
ATOM   415   O OG  . SER A  1 62  ? 123.861 81.858  -18.602 1.00   40.14  ? 62  SER A OG  1 
ATOM   416   N N   . SER A  1 63  ? 126.419 82.755  -20.196 1.00   47.84  ? 63  SER A N   1 
ATOM   417   C CA  . SER A  1 63  ? 127.812 82.703  -19.816 1.00   44.35  ? 63  SER A CA  1 
ATOM   418   C C   . SER A  1 63  ? 127.971 82.295  -18.358 1.00   43.30  ? 63  SER A C   1 
ATOM   419   O O   . SER A  1 63  ? 129.084 82.180  -17.864 1.00   43.76  ? 63  SER A O   1 
ATOM   420   C CB  . SER A  1 63  ? 128.495 84.051  -20.067 1.00   45.29  ? 63  SER A CB  1 
ATOM   421   O OG  . SER A  1 63  ? 128.010 85.050  -19.201 1.00   44.75  ? 63  SER A OG  1 
ATOM   422   N N   . THR A  1 64  ? 126.872 82.070  -17.654 1.00   40.86  ? 64  THR A N   1 
ATOM   423   C CA  . THR A  1 64  ? 126.996 81.676  -16.255 1.00   38.30  ? 64  THR A CA  1 
ATOM   424   C C   . THR A  1 64  ? 126.378 80.314  -15.923 1.00   37.24  ? 64  THR A C   1 
ATOM   425   O O   . THR A  1 64  ? 126.255 79.946  -14.755 1.00   34.92  ? 64  THR A O   1 
ATOM   426   C CB  . THR A  1 64  ? 126.389 82.725  -15.361 1.00   36.14  ? 64  THR A CB  1 
ATOM   427   O OG1 . THR A  1 64  ? 125.157 83.169  -15.932 1.00   39.13  ? 64  THR A OG1 1 
ATOM   428   C CG2 . THR A  1 64  ? 127.340 83.881  -15.274 1.00   35.10  ? 64  THR A CG2 1 
ATOM   429   N N   . TYR A  1 65  ? 126.003 79.567  -16.952 1.00   37.95  ? 65  TYR A N   1 
ATOM   430   C CA  . TYR A  1 65  ? 125.385 78.267  -16.762 1.00   37.77  ? 65  TYR A CA  1 
ATOM   431   C C   . TYR A  1 65  ? 126.409 77.228  -16.366 1.00   38.84  ? 65  TYR A C   1 
ATOM   432   O O   . TYR A  1 65  ? 127.499 77.189  -16.916 1.00   42.48  ? 65  TYR A O   1 
ATOM   433   C CB  . TYR A  1 65  ? 124.687 77.816  -18.039 1.00   37.12  ? 65  TYR A CB  1 
ATOM   434   C CG  . TYR A  1 65  ? 124.345 76.351  -18.038 1.00   35.09  ? 65  TYR A CG  1 
ATOM   435   C CD1 . TYR A  1 65  ? 123.181 75.888  -17.458 1.00   34.43  ? 65  TYR A CD1 1 
ATOM   436   C CD2 . TYR A  1 65  ? 125.221 75.419  -18.589 1.00   36.07  ? 65  TYR A CD2 1 
ATOM   437   C CE1 . TYR A  1 65  ? 122.881 74.532  -17.447 1.00   34.82  ? 65  TYR A CE1 1 
ATOM   438   C CE2 . TYR A  1 65  ? 124.941 74.085  -18.574 1.00   35.27  ? 65  TYR A CE2 1 
ATOM   439   C CZ  . TYR A  1 65  ? 123.772 73.644  -18.001 1.00   35.75  ? 65  TYR A CZ  1 
ATOM   440   O OH  . TYR A  1 65  ? 123.503 72.306  -18.007 1.00   38.18  ? 65  TYR A OH  1 
ATOM   441   N N   . GLN A  1 66  ? 126.042 76.362  -15.434 1.00   37.00  ? 66  GLN A N   1 
ATOM   442   C CA  . GLN A  1 66  ? 126.858 75.212  -15.087 1.00   37.11  ? 66  GLN A CA  1 
ATOM   443   C C   . GLN A  1 66  ? 125.995 74.021  -14.759 1.00   33.19  ? 66  GLN A C   1 
ATOM   444   O O   . GLN A  1 66  ? 124.918 74.175  -14.189 1.00   32.65  ? 66  GLN A O   1 
ATOM   445   C CB  . GLN A  1 66  ? 127.725 75.514  -13.890 1.00   44.06  ? 66  GLN A CB  1 
ATOM   446   C CG  . GLN A  1 66  ? 128.864 76.433  -14.160 1.00   55.84  ? 66  GLN A CG  1 
ATOM   447   C CD  . GLN A  1 66  ? 129.582 76.826  -12.881 1.00   63.57  ? 66  GLN A CD  1 
ATOM   448   O OE1 . GLN A  1 66  ? 129.858 75.984  -12.020 1.00   66.13  ? 66  GLN A OE1 1 
ATOM   449   N NE2 . GLN A  1 66  ? 129.905 78.108  -12.758 1.00   65.80  ? 66  GLN A NE2 1 
ATOM   450   N N   . ALA A  1 67  ? 126.490 72.833  -15.087 1.00   30.45  ? 67  ALA A N   1 
ATOM   451   C CA  . ALA A  1 67  ? 125.859 71.601  -14.639 1.00   31.07  ? 67  ALA A CA  1 
ATOM   452   C C   . ALA A  1 67  ? 126.724 71.010  -13.542 1.00   33.97  ? 67  ALA A C   1 
ATOM   453   O O   . ALA A  1 67  ? 127.804 70.511  -13.834 1.00   35.74  ? 67  ALA A O   1 
ATOM   454   C CB  . ALA A  1 67  ? 125.709 70.619  -15.783 1.00   30.93  ? 67  ALA A CB  1 
ATOM   455   N N   . PRO A  1 68  ? 126.271 71.082  -12.268 1.00   31.11  ? 68  PRO A N   1 
ATOM   456   C CA  . PRO A  1 68  ? 127.071 70.576  -11.138 1.00   27.29  ? 68  PRO A CA  1 
ATOM   457   C C   . PRO A  1 68  ? 127.478 69.116  -11.318 1.00   28.45  ? 68  PRO A C   1 
ATOM   458   O O   . PRO A  1 68  ? 126.726 68.350  -11.928 1.00   30.04  ? 68  PRO A O   1 
ATOM   459   C CB  . PRO A  1 68  ? 126.125 70.732  -9.946  1.00   25.61  ? 68  PRO A CB  1 
ATOM   460   C CG  . PRO A  1 68  ? 125.259 71.871  -10.312 1.00   28.27  ? 68  PRO A CG  1 
ATOM   461   C CD  . PRO A  1 68  ? 125.051 71.770  -11.813 1.00   29.49  ? 68  PRO A CD  1 
ATOM   462   N N   . PHE A  1 69  ? 128.641 68.724  -10.807 1.00   30.46  ? 69  PHE A N   1 
ATOM   463   C CA  . PHE A  1 69  ? 129.062 67.333  -10.970 1.00   29.45  ? 69  PHE A CA  1 
ATOM   464   C C   . PHE A  1 69  ? 128.412 66.436  -9.931  1.00   28.96  ? 69  PHE A C   1 
ATOM   465   O O   . PHE A  1 69  ? 128.007 66.884  -8.870  1.00   32.10  ? 69  PHE A O   1 
ATOM   466   C CB  . PHE A  1 69  ? 130.607 67.200  -10.946 1.00   38.26  ? 69  PHE A CB  1 
ATOM   467   C CG  . PHE A  1 69  ? 131.281 67.730  -9.691  1.00   37.59  ? 69  PHE A CG  1 
ATOM   468   C CD1 . PHE A  1 69  ? 131.354 66.963  -8.537  1.00   35.03  ? 69  PHE A CD1 1 
ATOM   469   C CD2 . PHE A  1 69  ? 131.913 68.966  -9.694  1.00   38.39  ? 69  PHE A CD2 1 
ATOM   470   C CE1 . PHE A  1 69  ? 131.999 67.430  -7.397  1.00   31.75  ? 69  PHE A CE1 1 
ATOM   471   C CE2 . PHE A  1 69  ? 132.568 69.441  -8.549  1.00   35.81  ? 69  PHE A CE2 1 
ATOM   472   C CZ  . PHE A  1 69  ? 132.603 68.666  -7.404  1.00   31.87  ? 69  PHE A CZ  1 
ATOM   473   N N   . CYS A  1 70  ? 128.297 65.160  -10.254 1.00   30.53  ? 70  CYS A N   1 
ATOM   474   C CA  . CYS A  1 70  ? 127.657 64.226  -9.355  1.00   31.93  ? 70  CYS A CA  1 
ATOM   475   C C   . CYS A  1 70  ? 128.421 64.168  -8.042  1.00   34.01  ? 70  CYS A C   1 
ATOM   476   O O   . CYS A  1 70  ? 129.646 64.212  -8.033  1.00   37.02  ? 70  CYS A O   1 
ATOM   477   C CB  . CYS A  1 70  ? 127.572 62.847  -9.997  1.00   35.69  ? 70  CYS A CB  1 
ATOM   478   S SG  . CYS A  1 70  ? 126.315 61.801  -9.281  1.00   39.51  ? 70  CYS A SG  1 
ATOM   479   N N   . HIS A  1 71  ? 127.684 64.108  -6.940  1.00   31.94  ? 71  HIS A N   1 
ATOM   480   C CA  . HIS A  1 71  ? 128.251 64.090  -5.590  1.00   28.52  ? 71  HIS A CA  1 
ATOM   481   C C   . HIS A  1 71  ? 128.809 65.442  -5.175  1.00   27.06  ? 71  HIS A C   1 
ATOM   482   O O   . HIS A  1 71  ? 129.557 65.529  -4.206  1.00   28.50  ? 71  HIS A O   1 
ATOM   483   C CB  . HIS A  1 71  ? 129.350 63.030  -5.453  1.00   29.25  ? 71  HIS A CB  1 
ATOM   484   C CG  . HIS A  1 71  ? 128.971 61.687  -5.990  1.00   30.69  ? 71  HIS A CG  1 
ATOM   485   N ND1 . HIS A  1 71  ? 127.937 60.942  -5.470  1.00   30.86  ? 71  HIS A ND1 1 
ATOM   486   C CD2 . HIS A  1 71  ? 129.505 60.944  -6.985  1.00   31.83  ? 71  HIS A CD2 1 
ATOM   487   C CE1 . HIS A  1 71  ? 127.840 59.804  -6.129  1.00   30.96  ? 71  HIS A CE1 1 
ATOM   488   N NE2 . HIS A  1 71  ? 128.783 59.777  -7.052  1.00   32.13  ? 71  HIS A NE2 1 
ATOM   489   N N   . SER A  1 72  ? 128.487 66.492  -5.919  1.00   25.48  ? 72  SER A N   1 
ATOM   490   C CA  . SER A  1 72  ? 128.887 67.818  -5.503  1.00   25.08  ? 72  SER A CA  1 
ATOM   491   C C   . SER A  1 72  ? 128.023 68.317  -4.338  1.00   24.57  ? 72  SER A C   1 
ATOM   492   O O   . SER A  1 72  ? 126.982 67.747  -4.012  1.00   26.30  ? 72  SER A O   1 
ATOM   493   C CB  . SER A  1 72  ? 128.802 68.784  -6.677  1.00   25.14  ? 72  SER A CB  1 
ATOM   494   O OG  . SER A  1 72  ? 127.461 68.826  -7.143  1.00   24.91  ? 72  SER A OG  1 
ATOM   495   N N   . THR A  1 73  ? 128.466 69.399  -3.718  1.00   23.61  ? 73  THR A N   1 
ATOM   496   C CA  . THR A  1 73  ? 127.691 70.049  -2.680  1.00   23.77  ? 73  THR A CA  1 
ATOM   497   C C   . THR A  1 73  ? 126.395 70.583  -3.255  1.00   25.65  ? 73  THR A C   1 
ATOM   498   O O   . THR A  1 73  ? 125.393 70.657  -2.556  1.00   27.69  ? 73  THR A O   1 
ATOM   499   C CB  . THR A  1 73  ? 128.467 71.194  -2.028  1.00   24.94  ? 73  THR A CB  1 
ATOM   500   O OG1 . THR A  1 73  ? 128.927 72.105  -3.040  1.00   27.50  ? 73  THR A OG1 1 
ATOM   501   C CG2 . THR A  1 73  ? 129.656 70.657  -1.255  1.00   24.13  ? 73  THR A CG2 1 
ATOM   502   N N   . GLN A  1 74  ? 126.411 70.982  -4.523  1.00   25.04  ? 74  GLN A N   1 
ATOM   503   C CA  . GLN A  1 74  ? 125.188 71.414  -5.173  1.00   25.05  ? 74  GLN A CA  1 
ATOM   504   C C   . GLN A  1 74  ? 124.166 70.295  -5.331  1.00   23.12  ? 74  GLN A C   1 
ATOM   505   O O   . GLN A  1 74  ? 122.993 70.499  -5.091  1.00   25.61  ? 74  GLN A O   1 
ATOM   506   C CB  . GLN A  1 74  ? 125.498 72.031  -6.533  1.00   28.76  ? 74  GLN A CB  1 
ATOM   507   C CG  . GLN A  1 74  ? 126.318 73.328  -6.454  1.00   27.57  ? 74  GLN A CG  1 
ATOM   508   C CD  . GLN A  1 74  ? 127.777 73.091  -6.744  1.00   30.62  ? 74  GLN A CD  1 
ATOM   509   O OE1 . GLN A  1 74  ? 128.298 72.020  -6.502  1.00   31.77  ? 74  GLN A OE1 1 
ATOM   510   N NE2 . GLN A  1 74  ? 128.434 74.085  -7.299  1.00   36.39  ? 74  GLN A NE2 1 
ATOM   511   N N   . CYS A  1 75  ? 124.609 69.112  -5.715  1.00   23.04  ? 75  CYS A N   1 
ATOM   512   C CA  . CYS A  1 75  ? 123.718 67.972  -5.833  1.00   24.01  ? 75  CYS A CA  1 
ATOM   513   C C   . CYS A  1 75  ? 123.216 67.534  -4.469  1.00   23.24  ? 75  CYS A C   1 
ATOM   514   O O   . CYS A  1 75  ? 122.111 67.046  -4.326  1.00   22.88  ? 75  CYS A O   1 
ATOM   515   C CB  . CYS A  1 75  ? 124.427 66.835  -6.525  1.00   26.46  ? 75  CYS A CB  1 
ATOM   516   S SG  . CYS A  1 75  ? 124.885 67.293  -8.171  1.00   36.00  ? 75  CYS A SG  1 
ATOM   517   N N   . SER A  1 76  ? 124.067 67.671  -3.474  1.00   24.14  ? 76  SER A N   1 
ATOM   518   C CA  . SER A  1 76  ? 123.674 67.424  -2.100  1.00   23.69  ? 76  SER A CA  1 
ATOM   519   C C   . SER A  1 76  ? 122.548 68.356  -1.611  1.00   25.31  ? 76  SER A C   1 
ATOM   520   O O   . SER A  1 76  ? 121.565 67.895  -1.053  1.00   27.62  ? 76  SER A O   1 
ATOM   521   C CB  . SER A  1 76  ? 124.905 67.552  -1.203  1.00   26.08  ? 76  SER A CB  1 
ATOM   522   O OG  . SER A  1 76  ? 124.551 67.325  0.143   1.00   29.19  ? 76  SER A OG  1 
ATOM   523   N N   . ARG A  1 77  ? 122.677 69.662  -1.826  1.00   25.43  ? 77  ARG A N   1 
ATOM   524   C CA  . ARG A  1 77  ? 121.652 70.603  -1.410  1.00   23.78  ? 77  ARG A CA  1 
ATOM   525   C C   . ARG A  1 77  ? 120.322 70.336  -2.092  1.00   28.16  ? 77  ARG A C   1 
ATOM   526   O O   . ARG A  1 77  ? 119.273 70.469  -1.472  1.00   27.39  ? 77  ARG A O   1 
ATOM   527   C CB  . ARG A  1 77  ? 122.084 72.030  -1.686  1.00   25.10  ? 77  ARG A CB  1 
ATOM   528   C CG  . ARG A  1 77  ? 121.125 73.028  -1.103  1.00   25.61  ? 77  ARG A CG  1 
ATOM   529   C CD  . ARG A  1 77  ? 121.532 74.463  -1.339  1.00   27.39  ? 77  ARG A CD  1 
ATOM   530   N NE  . ARG A  1 77  ? 120.509 75.344  -0.777  1.00   31.47  ? 77  ARG A NE  1 
ATOM   531   C CZ  . ARG A  1 77  ? 120.395 76.638  -1.034  1.00   30.84  ? 77  ARG A CZ  1 
ATOM   532   N NH1 . ARG A  1 77  ? 121.259 77.224  -1.848  1.00   33.63  ? 77  ARG A NH1 1 
ATOM   533   N NH2 . ARG A  1 77  ? 119.429 77.338  -0.448  1.00   30.73  ? 77  ARG A NH2 1 
ATOM   534   N N   . ALA A  1 78  ? 120.377 69.952  -3.366  1.00   29.45  ? 78  ALA A N   1 
ATOM   535   C CA  . ALA A  1 78  ? 119.185 69.626  -4.163  1.00   29.96  ? 78  ALA A CA  1 
ATOM   536   C C   . ALA A  1 78  ? 118.607 68.272  -3.816  1.00   29.29  ? 78  ALA A C   1 
ATOM   537   O O   . ALA A  1 78  ? 117.575 67.904  -4.330  1.00   28.92  ? 78  ALA A O   1 
ATOM   538   C CB  . ALA A  1 78  ? 119.500 69.671  -5.661  1.00   30.99  ? 78  ALA A CB  1 
ATOM   539   N N   . ASN A  1 79  ? 119.314 67.532  -2.974  1.00   32.07  ? 79  ASN A N   1 
ATOM   540   C CA  . ASN A  1 79  ? 118.872 66.241  -2.500  1.00   36.51  ? 79  ASN A CA  1 
ATOM   541   C C   . ASN A  1 79  ? 118.757 65.214  -3.612  1.00   37.19  ? 79  ASN A C   1 
ATOM   542   O O   . ASN A  1 79  ? 117.805 64.437  -3.671  1.00   36.03  ? 79  ASN A O   1 
ATOM   543   C CB  . ASN A  1 79  ? 117.547 66.406  -1.753  1.00   42.55  ? 79  ASN A CB  1 
ATOM   544   C CG  . ASN A  1 79  ? 117.188 65.198  -0.932  1.00   46.46  ? 79  ASN A CG  1 
ATOM   545   O OD1 . ASN A  1 79  ? 118.052 64.426  -0.529  1.00   45.04  ? 79  ASN A OD1 1 
ATOM   546   N ND2 . ASN A  1 79  ? 115.909 65.041  -0.657  1.00   51.25  ? 79  ASN A ND2 1 
ATOM   547   N N   . THR A  1 80  ? 119.734 65.218  -4.509  1.00   37.79  ? 80  THR A N   1 
ATOM   548   C CA  . THR A  1 80  ? 119.824 64.167  -5.505  1.00   40.60  ? 80  THR A CA  1 
ATOM   549   C C   . THR A  1 80  ? 121.205 63.542  -5.491  1.00   45.95  ? 80  THR A C   1 
ATOM   550   O O   . THR A  1 80  ? 122.230 64.239  -5.604  1.00   44.18  ? 80  THR A O   1 
ATOM   551   C CB  . THR A  1 80  ? 119.546 64.666  -6.906  1.00   39.85  ? 80  THR A CB  1 
ATOM   552   O OG1 . THR A  1 80  ? 119.899 63.630  -7.828  1.00   45.79  ? 80  THR A OG1 1 
ATOM   553   C CG2 . THR A  1 80  ? 120.353 65.931  -7.217  1.00   34.65  ? 80  THR A CG2 1 
ATOM   554   N N   . HIS A  1 81  ? 121.234 62.225  -5.329  1.00   51.15  ? 81  HIS A N   1 
ATOM   555   C CA  . HIS A  1 81  ? 122.498 61.490  -5.358  1.00   55.66  ? 81  HIS A CA  1 
ATOM   556   C C   . HIS A  1 81  ? 122.494 60.390  -6.447  1.00   56.47  ? 81  HIS A C   1 
ATOM   557   O O   . HIS A  1 81  ? 123.311 59.466  -6.418  1.00   58.72  ? 81  HIS A O   1 
ATOM   558   C CB  . HIS A  1 81  ? 122.826 60.948  -3.954  1.00   57.39  ? 81  HIS A CB  1 
ATOM   559   C CG  . HIS A  1 81  ? 123.151 62.032  -2.958  1.00   59.54  ? 81  HIS A CG  1 
ATOM   560   N ND1 . HIS A  1 81  ? 124.440 62.470  -2.722  1.00   59.40  ? 81  HIS A ND1 1 
ATOM   561   C CD2 . HIS A  1 81  ? 122.349 62.797  -2.175  1.00   58.53  ? 81  HIS A CD2 1 
ATOM   562   C CE1 . HIS A  1 81  ? 124.419 63.435  -1.818  1.00   57.25  ? 81  HIS A CE1 1 
ATOM   563   N NE2 . HIS A  1 81  ? 123.163 63.653  -1.470  1.00   56.57  ? 81  HIS A NE2 1 
ATOM   564   N N   . GLN A  1 82  ? 121.575 60.529  -7.409  1.00   52.72  ? 82  GLN A N   1 
ATOM   565   C CA  . GLN A  1 82  ? 121.522 59.685  -8.597  1.00   49.73  ? 82  GLN A CA  1 
ATOM   566   C C   . GLN A  1 82  ? 122.266 60.383  -9.754  1.00   47.47  ? 82  GLN A C   1 
ATOM   567   O O   . GLN A  1 82  ? 121.892 61.477  -10.155 1.00   44.15  ? 82  GLN A O   1 
ATOM   568   C CB  . GLN A  1 82  ? 120.077 59.422  -9.015  1.00   53.29  ? 82  GLN A CB  1 
ATOM   569   C CG  . GLN A  1 82  ? 119.964 58.931  -10.458 1.00   61.46  ? 82  GLN A CG  1 
ATOM   570   C CD  . GLN A  1 82  ? 118.532 58.704  -10.924 1.00   68.83  ? 82  GLN A CD  1 
ATOM   571   O OE1 . GLN A  1 82  ? 117.581 58.874  -10.158 1.00   73.78  ? 82  GLN A OE1 1 
ATOM   572   N NE2 . GLN A  1 82  ? 118.379 58.255  -12.165 1.00   68.76  ? 82  GLN A NE2 1 
ATOM   573   N N   . CYS A  1 83  ? 123.291 59.748  -10.319 1.00   50.10  ? 83  CYS A N   1 
ATOM   574   C CA  . CYS A  1 83  ? 124.081 60.400  -11.364 1.00   48.62  ? 83  CYS A CA  1 
ATOM   575   C C   . CYS A  1 83  ? 123.376 60.453  -12.694 1.00   48.02  ? 83  CYS A C   1 
ATOM   576   O O   . CYS A  1 83  ? 122.549 59.606  -13.009 1.00   51.69  ? 83  CYS A O   1 
ATOM   577   C CB  . CYS A  1 83  ? 125.418 59.707  -11.547 1.00   48.34  ? 83  CYS A CB  1 
ATOM   578   S SG  . CYS A  1 83  ? 126.471 59.974  -10.148 1.00   55.82  ? 83  CYS A SG  1 
ATOM   579   N N   . PHE A  1 84  ? 123.734 61.445  -13.490 1.00   42.22  ? 84  PHE A N   1 
ATOM   580   C CA  . PHE A  1 84  ? 123.028 61.676  -14.725 1.00   40.74  ? 84  PHE A CA  1 
ATOM   581   C C   . PHE A  1 84  ? 123.879 61.194  -15.879 1.00   44.49  ? 84  PHE A C   1 
ATOM   582   O O   . PHE A  1 84  ? 125.085 61.405  -15.909 1.00   44.84  ? 84  PHE A O   1 
ATOM   583   C CB  . PHE A  1 84  ? 122.698 63.159  -14.867 1.00   37.12  ? 84  PHE A CB  1 
ATOM   584   C CG  . PHE A  1 84  ? 121.819 63.483  -16.033 1.00   34.18  ? 84  PHE A CG  1 
ATOM   585   C CD1 . PHE A  1 84  ? 120.450 63.480  -15.891 1.00   31.54  ? 84  PHE A CD1 1 
ATOM   586   C CD2 . PHE A  1 84  ? 122.359 63.814  -17.255 1.00   37.19  ? 84  PHE A CD2 1 
ATOM   587   C CE1 . PHE A  1 84  ? 119.633 63.783  -16.948 1.00   34.93  ? 84  PHE A CE1 1 
ATOM   588   C CE2 . PHE A  1 84  ? 121.542 64.119  -18.320 1.00   38.99  ? 84  PHE A CE2 1 
ATOM   589   C CZ  . PHE A  1 84  ? 120.176 64.111  -18.163 1.00   38.33  ? 84  PHE A CZ  1 
ATOM   590   N N   . THR A  1 85  ? 123.235 60.508  -16.812 1.00   49.86  ? 85  THR A N   1 
ATOM   591   C CA  . THR A  1 85  ? 123.878 60.066  -18.037 1.00   54.33  ? 85  THR A CA  1 
ATOM   592   C C   . THR A  1 85  ? 123.040 60.558  -19.218 1.00   55.47  ? 85  THR A C   1 
ATOM   593   O O   . THR A  1 85  ? 121.842 60.264  -19.292 1.00   54.76  ? 85  THR A O   1 
ATOM   594   C CB  . THR A  1 85  ? 124.008 58.544  -18.082 1.00   57.48  ? 85  THR A CB  1 
ATOM   595   O OG1 . THR A  1 85  ? 124.759 58.088  -16.948 1.00   57.68  ? 85  THR A OG1 1 
ATOM   596   C CG2 . THR A  1 85  ? 124.672 58.115  -19.364 1.00   58.27  ? 85  THR A CG2 1 
ATOM   597   N N   . CYS A  1 86  ? 123.644 61.310  -20.134 1.00   55.16  ? 86  CYS A N   1 
ATOM   598   C CA  . CYS A  1 86  ? 122.853 61.847  -21.229 1.00   57.12  ? 86  CYS A CA  1 
ATOM   599   C C   . CYS A  1 86  ? 122.724 60.786  -22.308 1.00   58.03  ? 86  CYS A C   1 
ATOM   600   O O   . CYS A  1 86  ? 123.709 60.282  -22.836 1.00   58.26  ? 86  CYS A O   1 
ATOM   601   C CB  . CYS A  1 86  ? 123.449 63.127  -21.800 1.00   58.78  ? 86  CYS A CB  1 
ATOM   602   S SG  . CYS A  1 86  ? 122.276 64.052  -22.879 1.00   61.96  ? 86  CYS A SG  1 
ATOM   603   N N   . THR A  1 87  ? 121.481 60.423  -22.588 1.00   58.58  ? 87  THR A N   1 
ATOM   604   C CA  . THR A  1 87  ? 121.174 59.419  -23.580 1.00   62.43  ? 87  THR A CA  1 
ATOM   605   C C   . THR A  1 87  ? 120.471 59.977  -24.797 1.00   67.20  ? 87  THR A C   1 
ATOM   606   O O   . THR A  1 87  ? 120.075 59.213  -25.671 1.00   71.30  ? 87  THR A O   1 
ATOM   607   C CB  . THR A  1 87  ? 120.266 58.369  -22.990 1.00   62.67  ? 87  THR A CB  1 
ATOM   608   O OG1 . THR A  1 87  ? 119.128 59.033  -22.420 1.00   63.22  ? 87  THR A OG1 1 
ATOM   609   C CG2 . THR A  1 87  ? 120.977 57.627  -21.885 1.00   60.94  ? 87  THR A CG2 1 
ATOM   610   N N   . ASP A  1 88  ? 120.386 61.301  -24.895 1.00   68.42  ? 88  ASP A N   1 
ATOM   611   C CA  . ASP A  1 88  ? 119.830 61.945  -26.079 1.00   73.98  ? 88  ASP A CA  1 
ATOM   612   C C   . ASP A  1 88  ? 120.886 62.426  -27.024 1.00   75.41  ? 88  ASP A C   1 
ATOM   613   O O   . ASP A  1 88  ? 121.251 61.695  -27.939 1.00   83.72  ? 88  ASP A O   1 
ATOM   614   C CB  . ASP A  1 88  ? 118.903 63.093  -25.720 1.00   76.88  ? 88  ASP A CB  1 
ATOM   615   C CG  . ASP A  1 88  ? 117.591 62.611  -25.156 1.00   81.33  ? 88  ASP A CG  1 
ATOM   616   O OD1 . ASP A  1 88  ? 117.146 61.511  -25.552 1.00   82.32  ? 88  ASP A OD1 1 
ATOM   617   O OD2 . ASP A  1 88  ? 117.003 63.333  -24.324 1.00   83.38  ? 88  ASP A OD2 1 
ATOM   618   N N   . SER A  1 89  ? 121.353 63.652  -26.855 1.00   69.56  ? 89  SER A N   1 
ATOM   619   C CA  . SER A  1 89  ? 122.361 64.142  -27.773 1.00   70.88  ? 89  SER A CA  1 
ATOM   620   C C   . SER A  1 89  ? 123.583 63.219  -27.578 1.00   73.22  ? 89  SER A C   1 
ATOM   621   O O   . SER A  1 89  ? 123.707 62.574  -26.531 1.00   69.67  ? 89  SER A O   1 
ATOM   622   C CB  . SER A  1 89  ? 122.658 65.631  -27.496 1.00   67.09  ? 89  SER A CB  1 
ATOM   623   O OG  . SER A  1 89  ? 123.871 66.124  -28.044 1.00   67.37  ? 89  SER A OG  1 
ATOM   624   N N   . THR A  1 90  ? 124.463 63.132  -28.582 1.00   76.88  ? 90  THR A N   1 
ATOM   625   C CA  . THR A  1 90  ? 125.732 62.400  -28.453 1.00   74.83  ? 90  THR A CA  1 
ATOM   626   C C   . THR A  1 90  ? 126.864 63.416  -28.299 1.00   71.36  ? 90  THR A C   1 
ATOM   627   O O   . THR A  1 90  ? 128.051 63.067  -28.247 1.00   70.68  ? 90  THR A O   1 
ATOM   628   C CB  . THR A  1 90  ? 126.001 61.475  -29.671 1.00   73.07  ? 90  THR A CB  1 
ATOM   629   O OG1 . THR A  1 90  ? 125.934 62.235  -30.888 1.00   75.29  ? 90  THR A OG1 1 
ATOM   630   C CG2 . THR A  1 90  ? 124.974 60.369  -29.741 1.00   73.41  ? 90  THR A CG2 1 
ATOM   631   N N   . THR A  1 91  ? 126.455 64.679  -28.208 1.00   69.85  ? 91  THR A N   1 
ATOM   632   C CA  . THR A  1 91  ? 127.324 65.775  -27.837 1.00   69.16  ? 91  THR A CA  1 
ATOM   633   C C   . THR A  1 91  ? 126.738 66.436  -26.592 1.00   64.62  ? 91  THR A C   1 
ATOM   634   O O   . THR A  1 91  ? 125.550 66.290  -26.300 1.00   63.14  ? 91  THR A O   1 
ATOM   635   C CB  . THR A  1 91  ? 127.473 66.822  -28.996 1.00   64.01  ? 91  THR A CB  1 
ATOM   636   O OG1 . THR A  1 91  ? 126.182 67.294  -29.429 1.00   61.25  ? 91  THR A OG1 1 
ATOM   637   C CG2 . THR A  1 91  ? 128.263 66.237  -30.155 1.00   58.25  ? 91  THR A CG2 1 
ATOM   638   N N   . THR A  1 92  ? 127.569 67.141  -25.838 1.00   62.14  ? 92  THR A N   1 
ATOM   639   C CA  . THR A  1 92  ? 127.076 67.787  -24.633 1.00   58.81  ? 92  THR A CA  1 
ATOM   640   C C   . THR A  1 92  ? 126.498 69.161  -24.979 1.00   58.60  ? 92  THR A C   1 
ATOM   641   O O   . THR A  1 92  ? 126.908 69.816  -25.943 1.00   58.01  ? 92  THR A O   1 
ATOM   642   C CB  . THR A  1 92  ? 128.161 67.912  -23.552 1.00   55.41  ? 92  THR A CB  1 
ATOM   643   O OG1 . THR A  1 92  ? 129.172 68.811  -24.011 1.00   55.63  ? 92  THR A OG1 1 
ATOM   644   C CG2 . THR A  1 92  ? 128.789 66.553  -23.255 1.00   55.23  ? 92  THR A CG2 1 
ATOM   645   N N   . ARG A  1 93  ? 125.535 69.573  -24.168 1.00   56.88  ? 93  ARG A N   1 
ATOM   646   C CA  . ARG A  1 93  ? 124.824 70.825  -24.337 1.00   57.91  ? 93  ARG A CA  1 
ATOM   647   C C   . ARG A  1 93  ? 124.139 71.015  -22.996 1.00   52.29  ? 93  ARG A C   1 
ATOM   648   O O   . ARG A  1 93  ? 124.163 70.091  -22.173 1.00   50.13  ? 93  ARG A O   1 
ATOM   649   C CB  . ARG A  1 93  ? 123.842 70.740  -25.509 1.00   65.56  ? 93  ARG A CB  1 
ATOM   650   C CG  . ARG A  1 93  ? 122.829 69.644  -25.348 1.00   71.50  ? 93  ARG A CG  1 
ATOM   651   C CD  . ARG A  1 93  ? 122.124 69.298  -26.638 1.00   81.12  ? 93  ARG A CD  1 
ATOM   652   N NE  . ARG A  1 93  ? 121.069 68.312  -26.386 1.00   87.10  ? 93  ARG A NE  1 
ATOM   653   C CZ  . ARG A  1 93  ? 120.334 67.717  -27.329 1.00   92.34  ? 93  ARG A CZ  1 
ATOM   654   N NH1 . ARG A  1 93  ? 120.574 67.942  -28.620 1.00   94.54  ? 93  ARG A NH1 1 
ATOM   655   N NH2 . ARG A  1 93  ? 119.396 66.840  -26.980 1.00   92.83  ? 93  ARG A NH2 1 
ATOM   656   N N   . PRO A  1 94  ? 123.597 72.215  -22.722 1.00   46.80  ? 94  PRO A N   1 
ATOM   657   C CA  . PRO A  1 94  ? 122.843 72.353  -21.476 1.00   41.31  ? 94  PRO A CA  1 
ATOM   658   C C   . PRO A  1 94  ? 121.741 71.326  -21.396 1.00   39.97  ? 94  PRO A C   1 
ATOM   659   O O   . PRO A  1 94  ? 120.997 71.131  -22.347 1.00   40.51  ? 94  PRO A O   1 
ATOM   660   C CB  . PRO A  1 94  ? 122.307 73.773  -21.539 1.00   37.42  ? 94  PRO A CB  1 
ATOM   661   C CG  . PRO A  1 94  ? 123.317 74.485  -22.347 1.00   39.78  ? 94  PRO A CG  1 
ATOM   662   C CD  . PRO A  1 94  ? 123.747 73.507  -23.404 1.00   46.00  ? 94  PRO A CD  1 
ATOM   663   N N   . GLY A  1 95  ? 121.709 70.617  -20.278 1.00   39.22  ? 95  GLY A N   1 
ATOM   664   C CA  . GLY A  1 95  ? 120.724 69.581  -20.058 1.00   40.59  ? 95  GLY A CA  1 
ATOM   665   C C   . GLY A  1 95  ? 121.250 68.225  -20.463 1.00   43.53  ? 95  GLY A C   1 
ATOM   666   O O   . GLY A  1 95  ? 120.635 67.204  -20.151 1.00   45.39  ? 95  GLY A O   1 
ATOM   667   N N   . CYS A  1 96  ? 122.396 68.215  -21.139 1.00   44.06  ? 96  CYS A N   1 
ATOM   668   C CA  . CYS A  1 96  ? 122.987 66.977  -21.625 1.00   46.02  ? 96  CYS A CA  1 
ATOM   669   C C   . CYS A  1 96  ? 124.504 66.889  -21.352 1.00   44.09  ? 96  CYS A C   1 
ATOM   670   O O   . CYS A  1 96  ? 125.328 67.384  -22.124 1.00   42.35  ? 96  CYS A O   1 
ATOM   671   C CB  . CYS A  1 96  ? 122.693 66.824  -23.127 1.00   50.33  ? 96  CYS A CB  1 
ATOM   672   S SG  . CYS A  1 96  ? 123.422 65.377  -23.917 1.00   76.64  ? 96  CYS A SG  1 
ATOM   673   N N   . HIS A  1 97  ? 124.849 66.255  -20.232 1.00   43.27  ? 97  HIS A N   1 
ATOM   674   C CA  . HIS A  1 97  ? 126.231 65.921  -19.892 1.00   44.70  ? 97  HIS A CA  1 
ATOM   675   C C   . HIS A  1 97  ? 126.285 64.516  -19.255 1.00   45.56  ? 97  HIS A C   1 
ATOM   676   O O   . HIS A  1 97  ? 125.234 63.943  -18.953 1.00   46.94  ? 97  HIS A O   1 
ATOM   677   C CB  . HIS A  1 97  ? 126.830 66.952  -18.921 1.00   44.02  ? 97  HIS A CB  1 
ATOM   678   C CG  . HIS A  1 97  ? 126.650 68.387  -19.330 1.00   45.78  ? 97  HIS A CG  1 
ATOM   679   N ND1 . HIS A  1 97  ? 125.500 69.099  -19.062 1.00   45.15  ? 97  HIS A ND1 1 
ATOM   680   C CD2 . HIS A  1 97  ? 127.499 69.258  -19.930 1.00   47.38  ? 97  HIS A CD2 1 
ATOM   681   C CE1 . HIS A  1 97  ? 125.636 70.336  -19.509 1.00   45.80  ? 97  HIS A CE1 1 
ATOM   682   N NE2 . HIS A  1 97  ? 126.839 70.458  -20.041 1.00   47.48  ? 97  HIS A NE2 1 
ATOM   683   N N   . ASN A  1 98  ? 127.494 63.979  -19.039 1.00   45.17  ? 98  ASN A N   1 
ATOM   684   C CA  . ASN A  1 98  ? 127.695 62.771  -18.238 1.00   49.21  ? 98  ASN A CA  1 
ATOM   685   C C   . ASN A  1 98  ? 128.325 63.142  -16.895 1.00   44.93  ? 98  ASN A C   1 
ATOM   686   O O   . ASN A  1 98  ? 128.876 64.244  -16.733 1.00   43.53  ? 98  ASN A O   1 
ATOM   687   C CB  . ASN A  1 98  ? 128.556 61.731  -18.970 1.00   61.41  ? 98  ASN A CB  1 
ATOM   688   C CG  . ASN A  1 98  ? 127.766 60.917  -19.991 1.00   73.94  ? 98  ASN A CG  1 
ATOM   689   O OD1 . ASN A  1 98  ? 126.552 60.793  -19.894 1.00   74.73  ? 98  ASN A OD1 1 
ATOM   690   N ND2 . ASN A  1 98  ? 128.463 60.366  -20.983 1.00   85.86  ? 98  ASN A ND2 1 
ATOM   691   N N   . ASN A  1 99  ? 128.150 62.260  -15.914 1.00   41.26  ? 99  ASN A N   1 
ATOM   692   C CA  . ASN A  1 99  ? 128.649 62.498  -14.572 1.00   39.88  ? 99  ASN A CA  1 
ATOM   693   C C   . ASN A  1 99  ? 128.088 63.748  -13.949 1.00   35.55  ? 99  ASN A C   1 
ATOM   694   O O   . ASN A  1 99  ? 128.772 64.413  -13.179 1.00   33.82  ? 99  ASN A O   1 
ATOM   695   C CB  . ASN A  1 99  ? 130.174 62.589  -14.582 1.00   49.80  ? 99  ASN A CB  1 
ATOM   696   C CG  . ASN A  1 99  ? 130.823 61.402  -15.271 1.00   61.11  ? 99  ASN A CG  1 
ATOM   697   O OD1 . ASN A  1 99  ? 130.549 60.257  -14.923 1.00   65.75  ? 99  ASN A OD1 1 
ATOM   698   N ND2 . ASN A  1 99  ? 131.660 61.672  -16.285 1.00   63.65  ? 99  ASN A ND2 1 
ATOM   699   N N   . THR A  1 100 ? 126.841 64.069  -14.280 1.00   35.12  ? 100 THR A N   1 
ATOM   700   C CA  . THR A  1 100 ? 126.124 65.142  -13.603 1.00   31.82  ? 100 THR A CA  1 
ATOM   701   C C   . THR A  1 100 ? 125.107 64.497  -12.669 1.00   30.96  ? 100 THR A C   1 
ATOM   702   O O   . THR A  1 100 ? 125.207 63.299  -12.427 1.00   29.94  ? 100 THR A O   1 
ATOM   703   C CB  . THR A  1 100 ? 125.440 66.092  -14.611 1.00   33.46  ? 100 THR A CB  1 
ATOM   704   O OG1 . THR A  1 100 ? 124.873 65.334  -15.679 1.00   29.24  ? 100 THR A OG1 1 
ATOM   705   C CG2 . THR A  1 100 ? 126.451 66.994  -15.223 1.00   34.17  ? 100 THR A CG2 1 
ATOM   706   N N   . CYS A  1 101 ? 124.146 65.260  -12.128 1.00   32.35  ? 101 CYS A N   1 
ATOM   707   C CA  . CYS A  1 101 ? 123.103 64.625  -11.308 1.00   32.69  ? 101 CYS A CA  1 
ATOM   708   C C   . CYS A  1 101 ? 121.707 64.841  -11.848 1.00   30.76  ? 101 CYS A C   1 
ATOM   709   O O   . CYS A  1 101 ? 121.382 65.864  -12.464 1.00   28.79  ? 101 CYS A O   1 
ATOM   710   C CB  A CYS A  1 101 ? 123.178 65.060  -9.834  0.50   30.01  ? 101 CYS A CB  1 
ATOM   711   C CB  B CYS A  1 101 ? 123.123 65.156  -9.881  0.50   29.94  ? 101 CYS A CB  1 
ATOM   712   S SG  A CYS A  1 101 ? 123.420 66.780  -9.474  0.50   37.50  ? 101 CYS A SG  1 
ATOM   713   S SG  B CYS A  1 101 ? 124.705 65.691  -9.363  0.50   37.44  ? 101 CYS A SG  1 
ATOM   714   N N   . GLY A  1 102 ? 120.899 63.820  -11.593 1.00   32.80  ? 102 GLY A N   1 
ATOM   715   C CA  . GLY A  1 102 ? 119.556 63.707  -12.116 1.00   38.56  ? 102 GLY A CA  1 
ATOM   716   C C   . GLY A  1 102 ? 118.513 64.182  -11.133 1.00   39.88  ? 102 GLY A C   1 
ATOM   717   O O   . GLY A  1 102 ? 118.652 64.004  -9.923  1.00   39.03  ? 102 GLY A O   1 
ATOM   718   N N   . LEU A  1 103 ? 117.480 64.817  -11.671 1.00   41.67  ? 103 LEU A N   1 
ATOM   719   C CA  . LEU A  1 103 ? 116.423 65.413  -10.882 1.00   41.47  ? 103 LEU A CA  1 
ATOM   720   C C   . LEU A  1 103 ? 115.109 65.102  -11.579 1.00   39.96  ? 103 LEU A C   1 
ATOM   721   O O   . LEU A  1 103 ? 114.965 65.362  -12.769 1.00   41.82  ? 103 LEU A O   1 
ATOM   722   C CB  . LEU A  1 103 ? 116.640 66.919  -10.775 1.00   43.98  ? 103 LEU A CB  1 
ATOM   723   C CG  . LEU A  1 103 ? 115.972 67.756  -9.691  1.00   46.22  ? 103 LEU A CG  1 
ATOM   724   C CD1 . LEU A  1 103 ? 116.241 67.182  -8.309  1.00   48.20  ? 103 LEU A CD1 1 
ATOM   725   C CD2 . LEU A  1 103 ? 116.453 69.178  -9.780  1.00   45.84  ? 103 LEU A CD2 1 
ATOM   726   N N   . LEU A  1 104 ? 114.157 64.532  -10.864 1.00   35.49  ? 104 LEU A N   1 
ATOM   727   C CA  . LEU A  1 104 ? 112.849 64.265  -11.446 1.00   36.97  ? 104 LEU A CA  1 
ATOM   728   C C   . LEU A  1 104 ? 111.930 65.471  -11.428 1.00   31.56  ? 104 LEU A C   1 
ATOM   729   O O   . LEU A  1 104 ? 111.594 65.967  -10.368 1.00   29.50  ? 104 LEU A O   1 
ATOM   730   C CB  . LEU A  1 104 ? 112.179 63.140  -10.691 1.00   41.33  ? 104 LEU A CB  1 
ATOM   731   C CG  . LEU A  1 104 ? 110.999 62.483  -11.365 1.00   44.36  ? 104 LEU A CG  1 
ATOM   732   C CD1 . LEU A  1 104 ? 111.411 61.731  -12.606 1.00   47.22  ? 104 LEU A CD1 1 
ATOM   733   C CD2 . LEU A  1 104 ? 110.409 61.580  -10.324 1.00   47.11  ? 104 LEU A CD2 1 
ATOM   734   N N   . SER A  1 105 ? 111.506 65.908  -12.605 1.00   30.75  ? 105 SER A N   1 
ATOM   735   C CA  . SER A  1 105 ? 110.623 67.061  -12.742 1.00   29.65  ? 105 SER A CA  1 
ATOM   736   C C   . SER A  1 105 ? 109.238 66.624  -13.183 1.00   35.07  ? 105 SER A C   1 
ATOM   737   O O   . SER A  1 105 ? 109.098 65.657  -13.916 1.00   36.29  ? 105 SER A O   1 
ATOM   738   C CB  . SER A  1 105 ? 111.195 68.068  -13.749 1.00   29.83  ? 105 SER A CB  1 
ATOM   739   O OG  . SER A  1 105 ? 112.473 68.547  -13.370 1.00   28.56  ? 105 SER A OG  1 
ATOM   740   N N   . SER A  1 106 ? 108.208 67.329  -12.727 1.00   42.60  ? 106 SER A N   1 
ATOM   741   C CA  . SER A  1 106 ? 106.828 66.993  -13.093 1.00   47.66  ? 106 SER A CA  1 
ATOM   742   C C   . SER A  1 106 ? 106.005 68.110  -13.741 1.00   41.72  ? 106 SER A C   1 
ATOM   743   O O   . SER A  1 106 ? 106.012 69.252  -13.291 1.00   37.65  ? 106 SER A O   1 
ATOM   744   C CB  . SER A  1 106 ? 106.073 66.483  -11.867 1.00   54.91  ? 106 SER A CB  1 
ATOM   745   O OG  . SER A  1 106 ? 106.408 65.132  -11.607 1.00   60.40  ? 106 SER A OG  1 
ATOM   746   N N   . ASN A  1 107 ? 105.276 67.738  -14.785 1.00   41.99  ? 107 ASN A N   1 
ATOM   747   C CA  . ASN A  1 107 ? 104.215 68.573  -15.336 1.00   41.54  ? 107 ASN A CA  1 
ATOM   748   C C   . ASN A  1 107 ? 102.978 68.388  -14.487 1.00   38.71  ? 107 ASN A C   1 
ATOM   749   O O   . ASN A  1 107 ? 102.348 67.341  -14.547 1.00   37.81  ? 107 ASN A O   1 
ATOM   750   C CB  . ASN A  1 107 ? 103.933 68.176  -16.780 1.00   44.20  ? 107 ASN A CB  1 
ATOM   751   C CG  . ASN A  1 107 ? 102.829 68.994  -17.418 1.00   46.60  ? 107 ASN A CG  1 
ATOM   752   O OD1 . ASN A  1 107 ? 101.854 69.368  -16.772 1.00   45.23  ? 107 ASN A OD1 1 
ATOM   753   N ND2 . ASN A  1 107 ? 102.976 69.265  -18.712 1.00   49.14  ? 107 ASN A ND2 1 
ATOM   754   N N   . PRO A  1 108 ? 102.611 69.411  -13.704 1.00   37.27  ? 108 PRO A N   1 
ATOM   755   C CA  . PRO A  1 108 ? 101.563 69.232  -12.689 1.00   36.74  ? 108 PRO A CA  1 
ATOM   756   C C   . PRO A  1 108 ? 100.180 69.153  -13.302 1.00   41.96  ? 108 PRO A C   1 
ATOM   757   O O   . PRO A  1 108 ? 99.211  68.707  -12.675 1.00   45.35  ? 108 PRO A O   1 
ATOM   758   C CB  . PRO A  1 108 ? 101.727 70.473  -11.813 1.00   34.65  ? 108 PRO A CB  1 
ATOM   759   C CG  . PRO A  1 108 ? 102.272 71.514  -12.742 1.00   33.29  ? 108 PRO A CG  1 
ATOM   760   C CD  . PRO A  1 108 ? 103.173 70.777  -13.690 1.00   34.36  ? 108 PRO A CD  1 
ATOM   761   N N   . VAL A  1 109 ? 100.106 69.585  -14.553 1.00   41.60  ? 109 VAL A N   1 
ATOM   762   C CA  . VAL A  1 109 ? 98.871  69.566  -15.301 1.00   41.59  ? 109 VAL A CA  1 
ATOM   763   C C   . VAL A  1 109 ? 98.616  68.198  -15.888 1.00   44.74  ? 109 VAL A C   1 
ATOM   764   O O   . VAL A  1 109 ? 97.553  67.618  -15.674 1.00   48.39  ? 109 VAL A O   1 
ATOM   765   C CB  . VAL A  1 109 ? 98.899  70.621  -16.425 1.00   41.66  ? 109 VAL A CB  1 
ATOM   766   C CG1 . VAL A  1 109 ? 97.765  70.395  -17.399 1.00   44.40  ? 109 VAL A CG1 1 
ATOM   767   C CG2 . VAL A  1 109 ? 98.897  72.047  -15.829 1.00   36.01  ? 109 VAL A CG2 1 
ATOM   768   N N   . THR A  1 110 ? 99.589  67.660  -16.608 1.00   44.61  ? 110 THR A N   1 
ATOM   769   C CA  . THR A  1 110 ? 99.372  66.372  -17.235 1.00   48.01  ? 110 THR A CA  1 
ATOM   770   C C   . THR A  1 110 ? 99.784  65.274  -16.299 1.00   49.47  ? 110 THR A C   1 
ATOM   771   O O   . THR A  1 110 ? 99.402  64.126  -16.496 1.00   55.00  ? 110 THR A O   1 
ATOM   772   C CB  . THR A  1 110 ? 100.167 66.211  -18.557 1.00   46.78  ? 110 THR A CB  1 
ATOM   773   O OG1 . THR A  1 110 ? 101.578 66.186  -18.285 1.00   47.07  ? 110 THR A OG1 1 
ATOM   774   C CG2 . THR A  1 110 ? 99.885  67.348  -19.486 1.00   47.80  ? 110 THR A CG2 1 
ATOM   775   N N   . GLN A  1 111 ? 100.557 65.637  -15.282 1.00   46.75  ? 111 GLN A N   1 
ATOM   776   C CA  . GLN A  1 111 ? 101.122 64.669  -14.344 1.00   49.91  ? 111 GLN A CA  1 
ATOM   777   C C   . GLN A  1 111 ? 102.124 63.713  -14.997 1.00   50.54  ? 111 GLN A C   1 
ATOM   778   O O   . GLN A  1 111 ? 102.458 62.675  -14.429 1.00   50.54  ? 111 GLN A O   1 
ATOM   779   C CB  . GLN A  1 111 ? 100.023 63.935  -13.610 1.00   56.29  ? 111 GLN A CB  1 
ATOM   780   C CG  . GLN A  1 111 ? 99.442  64.834  -12.554 1.00   62.92  ? 111 GLN A CG  1 
ATOM   781   C CD  . GLN A  1 111 ? 98.162  64.309  -12.008 1.00   73.23  ? 111 GLN A CD  1 
ATOM   782   O OE1 . GLN A  1 111 ? 98.170  63.528  -11.059 1.00   78.33  ? 111 GLN A OE1 1 
ATOM   783   N NE2 . GLN A  1 111 ? 97.037  64.743  -12.583 1.00   76.27  ? 111 GLN A NE2 1 
ATOM   784   N N   . GLU A  1 112 ? 102.560 64.053  -16.211 1.00   50.61  ? 112 GLU A N   1 
ATOM   785   C CA  . GLU A  1 112 ? 103.744 63.454  -16.811 1.00   49.09  ? 112 GLU A CA  1 
ATOM   786   C C   . GLU A  1 112 ? 104.939 63.891  -15.976 1.00   46.10  ? 112 GLU A C   1 
ATOM   787   O O   . GLU A  1 112 ? 104.952 64.999  -15.429 1.00   43.35  ? 112 GLU A O   1 
ATOM   788   C CB  . GLU A  1 112 ? 103.983 63.932  -18.241 1.00   52.20  ? 112 GLU A CB  1 
ATOM   789   C CG  . GLU A  1 112 ? 103.123 63.396  -19.340 1.00   59.18  ? 112 GLU A CG  1 
ATOM   790   C CD  . GLU A  1 112 ? 103.305 64.235  -20.591 1.00   65.78  ? 112 GLU A CD  1 
ATOM   791   O OE1 . GLU A  1 112 ? 103.358 63.667  -21.706 1.00   69.80  ? 112 GLU A OE1 1 
ATOM   792   O OE2 . GLU A  1 112 ? 103.457 65.471  -20.444 1.00   66.56  1 112 GLU A OE2 1 
ATOM   793   N N   . SER A  1 113 ? 105.961 63.050  -15.904 1.00   46.84  ? 113 SER A N   1 
ATOM   794   C CA  . SER A  1 113 ? 107.225 63.474  -15.314 1.00   49.39  ? 113 SER A CA  1 
ATOM   795   C C   . SER A  1 113 ? 108.452 63.073  -16.164 1.00   48.14  ? 113 SER A C   1 
ATOM   796   O O   . SER A  1 113 ? 108.351 62.261  -17.076 1.00   51.33  ? 113 SER A O   1 
ATOM   797   C CB  . SER A  1 113 ? 107.335 62.946  -13.877 1.00   53.67  ? 113 SER A CB  1 
ATOM   798   O OG  . SER A  1 113 ? 107.354 61.538  -13.842 1.00   57.92  ? 113 SER A OG  1 
ATOM   799   N N   . GLY A  1 114 ? 109.593 63.713  -15.911 1.00   44.99  ? 114 GLY A N   1 
ATOM   800   C CA  . GLY A  1 114 ? 110.808 63.429  -16.660 1.00   44.22  ? 114 GLY A CA  1 
ATOM   801   C C   . GLY A  1 114 ? 112.101 63.682  -15.892 1.00   40.03  ? 114 GLY A C   1 
ATOM   802   O O   . GLY A  1 114 ? 112.144 64.517  -15.001 1.00   37.61  ? 114 GLY A O   1 
ATOM   803   N N   . LEU A  1 115 ? 113.167 62.971  -16.253 1.00   42.75  ? 115 LEU A N   1 
ATOM   804   C CA  . LEU A  1 115 ? 114.441 63.133  -15.559 1.00   41.85  ? 115 LEU A CA  1 
ATOM   805   C C   . LEU A  1 115 ? 115.251 64.281  -16.154 1.00   37.20  ? 115 LEU A C   1 
ATOM   806   O O   . LEU A  1 115 ? 115.688 64.226  -17.304 1.00   39.40  ? 115 LEU A O   1 
ATOM   807   C CB  . LEU A  1 115 ? 115.276 61.839  -15.594 1.00   42.94  ? 115 LEU A CB  1 
ATOM   808   C CG  . LEU A  1 115 ? 116.437 61.916  -14.580 1.00   45.36  ? 115 LEU A CG  1 
ATOM   809   C CD1 . LEU A  1 115 ? 115.990 61.598  -13.153 1.00   44.41  ? 115 LEU A CD1 1 
ATOM   810   C CD2 . LEU A  1 115 ? 117.632 61.071  -14.960 1.00   51.97  ? 115 LEU A CD2 1 
ATOM   811   N N   . GLY A  1 116 ? 115.468 65.312  -15.353 1.00   33.86  ? 116 GLY A N   1 
ATOM   812   C CA  . GLY A  1 116 ? 116.282 66.420  -15.797 1.00   35.70  ? 116 GLY A CA  1 
ATOM   813   C C   . GLY A  1 116 ? 117.678 66.396  -15.202 1.00   36.13  ? 116 GLY A C   1 
ATOM   814   O O   . GLY A  1 116 ? 118.027 65.545  -14.383 1.00   39.12  ? 116 GLY A O   1 
ATOM   815   N N   . GLU A  1 117 ? 118.481 67.355  -15.609 1.00   33.01  ? 117 GLU A N   1 
ATOM   816   C CA  . GLU A  1 117 ? 119.830 67.445  -15.129 1.00   33.68  ? 117 GLU A CA  1 
ATOM   817   C C   . GLU A  1 117 ? 119.877 68.659  -14.242 1.00   31.74  ? 117 GLU A C   1 
ATOM   818   O O   . GLU A  1 117 ? 119.297 69.681  -14.600 1.00   30.96  ? 117 GLU A O   1 
ATOM   819   C CB  . GLU A  1 117 ? 120.793 67.557  -16.290 1.00   36.13  ? 117 GLU A CB  1 
ATOM   820   C CG  . GLU A  1 117 ? 122.242 67.469  -15.905 1.00   38.78  ? 117 GLU A CG  1 
ATOM   821   C CD  . GLU A  1 117 ? 123.142 67.727  -17.102 1.00   42.32  ? 117 GLU A CD  1 
ATOM   822   O OE1 . GLU A  1 117 ? 122.946 68.755  -17.786 1.00   41.81  ? 117 GLU A OE1 1 
ATOM   823   O OE2 . GLU A  1 117 ? 124.039 66.901  -17.351 1.00   43.12  1 117 GLU A OE2 1 
ATOM   824   N N   . LEU A  1 118 ? 120.500 68.545  -13.073 1.00   27.74  ? 118 LEU A N   1 
ATOM   825   C CA  . LEU A  1 118 ? 120.619 69.702  -12.199 1.00   27.63  ? 118 LEU A CA  1 
ATOM   826   C C   . LEU A  1 118 ? 121.438 70.779  -12.924 1.00   28.93  ? 118 LEU A C   1 
ATOM   827   O O   . LEU A  1 118 ? 122.408 70.475  -13.588 1.00   30.92  ? 118 LEU A O   1 
ATOM   828   C CB  . LEU A  1 118 ? 121.241 69.321  -10.849 1.00   23.51  ? 118 LEU A CB  1 
ATOM   829   C CG  . LEU A  1 118 ? 121.244 70.377  -9.745  1.00   22.53  ? 118 LEU A CG  1 
ATOM   830   C CD1 . LEU A  1 118 ? 119.846 70.750  -9.289  1.00   21.48  ? 118 LEU A CD1 1 
ATOM   831   C CD2 . LEU A  1 118 ? 122.031 69.903  -8.568  1.00   22.88  ? 118 LEU A CD2 1 
ATOM   832   N N   . ALA A  1 119 ? 121.002 72.030  -12.816 1.00   29.57  ? 119 ALA A N   1 
ATOM   833   C CA  . ALA A  1 119 ? 121.638 73.122  -13.502 1.00   24.56  ? 119 ALA A CA  1 
ATOM   834   C C   . ALA A  1 119 ? 121.855 74.257  -12.529 1.00   28.76  ? 119 ALA A C   1 
ATOM   835   O O   . ALA A  1 119 ? 121.248 74.321  -11.480 1.00   27.55  ? 119 ALA A O   1 
ATOM   836   C CB  . ALA A  1 119 ? 120.797 73.569  -14.679 1.00   25.73  ? 119 ALA A CB  1 
ATOM   837   N N   . GLN A  1 120 ? 122.749 75.156  -12.879 1.00   32.15  ? 120 GLN A N   1 
ATOM   838   C CA  . GLN A  1 120 ? 123.034 76.291  -12.032 1.00   31.16  ? 120 GLN A CA  1 
ATOM   839   C C   . GLN A  1 120 ? 123.208 77.483  -12.940 1.00   32.89  ? 120 GLN A C   1 
ATOM   840   O O   . GLN A  1 120 ? 123.843 77.371  -13.988 1.00   33.54  ? 120 GLN A O   1 
ATOM   841   C CB  . GLN A  1 120 ? 124.281 76.041  -11.195 1.00   33.30  ? 120 GLN A CB  1 
ATOM   842   C CG  . GLN A  1 120 ? 124.677 77.160  -10.293 1.00   34.97  ? 120 GLN A CG  1 
ATOM   843   C CD  . GLN A  1 120 ? 126.003 76.905  -9.627  1.00   39.31  ? 120 GLN A CD  1 
ATOM   844   O OE1 . GLN A  1 120 ? 126.124 76.088  -8.717  1.00   39.17  ? 120 GLN A OE1 1 
ATOM   845   N NE2 . GLN A  1 120 ? 127.023 77.578  -10.108 1.00   43.40  ? 120 GLN A NE2 1 
ATOM   846   N N   . ASP A  1 121 ? 122.571 78.600  -12.598 1.00   32.96  ? 121 ASP A N   1 
ATOM   847   C CA  . ASP A  1 121 ? 122.706 79.821  -13.388 1.00   31.32  ? 121 ASP A CA  1 
ATOM   848   C C   . ASP A  1 121 ? 122.230 81.034  -12.616 1.00   29.82  ? 121 ASP A C   1 
ATOM   849   O O   . ASP A  1 121 ? 121.852 80.925  -11.453 1.00   32.44  ? 121 ASP A O   1 
ATOM   850   C CB  . ASP A  1 121 ? 121.946 79.692  -14.705 1.00   31.41  ? 121 ASP A CB  1 
ATOM   851   C CG  . ASP A  1 121 ? 122.527 80.541  -15.800 1.00   34.91  ? 121 ASP A CG  1 
ATOM   852   O OD1 . ASP A  1 121 ? 123.154 81.589  -15.513 1.00   36.09  ? 121 ASP A OD1 1 
ATOM   853   O OD2 . ASP A  1 121 ? 122.336 80.168  -16.970 1.00   38.38  1 121 ASP A OD2 1 
ATOM   854   N N   . VAL A  1 122 ? 122.281 82.196  -13.253 1.00   30.44  ? 122 VAL A N   1 
ATOM   855   C CA  . VAL A  1 122 ? 121.739 83.416  -12.661 1.00   33.72  ? 122 VAL A CA  1 
ATOM   856   C C   . VAL A  1 122 ? 120.204 83.498  -12.690 1.00   35.21  ? 122 VAL A C   1 
ATOM   857   O O   . VAL A  1 122 ? 119.599 83.267  -13.721 1.00   36.06  ? 122 VAL A O   1 
ATOM   858   C CB  . VAL A  1 122 ? 122.303 84.642  -13.382 1.00   37.97  ? 122 VAL A CB  1 
ATOM   859   C CG1 . VAL A  1 122 ? 121.618 85.913  -12.899 1.00   37.63  ? 122 VAL A CG1 1 
ATOM   860   C CG2 . VAL A  1 122 ? 123.792 84.719  -13.154 1.00   39.69  ? 122 VAL A CG2 1 
ATOM   861   N N   . LEU A  1 123 ? 119.584 83.828  -11.557 1.00   34.15  ? 123 LEU A N   1 
ATOM   862   C CA  . LEU A  1 123 ? 118.194 84.272  -11.528 1.00   32.19  ? 123 LEU A CA  1 
ATOM   863   C C   . LEU A  1 123 ? 118.106 85.694  -10.966 1.00   34.37  ? 123 LEU A C   1 
ATOM   864   O O   . LEU A  1 123 ? 118.786 86.031  -10.000 1.00   35.81  ? 123 LEU A O   1 
ATOM   865   C CB  . LEU A  1 123 ? 117.325 83.330  -10.693 1.00   28.95  ? 123 LEU A CB  1 
ATOM   866   C CG  . LEU A  1 123 ? 115.847 83.712  -10.463 1.00   29.86  ? 123 LEU A CG  1 
ATOM   867   C CD1 . LEU A  1 123 ? 114.949 82.498  -10.450 1.00   27.05  ? 123 LEU A CD1 1 
ATOM   868   C CD2 . LEU A  1 123 ? 115.638 84.483  -9.156  1.00   28.51  ? 123 LEU A CD2 1 
ATOM   869   N N   . ALA A  1 124 ? 117.260 86.523  -11.567 1.00   32.18  ? 124 ALA A N   1 
ATOM   870   C CA  . ALA A  1 124 ? 117.031 87.864  -11.066 1.00   29.82  ? 124 ALA A CA  1 
ATOM   871   C C   . ALA A  1 124 ? 115.558 88.095  -10.755 1.00   32.74  ? 124 ALA A C   1 
ATOM   872   O O   . ALA A  1 124 ? 114.668 87.519  -11.397 1.00   33.44  ? 124 ALA A O   1 
ATOM   873   C CB  . ALA A  1 124 ? 117.529 88.896  -12.066 1.00   30.11  ? 124 ALA A CB  1 
ATOM   874   N N   . ILE A  1 125 ? 115.325 88.972  -9.781  1.00   33.42  ? 125 ILE A N   1 
ATOM   875   C CA  . ILE A  1 125 ? 113.996 89.311  -9.285  1.00   33.80  ? 125 ILE A CA  1 
ATOM   876   C C   . ILE A  1 125 ? 113.989 90.755  -8.740  1.00   33.74  ? 125 ILE A C   1 
ATOM   877   O O   . ILE A  1 125 ? 115.016 91.250  -8.269  1.00   37.56  ? 125 ILE A O   1 
ATOM   878   C CB  . ILE A  1 125 ? 113.561 88.324  -8.182  1.00   31.07  ? 125 ILE A CB  1 
ATOM   879   C CG1 . ILE A  1 125 ? 112.084 88.525  -7.810  1.00   29.44  ? 125 ILE A CG1 1 
ATOM   880   C CG2 . ILE A  1 125 ? 114.498 88.429  -6.970  1.00   30.86  ? 125 ILE A CG2 1 
ATOM   881   C CD1 . ILE A  1 125 ? 111.557 87.549  -6.793  1.00   28.05  ? 125 ILE A CD1 1 
ATOM   882   N N   . HIS A  1 126 ? 112.848 91.429  -8.818  1.00   31.80  ? 126 HIS A N   1 
ATOM   883   C CA  . HIS A  1 126 ? 112.707 92.815  -8.363  1.00   34.07  ? 126 HIS A CA  1 
ATOM   884   C C   . HIS A  1 126 ? 112.826 93.021  -6.875  1.00   33.95  ? 126 HIS A C   1 
ATOM   885   O O   . HIS A  1 126 ? 112.197 92.326  -6.100  1.00   31.78  ? 126 HIS A O   1 
ATOM   886   C CB  . HIS A  1 126 ? 111.357 93.378  -8.780  1.00   37.13  ? 126 HIS A CB  1 
ATOM   887   C CG  . HIS A  1 126 ? 111.316 93.861  -10.189 1.00   41.46  ? 126 HIS A CG  1 
ATOM   888   N ND1 . HIS A  1 126 ? 110.611 93.213  -11.176 1.00   43.06  ? 126 HIS A ND1 1 
ATOM   889   C CD2 . HIS A  1 126 ? 111.899 94.930  -10.779 1.00   44.53  ? 126 HIS A CD2 1 
ATOM   890   C CE1 . HIS A  1 126 ? 110.759 93.862  -12.317 1.00   45.82  ? 126 HIS A CE1 1 
ATOM   891   N NE2 . HIS A  1 126 ? 111.537 94.906  -12.103 1.00   47.08  ? 126 HIS A NE2 1 
ATOM   892   N N   . SER A  1 127 ? 113.568 94.043  -6.481  1.00   36.21  ? 127 SER A N   1 
ATOM   893   C CA  . SER A  1 127 ? 113.481 94.515  -5.118  1.00   39.76  ? 127 SER A CA  1 
ATOM   894   C C   . SER A  1 127 ? 112.431 95.615  -5.078  1.00   44.74  ? 127 SER A C   1 
ATOM   895   O O   . SER A  1 127 ? 111.648 95.765  -6.010  1.00   45.39  ? 127 SER A O   1 
ATOM   896   C CB  . SER A  1 127 ? 114.831 95.022  -4.633  1.00   40.13  ? 127 SER A CB  1 
ATOM   897   O OG  . SER A  1 127 ? 115.321 95.992  -5.531  1.00   41.27  ? 127 SER A OG  1 
ATOM   898   N N   . THR A  1 128 ? 112.386 96.376  -3.995  1.00   45.51  ? 128 THR A N   1 
ATOM   899   C CA  . THR A  1 128 ? 111.501 97.521  -3.967  1.00   44.41  ? 128 THR A CA  1 
ATOM   900   C C   . THR A  1 128 ? 112.298 98.777  -3.696  1.00   47.09  ? 128 THR A C   1 
ATOM   901   O O   . THR A  1 128 ? 113.400 98.735  -3.158  1.00   47.44  ? 128 THR A O   1 
ATOM   902   C CB  . THR A  1 128 ? 110.402 97.397  -2.910  1.00   41.14  ? 128 THR A CB  1 
ATOM   903   O OG1 . THR A  1 128 ? 110.966 97.541  -1.603  1.00   43.36  ? 128 THR A OG1 1 
ATOM   904   C CG2 . THR A  1 128 ? 109.656 96.068  -3.046  1.00   33.78  ? 128 THR A CG2 1 
ATOM   905   N N   . HIS A  1 129 ? 111.743 99.893  -4.124  1.00   46.95  ? 129 HIS A N   1 
ATOM   906   C CA  . HIS A  1 129 ? 112.343 101.187 -3.898  1.00   49.12  ? 129 HIS A CA  1 
ATOM   907   C C   . HIS A  1 129 ? 111.248 102.148 -3.522  1.00   46.50  ? 129 HIS A C   1 
ATOM   908   O O   . HIS A  1 129 ? 110.541 102.628 -4.394  1.00   48.08  ? 129 HIS A O   1 
ATOM   909   C CB  . HIS A  1 129 ? 113.065 101.669 -5.151  1.00   57.04  ? 129 HIS A CB  1 
ATOM   910   C CG  . HIS A  1 129 ? 113.775 102.966 -4.963  1.00   66.99  ? 129 HIS A CG  1 
ATOM   911   N ND1 . HIS A  1 129 ? 114.743 103.150 -3.999  1.00   70.64  ? 129 HIS A ND1 1 
ATOM   912   C CD2 . HIS A  1 129 ? 113.629 104.161 -5.583  1.00   72.63  ? 129 HIS A CD2 1 
ATOM   913   C CE1 . HIS A  1 129 ? 115.175 104.399 -4.045  1.00   74.27  ? 129 HIS A CE1 1 
ATOM   914   N NE2 . HIS A  1 129 ? 114.515 105.033 -4.999  1.00   75.80  ? 129 HIS A NE2 1 
ATOM   915   N N   . GLY A  1 130 ? 111.100 102.448 -2.240  1.00   46.60  ? 130 GLY A N   1 
ATOM   916   C CA  . GLY A  1 130 ? 109.961 103.239 -1.802  1.00   49.20  ? 130 GLY A CA  1 
ATOM   917   C C   . GLY A  1 130 ? 108.630 102.534 -2.047  1.00   50.55  ? 130 GLY A C   1 
ATOM   918   O O   . GLY A  1 130 ? 108.457 101.398 -1.628  1.00   50.86  ? 130 GLY A O   1 
ATOM   919   N N   . SER A  1 131 ? 107.693 103.177 -2.739  1.00   52.90  ? 131 SER A N   1 
ATOM   920   C CA  . SER A  1 131 ? 106.399 102.543 -2.990  1.00   51.99  ? 131 SER A CA  1 
ATOM   921   C C   . SER A  1 131 ? 106.424 101.793 -4.300  1.00   51.26  ? 131 SER A C   1 
ATOM   922   O O   . SER A  1 131 ? 105.438 101.165 -4.670  1.00   52.91  ? 131 SER A O   1 
ATOM   923   C CB  . SER A  1 131 ? 105.247 103.579 -3.021  1.00   52.42  ? 131 SER A CB  1 
ATOM   924   O OG  . SER A  1 131 ? 105.198 104.330 -4.236  1.00   50.38  ? 131 SER A OG  1 
ATOM   925   N N   . LYS A  1 132 ? 107.557 101.842 -4.996  1.00   49.72  ? 132 LYS A N   1 
ATOM   926   C CA  . LYS A  1 132 ? 107.655 101.212 -6.307  1.00   47.15  ? 132 LYS A CA  1 
ATOM   927   C C   . LYS A  1 132 ? 108.531 99.992  -6.319  1.00   44.85  ? 132 LYS A C   1 
ATOM   928   O O   . LYS A  1 132 ? 109.233 99.692  -5.355  1.00   43.66  ? 132 LYS A O   1 
ATOM   929   C CB  . LYS A  1 132 ? 108.167 102.190 -7.373  1.00   47.92  ? 132 LYS A CB  1 
ATOM   930   C CG  . LYS A  1 132 ? 107.179 103.202 -7.877  1.00   52.41  ? 132 LYS A CG  1 
ATOM   931   C CD  . LYS A  1 132 ? 107.394 103.326 -9.385  1.00   57.95  ? 132 LYS A CD  1 
ATOM   932   C CE  . LYS A  1 132 ? 106.495 104.371 -10.039 1.00   66.08  ? 132 LYS A CE  1 
ATOM   933   N NZ  . LYS A  1 132 ? 106.445 105.699 -9.362  1.00   70.43  ? 132 LYS A NZ  1 
ATOM   934   N N   . LEU A  1 133 ? 108.484 99.299  -7.447  1.00   45.51  ? 133 LEU A N   1 
ATOM   935   C CA  . LEU A  1 133 ? 109.412 98.223  -7.724  1.00   47.00  ? 133 LEU A CA  1 
ATOM   936   C C   . LEU A  1 133 ? 110.797 98.825  -7.815  1.00   48.89  ? 133 LEU A C   1 
ATOM   937   O O   . LEU A  1 133 ? 110.944 99.901  -8.363  1.00   53.34  ? 133 LEU A O   1 
ATOM   938   C CB  . LEU A  1 133 ? 109.028 97.524  -9.028  1.00   46.94  ? 133 LEU A CB  1 
ATOM   939   C CG  . LEU A  1 133 ? 107.733 96.715  -8.981  1.00   43.70  ? 133 LEU A CG  1 
ATOM   940   C CD1 . LEU A  1 133 ? 107.432 96.116  -10.330 1.00   42.23  ? 133 LEU A CD1 1 
ATOM   941   C CD2 . LEU A  1 133 ? 107.877 95.627  -7.930  1.00   37.07  ? 133 LEU A CD2 1 
ATOM   942   N N   . GLY A  1 134 ? 111.801 98.152  -7.264  1.00   47.49  ? 134 GLY A N   1 
ATOM   943   C CA  . GLY A  1 134 ? 113.165 98.647  -7.313  1.00   46.32  ? 134 GLY A CA  1 
ATOM   944   C C   . GLY A  1 134 ? 113.992 97.852  -8.305  1.00   45.72  ? 134 GLY A C   1 
ATOM   945   O O   . GLY A  1 134 ? 113.454 97.050  -9.071  1.00   42.98  ? 134 GLY A O   1 
ATOM   946   N N   . PRO A  1 135 ? 115.314 98.049  -8.286  1.00   48.52  ? 135 PRO A N   1 
ATOM   947   C CA  . PRO A  1 135 ? 116.168 97.344  -9.245  1.00   49.50  ? 135 PRO A CA  1 
ATOM   948   C C   . PRO A  1 135 ? 116.153 95.831  -9.064  1.00   43.90  ? 135 PRO A C   1 
ATOM   949   O O   . PRO A  1 135 ? 115.824 95.307  -7.995  1.00   42.50  ? 135 PRO A O   1 
ATOM   950   C CB  . PRO A  1 135 ? 117.559 97.927  -8.971  1.00   52.74  ? 135 PRO A CB  1 
ATOM   951   C CG  . PRO A  1 135 ? 117.478 98.510  -7.611  1.00   52.35  ? 135 PRO A CG  1 
ATOM   952   C CD  . PRO A  1 135 ? 116.075 98.981  -7.443  1.00   50.93  ? 135 PRO A CD  1 
ATOM   953   N N   . MET A  1 136 ? 116.460 95.123  -10.141 1.00   42.18  ? 136 MET A N   1 
ATOM   954   C CA  . MET A  1 136 ? 116.597 93.679  -10.064 1.00   42.76  ? 136 MET A CA  1 
ATOM   955   C C   . MET A  1 136 ? 117.768 93.310  -9.158  1.00   40.69  ? 136 MET A C   1 
ATOM   956   O O   . MET A  1 136 ? 118.817 93.940  -9.206  1.00   45.10  ? 136 MET A O   1 
ATOM   957   C CB  . MET A  1 136 ? 116.801 93.090  -11.454 1.00   44.36  ? 136 MET A CB  1 
ATOM   958   C CG  . MET A  1 136 ? 115.805 93.603  -12.450 1.00   45.79  ? 136 MET A CG  1 
ATOM   959   S SD  . MET A  1 136 ? 114.247 92.782  -12.244 1.00   49.39  ? 136 MET A SD  1 
ATOM   960   C CE  . MET A  1 136 ? 114.583 91.163  -12.882 1.00   52.39  ? 136 MET A CE  1 
ATOM   961   N N   . VAL A  1 137 ? 117.591 92.285  -8.340  1.00   35.72  ? 137 VAL A N   1 
ATOM   962   C CA  . VAL A  1 137 ? 118.681 91.768  -7.552  1.00   35.43  ? 137 VAL A CA  1 
ATOM   963   C C   . VAL A  1 137 ? 118.871 90.317  -8.003  1.00   35.59  ? 137 VAL A C   1 
ATOM   964   O O   . VAL A  1 137 ? 117.914 89.693  -8.434  1.00   36.32  ? 137 VAL A O   1 
ATOM   965   C CB  . VAL A  1 137 ? 118.379 91.898  -6.037  1.00   32.48  ? 137 VAL A CB  1 
ATOM   966   C CG1 . VAL A  1 137 ? 118.375 93.352  -5.634  1.00   35.93  ? 137 VAL A CG1 1 
ATOM   967   C CG2 . VAL A  1 137 ? 117.030 91.318  -5.718  1.00   30.39  ? 137 VAL A CG2 1 
ATOM   968   N N   . LYS A  1 138 ? 120.096 89.794  -7.935  1.00   34.28  ? 138 LYS A N   1 
ATOM   969   C CA  . LYS A  1 138 ? 120.427 88.474  -8.496  1.00   33.90  ? 138 LYS A CA  1 
ATOM   970   C C   . LYS A  1 138 ? 120.793 87.415  -7.462  1.00   34.28  ? 138 LYS A C   1 
ATOM   971   O O   . LYS A  1 138 ? 121.383 87.713  -6.418  1.00   35.63  ? 138 LYS A O   1 
ATOM   972   C CB  . LYS A  1 138 ? 121.595 88.575  -9.494  1.00   36.06  ? 138 LYS A CB  1 
ATOM   973   C CG  . LYS A  1 138 ? 121.354 89.455  -10.717 1.00   39.42  ? 138 LYS A CG  1 
ATOM   974   C CD  . LYS A  1 138 ? 122.586 89.486  -11.611 1.00   44.56  ? 138 LYS A CD  1 
ATOM   975   C CE  . LYS A  1 138 ? 122.384 90.363  -12.841 1.00   51.24  ? 138 LYS A CE  1 
ATOM   976   N NZ  . LYS A  1 138 ? 123.552 90.344  -13.772 1.00   55.37  ? 138 LYS A NZ  1 
ATOM   977   N N   . VAL A  1 139 ? 120.417 86.174  -7.776  1.00   32.99  ? 139 VAL A N   1 
ATOM   978   C CA  . VAL A  1 139 ? 120.987 84.962  -7.196  1.00   29.15  ? 139 VAL A CA  1 
ATOM   979   C C   . VAL A  1 139 ? 121.887 84.339  -8.263  1.00   32.48  ? 139 VAL A C   1 
ATOM   980   O O   . VAL A  1 139 ? 121.404 83.654  -9.153  1.00   35.28  ? 139 VAL A O   1 
ATOM   981   C CB  . VAL A  1 139 ? 119.881 83.969  -6.798  1.00   30.56  ? 139 VAL A CB  1 
ATOM   982   C CG1 . VAL A  1 139 ? 120.459 82.717  -6.156  1.00   29.16  ? 139 VAL A CG1 1 
ATOM   983   C CG2 . VAL A  1 139 ? 118.873 84.632  -5.881  1.00   30.86  ? 139 VAL A CG2 1 
ATOM   984   N N   . PRO A  1 140 ? 123.203 84.553  -8.174  1.00   33.61  ? 140 PRO A N   1 
ATOM   985   C CA  . PRO A  1 140 ? 124.092 84.183  -9.276  1.00   35.03  ? 140 PRO A CA  1 
ATOM   986   C C   . PRO A  1 140 ? 124.258 82.671  -9.503  1.00   34.22  ? 140 PRO A C   1 
ATOM   987   O O   . PRO A  1 140 ? 124.624 82.278  -10.606 1.00   32.94  ? 140 PRO A O   1 
ATOM   988   C CB  . PRO A  1 140 ? 125.429 84.811  -8.868  1.00   35.48  ? 140 PRO A CB  1 
ATOM   989   C CG  . PRO A  1 140 ? 125.106 85.777  -7.785  1.00   34.19  ? 140 PRO A CG  1 
ATOM   990   C CD  . PRO A  1 140 ? 123.934 85.207  -7.081  1.00   32.83  ? 140 PRO A CD  1 
ATOM   991   N N   . GLN A  1 141 ? 124.056 81.853  -8.477  1.00   36.12  ? 141 GLN A N   1 
ATOM   992   C CA  . GLN A  1 141 ? 124.084 80.398  -8.627  1.00   39.09  ? 141 GLN A CA  1 
ATOM   993   C C   . GLN A  1 141 ? 122.758 79.760  -8.232  1.00   36.14  ? 141 GLN A C   1 
ATOM   994   O O   . GLN A  1 141 ? 122.699 78.907  -7.337  1.00   34.71  ? 141 GLN A O   1 
ATOM   995   C CB  . GLN A  1 141 ? 125.209 79.769  -7.804  1.00   45.65  ? 141 GLN A CB  1 
ATOM   996   C CG  . GLN A  1 141 ? 126.580 80.127  -8.288  1.00   52.68  ? 141 GLN A CG  1 
ATOM   997   C CD  . GLN A  1 141 ? 127.066 81.383  -7.654  1.00   61.55  ? 141 GLN A CD  1 
ATOM   998   O OE1 . GLN A  1 141 ? 126.571 81.781  -6.601  1.00   63.12  ? 141 GLN A OE1 1 
ATOM   999   N NE2 . GLN A  1 141 ? 128.000 82.061  -8.316  1.00   68.67  ? 141 GLN A NE2 1 
ATOM   1000  N N   . PHE A  1 142 ? 121.693 80.170  -8.903  1.00   32.18  ? 142 PHE A N   1 
ATOM   1001  C CA  . PHE A  1 142 ? 120.397 79.593  -8.633  1.00   27.13  ? 142 PHE A CA  1 
ATOM   1002  C C   . PHE A  1 142 ? 120.343 78.154  -9.153  1.00   24.33  ? 142 PHE A C   1 
ATOM   1003  O O   . PHE A  1 142 ? 120.711 77.887  -10.282 1.00   26.50  ? 142 PHE A O   1 
ATOM   1004  C CB  . PHE A  1 142 ? 119.299 80.452  -9.264  1.00   25.95  ? 142 PHE A CB  1 
ATOM   1005  C CG  . PHE A  1 142 ? 117.919 80.005  -8.924  1.00   23.23  ? 142 PHE A CG  1 
ATOM   1006  C CD1 . PHE A  1 142 ? 117.341 80.345  -7.711  1.00   23.19  ? 142 PHE A CD1 1 
ATOM   1007  C CD2 . PHE A  1 142 ? 117.175 79.266  -9.828  1.00   26.36  ? 142 PHE A CD2 1 
ATOM   1008  C CE1 . PHE A  1 142 ? 116.044 79.937  -7.392  1.00   23.54  ? 142 PHE A CE1 1 
ATOM   1009  C CE2 . PHE A  1 142 ? 115.886 78.854  -9.520  1.00   25.00  ? 142 PHE A CE2 1 
ATOM   1010  C CZ  . PHE A  1 142 ? 115.325 79.197  -8.290  1.00   25.24  ? 142 PHE A CZ  1 
ATOM   1011  N N   . LEU A  1 143 ? 119.899 77.228  -8.316  1.00   22.69  ? 143 LEU A N   1 
ATOM   1012  C CA  . LEU A  1 143 ? 119.773 75.836  -8.711  1.00   24.17  ? 143 LEU A CA  1 
ATOM   1013  C C   . LEU A  1 143 ? 118.376 75.494  -9.208  1.00   24.62  ? 143 LEU A C   1 
ATOM   1014  O O   . LEU A  1 143 ? 117.360 75.880  -8.622  1.00   27.18  ? 143 LEU A O   1 
ATOM   1015  C CB  . LEU A  1 143 ? 120.131 74.916  -7.546  1.00   23.59  ? 143 LEU A CB  1 
ATOM   1016  C CG  . LEU A  1 143 ? 121.547 75.134  -7.021  1.00   22.81  ? 143 LEU A CG  1 
ATOM   1017  C CD1 . LEU A  1 143 ? 121.751 74.333  -5.769  1.00   25.43  ? 143 LEU A CD1 1 
ATOM   1018  C CD2 . LEU A  1 143 ? 122.572 74.770  -8.043  1.00   23.06  ? 143 LEU A CD2 1 
ATOM   1019  N N   . PHE A  1 144 ? 118.341 74.750  -10.302 1.00   27.59  ? 144 PHE A N   1 
ATOM   1020  C CA  . PHE A  1 144 ? 117.096 74.369  -10.937 1.00   28.53  ? 144 PHE A CA  1 
ATOM   1021  C C   . PHE A  1 144 ? 117.357 73.132  -11.811 1.00   29.03  ? 144 PHE A C   1 
ATOM   1022  O O   . PHE A  1 144 ? 118.466 72.603  -11.835 1.00   28.75  ? 144 PHE A O   1 
ATOM   1023  C CB  . PHE A  1 144 ? 116.524 75.536  -11.756 1.00   26.95  ? 144 PHE A CB  1 
ATOM   1024  C CG  . PHE A  1 144 ? 117.352 75.891  -12.961 1.00   29.17  ? 144 PHE A CG  1 
ATOM   1025  C CD1 . PHE A  1 144 ? 118.478 76.684  -12.835 1.00   28.59  ? 144 PHE A CD1 1 
ATOM   1026  C CD2 . PHE A  1 144 ? 117.003 75.434  -14.217 1.00   31.09  ? 144 PHE A CD2 1 
ATOM   1027  C CE1 . PHE A  1 144 ? 119.243 77.013  -13.930 1.00   30.79  ? 144 PHE A CE1 1 
ATOM   1028  C CE2 . PHE A  1 144 ? 117.764 75.759  -15.316 1.00   33.34  ? 144 PHE A CE2 1 
ATOM   1029  C CZ  . PHE A  1 144 ? 118.893 76.547  -15.171 1.00   32.77  ? 144 PHE A CZ  1 
ATOM   1030  N N   . SER A  1 145 ? 116.328 72.690  -12.527 1.00   28.32  ? 145 SER A N   1 
ATOM   1031  C CA  . SER A  1 145 ? 116.409 71.527  -13.378 1.00   27.56  ? 145 SER A CA  1 
ATOM   1032  C C   . SER A  1 145 ? 116.309 71.873  -14.871 1.00   29.63  ? 145 SER A C   1 
ATOM   1033  O O   . SER A  1 145 ? 115.449 72.620  -15.282 1.00   31.22  ? 145 SER A O   1 
ATOM   1034  C CB  . SER A  1 145 ? 115.295 70.546  -12.988 1.00   28.72  ? 145 SER A CB  1 
ATOM   1035  O OG  . SER A  1 145 ? 115.212 69.432  -13.873 1.00   31.50  ? 145 SER A OG  1 
ATOM   1036  N N   . CYS A  1 146 ? 117.222 71.336  -15.671 1.00   32.24  ? 146 CYS A N   1 
ATOM   1037  C CA  . CYS A  1 146 ? 117.078 71.312  -17.124 1.00   34.02  ? 146 CYS A CA  1 
ATOM   1038  C C   . CYS A  1 146 ? 116.300 70.084  -17.537 1.00   39.93  ? 146 CYS A C   1 
ATOM   1039  O O   . CYS A  1 146 ? 116.841 68.985  -17.510 1.00   41.98  ? 146 CYS A O   1 
ATOM   1040  C CB  . CYS A  1 146 ? 118.434 71.318  -17.831 1.00   33.24  ? 146 CYS A CB  1 
ATOM   1041  S SG  . CYS A  1 146 ? 119.142 72.960  -18.037 1.00   40.77  ? 146 CYS A SG  1 
ATOM   1042  N N   . ALA A  1 147 ? 115.037 70.272  -17.917 1.00   44.40  ? 147 ALA A N   1 
ATOM   1043  C CA  . ALA A  1 147 ? 114.119 69.169  -18.213 1.00   45.06  ? 147 ALA A CA  1 
ATOM   1044  C C   . ALA A  1 147 ? 114.186 68.738  -19.681 1.00   48.02  ? 147 ALA A C   1 
ATOM   1045  O O   . ALA A  1 147 ? 114.681 69.492  -20.523 1.00   52.25  ? 147 ALA A O   1 
ATOM   1046  C CB  . ALA A  1 147 ? 112.709 69.575  -17.853 1.00   43.32  ? 147 ALA A CB  1 
ATOM   1047  N N   . PRO A  1 148 ? 113.764 67.491  -19.983 1.00   46.58  ? 148 PRO A N   1 
ATOM   1048  C CA  . PRO A  1 148 ? 113.629 67.028  -21.374 1.00   49.90  ? 148 PRO A CA  1 
ATOM   1049  C C   . PRO A  1 148 ? 112.568 67.850  -22.113 1.00   51.70  ? 148 PRO A C   1 
ATOM   1050  O O   . PRO A  1 148 ? 111.580 68.251  -21.506 1.00   52.80  ? 148 PRO A O   1 
ATOM   1051  C CB  . PRO A  1 148 ? 113.209 65.562  -21.230 1.00   48.93  ? 148 PRO A CB  1 
ATOM   1052  C CG  . PRO A  1 148 ? 112.755 65.417  -19.834 1.00   44.19  ? 148 PRO A CG  1 
ATOM   1053  C CD  . PRO A  1 148 ? 113.507 66.406  -19.024 1.00   42.91  ? 148 PRO A CD  1 
ATOM   1054  N N   . SER A  1 149 ? 112.784 68.135  -23.385 1.00   51.98  ? 149 SER A N   1 
ATOM   1055  C CA  . SER A  1 149 ? 111.906 69.042  -24.119 1.00   54.33  ? 149 SER A CA  1 
ATOM   1056  C C   . SER A  1 149 ? 110.409 68.673  -24.144 1.00   53.02  ? 149 SER A C   1 
ATOM   1057  O O   . SER A  1 149 ? 109.563 69.565  -24.161 1.00   53.34  ? 149 SER A O   1 
ATOM   1058  C CB  . SER A  1 149 ? 112.431 69.199  -25.548 1.00   60.42  ? 149 SER A CB  1 
ATOM   1059  O OG  . SER A  1 149 ? 112.355 67.979  -26.253 1.00   65.74  ? 149 SER A OG  1 
ATOM   1060  N N   . PHE A  1 150 ? 110.083 67.381  -24.167 1.00   51.97  ? 150 PHE A N   1 
ATOM   1061  C CA  . PHE A  1 150 ? 108.691 66.926  -24.301 1.00   52.81  ? 150 PHE A CA  1 
ATOM   1062  C C   . PHE A  1 150 ? 107.817 67.332  -23.125 1.00   52.27  ? 150 PHE A C   1 
ATOM   1063  O O   . PHE A  1 150 ? 106.593 67.386  -23.219 1.00   53.27  ? 150 PHE A O   1 
ATOM   1064  C CB  . PHE A  1 150 ? 108.622 65.405  -24.415 1.00   55.18  ? 150 PHE A CB  1 
ATOM   1065  C CG  . PHE A  1 150 ? 108.649 64.705  -23.086 1.00   53.46  ? 150 PHE A CG  1 
ATOM   1066  C CD1 . PHE A  1 150 ? 109.842 64.436  -22.454 1.00   52.52  ? 150 PHE A CD1 1 
ATOM   1067  C CD2 . PHE A  1 150 ? 107.470 64.331  -22.461 1.00   54.25  ? 150 PHE A CD2 1 
ATOM   1068  C CE1 . PHE A  1 150 ? 109.856 63.811  -21.229 1.00   49.95  ? 150 PHE A CE1 1 
ATOM   1069  C CE2 . PHE A  1 150 ? 107.482 63.708  -21.244 1.00   52.77  ? 150 PHE A CE2 1 
ATOM   1070  C CZ  . PHE A  1 150 ? 108.673 63.447  -20.626 1.00   50.31  ? 150 PHE A CZ  1 
ATOM   1071  N N   . LEU A  1 151 ? 108.459 67.582  -21.999 1.00   52.06  ? 151 LEU A N   1 
ATOM   1072  C CA  . LEU A  1 151 ? 107.747 67.653  -20.738 1.00   49.57  ? 151 LEU A CA  1 
ATOM   1073  C C   . LEU A  1 151 ? 106.793 68.837  -20.669 1.00   47.91  ? 151 LEU A C   1 
ATOM   1074  O O   . LEU A  1 151 ? 105.749 68.760  -20.024 1.00   46.59  ? 151 LEU A O   1 
ATOM   1075  C CB  . LEU A  1 151 ? 108.752 67.717  -19.590 1.00   45.93  ? 151 LEU A CB  1 
ATOM   1076  C CG  . LEU A  1 151 ? 108.160 67.351  -18.237 1.00   43.32  ? 151 LEU A CG  1 
ATOM   1077  C CD1 . LEU A  1 151 ? 107.555 65.969  -18.332 1.00   46.65  ? 151 LEU A CD1 1 
ATOM   1078  C CD2 . LEU A  1 151 ? 109.206 67.434  -17.134 1.00   39.86  ? 151 LEU A CD2 1 
ATOM   1079  N N   . ALA A  1 152 ? 107.142 69.925  -21.348 1.00   47.59  ? 152 ALA A N   1 
ATOM   1080  C CA  . ALA A  1 152 ? 106.307 71.116  -21.334 1.00   47.29  ? 152 ALA A CA  1 
ATOM   1081  C C   . ALA A  1 152 ? 105.463 71.216  -22.601 1.00   53.08  ? 152 ALA A C   1 
ATOM   1082  O O   . ALA A  1 152 ? 104.731 72.183  -22.797 1.00   56.04  ? 152 ALA A O   1 
ATOM   1083  C CB  . ALA A  1 152 ? 107.172 72.370  -21.167 1.00   42.35  ? 152 ALA A CB  1 
ATOM   1084  N N   . GLN A  1 153 ? 105.522 70.204  -23.452 1.00   54.26  ? 153 GLN A N   1 
ATOM   1085  C CA  . GLN A  1 153 ? 104.938 70.370  -24.761 1.00   58.88  ? 153 GLN A CA  1 
ATOM   1086  C C   . GLN A  1 153 ? 103.424 70.206  -24.722 1.00   59.74  ? 153 GLN A C   1 
ATOM   1087  O O   . GLN A  1 153 ? 102.728 70.484  -25.702 1.00   62.21  ? 153 GLN A O   1 
ATOM   1088  C CB  . GLN A  1 153 ? 105.633 69.437  -25.765 1.00   65.25  ? 153 GLN A CB  1 
ATOM   1089  C CG  . GLN A  1 153 ? 106.958 70.078  -26.247 1.00   70.38  ? 153 GLN A CG  1 
ATOM   1090  C CD  . GLN A  1 153 ? 107.795 69.226  -27.197 1.00   78.37  ? 153 GLN A CD  1 
ATOM   1091  O OE1 . GLN A  1 153 ? 107.720 67.995  -27.196 1.00   79.95  ? 153 GLN A OE1 1 
ATOM   1092  N NE2 . GLN A  1 153 ? 108.611 69.895  -28.015 1.00   81.97  ? 153 GLN A NE2 1 
ATOM   1093  N N   . LYS A  1 154 ? 102.898 69.788  -23.583 1.00   58.42  ? 154 LYS A N   1 
ATOM   1094  C CA  . LYS A  1 154 ? 101.463 69.606  -23.499 1.00   61.75  ? 154 LYS A CA  1 
ATOM   1095  C C   . LYS A  1 154 ? 100.891 70.167  -22.187 1.00   60.93  ? 154 LYS A C   1 
ATOM   1096  O O   . LYS A  1 154 ? 101.449 69.960  -21.119 1.00   59.87  ? 154 LYS A O   1 
ATOM   1097  C CB  . LYS A  1 154 ? 101.145 68.119  -23.705 1.00   64.42  ? 154 LYS A CB  1 
ATOM   1098  C CG  . LYS A  1 154 ? 101.275 67.781  -25.193 1.00   71.19  ? 154 LYS A CG  1 
ATOM   1099  C CD  . LYS A  1 154 ? 100.883 66.373  -25.637 1.00   76.99  ? 154 LYS A CD  1 
ATOM   1100  C CE  . LYS A  1 154 ? 101.720 65.271  -24.995 1.00   76.70  ? 154 LYS A CE  1 
ATOM   1101  N NZ  . LYS A  1 154 ? 101.409 63.939  -25.617 1.00   79.37  ? 154 LYS A NZ  1 
ATOM   1102  N N   . GLY A  1 155 ? 99.786  70.906  -22.288 1.00   60.64  ? 155 GLY A N   1 
ATOM   1103  C CA  . GLY A  1 155 ? 99.014  71.308  -21.121 1.00   57.43  ? 155 GLY A CA  1 
ATOM   1104  C C   . GLY A  1 155 ? 99.233  72.675  -20.491 1.00   54.10  ? 155 GLY A C   1 
ATOM   1105  O O   . GLY A  1 155 ? 98.414  73.116  -19.680 1.00   51.51  ? 155 GLY A O   1 
ATOM   1106  N N   . LEU A  1 156 ? 100.324 73.346  -20.843 1.00   53.45  ? 156 LEU A N   1 
ATOM   1107  C CA  . LEU A  1 156 ? 100.670 74.629  -20.226 1.00   48.37  ? 156 LEU A CA  1 
ATOM   1108  C C   . LEU A  1 156 ? 100.199 75.790  -21.085 1.00   48.08  ? 156 LEU A C   1 
ATOM   1109  O O   . LEU A  1 156 ? 99.966  75.601  -22.275 1.00   49.38  ? 156 LEU A O   1 
ATOM   1110  C CB  . LEU A  1 156 ? 102.177 74.718  -19.996 1.00   42.70  ? 156 LEU A CB  1 
ATOM   1111  C CG  . LEU A  1 156 ? 102.815 73.539  -19.273 1.00   39.20  ? 156 LEU A CG  1 
ATOM   1112  C CD1 . LEU A  1 156 ? 104.292 73.788  -19.039 1.00   35.89  ? 156 LEU A CD1 1 
ATOM   1113  C CD2 . LEU A  1 156 ? 102.127 73.374  -17.954 1.00   38.78  ? 156 LEU A CD2 1 
ATOM   1114  N N   . PRO A  1 157 ? 100.089 77.004  -20.498 1.00   47.16  ? 157 PRO A N   1 
ATOM   1115  C CA  . PRO A  1 157 ? 99.734  78.170  -21.312 1.00   48.30  ? 157 PRO A CA  1 
ATOM   1116  C C   . PRO A  1 157 ? 100.687 78.349  -22.468 1.00   55.68  ? 157 PRO A C   1 
ATOM   1117  O O   . PRO A  1 157 ? 101.813 77.820  -22.442 1.00   60.13  ? 157 PRO A O   1 
ATOM   1118  C CB  . PRO A  1 157 ? 99.868  79.341  -20.342 1.00   43.27  ? 157 PRO A CB  1 
ATOM   1119  C CG  . PRO A  1 157 ? 99.653  78.755  -19.017 1.00   39.51  ? 157 PRO A CG  1 
ATOM   1120  C CD  . PRO A  1 157 ? 100.251 77.379  -19.082 1.00   38.95  ? 157 PRO A CD  1 
ATOM   1121  N N   . ASN A  1 158 ? 100.257 79.088  -23.474 1.00   57.09  ? 158 ASN A N   1 
ATOM   1122  C CA  . ASN A  1 158 ? 101.052 79.209  -24.681 1.00   60.86  ? 158 ASN A CA  1 
ATOM   1123  C C   . ASN A  1 158 ? 102.398 79.884  -24.420 1.00   58.46  ? 158 ASN A C   1 
ATOM   1124  O O   . ASN A  1 158 ? 102.463 80.854  -23.662 1.00   54.53  ? 158 ASN A O   1 
ATOM   1125  C CB  . ASN A  1 158 ? 100.245 79.984  -25.720 1.00   67.57  ? 158 ASN A CB  1 
ATOM   1126  C CG  . ASN A  1 158 ? 100.857 79.950  -27.095 1.00   73.28  ? 158 ASN A CG  1 
ATOM   1127  O OD1 . ASN A  1 158 ? 101.753 80.722  -27.403 1.00   75.23  ? 158 ASN A OD1 1 
ATOM   1128  N ND2 . ASN A  1 158 ? 100.372 79.041  -27.935 1.00   75.02  ? 158 ASN A ND2 1 
ATOM   1129  N N   . ASN A  1 159 ? 103.452 79.344  -25.036 1.00   61.77  ? 159 ASN A N   1 
ATOM   1130  C CA  . ASN A  1 159 ? 104.818 79.841  -24.875 1.00   64.96  ? 159 ASN A CA  1 
ATOM   1131  C C   . ASN A  1 159 ? 105.479 79.582  -23.528 1.00   59.29  ? 159 ASN A C   1 
ATOM   1132  O O   . ASN A  1 159 ? 106.604 80.000  -23.322 1.00   58.73  ? 159 ASN A O   1 
ATOM   1133  C CB  . ASN A  1 159 ? 104.869 81.352  -25.165 1.00   71.41  ? 159 ASN A CB  1 
ATOM   1134  C CG  . ASN A  1 159 ? 104.782 81.659  -26.645 1.00   79.62  ? 159 ASN A CG  1 
ATOM   1135  O OD1 . ASN A  1 159 ? 104.251 80.867  -27.436 1.00   80.29  ? 159 ASN A OD1 1 
ATOM   1136  N ND2 . ASN A  1 159 ? 105.222 82.847  -27.016 1.00   83.85  ? 159 ASN A ND2 1 
ATOM   1137  N N   . VAL A  1 160 ? 104.782 78.938  -22.602 1.00   53.36  ? 160 VAL A N   1 
ATOM   1138  C CA  . VAL A  1 160 ? 105.376 78.602  -21.310 1.00   47.65  ? 160 VAL A CA  1 
ATOM   1139  C C   . VAL A  1 160 ? 106.242 77.361  -21.402 1.00   46.07  ? 160 VAL A C   1 
ATOM   1140  O O   . VAL A  1 160 ? 105.867 76.363  -21.981 1.00   47.67  ? 160 VAL A O   1 
ATOM   1141  C CB  . VAL A  1 160 ? 104.306 78.427  -20.247 1.00   42.41  ? 160 VAL A CB  1 
ATOM   1142  C CG1 . VAL A  1 160 ? 104.815 77.639  -19.066 1.00   37.16  ? 160 VAL A CG1 1 
ATOM   1143  C CG2 . VAL A  1 160 ? 103.846 79.807  -19.813 1.00   39.90  ? 160 VAL A CG2 1 
ATOM   1144  N N   . GLN A  1 161 ? 107.435 77.438  -20.854 1.00   44.61  ? 161 GLN A N   1 
ATOM   1145  C CA  . GLN A  1 161 ? 108.447 76.436  -21.123 1.00   44.75  ? 161 GLN A CA  1 
ATOM   1146  C C   . GLN A  1 161 ? 109.052 75.782  -19.841 1.00   41.36  ? 161 GLN A C   1 
ATOM   1147  O O   . GLN A  1 161 ? 110.199 75.313  -19.829 1.00   40.40  ? 161 GLN A O   1 
ATOM   1148  C CB  . GLN A  1 161 ? 109.448 77.059  -22.115 1.00   51.99  ? 161 GLN A CB  1 
ATOM   1149  C CG  . GLN A  1 161 ? 109.005 76.653  -23.519 1.00   64.45  ? 161 GLN A CG  1 
ATOM   1150  C CD  . GLN A  1 161 ? 110.000 75.736  -24.198 1.00   75.70  ? 161 GLN A CD  1 
ATOM   1151  O OE1 . GLN A  1 161 ? 110.397 74.716  -23.641 1.00   80.73  ? 161 GLN A OE1 1 
ATOM   1152  N NE2 . GLN A  1 161 ? 110.139 75.948  -25.537 1.00   80.58  ? 161 GLN A NE2 1 
ATOM   1153  N N   . GLY A  1 162 ? 108.269 75.796  -18.754 1.00   36.79  ? 162 GLY A N   1 
ATOM   1154  C CA  . GLY A  1 162 ? 108.633 75.178  -17.488 1.00   35.31  ? 162 GLY A CA  1 
ATOM   1155  C C   . GLY A  1 162 ? 107.690 75.621  -16.377 1.00   35.42  ? 162 GLY A C   1 
ATOM   1156  O O   . GLY A  1 162 ? 106.611 76.142  -16.652 1.00   39.61  ? 162 GLY A O   1 
ATOM   1157  N N   . ALA A  1 163 ? 108.095 75.406  -15.131 1.00   31.03  ? 163 ALA A N   1 
ATOM   1158  C CA  . ALA A  1 163 ? 107.293 75.761  -13.981 1.00   29.92  ? 163 ALA A CA  1 
ATOM   1159  C C   . ALA A  1 163 ? 108.253 76.258  -12.931 1.00   29.96  ? 163 ALA A C   1 
ATOM   1160  O O   . ALA A  1 163 ? 109.391 75.809  -12.876 1.00   28.91  ? 163 ALA A O   1 
ATOM   1161  C CB  . ALA A  1 163 ? 106.499 74.561  -13.467 1.00   27.25  ? 163 ALA A CB  1 
ATOM   1162  N N   . LEU A  1 164 ? 107.796 77.187  -12.105 1.00   30.21  ? 164 LEU A N   1 
ATOM   1163  C CA  . LEU A  1 164 ? 108.553 77.598  -10.945 1.00   29.54  ? 164 LEU A CA  1 
ATOM   1164  C C   . LEU A  1 164 ? 107.820 77.023  -9.766  1.00   29.20  ? 164 LEU A C   1 
ATOM   1165  O O   . LEU A  1 164 ? 106.617 77.210  -9.636  1.00   33.50  ? 164 LEU A O   1 
ATOM   1166  C CB  . LEU A  1 164 ? 108.664 79.117  -10.883 1.00   31.03  ? 164 LEU A CB  1 
ATOM   1167  C CG  . LEU A  1 164 ? 107.378 79.925  -10.756 1.00   35.69  ? 164 LEU A CG  1 
ATOM   1168  C CD1 . LEU A  1 164 ? 107.300 80.563  -9.402  1.00   34.71  ? 164 LEU A CD1 1 
ATOM   1169  C CD2 . LEU A  1 164 ? 107.225 80.943  -11.848 1.00   39.69  ? 164 LEU A CD2 1 
ATOM   1170  N N   . GLY A  1 165 ? 108.527 76.300  -8.916  1.00   27.88  ? 165 GLY A N   1 
ATOM   1171  C CA  . GLY A  1 165 ? 107.891 75.606  -7.820  1.00   25.64  ? 165 GLY A CA  1 
ATOM   1172  C C   . GLY A  1 165 ? 108.141 76.297  -6.509  1.00   26.42  ? 165 GLY A C   1 
ATOM   1173  O O   . GLY A  1 165 ? 109.260 76.710  -6.220  1.00   25.98  ? 165 GLY A O   1 
ATOM   1174  N N   . LEU A  1 166 ? 107.092 76.394  -5.703  1.00   25.45  ? 166 LEU A N   1 
ATOM   1175  C CA  . LEU A  1 166 ? 107.176 77.071  -4.427  1.00   25.87  ? 166 LEU A CA  1 
ATOM   1176  C C   . LEU A  1 166 ? 106.898 76.141  -3.280  1.00   27.14  ? 166 LEU A C   1 
ATOM   1177  O O   . LEU A  1 166 ? 106.484 76.596  -2.216  1.00   29.02  ? 166 LEU A O   1 
ATOM   1178  C CB  . LEU A  1 166 ? 106.175 78.212  -4.369  1.00   27.52  ? 166 LEU A CB  1 
ATOM   1179  C CG  . LEU A  1 166 ? 106.317 79.332  -5.383  1.00   28.67  ? 166 LEU A CG  1 
ATOM   1180  C CD1 . LEU A  1 166 ? 105.152 80.289  -5.245  1.00   31.71  ? 166 LEU A CD1 1 
ATOM   1181  C CD2 . LEU A  1 166 ? 107.601 80.032  -5.106  1.00   28.17  ? 166 LEU A CD2 1 
ATOM   1182  N N   . GLY A  1 167 ? 107.106 74.849  -3.498  1.00   24.73  ? 167 GLY A N   1 
ATOM   1183  C CA  . GLY A  1 167 ? 106.774 73.869  -2.498  1.00   25.64  ? 167 GLY A CA  1 
ATOM   1184  C C   . GLY A  1 167 ? 107.764 73.820  -1.368  1.00   26.00  ? 167 GLY A C   1 
ATOM   1185  O O   . GLY A  1 167 ? 108.773 74.497  -1.404  1.00   26.56  ? 167 GLY A O   1 
ATOM   1186  N N   . GLN A  1 168 ? 107.455 73.011  -0.359  1.00   25.75  ? 168 GLN A N   1 
ATOM   1187  C CA  . GLN A  1 168 ? 108.350 72.766  0.769   1.00   26.21  ? 168 GLN A CA  1 
ATOM   1188  C C   . GLN A  1 168 ? 109.405 71.711  0.416   1.00   26.35  ? 168 GLN A C   1 
ATOM   1189  O O   . GLN A  1 168 ? 109.222 70.529  0.654   1.00   28.78  ? 168 GLN A O   1 
ATOM   1190  C CB  . GLN A  1 168 ? 107.537 72.300  1.967   1.00   26.48  ? 168 GLN A CB  1 
ATOM   1191  C CG  . GLN A  1 168 ? 106.753 73.375  2.563   1.00   24.13  ? 168 GLN A CG  1 
ATOM   1192  C CD  . GLN A  1 168 ? 107.652 74.421  3.093   1.00   27.65  ? 168 GLN A CD  1 
ATOM   1193  O OE1 . GLN A  1 168 ? 108.403 74.177  4.037   1.00   31.15  ? 168 GLN A OE1 1 
ATOM   1194  N NE2 . GLN A  1 168 ? 107.635 75.596  2.466   1.00   27.01  ? 168 GLN A NE2 1 
ATOM   1195  N N   . ALA A  1 169 ? 110.494 72.141  -0.189  1.00   27.19  ? 169 ALA A N   1 
ATOM   1196  C CA  . ALA A  1 169 ? 111.499 71.225  -0.712  1.00   26.27  ? 169 ALA A CA  1 
ATOM   1197  C C   . ALA A  1 169 ? 112.777 72.032  -0.792  1.00   24.45  ? 169 ALA A C   1 
ATOM   1198  O O   . ALA A  1 169 ? 112.698 73.241  -0.952  1.00   25.83  ? 169 ALA A O   1 
ATOM   1199  C CB  . ALA A  1 169 ? 111.085 70.675  -2.080  1.00   26.84  ? 169 ALA A CB  1 
ATOM   1200  N N   . PRO A  1 170 ? 113.953 71.384  -0.681  1.00   23.27  ? 170 PRO A N   1 
ATOM   1201  C CA  . PRO A  1 170 ? 115.176 72.143  -0.436  1.00   22.96  ? 170 PRO A CA  1 
ATOM   1202  C C   . PRO A  1 170 ? 115.614 73.182  -1.496  1.00   26.42  ? 170 PRO A C   1 
ATOM   1203  O O   . PRO A  1 170 ? 116.192 74.194  -1.119  1.00   27.38  ? 170 PRO A O   1 
ATOM   1204  C CB  . PRO A  1 170 ? 116.232 71.032  -0.317  1.00   22.95  ? 170 PRO A CB  1 
ATOM   1205  C CG  . PRO A  1 170 ? 115.630 69.843  -0.913  1.00   23.19  ? 170 PRO A CG  1 
ATOM   1206  C CD  . PRO A  1 170 ? 114.204 69.936  -0.614  1.00   24.30  ? 170 PRO A CD  1 
ATOM   1207  N N   . ILE A  1 171 ? 115.351 72.978  -2.779  1.00   26.48  ? 171 ILE A N   1 
ATOM   1208  C CA  . ILE A  1 171 ? 115.697 74.025  -3.724  1.00   23.59  ? 171 ILE A CA  1 
ATOM   1209  C C   . ILE A  1 171 ? 114.479 74.654  -4.402  1.00   26.20  ? 171 ILE A C   1 
ATOM   1210  O O   . ILE A  1 171 ? 114.532 75.067  -5.557  1.00   25.46  ? 171 ILE A O   1 
ATOM   1211  C CB  . ILE A  1 171 ? 116.690 73.510  -4.796  1.00   24.40  ? 171 ILE A CB  1 
ATOM   1212  C CG1 . ILE A  1 171 ? 116.150 72.306  -5.571  1.00   22.34  ? 171 ILE A CG1 1 
ATOM   1213  C CG2 . ILE A  1 171 ? 118.031 73.166  -4.156  1.00   25.41  ? 171 ILE A CG2 1 
ATOM   1214  C CD1 . ILE A  1 171 ? 116.876 72.102  -6.901  1.00   21.15  ? 171 ILE A CD1 1 
ATOM   1215  N N   . SER A  1 172 ? 113.385 74.766  -3.662  1.00   27.23  ? 172 SER A N   1 
ATOM   1216  C CA  . SER A  1 172 ? 112.251 75.508  -4.150  1.00   28.32  ? 172 SER A CA  1 
ATOM   1217  C C   . SER A  1 172 ? 112.699 76.922  -4.354  1.00   30.81  ? 172 SER A C   1 
ATOM   1218  O O   . SER A  1 172 ? 113.727 77.323  -3.836  1.00   29.59  ? 172 SER A O   1 
ATOM   1219  C CB  . SER A  1 172 ? 111.103 75.472  -3.166  1.00   26.40  ? 172 SER A CB  1 
ATOM   1220  O OG  . SER A  1 172 ? 111.515 76.082  -1.967  1.00   28.31  ? 172 SER A OG  1 
ATOM   1221  N N   . LEU A  1 173 ? 111.931 77.683  -5.111  1.00   30.65  ? 173 LEU A N   1 
ATOM   1222  C CA  . LEU A  1 173 ? 112.293 79.050  -5.400  1.00   30.18  ? 173 LEU A CA  1 
ATOM   1223  C C   . LEU A  1 173 ? 112.400 79.891  -4.133  1.00   28.95  ? 173 LEU A C   1 
ATOM   1224  O O   . LEU A  1 173 ? 113.368 80.612  -3.960  1.00   26.47  ? 173 LEU A O   1 
ATOM   1225  C CB  . LEU A  1 173 ? 111.280 79.666  -6.357  1.00   30.77  ? 173 LEU A CB  1 
ATOM   1226  C CG  . LEU A  1 173 ? 111.359 81.173  -6.549  1.00   31.91  ? 173 LEU A CG  1 
ATOM   1227  C CD1 . LEU A  1 173 ? 112.687 81.626  -7.176  1.00   31.48  ? 173 LEU A CD1 1 
ATOM   1228  C CD2 . LEU A  1 173 ? 110.197 81.647  -7.372  1.00   34.77  ? 173 LEU A CD2 1 
ATOM   1229  N N   . GLN A  1 174 ? 111.408 79.812  -3.253  1.00   29.12  ? 174 GLN A N   1 
ATOM   1230  C CA  . GLN A  1 174 ? 111.405 80.668  -2.064  1.00   27.75  ? 174 GLN A CA  1 
ATOM   1231  C C   . GLN A  1 174 ? 112.538 80.275  -1.111  1.00   28.03  ? 174 GLN A C   1 
ATOM   1232  O O   . GLN A  1 174 ? 113.159 81.137  -0.500  1.00   29.22  ? 174 GLN A O   1 
ATOM   1233  C CB  . GLN A  1 174 ? 110.027 80.656  -1.354  1.00   23.89  ? 174 GLN A CB  1 
ATOM   1234  C CG  . GLN A  1 174 ? 109.727 79.506  -0.400  1.00   24.12  ? 174 GLN A CG  1 
ATOM   1235  C CD  . GLN A  1 174 ? 109.306 78.258  -1.116  1.00   26.45  ? 174 GLN A CD  1 
ATOM   1236  O OE1 . GLN A  1 174 ? 109.180 78.251  -2.331  1.00   27.23  ? 174 GLN A OE1 1 
ATOM   1237  N NE2 . GLN A  1 174 ? 109.091 77.190  -0.368  1.00   27.64  ? 174 GLN A NE2 1 
ATOM   1238  N N   . ASN A  1 175 ? 112.827 78.986  -1.011  1.00   28.17  ? 175 ASN A N   1 
ATOM   1239  C CA  . ASN A  1 175 ? 113.882 78.507  -0.125  1.00   27.82  ? 175 ASN A CA  1 
ATOM   1240  C C   . ASN A  1 175 ? 115.239 79.095  -0.542  1.00   27.79  ? 175 ASN A C   1 
ATOM   1241  O O   . ASN A  1 175 ? 116.033 79.499  0.308   1.00   26.98  ? 175 ASN A O   1 
ATOM   1242  C CB  A ASN A  1 175 ? 113.950 76.969  -0.157  0.50   29.36  ? 175 ASN A CB  1 
ATOM   1243  C CB  B ASN A  1 175 ? 113.856 76.979  -0.080  0.50   29.72  ? 175 ASN A CB  1 
ATOM   1244  C CG  A ASN A  1 175 ? 115.125 76.385  0.665   0.50   32.62  ? 175 ASN A CG  1 
ATOM   1245  C CG  B ASN A  1 175 ? 112.685 76.449  0.769   0.50   34.10  ? 175 ASN A CG  1 
ATOM   1246  O OD1 A ASN A  1 175 ? 116.301 76.554  0.322   0.50   33.40  ? 175 ASN A OD1 1 
ATOM   1247  O OD1 B ASN A  1 175 ? 112.158 75.354  0.549   0.50   33.22  ? 175 ASN A OD1 1 
ATOM   1248  N ND2 A ASN A  1 175 ? 114.795 75.660  1.728   0.50   32.88  ? 175 ASN A ND2 1 
ATOM   1249  N ND2 B ASN A  1 175 ? 112.269 77.253  1.742   0.50   36.24  ? 175 ASN A ND2 1 
ATOM   1250  N N   . GLN A  1 176 ? 115.474 79.211  -1.850  1.00   27.73  ? 176 GLN A N   1 
ATOM   1251  C CA  . GLN A  1 176 ? 116.724 79.772  -2.361  1.00   25.67  ? 176 GLN A CA  1 
ATOM   1252  C C   . GLN A  1 176 ? 116.792 81.301  -2.238  1.00   29.76  ? 176 GLN A C   1 
ATOM   1253  O O   . GLN A  1 176 ? 117.862 81.845  -1.971  1.00   32.97  ? 176 GLN A O   1 
ATOM   1254  C CB  . GLN A  1 176 ? 116.943 79.349  -3.814  1.00   25.04  ? 176 GLN A CB  1 
ATOM   1255  C CG  . GLN A  1 176 ? 117.293 77.855  -3.977  1.00   22.32  ? 176 GLN A CG  1 
ATOM   1256  C CD  . GLN A  1 176 ? 117.793 77.491  -5.371  1.00   20.75  ? 176 GLN A CD  1 
ATOM   1257  O OE1 . GLN A  1 176 ? 118.922 77.796  -5.730  1.00   21.99  ? 176 GLN A OE1 1 
ATOM   1258  N NE2 . GLN A  1 176 ? 116.947 76.853  -6.158  1.00   20.31  ? 176 GLN A NE2 1 
ATOM   1259  N N   . LEU A  1 177 ? 115.664 81.992  -2.427  1.00   28.87  ? 177 LEU A N   1 
ATOM   1260  C CA  . LEU A  1 177 ? 115.596 83.440  -2.203  1.00   26.87  ? 177 LEU A CA  1 
ATOM   1261  C C   . LEU A  1 177 ? 115.736 83.782  -0.724  1.00   24.36  ? 177 LEU A C   1 
ATOM   1262  O O   . LEU A  1 177 ? 116.455 84.703  -0.383  1.00   27.65  ? 177 LEU A O   1 
ATOM   1263  C CB  . LEU A  1 177 ? 114.289 84.019  -2.732  1.00   26.41  ? 177 LEU A CB  1 
ATOM   1264  C CG  . LEU A  1 177 ? 114.055 83.956  -4.248  1.00   25.28  ? 177 LEU A CG  1 
ATOM   1265  C CD1 . LEU A  1 177 ? 112.672 84.428  -4.576  1.00   22.67  ? 177 LEU A CD1 1 
ATOM   1266  C CD2 . LEU A  1 177 ? 115.105 84.766  -5.035  1.00   27.75  ? 177 LEU A CD2 1 
ATOM   1267  N N   . PHE A  1 178 ? 115.061 83.047  0.154   1.00   22.35  ? 178 PHE A N   1 
ATOM   1268  C CA  . PHE A  1 178 ? 115.194 83.278  1.600   1.00   21.18  ? 178 PHE A CA  1 
ATOM   1269  C C   . PHE A  1 178 ? 116.642 83.258  2.021   1.00   23.45  ? 178 PHE A C   1 
ATOM   1270  O O   . PHE A  1 178 ? 117.126 84.123  2.748   1.00   25.08  ? 178 PHE A O   1 
ATOM   1271  C CB  . PHE A  1 178 ? 114.472 82.217  2.423   1.00   20.22  ? 178 PHE A CB  1 
ATOM   1272  C CG  . PHE A  1 178 ? 112.990 82.226  2.280   1.00   23.16  ? 178 PHE A CG  1 
ATOM   1273  C CD1 . PHE A  1 178 ? 112.324 83.337  1.792   1.00   23.56  ? 178 PHE A CD1 1 
ATOM   1274  C CD2 . PHE A  1 178 ? 112.255 81.137  2.674   1.00   21.37  ? 178 PHE A CD2 1 
ATOM   1275  C CE1 . PHE A  1 178 ? 110.954 83.340  1.667   1.00   23.76  ? 178 PHE A CE1 1 
ATOM   1276  C CE2 . PHE A  1 178 ? 110.876 81.135  2.570   1.00   24.57  ? 178 PHE A CE2 1 
ATOM   1277  C CZ  . PHE A  1 178 ? 110.222 82.244  2.062   1.00   23.01  ? 178 PHE A CZ  1 
ATOM   1278  N N   . SER A  1 179 ? 117.327 82.221  1.574   1.00   23.41  ? 179 SER A N   1 
ATOM   1279  C CA  . SER A  1 179 ? 118.643 81.953  2.080   1.00   27.78  ? 179 SER A CA  1 
ATOM   1280  C C   . SER A  1 179 ? 119.678 82.877  1.503   1.00   25.92  ? 179 SER A C   1 
ATOM   1281  O O   . SER A  1 179 ? 120.586 83.314  2.194   1.00   23.09  ? 179 SER A O   1 
ATOM   1282  C CB  . SER A  1 179 ? 119.003 80.482  1.804   1.00   33.06  ? 179 SER A CB  1 
ATOM   1283  O OG  . SER A  1 179 ? 119.295 80.234  0.438   1.00   39.44  ? 179 SER A OG  1 
ATOM   1284  N N   . HIS A  1 180 ? 119.514 83.212  0.238   1.00   24.71  ? 180 HIS A N   1 
ATOM   1285  C CA  . HIS A  1 180 ? 120.466 84.077  -0.418  1.00   26.19  ? 180 HIS A CA  1 
ATOM   1286  C C   . HIS A  1 180 ? 120.414 85.500  0.117   1.00   27.64  ? 180 HIS A C   1 
ATOM   1287  O O   . HIS A  1 180 ? 121.445 86.163  0.263   1.00   27.31  ? 180 HIS A O   1 
ATOM   1288  C CB  . HIS A  1 180 ? 120.231 84.090  -1.923  1.00   26.23  ? 180 HIS A CB  1 
ATOM   1289  C CG  . HIS A  1 180 ? 121.297 84.816  -2.658  1.00   24.84  ? 180 HIS A CG  1 
ATOM   1290  N ND1 . HIS A  1 180 ? 122.559 84.293  -2.848  1.00   28.20  ? 180 HIS A ND1 1 
ATOM   1291  C CD2 . HIS A  1 180 ? 121.327 86.065  -3.162  1.00   24.01  ? 180 HIS A CD2 1 
ATOM   1292  C CE1 . HIS A  1 180 ? 123.305 85.176  -3.483  1.00   27.47  ? 180 HIS A CE1 1 
ATOM   1293  N NE2 . HIS A  1 180 ? 122.581 86.262  -3.685  1.00   28.21  ? 180 HIS A NE2 1 
ATOM   1294  N N   . PHE A  1 181 ? 119.215 85.980  0.405   1.00   27.30  ? 181 PHE A N   1 
ATOM   1295  C CA  . PHE A  1 181 ? 119.081 87.356  0.826   1.00   26.94  ? 181 PHE A CA  1 
ATOM   1296  C C   . PHE A  1 181 ? 118.857 87.465  2.336   1.00   30.83  ? 181 PHE A C   1 
ATOM   1297  O O   . PHE A  1 181 ? 118.824 88.566  2.857   1.00   34.37  ? 181 PHE A O   1 
ATOM   1298  C CB  . PHE A  1 181 ? 117.954 88.072  0.040   1.00   25.33  ? 181 PHE A CB  1 
ATOM   1299  C CG  . PHE A  1 181 ? 118.261 88.259  -1.446  1.00   26.16  ? 181 PHE A CG  1 
ATOM   1300  C CD1 . PHE A  1 181 ? 119.162 89.234  -1.868  1.00   25.25  ? 181 PHE A CD1 1 
ATOM   1301  C CD2 . PHE A  1 181 ? 117.658 87.454  -2.417  1.00   25.82  ? 181 PHE A CD2 1 
ATOM   1302  C CE1 . PHE A  1 181 ? 119.465 89.388  -3.212  1.00   25.58  ? 181 PHE A CE1 1 
ATOM   1303  C CE2 . PHE A  1 181 ? 117.958 87.625  -3.778  1.00   23.84  ? 181 PHE A CE2 1 
ATOM   1304  C CZ  . PHE A  1 181 ? 118.862 88.581  -4.159  1.00   23.91  ? 181 PHE A CZ  1 
ATOM   1305  N N   . GLY A  1 182 ? 118.742 86.357  3.059   1.00   25.77  ? 182 GLY A N   1 
ATOM   1306  C CA  . GLY A  1 182 ? 118.520 86.473  4.496   1.00   23.09  ? 182 GLY A CA  1 
ATOM   1307  C C   . GLY A  1 182 ? 117.156 87.030  4.866   1.00   25.19  ? 182 GLY A C   1 
ATOM   1308  O O   . GLY A  1 182 ? 117.004 87.799  5.817   1.00   25.21  ? 182 GLY A O   1 
ATOM   1309  N N   . LEU A  1 183 ? 116.150 86.627  4.100   1.00   26.55  ? 183 LEU A N   1 
ATOM   1310  C CA  . LEU A  1 183 ? 114.765 87.075  4.291   1.00   25.19  ? 183 LEU A CA  1 
ATOM   1311  C C   . LEU A  1 183 ? 114.046 86.345  5.415   1.00   24.03  ? 183 LEU A C   1 
ATOM   1312  O O   . LEU A  1 183 ? 114.429 85.240  5.759   1.00   27.16  ? 183 LEU A O   1 
ATOM   1313  C CB  . LEU A  1 183 ? 113.973 86.871  3.006   1.00   24.15  ? 183 LEU A CB  1 
ATOM   1314  C CG  . LEU A  1 183 ? 114.558 87.490  1.734   1.00   25.13  ? 183 LEU A CG  1 
ATOM   1315  C CD1 . LEU A  1 183 ? 113.695 87.056  0.563   1.00   24.91  ? 183 LEU A CD1 1 
ATOM   1316  C CD2 . LEU A  1 183 ? 114.622 88.997  1.845   1.00   26.68  ? 183 LEU A CD2 1 
ATOM   1317  N N   . LYS A  1 184 ? 112.999 86.952  5.970   1.00   25.89  ? 184 LYS A N   1 
ATOM   1318  C CA  . LYS A  1 184 ? 112.069 86.234  6.852   1.00   27.02  ? 184 LYS A CA  1 
ATOM   1319  C C   . LYS A  1 184 ? 111.409 85.129  6.029   1.00   27.87  ? 184 LYS A C   1 
ATOM   1320  O O   . LYS A  1 184 ? 111.158 85.352  4.858   1.00   28.54  ? 184 LYS A O   1 
ATOM   1321  C CB  . LYS A  1 184 ? 111.033 87.190  7.453   1.00   29.76  ? 184 LYS A CB  1 
ATOM   1322  C CG  . LYS A  1 184 ? 109.868 86.491  8.139   1.00   34.28  ? 184 LYS A CG  1 
ATOM   1323  C CD  . LYS A  1 184 ? 109.125 87.406  9.080   1.00   42.10  ? 184 LYS A CD  1 
ATOM   1324  C CE  . LYS A  1 184 ? 107.899 86.745  9.722   1.00   47.16  ? 184 LYS A CE  1 
ATOM   1325  N NZ  . LYS A  1 184 ? 107.799 85.270  9.542   1.00   49.76  ? 184 LYS A NZ  1 
ATOM   1326  N N   . ARG A  1 185 ? 111.175 83.940  6.612   1.00   26.03  ? 185 ARG A N   1 
ATOM   1327  C CA  . ARG A  1 185 ? 110.597 82.787  5.893   1.00   25.05  ? 185 ARG A CA  1 
ATOM   1328  C C   . ARG A  1 185 ? 109.066 82.873  5.792   1.00   25.83  ? 185 ARG A C   1 
ATOM   1329  O O   . ARG A  1 185 ? 108.322 82.286  6.586   1.00   27.06  ? 185 ARG A O   1 
ATOM   1330  C CB  . ARG A  1 185 ? 111.025 81.470  6.550   1.00   24.86  ? 185 ARG A CB  1 
ATOM   1331  C CG  . ARG A  1 185 ? 112.560 81.319  6.632   1.00   26.07  ? 185 ARG A CG  1 
ATOM   1332  C CD  . ARG A  1 185 ? 113.013 79.945  7.133   1.00   27.53  ? 185 ARG A CD  1 
ATOM   1333  N NE  . ARG A  1 185 ? 112.834 78.908  6.127   1.00   29.43  ? 185 ARG A NE  1 
ATOM   1334  C CZ  . ARG A  1 185 ? 113.732 78.622  5.189   1.00   29.51  ? 185 ARG A CZ  1 
ATOM   1335  N NH1 . ARG A  1 185 ? 113.481 77.672  4.306   1.00   30.88  ? 185 ARG A NH1 1 
ATOM   1336  N NH2 . ARG A  1 185 ? 114.884 79.278  5.137   1.00   27.88  ? 185 ARG A NH2 1 
ATOM   1337  N N   . GLN A  1 186 ? 108.632 83.618  4.780   1.00   25.74  ? 186 GLN A N   1 
ATOM   1338  C CA  . GLN A  1 186 ? 107.241 83.944  4.548   1.00   26.41  ? 186 GLN A CA  1 
ATOM   1339  C C   . GLN A  1 186 ? 107.086 84.359  3.101   1.00   27.07  ? 186 GLN A C   1 
ATOM   1340  O O   . GLN A  1 186 ? 107.955 85.035  2.569   1.00   25.85  ? 186 GLN A O   1 
ATOM   1341  C CB  . GLN A  1 186 ? 106.836 85.054  5.488   1.00   27.89  ? 186 GLN A CB  1 
ATOM   1342  C CG  . GLN A  1 186 ? 105.440 85.549  5.437   1.00   30.13  ? 186 GLN A CG  1 
ATOM   1343  C CD  . GLN A  1 186 ? 105.339 86.847  6.193   1.00   32.64  ? 186 GLN A CD  1 
ATOM   1344  O OE1 . GLN A  1 186 ? 105.265 87.902  5.598   1.00   34.67  ? 186 GLN A OE1 1 
ATOM   1345  N NE2 . GLN A  1 186 ? 105.403 86.781  7.508   1.00   35.43  ? 186 GLN A NE2 1 
ATOM   1346  N N   . PHE A  1 187 ? 106.031 83.913  2.428   1.00   28.17  ? 187 PHE A N   1 
ATOM   1347  C CA  . PHE A  1 187 ? 105.704 84.494  1.131   1.00   27.07  ? 187 PHE A CA  1 
ATOM   1348  C C   . PHE A  1 187 ? 104.205 84.676  1.022   1.00   26.12  ? 187 PHE A C   1 
ATOM   1349  O O   . PHE A  1 187 ? 103.454 83.959  1.643   1.00   29.62  ? 187 PHE A O   1 
ATOM   1350  C CB  . PHE A  1 187 ? 106.260 83.653  -0.036  1.00   26.78  ? 187 PHE A CB  1 
ATOM   1351  C CG  . PHE A  1 187 ? 105.647 82.264  -0.187  1.00   28.00  ? 187 PHE A CG  1 
ATOM   1352  C CD1 . PHE A  1 187 ? 106.162 81.174  0.497   1.00   26.78  ? 187 PHE A CD1 1 
ATOM   1353  C CD2 . PHE A  1 187 ? 104.607 82.041  -1.068  1.00   27.42  ? 187 PHE A CD2 1 
ATOM   1354  C CE1 . PHE A  1 187 ? 105.630 79.913  0.327   1.00   26.34  ? 187 PHE A CE1 1 
ATOM   1355  C CE2 . PHE A  1 187 ? 104.085 80.765  -1.233  1.00   24.74  ? 187 PHE A CE2 1 
ATOM   1356  C CZ  . PHE A  1 187 ? 104.594 79.713  -0.541  1.00   24.62  ? 187 PHE A CZ  1 
ATOM   1357  N N   . SER A  1 188 ? 103.799 85.647  0.215   1.00   27.20  ? 188 SER A N   1 
ATOM   1358  C CA  . SER A  1 188 ? 102.417 86.057  0.106   1.00   30.47  ? 188 SER A CA  1 
ATOM   1359  C C   . SER A  1 188 ? 101.959 86.038  -1.335  1.00   33.67  ? 188 SER A C   1 
ATOM   1360  O O   . SER A  1 188 ? 102.630 86.607  -2.183  1.00   34.70  ? 188 SER A O   1 
ATOM   1361  C CB  . SER A  1 188 ? 102.247 87.458  0.647   1.00   30.21  ? 188 SER A CB  1 
ATOM   1362  O OG  . SER A  1 188 ? 102.663 87.511  1.982   1.00   32.72  ? 188 SER A OG  1 
ATOM   1363  N N   . VAL A  1 189 ? 100.770 85.483  -1.577  1.00   33.68  ? 189 VAL A N   1 
ATOM   1364  C CA  . VAL A  1 189 ? 100.234 85.308  -2.926  1.00   32.26  ? 189 VAL A CA  1 
ATOM   1365  C C   . VAL A  1 189 ? 98.981  86.152  -3.122  1.00   29.72  ? 189 VAL A C   1 
ATOM   1366  O O   . VAL A  1 189 ? 98.003  86.041  -2.381  1.00   29.29  ? 189 VAL A O   1 
ATOM   1367  C CB  . VAL A  1 189 ? 99.921  83.809  -3.198  1.00   29.68  ? 189 VAL A CB  1 
ATOM   1368  C CG1 . VAL A  1 189 ? 99.476  83.577  -4.642  1.00   31.24  ? 189 VAL A CG1 1 
ATOM   1369  C CG2 . VAL A  1 189 ? 101.127 82.977  -2.876  1.00   25.04  ? 189 VAL A CG2 1 
ATOM   1370  N N   . CYS A  1 190 ? 99.017  87.021  -4.120  1.00   31.39  ? 190 CYS A N   1 
ATOM   1371  C CA  . CYS A  1 190 ? 97.845  87.787  -4.464  1.00   35.61  ? 190 CYS A CA  1 
ATOM   1372  C C   . CYS A  1 190 ? 97.582  87.647  -5.961  1.00   37.43  ? 190 CYS A C   1 
ATOM   1373  O O   . CYS A  1 190 ? 98.015  88.478  -6.765  1.00   32.61  ? 190 CYS A O   1 
ATOM   1374  C CB  . CYS A  1 190 ? 98.001  89.275  -4.069  1.00   29.58  ? 190 CYS A CB  1 
ATOM   1375  S SG  . CYS A  1 190 ? 96.429  90.106  -3.670  1.00   39.84  ? 190 CYS A SG  1 
ATOM   1376  N N   . LEU A  1 191 ? 96.842  86.610  -6.332  1.00   38.65  ? 191 LEU A N   1 
ATOM   1377  C CA  . LEU A  1 191 ? 96.539  86.413  -7.742  1.00   39.72  ? 191 LEU A CA  1 
ATOM   1378  C C   . LEU A  1 191 ? 95.436  87.344  -8.234  1.00   41.21  ? 191 LEU A C   1 
ATOM   1379  O O   . LEU A  1 191 ? 94.448  87.577  -7.533  1.00   42.56  ? 191 LEU A O   1 
ATOM   1380  C CB  . LEU A  1 191 ? 96.140  84.963  -7.992  1.00   37.89  ? 191 LEU A CB  1 
ATOM   1381  C CG  . LEU A  1 191 ? 97.145  83.921  -7.515  1.00   35.12  ? 191 LEU A CG  1 
ATOM   1382  C CD1 . LEU A  1 191 ? 96.609  82.569  -7.929  1.00   35.25  ? 191 LEU A CD1 1 
ATOM   1383  C CD2 . LEU A  1 191 ? 98.596  84.163  -8.012  1.00   31.33  ? 191 LEU A CD2 1 
ATOM   1384  N N   . SER A  1 192 ? 95.604  87.867  -9.448  1.00   40.20  ? 192 SER A N   1 
ATOM   1385  C CA  . SER A  1 192 ? 94.576  88.681  -10.068 1.00   40.85  ? 192 SER A CA  1 
ATOM   1386  C C   . SER A  1 192 ? 93.660  87.821  -10.935 1.00   38.28  ? 192 SER A C   1 
ATOM   1387  O O   . SER A  1 192 ? 94.110  87.050  -11.768 1.00   38.14  ? 192 SER A O   1 
ATOM   1388  C CB  . SER A  1 192 ? 95.202  89.782  -10.913 1.00   42.51  ? 192 SER A CB  1 
ATOM   1389  O OG  . SER A  1 192 ? 94.199  90.498  -11.602 1.00   44.45  ? 192 SER A OG  1 
ATOM   1390  N N   . ARG A  1 193 ? 92.365  87.967  -10.740 1.00   39.74  ? 193 ARG A N   1 
ATOM   1391  C CA  . ARG A  1 193 ? 91.379  87.231  -11.509 1.00   53.37  ? 193 ARG A CA  1 
ATOM   1392  C C   . ARG A  1 193 ? 91.345  87.631  -12.992 1.00   55.63  ? 193 ARG A C   1 
ATOM   1393  O O   . ARG A  1 193 ? 90.782  86.905  -13.813 1.00   56.19  ? 193 ARG A O   1 
ATOM   1394  C CB  . ARG A  1 193 ? 90.015  87.395  -10.851 1.00   57.68  ? 193 ARG A CB  1 
ATOM   1395  C CG  . ARG A  1 193 ? 89.292  88.624  -11.264 1.00   66.90  ? 193 ARG A CG  1 
ATOM   1396  C CD  . ARG A  1 193 ? 87.871  88.627  -10.714 1.00   76.23  ? 193 ARG A CD  1 
ATOM   1397  N NE  . ARG A  1 193 ? 87.230  87.317  -10.807 1.00   82.58  ? 193 ARG A NE  1 
ATOM   1398  C CZ  . ARG A  1 193 ? 86.431  86.812  -9.867  1.00   85.46  ? 193 ARG A CZ  1 
ATOM   1399  N NH1 . ARG A  1 193 ? 86.162  87.512  -8.768  1.00   86.03  ? 193 ARG A NH1 1 
ATOM   1400  N NH2 . ARG A  1 193 ? 85.896  85.608  -10.020 1.00   85.58  ? 193 ARG A NH2 1 
ATOM   1401  N N   . TYR A  1 194 ? 91.910  88.797  -13.322 1.00   54.68  ? 194 TYR A N   1 
ATOM   1402  C CA  . TYR A  1 194 ? 91.841  89.332  -14.682 1.00   54.72  ? 194 TYR A CA  1 
ATOM   1403  C C   . TYR A  1 194 ? 93.118  89.052  -15.473 1.00   49.43  ? 194 TYR A C   1 
ATOM   1404  O O   . TYR A  1 194 ? 94.219  89.314  -15.004 1.00   45.56  ? 194 TYR A O   1 
ATOM   1405  C CB  . TYR A  1 194 ? 91.591  90.836  -14.663 1.00   58.71  ? 194 TYR A CB  1 
ATOM   1406  C CG  . TYR A  1 194 ? 90.519  91.286  -13.711 1.00   62.52  ? 194 TYR A CG  1 
ATOM   1407  C CD1 . TYR A  1 194 ? 89.174  91.163  -14.046 1.00   65.78  ? 194 TYR A CD1 1 
ATOM   1408  C CD2 . TYR A  1 194 ? 90.846  91.841  -12.477 1.00   63.76  ? 194 TYR A CD2 1 
ATOM   1409  C CE1 . TYR A  1 194 ? 88.176  91.580  -13.180 1.00   68.10  ? 194 TYR A CE1 1 
ATOM   1410  C CE2 . TYR A  1 194 ? 89.858  92.264  -11.601 1.00   67.00  ? 194 TYR A CE2 1 
ATOM   1411  C CZ  . TYR A  1 194 ? 88.520  92.129  -11.959 1.00   69.34  ? 194 TYR A CZ  1 
ATOM   1412  O OH  . TYR A  1 194 ? 87.532  92.538  -11.088 1.00   70.76  ? 194 TYR A OH  1 
ATOM   1413  N N   . SER A  1 195 ? 92.956  88.561  -16.698 1.00   50.54  ? 195 SER A N   1 
ATOM   1414  C CA  . SER A  1 195 ? 94.100  88.253  -17.539 1.00   50.06  ? 195 SER A CA  1 
ATOM   1415  C C   . SER A  1 195 ? 94.779  89.522  -17.996 1.00   52.72  ? 195 SER A C   1 
ATOM   1416  O O   . SER A  1 195 ? 95.941  89.495  -18.380 1.00   53.44  ? 195 SER A O   1 
ATOM   1417  C CB  . SER A  1 195 ? 93.686  87.391  -18.735 1.00   49.27  ? 195 SER A CB  1 
ATOM   1418  O OG  . SER A  1 195 ? 92.668  88.004  -19.495 1.00   53.46  ? 195 SER A OG  1 
ATOM   1419  N N   . THR A  1 196 ? 94.063  90.639  -17.908 1.00   56.01  ? 196 THR A N   1 
ATOM   1420  C CA  . THR A  1 196 ? 94.578  91.915  -18.385 1.00   58.39  ? 196 THR A CA  1 
ATOM   1421  C C   . THR A  1 196 ? 95.371  92.695  -17.328 1.00   59.03  ? 196 THR A C   1 
ATOM   1422  O O   . THR A  1 196 ? 95.903  93.759  -17.643 1.00   63.70  ? 196 THR A O   1 
ATOM   1423  C CB  . THR A  1 196 ? 93.450  92.833  -18.899 1.00   60.90  ? 196 THR A CB  1 
ATOM   1424  O OG1 . THR A  1 196 ? 92.539  93.092  -17.823 1.00   54.32  ? 196 THR A OG1 1 
ATOM   1425  C CG2 . THR A  1 196 ? 92.700  92.196  -20.078 1.00   57.22  ? 196 THR A CG2 1 
ATOM   1426  N N   . SER A  1 197 ? 95.469  92.189  -16.094 1.00   52.67  ? 197 SER A N   1 
ATOM   1427  C CA  . SER A  1 197 ? 96.298  92.855  -15.089 1.00   50.06  ? 197 SER A CA  1 
ATOM   1428  C C   . SER A  1 197 ? 96.962  91.835  -14.195 1.00   49.96  ? 197 SER A C   1 
ATOM   1429  O O   . SER A  1 197 ? 96.394  90.782  -13.893 1.00   51.42  ? 197 SER A O   1 
ATOM   1430  C CB  . SER A  1 197 ? 95.492  93.816  -14.230 1.00   52.82  ? 197 SER A CB  1 
ATOM   1431  O OG  . SER A  1 197 ? 94.503  93.117  -13.504 1.00   53.09  ? 197 SER A OG  1 
ATOM   1432  N N   . ASN A  1 198 ? 98.160  92.172  -13.739 1.00   49.46  ? 198 ASN A N   1 
ATOM   1433  C CA  . ASN A  1 198 ? 98.983  91.240  -12.993 1.00   47.60  ? 198 ASN A CA  1 
ATOM   1434  C C   . ASN A  1 198 ? 98.606  91.124  -11.531 1.00   47.99  ? 198 ASN A C   1 
ATOM   1435  O O   . ASN A  1 198 ? 98.109  92.078  -10.932 1.00   46.52  ? 198 ASN A O   1 
ATOM   1436  C CB  . ASN A  1 198 ? 100.460 91.650  -13.073 1.00   47.60  ? 198 ASN A CB  1 
ATOM   1437  C CG  . ASN A  1 198 ? 101.089 91.381  -14.440 1.00   50.86  ? 198 ASN A CG  1 
ATOM   1438  O OD1 . ASN A  1 198 ? 100.570 90.619  -15.257 1.00   52.33  ? 198 ASN A OD1 1 
ATOM   1439  N ND2 . ASN A  1 198 ? 102.211 92.027  -14.692 1.00   51.96  ? 198 ASN A ND2 1 
ATOM   1440  N N   . GLY A  1 199 ? 98.883  89.941  -10.971 1.00   49.79  ? 199 GLY A N   1 
ATOM   1441  C CA  . GLY A  1 199 ? 98.897  89.720  -9.537  1.00   46.39  ? 199 GLY A CA  1 
ATOM   1442  C C   . GLY A  1 199 ? 100.361 89.565  -9.147  1.00   43.25  ? 199 GLY A C   1 
ATOM   1443  O O   . GLY A  1 199 ? 101.253 89.754  -9.966  1.00   41.27  ? 199 GLY A O   1 
ATOM   1444  N N   . ALA A  1 200 ? 100.626 89.174  -7.914  1.00   42.08  ? 200 ALA A N   1 
ATOM   1445  C CA  . ALA A  1 200 ? 102.006 89.120  -7.482  1.00   40.36  ? 200 ALA A CA  1 
ATOM   1446  C C   . ALA A  1 200 ? 102.262 88.096  -6.418  1.00   36.10  ? 200 ALA A C   1 
ATOM   1447  O O   . ALA A  1 200 ? 101.355 87.650  -5.700  1.00   33.07  ? 200 ALA A O   1 
ATOM   1448  C CB  . ALA A  1 200 ? 102.456 90.497  -6.983  1.00   41.36  ? 200 ALA A CB  1 
ATOM   1449  N N   . ILE A  1 201 ? 103.527 87.708  -6.346  1.00   35.61  ? 201 ILE A N   1 
ATOM   1450  C CA  . ILE A  1 201 ? 104.030 87.002  -5.199  1.00   33.26  ? 201 ILE A CA  1 
ATOM   1451  C C   . ILE A  1 201 ? 105.129 87.846  -4.538  1.00   30.83  ? 201 ILE A C   1 
ATOM   1452  O O   . ILE A  1 201 ? 105.971 88.437  -5.199  1.00   30.37  ? 201 ILE A O   1 
ATOM   1453  C CB  . ILE A  1 201 ? 104.488 85.588  -5.594  1.00   32.40  ? 201 ILE A CB  1 
ATOM   1454  C CG1 . ILE A  1 201 ? 103.327 84.915  -6.322  1.00   35.86  ? 201 ILE A CG1 1 
ATOM   1455  C CG2 . ILE A  1 201 ? 104.822 84.775  -4.369  1.00   29.87  ? 201 ILE A CG2 1 
ATOM   1456  C CD1 . ILE A  1 201 ? 103.548 83.521  -6.667  1.00   38.85  ? 201 ILE A CD1 1 
ATOM   1457  N N   . LEU A  1 202 ? 105.049 87.928  -3.216  1.00   32.60  ? 202 LEU A N   1 
ATOM   1458  C CA  . LEU A  1 202 ? 105.962 88.705  -2.387  1.00   31.86  ? 202 LEU A CA  1 
ATOM   1459  C C   . LEU A  1 202 ? 106.772 87.789  -1.494  1.00   29.77  ? 202 LEU A C   1 
ATOM   1460  O O   . LEU A  1 202 ? 106.248 86.820  -0.968  1.00   28.75  ? 202 LEU A O   1 
ATOM   1461  C CB  . LEU A  1 202 ? 105.202 89.725  -1.527  1.00   31.66  ? 202 LEU A CB  1 
ATOM   1462  C CG  . LEU A  1 202 ? 104.921 91.091  -2.142  1.00   37.52  ? 202 LEU A CG  1 
ATOM   1463  C CD1 . LEU A  1 202 ? 103.967 91.007  -3.307  1.00   39.74  ? 202 LEU A CD1 1 
ATOM   1464  C CD2 . LEU A  1 202 ? 104.387 92.001  -1.089  1.00   40.47  ? 202 LEU A CD2 1 
ATOM   1465  N N   . PHE A  1 203 ? 108.065 88.072  -1.392  1.00   30.48  ? 203 PHE A N   1 
ATOM   1466  C CA  . PHE A  1 203 ? 109.000 87.281  -0.594  1.00   30.70  ? 203 PHE A CA  1 
ATOM   1467  C C   . PHE A  1 203 ? 109.667 88.074  0.510   1.00   32.70  ? 203 PHE A C   1 
ATOM   1468  O O   . PHE A  1 203 ? 110.409 88.997  0.235   1.00   33.66  ? 203 PHE A O   1 
ATOM   1469  C CB  . PHE A  1 203 ? 110.089 86.679  -1.495  1.00   29.61  ? 203 PHE A CB  1 
ATOM   1470  C CG  . PHE A  1 203 ? 109.541 85.814  -2.591  1.00   28.28  ? 203 PHE A CG  1 
ATOM   1471  C CD1 . PHE A  1 203 ? 109.316 84.463  -2.370  1.00   27.18  ? 203 PHE A CD1 1 
ATOM   1472  C CD2 . PHE A  1 203 ? 109.211 86.357  -3.824  1.00   29.02  ? 203 PHE A CD2 1 
ATOM   1473  C CE1 . PHE A  1 203 ? 108.805 83.661  -3.365  1.00   26.12  ? 203 PHE A CE1 1 
ATOM   1474  C CE2 . PHE A  1 203 ? 108.680 85.577  -4.827  1.00   28.65  ? 203 PHE A CE2 1 
ATOM   1475  C CZ  . PHE A  1 203 ? 108.484 84.218  -4.601  1.00   28.84  ? 203 PHE A CZ  1 
ATOM   1476  N N   . GLY A  1 204 ? 109.466 87.657  1.751   1.00   31.75  ? 204 GLY A N   1 
ATOM   1477  C CA  . GLY A  1 204 ? 110.012 88.363  2.882   1.00   33.48  ? 204 GLY A CA  1 
ATOM   1478  C C   . GLY A  1 204 ? 108.913 88.885  3.784   1.00   34.54  ? 204 GLY A C   1 
ATOM   1479  O O   . GLY A  1 204 ? 107.726 88.690  3.540   1.00   33.53  ? 204 GLY A O   1 
ATOM   1480  N N   . ASP A  1 205 ? 109.324 89.582  4.831   1.00   39.02  ? 205 ASP A N   1 
ATOM   1481  C CA  . ASP A  1 205 ? 108.398 90.052  5.847   1.00   41.71  ? 205 ASP A CA  1 
ATOM   1482  C C   . ASP A  1 205 ? 107.569 91.243  5.387   1.00   42.45  ? 205 ASP A C   1 
ATOM   1483  O O   . ASP A  1 205 ? 108.105 92.302  5.062   1.00   41.81  ? 205 ASP A O   1 
ATOM   1484  C CB  . ASP A  1 205 ? 109.168 90.429  7.096   1.00   43.79  ? 205 ASP A CB  1 
ATOM   1485  C CG  . ASP A  1 205 ? 108.269 90.755  8.261   1.00   47.13  ? 205 ASP A CG  1 
ATOM   1486  O OD1 . ASP A  1 205 ? 107.037 90.495  8.205   1.00   43.79  ? 205 ASP A OD1 1 
ATOM   1487  O OD2 . ASP A  1 205 ? 108.828 91.260  9.256   1.00   53.35  1 205 ASP A OD2 1 
ATOM   1488  N N   . ILE A  1 206 ? 106.253 91.086  5.408   1.00   43.49  ? 206 ILE A N   1 
ATOM   1489  C CA  . ILE A  1 206 ? 105.406 92.174  4.978   1.00   45.47  ? 206 ILE A CA  1 
ATOM   1490  C C   . ILE A  1 206 ? 105.009 93.053  6.141   1.00   54.75  ? 206 ILE A C   1 
ATOM   1491  O O   . ILE A  1 206 ? 104.300 94.032  5.956   1.00   61.84  ? 206 ILE A O   1 
ATOM   1492  C CB  . ILE A  1 206 ? 104.156 91.661  4.293   1.00   40.64  ? 206 ILE A CB  1 
ATOM   1493  C CG1 . ILE A  1 206 ? 103.517 90.576  5.143   1.00   39.26  ? 206 ILE A CG1 1 
ATOM   1494  C CG2 . ILE A  1 206 ? 104.485 91.098  2.941   1.00   37.84  ? 206 ILE A CG2 1 
ATOM   1495  C CD1 . ILE A  1 206 ? 102.250 90.052  4.564   1.00   38.47  ? 206 ILE A CD1 1 
ATOM   1496  N N   . ASN A  1 207 ? 105.464 92.722  7.341   1.00   57.81  ? 207 ASN A N   1 
ATOM   1497  C CA  . ASN A  1 207 ? 105.147 93.526  8.516   1.00   63.72  ? 207 ASN A CA  1 
ATOM   1498  C C   . ASN A  1 207 ? 106.436 94.145  8.960   1.00   69.88  ? 207 ASN A C   1 
ATOM   1499  O O   . ASN A  1 207 ? 106.653 94.383  10.139  1.00   76.95  ? 207 ASN A O   1 
ATOM   1500  C CB  . ASN A  1 207 ? 104.533 92.725  9.650   1.00   66.63  ? 207 ASN A CB  1 
ATOM   1501  C CG  . ASN A  1 207 ? 103.445 91.826  9.189   1.00   70.97  ? 207 ASN A CG  1 
ATOM   1502  O OD1 . ASN A  1 207 ? 102.314 92.262  8.997   1.00   73.82  ? 207 ASN A OD1 1 
ATOM   1503  N ND2 . ASN A  1 207 ? 103.751 90.535  9.081   1.00   72.01  ? 207 ASN A ND2 1 
ATOM   1504  N N   . ASP A  1 208 ? 107.296 94.411  7.998   1.00   67.46  ? 208 ASP A N   1 
ATOM   1505  C CA  . ASP A  1 208 ? 108.606 94.896  8.317   1.00   69.34  ? 208 ASP A CA  1 
ATOM   1506  C C   . ASP A  1 208 ? 108.597 96.365  7.990   1.00   75.15  ? 208 ASP A C   1 
ATOM   1507  O O   . ASP A  1 208 ? 108.401 96.743  6.838   1.00   75.20  ? 208 ASP A O   1 
ATOM   1508  C CB  . ASP A  1 208 ? 109.677 94.121  7.549   1.00   68.36  ? 208 ASP A CB  1 
ATOM   1509  C CG  . ASP A  1 208 ? 111.078 94.534  7.933   1.00   72.48  ? 208 ASP A CG  1 
ATOM   1510  O OD1 . ASP A  1 208 ? 111.217 95.473  8.746   1.00   78.87  1 208 ASP A OD1 1 
ATOM   1511  O OD2 . ASP A  1 208 ? 112.046 93.913  7.454   1.00   70.47  ? 208 ASP A OD2 1 
ATOM   1512  N N   . PRO A  1 209 ? 108.698 97.199  9.037   1.00   81.81  ? 209 PRO A N   1 
ATOM   1513  C CA  . PRO A  1 209 ? 108.691 98.670  8.995   1.00   85.74  ? 209 PRO A CA  1 
ATOM   1514  C C   . PRO A  1 209 ? 109.600 99.217  7.894   1.00   83.82  ? 209 PRO A C   1 
ATOM   1515  O O   . PRO A  1 209 ? 109.354 100.301 7.368   1.00   85.68  ? 209 PRO A O   1 
ATOM   1516  C CB  . PRO A  1 209 ? 109.214 99.070  10.383  1.00   90.23  ? 209 PRO A CB  1 
ATOM   1517  C CG  . PRO A  1 209 ? 109.886 97.823  10.925  1.00   88.33  ? 209 PRO A CG  1 
ATOM   1518  C CD  . PRO A  1 209 ? 109.085 96.694  10.367  1.00   83.01  ? 209 PRO A CD  1 
ATOM   1519  N N   . ASN A  1 210 ? 110.660 98.480  7.580   1.00   79.38  ? 210 ASN A N   1 
ATOM   1520  C CA  . ASN A  1 210 ? 111.524 98.849  6.477   1.00   79.76  ? 210 ASN A CA  1 
ATOM   1521  C C   . ASN A  1 210 ? 110.765 98.754  5.176   1.00   78.20  ? 210 ASN A C   1 
ATOM   1522  O O   . ASN A  1 210 ? 111.015 99.501  4.231   1.00   80.19  ? 210 ASN A O   1 
ATOM   1523  C CB  . ASN A  1 210 ? 112.733 97.927  6.377   1.00   80.17  ? 210 ASN A CB  1 
ATOM   1524  C CG  . ASN A  1 210 ? 113.642 98.034  7.554   1.00   86.50  ? 210 ASN A CG  1 
ATOM   1525  O OD1 . ASN A  1 210 ? 113.208 98.352  8.662   1.00   91.65  ? 210 ASN A OD1 1 
ATOM   1526  N ND2 . ASN A  1 210 ? 114.926 97.779  7.326   1.00   87.30  ? 210 ASN A ND2 1 
ATOM   1527  N N   . ASN A  1 211 ? 109.805 97.840  5.144   1.00   75.11  ? 211 ASN A N   1 
ATOM   1528  C CA  . ASN A  1 211 ? 109.076 97.623  3.922   1.00   74.11  ? 211 ASN A CA  1 
ATOM   1529  C C   . ASN A  1 211 ? 107.783 98.406  4.012   1.00   80.07  ? 211 ASN A C   1 
ATOM   1530  O O   . ASN A  1 211 ? 106.950 98.317  3.116   1.00   82.81  ? 211 ASN A O   1 
ATOM   1531  C CB  . ASN A  1 211 ? 108.784 96.119  3.697   1.00   65.47  ? 211 ASN A CB  1 
ATOM   1532  C CG  . ASN A  1 211 ? 110.054 95.252  3.641   1.00   60.88  ? 211 ASN A CG  1 
ATOM   1533  O OD1 . ASN A  1 211 ? 111.091 95.646  3.084   1.00   58.50  ? 211 ASN A OD1 1 
ATOM   1534  N ND2 . ASN A  1 211 ? 109.959 94.048  4.209   1.00   59.42  ? 211 ASN A ND2 1 
ATOM   1535  N N   . ASN A  1 212 ? 107.655 99.234  5.049   1.00   81.37  ? 212 ASN A N   1 
ATOM   1536  C CA  . ASN A  1 212 ? 106.414 99.956  5.293   1.00   80.70  ? 212 ASN A CA  1 
ATOM   1537  C C   . ASN A  1 212 ? 106.025 100.792 4.090   1.00   77.53  ? 212 ASN A C   1 
ATOM   1538  O O   . ASN A  1 212 ? 104.852 100.957 3.789   1.00   78.17  ? 212 ASN A O   1 
ATOM   1539  C CB  . ASN A  1 212 ? 106.547 100.848 6.530   1.00   88.81  ? 212 ASN A CB  1 
ATOM   1540  C CG  . ASN A  1 212 ? 105.206 101.334 7.068   1.00   94.34  ? 212 ASN A CG  1 
ATOM   1541  O OD1 . ASN A  1 212 ? 104.224 101.458 6.337   1.00   93.50  ? 212 ASN A OD1 1 
ATOM   1542  N ND2 . ASN A  1 212 ? 105.166 101.611 8.366   1.00   99.91  ? 212 ASN A ND2 1 
ATOM   1543  N N   . ASN A  1 213 ? 107.010 101.283 3.362   1.00   74.46  ? 213 ASN A N   1 
ATOM   1544  C CA  . ASN A  1 213 ? 106.682 102.176 2.279   1.00   73.74  ? 213 ASN A CA  1 
ATOM   1545  C C   . ASN A  1 213 ? 106.084 101.472 1.067   1.00   69.02  ? 213 ASN A C   1 
ATOM   1546  O O   . ASN A  1 213 ? 105.153 101.983 0.447   1.00   71.56  ? 213 ASN A O   1 
ATOM   1547  C CB  . ASN A  1 213 ? 107.936 102.918 1.896   1.00   75.30  ? 213 ASN A CB  1 
ATOM   1548  C CG  . ASN A  1 213 ? 108.389 103.821 2.990   1.00   78.42  ? 213 ASN A CG  1 
ATOM   1549  O OD1 . ASN A  1 213 ? 107.574 104.478 3.627   1.00   80.84  ? 213 ASN A OD1 1 
ATOM   1550  N ND2 . ASN A  1 213 ? 109.686 103.809 3.273   1.00   78.39  ? 213 ASN A ND2 1 
ATOM   1551  N N   . TYR A  1 214 ? 106.585 100.284 0.745   1.00   60.50  ? 214 TYR A N   1 
ATOM   1552  C CA  . TYR A  1 214 ? 106.029 99.554  -0.382  1.00   54.93  ? 214 TYR A CA  1 
ATOM   1553  C C   . TYR A  1 214 ? 104.669 98.982  -0.042  1.00   53.70  ? 214 TYR A C   1 
ATOM   1554  O O   . TYR A  1 214 ? 103.766 98.957  -0.880  1.00   54.26  ? 214 TYR A O   1 
ATOM   1555  C CB  . TYR A  1 214 ? 106.954 98.419  -0.826  1.00   50.25  ? 214 TYR A CB  1 
ATOM   1556  C CG  . TYR A  1 214 ? 106.459 97.719  -2.078  1.00   47.32  ? 214 TYR A CG  1 
ATOM   1557  C CD1 . TYR A  1 214 ? 106.635 98.293  -3.331  1.00   50.42  ? 214 TYR A CD1 1 
ATOM   1558  C CD2 . TYR A  1 214 ? 105.792 96.495  -2.004  1.00   44.51  ? 214 TYR A CD2 1 
ATOM   1559  C CE1 . TYR A  1 214 ? 106.171 97.671  -4.474  1.00   49.17  ? 214 TYR A CE1 1 
ATOM   1560  C CE2 . TYR A  1 214 ? 105.328 95.860  -3.148  1.00   44.81  ? 214 TYR A CE2 1 
ATOM   1561  C CZ  . TYR A  1 214 ? 105.524 96.465  -4.380  1.00   47.65  ? 214 TYR A CZ  1 
ATOM   1562  O OH  . TYR A  1 214 ? 105.083 95.867  -5.532  1.00   47.70  ? 214 TYR A OH  1 
ATOM   1563  N N   . ILE A  1 215 ? 104.528 98.540  1.204   1.00   53.24  ? 215 ILE A N   1 
ATOM   1564  C CA  . ILE A  1 215 ? 103.322 97.845  1.635   1.00   54.56  ? 215 ILE A CA  1 
ATOM   1565  C C   . ILE A  1 215 ? 102.323 98.781  2.341   1.00   58.99  ? 215 ILE A C   1 
ATOM   1566  O O   . ILE A  1 215 ? 101.304 98.331  2.851   1.00   59.79  ? 215 ILE A O   1 
ATOM   1567  C CB  . ILE A  1 215 ? 103.669 96.614  2.552   1.00   55.08  ? 215 ILE A CB  1 
ATOM   1568  C CG1 . ILE A  1 215 ? 104.446 97.005  3.810   1.00   59.34  ? 215 ILE A CG1 1 
ATOM   1569  C CG2 . ILE A  1 215 ? 104.471 95.604  1.780   1.00   50.93  ? 215 ILE A CG2 1 
ATOM   1570  C CD1 . ILE A  1 215 ? 103.632 97.085  5.062   1.00   62.20  ? 215 ILE A CD1 1 
ATOM   1571  N N   . HIS A  1 216 ? 102.594 100.081 2.332   1.00   61.38  ? 216 HIS A N   1 
ATOM   1572  C CA  . HIS A  1 216 ? 101.741 101.030 3.039   1.00   63.77  ? 216 HIS A CA  1 
ATOM   1573  C C   . HIS A  1 216 ? 100.291 100.941 2.600   1.00   61.09  ? 216 HIS A C   1 
ATOM   1574  O O   . HIS A  1 216 ? 99.384  101.022 3.418   1.00   53.84  ? 216 HIS A O   1 
ATOM   1575  C CB  . HIS A  1 216 ? 102.247 102.460 2.838   1.00   71.64  ? 216 HIS A CB  1 
ATOM   1576  C CG  . HIS A  1 216 ? 101.423 103.495 3.544   1.00   79.93  ? 216 HIS A CG  1 
ATOM   1577  N ND1 . HIS A  1 216 ? 100.406 104.191 2.918   1.00   83.31  ? 216 HIS A ND1 1 
ATOM   1578  C CD2 . HIS A  1 216 ? 101.435 103.930 4.827   1.00   82.84  ? 216 HIS A CD2 1 
ATOM   1579  C CE1 . HIS A  1 216 ? 99.841  105.018 3.779   1.00   85.74  ? 216 HIS A CE1 1 
ATOM   1580  N NE2 . HIS A  1 216 ? 100.445 104.878 4.946   1.00   85.93  ? 216 HIS A NE2 1 
ATOM   1581  N N   . ASN A  1 217 ? 100.077 100.745 1.310   1.00   60.64  ? 217 ASN A N   1 
ATOM   1582  C CA  . ASN A  1 217 ? 98.730  100.697 0.770   1.00   63.95  ? 217 ASN A CA  1 
ATOM   1583  C C   . ASN A  1 217 ? 97.913  99.475  1.181   1.00   63.76  ? 217 ASN A C   1 
ATOM   1584  O O   . ASN A  1 217 ? 96.690  99.447  1.026   1.00   65.27  ? 217 ASN A O   1 
ATOM   1585  C CB  . ASN A  1 217 ? 98.799  100.761 -0.752  1.00   65.83  ? 217 ASN A CB  1 
ATOM   1586  C CG  . ASN A  1 217 ? 97.432  100.780 -1.391  1.00   67.15  ? 217 ASN A CG  1 
ATOM   1587  O OD1 . ASN A  1 217 ? 96.672  101.736 -1.237  1.00   69.57  ? 217 ASN A OD1 1 
ATOM   1588  N ND2 . ASN A  1 217 ? 97.105  99.716  -2.105  1.00   65.14  ? 217 ASN A ND2 1 
ATOM   1589  N N   . SER A  1 218 ? 98.580  98.463  1.716   1.00   60.89  ? 218 SER A N   1 
ATOM   1590  C CA  . SER A  1 218 ? 97.886  97.244  2.089   1.00   54.60  ? 218 SER A CA  1 
ATOM   1591  C C   . SER A  1 218 ? 97.682  97.104  3.593   1.00   53.24  ? 218 SER A C   1 
ATOM   1592  O O   . SER A  1 218 ? 97.148  96.101  4.047   1.00   52.68  ? 218 SER A O   1 
ATOM   1593  C CB  . SER A  1 218 ? 98.661  96.028  1.564   1.00   49.15  ? 218 SER A CB  1 
ATOM   1594  O OG  . SER A  1 218 ? 99.775  95.735  2.389   1.00   47.16  ? 218 SER A OG  1 
ATOM   1595  N N   . LEU A  1 219 ? 98.051  98.123  4.358   1.00   52.81  ? 219 LEU A N   1 
ATOM   1596  C CA  . LEU A  1 219 ? 98.134  97.999  5.812   1.00   50.72  ? 219 LEU A CA  1 
ATOM   1597  C C   . LEU A  1 219 ? 96.809  97.662  6.493   1.00   50.05  ? 219 LEU A C   1 
ATOM   1598  O O   . LEU A  1 219 ? 96.803  96.988  7.522   1.00   47.60  ? 219 LEU A O   1 
ATOM   1599  C CB  . LEU A  1 219 ? 98.689  99.292  6.418   1.00   53.01  ? 219 LEU A CB  1 
ATOM   1600  C CG  . LEU A  1 219 ? 100.200 99.486  6.334   1.00   53.95  ? 219 LEU A CG  1 
ATOM   1601  C CD1 . LEU A  1 219 ? 100.598 100.861 6.817   1.00   57.40  ? 219 LEU A CD1 1 
ATOM   1602  C CD2 . LEU A  1 219 ? 100.936 98.411  7.121   1.00   52.91  ? 219 LEU A CD2 1 
ATOM   1603  N N   . ASP A  1 220 ? 95.694  98.139  5.948   1.00   53.78  ? 220 ASP A N   1 
ATOM   1604  C CA  . ASP A  1 220 ? 94.393  97.831  6.550   1.00   57.27  ? 220 ASP A CA  1 
ATOM   1605  C C   . ASP A  1 220 ? 94.047  96.367  6.318   1.00   47.40  ? 220 ASP A C   1 
ATOM   1606  O O   . ASP A  1 220 ? 93.519  95.704  7.201   1.00   44.93  ? 220 ASP A O   1 
ATOM   1607  C CB  . ASP A  1 220 ? 93.283  98.762  6.022   1.00   68.20  ? 220 ASP A CB  1 
ATOM   1608  C CG  . ASP A  1 220 ? 93.411  99.069  4.529   1.00   76.10  ? 220 ASP A CG  1 
ATOM   1609  O OD1 . ASP A  1 220 ? 94.303  98.472  3.867   1.00   76.80  ? 220 ASP A OD1 1 
ATOM   1610  O OD2 . ASP A  1 220 ? 92.623  99.926  4.029   1.00   79.14  ? 220 ASP A OD2 1 
ATOM   1611  N N   . VAL A  1 221 ? 94.386  95.851  5.144   1.00   44.40  ? 221 VAL A N   1 
ATOM   1612  C CA  . VAL A  1 221 ? 94.171  94.438  4.841   1.00   41.13  ? 221 VAL A CA  1 
ATOM   1613  C C   . VAL A  1 221 ? 94.983  93.546  5.788   1.00   40.80  ? 221 VAL A C   1 
ATOM   1614  O O   . VAL A  1 221 ? 94.471  92.538  6.276   1.00   38.17  ? 221 VAL A O   1 
ATOM   1615  C CB  . VAL A  1 221 ? 94.543  94.114  3.380   1.00   40.11  ? 221 VAL A CB  1 
ATOM   1616  C CG1 . VAL A  1 221 ? 94.293  92.644  3.070   1.00   31.93  ? 221 VAL A CG1 1 
ATOM   1617  C CG2 . VAL A  1 221 ? 93.775  95.016  2.421   1.00   39.46  ? 221 VAL A CG2 1 
ATOM   1618  N N   . LEU A  1 222 ? 96.241  93.913  6.032   1.00   35.93  ? 222 LEU A N   1 
ATOM   1619  C CA  . LEU A  1 222 ? 97.136  93.143  6.897   1.00   36.38  ? 222 LEU A CA  1 
ATOM   1620  C C   . LEU A  1 222 ? 96.707  93.069  8.355   1.00   40.95  ? 222 LEU A C   1 
ATOM   1621  O O   . LEU A  1 222 ? 96.870  92.047  9.006   1.00   42.40  ? 222 LEU A O   1 
ATOM   1622  C CB  . LEU A  1 222 ? 98.534  93.743  6.856   1.00   39.18  ? 222 LEU A CB  1 
ATOM   1623  C CG  . LEU A  1 222 ? 99.218  93.708  5.503   1.00   39.12  ? 222 LEU A CG  1 
ATOM   1624  C CD1 . LEU A  1 222 ? 100.615 94.271  5.629   1.00   40.00  ? 222 LEU A CD1 1 
ATOM   1625  C CD2 . LEU A  1 222 ? 99.250  92.290  5.037   1.00   37.84  ? 222 LEU A CD2 1 
ATOM   1626  N N   . HIS A  1 223 ? 96.170  94.169  8.868   1.00   47.99  ? 223 HIS A N   1 
ATOM   1627  C CA  . HIS A  1 223 ? 95.714  94.262  10.259  1.00   53.85  ? 223 HIS A CA  1 
ATOM   1628  C C   . HIS A  1 223 ? 94.583  93.270  10.547  1.00   49.45  ? 223 HIS A C   1 
ATOM   1629  O O   . HIS A  1 223 ? 94.479  92.754  11.657  1.00   48.77  ? 223 HIS A O   1 
ATOM   1630  C CB  . HIS A  1 223 ? 95.267  95.709  10.559  1.00   63.31  ? 223 HIS A CB  1 
ATOM   1631  C CG  . HIS A  1 223 ? 94.796  95.951  11.972  1.00   73.66  ? 223 HIS A CG  1 
ATOM   1632  N ND1 . HIS A  1 223 ? 95.635  95.920  13.068  1.00   78.03  ? 223 HIS A ND1 1 
ATOM   1633  C CD2 . HIS A  1 223 ? 93.564  96.248  12.461  1.00   77.51  ? 223 HIS A CD2 1 
ATOM   1634  C CE1 . HIS A  1 223 ? 94.943  96.178  14.166  1.00   80.59  ? 223 HIS A CE1 1 
ATOM   1635  N NE2 . HIS A  1 223 ? 93.681  96.376  13.826  1.00   80.31  ? 223 HIS A NE2 1 
ATOM   1636  N N   . ASP A  1 224 ? 93.767  92.980  9.533   1.00   46.47  ? 224 ASP A N   1 
ATOM   1637  C CA  . ASP A  1 224 ? 92.557  92.171  9.711   1.00   45.11  ? 224 ASP A CA  1 
ATOM   1638  C C   . ASP A  1 224 ? 92.740  90.753  9.246   1.00   39.53  ? 224 ASP A C   1 
ATOM   1639  O O   . ASP A  1 224 ? 91.767  90.022  9.150   1.00   39.29  ? 224 ASP A O   1 
ATOM   1640  C CB  . ASP A  1 224 ? 91.345  92.736  8.936   1.00   48.67  ? 224 ASP A CB  1 
ATOM   1641  C CG  . ASP A  1 224 ? 90.906  94.127  9.387   1.00   50.99  ? 224 ASP A CG  1 
ATOM   1642  O OD1 . ASP A  1 224 ? 91.226  94.568  10.511  1.00   55.30  ? 224 ASP A OD1 1 
ATOM   1643  O OD2 . ASP A  1 224 ? 90.201  94.778  8.588   1.00   48.88  1 224 ASP A OD2 1 
ATOM   1644  N N   . LEU A  1 225 ? 93.979  90.363  8.957   1.00   38.63  ? 225 LEU A N   1 
ATOM   1645  C CA  . LEU A  1 225 ? 94.274  89.005  8.513   1.00   36.14  ? 225 LEU A CA  1 
ATOM   1646  C C   . LEU A  1 225 ? 93.817  87.991  9.548   1.00   35.16  ? 225 LEU A C   1 
ATOM   1647  O O   . LEU A  1 225 ? 93.930  88.218  10.750  1.00   38.38  ? 225 LEU A O   1 
ATOM   1648  C CB  . LEU A  1 225 ? 95.770  88.810  8.264   1.00   34.92  ? 225 LEU A CB  1 
ATOM   1649  C CG  . LEU A  1 225 ? 96.429  89.300  6.986   1.00   35.99  ? 225 LEU A CG  1 
ATOM   1650  C CD1 . LEU A  1 225 ? 97.869  88.851  6.936   1.00   37.76  ? 225 LEU A CD1 1 
ATOM   1651  C CD2 . LEU A  1 225 ? 95.703  88.769  5.788   1.00   34.44  ? 225 LEU A CD2 1 
ATOM   1652  N N   . VAL A  1 226 ? 93.297  86.879  9.061   1.00   32.15  ? 226 VAL A N   1 
ATOM   1653  C CA  . VAL A  1 226 ? 92.880  85.749  9.882   1.00   31.90  ? 226 VAL A CA  1 
ATOM   1654  C C   . VAL A  1 226 ? 93.798  84.558  9.565   1.00   29.84  ? 226 VAL A C   1 
ATOM   1655  O O   . VAL A  1 226 ? 94.151  84.375  8.409   1.00   28.31  ? 226 VAL A O   1 
ATOM   1656  C CB  . VAL A  1 226 ? 91.383  85.422  9.609   1.00   37.98  ? 226 VAL A CB  1 
ATOM   1657  C CG1 . VAL A  1 226 ? 91.042  84.029  10.009  1.00   41.91  ? 226 VAL A CG1 1 
ATOM   1658  C CG2 . VAL A  1 226 ? 90.478  86.410  10.329  1.00   38.12  ? 226 VAL A CG2 1 
ATOM   1659  N N   . TYR A  1 227 ? 94.207  83.778  10.574  1.00   32.32  ? 227 TYR A N   1 
ATOM   1660  C CA  . TYR A  1 227 ? 95.183  82.679  10.374  1.00   31.84  ? 227 TYR A CA  1 
ATOM   1661  C C   . TYR A  1 227 ? 94.639  81.274  10.714  1.00   34.69  ? 227 TYR A C   1 
ATOM   1662  O O   . TYR A  1 227 ? 93.757  81.120  11.554  1.00   38.92  ? 227 TYR A O   1 
ATOM   1663  C CB  . TYR A  1 227 ? 96.437  82.913  11.214  1.00   30.65  ? 227 TYR A CB  1 
ATOM   1664  C CG  . TYR A  1 227 ? 97.179  84.167  10.878  1.00   32.43  ? 227 TYR A CG  1 
ATOM   1665  C CD1 . TYR A  1 227 ? 98.131  84.188  9.895   1.00   33.72  ? 227 TYR A CD1 1 
ATOM   1666  C CD2 . TYR A  1 227 ? 96.894  85.343  11.549  1.00   36.95  ? 227 TYR A CD2 1 
ATOM   1667  C CE1 . TYR A  1 227 ? 98.801  85.344  9.594   1.00   37.56  ? 227 TYR A CE1 1 
ATOM   1668  C CE2 . TYR A  1 227 ? 97.545  86.497  11.261  1.00   41.86  ? 227 TYR A CE2 1 
ATOM   1669  C CZ  . TYR A  1 227 ? 98.503  86.496  10.281  1.00   42.73  ? 227 TYR A CZ  1 
ATOM   1670  O OH  . TYR A  1 227 ? 99.168  87.668  9.998   1.00   47.66  ? 227 TYR A OH  1 
ATOM   1671  N N   . THR A  1 228 ? 95.194  80.246  10.084  1.00   32.29  ? 228 THR A N   1 
ATOM   1672  C CA  . THR A  1 228 ? 94.836  78.877  10.403  1.00   30.14  ? 228 THR A CA  1 
ATOM   1673  C C   . THR A  1 228 ? 96.106  78.059  10.260  1.00   29.15  ? 228 THR A C   1 
ATOM   1674  O O   . THR A  1 228 ? 96.984  78.441  9.503   1.00   31.09  ? 228 THR A O   1 
ATOM   1675  C CB  . THR A  1 228 ? 93.691  78.361  9.474   1.00   34.71  ? 228 THR A CB  1 
ATOM   1676  O OG1 . THR A  1 228 ? 93.168  77.108  9.946   1.00   38.33  ? 228 THR A OG1 1 
ATOM   1677  C CG2 . THR A  1 228 ? 94.183  78.188  8.072   1.00   32.06  ? 228 THR A CG2 1 
ATOM   1678  N N   . PRO A  1 229 ? 96.231  76.951  11.009  1.00   28.59  ? 229 PRO A N   1 
ATOM   1679  C CA  . PRO A  1 229 ? 97.465  76.158  10.947  1.00   28.82  ? 229 PRO A CA  1 
ATOM   1680  C C   . PRO A  1 229 ? 97.793  75.562  9.562   1.00   27.07  ? 229 PRO A C   1 
ATOM   1681  O O   . PRO A  1 229 ? 96.924  75.088  8.843   1.00   27.08  ? 229 PRO A O   1 
ATOM   1682  C CB  . PRO A  1 229 ? 97.191  75.034  11.947  1.00   29.65  ? 229 PRO A CB  1 
ATOM   1683  C CG  . PRO A  1 229 ? 96.202  75.639  12.903  1.00   29.95  ? 229 PRO A CG  1 
ATOM   1684  C CD  . PRO A  1 229 ? 95.328  76.475  12.072  1.00   28.37  ? 229 PRO A CD  1 
ATOM   1685  N N   . LEU A  1 230 ? 99.073  75.572  9.218   1.00   26.58  ? 230 LEU A N   1 
ATOM   1686  C CA  . LEU A  1 230 ? 99.529  75.033  7.948   1.00   26.37  ? 230 LEU A CA  1 
ATOM   1687  C C   . LEU A  1 230 ? 100.221 73.696  8.181   1.00   27.53  ? 230 LEU A C   1 
ATOM   1688  O O   . LEU A  1 230 ? 101.114 73.588  9.027   1.00   30.94  ? 230 LEU A O   1 
ATOM   1689  C CB  . LEU A  1 230 ? 100.468 76.035  7.269   1.00   29.66  ? 230 LEU A CB  1 
ATOM   1690  C CG  . LEU A  1 230 ? 101.157 75.722  5.935   1.00   30.21  ? 230 LEU A CG  1 
ATOM   1691  C CD1 . LEU A  1 230 ? 100.120 75.510  4.815   1.00   27.48  ? 230 LEU A CD1 1 
ATOM   1692  C CD2 . LEU A  1 230 ? 102.169 76.847  5.565   1.00   26.90  ? 230 LEU A CD2 1 
ATOM   1693  N N   . THR A  1 231 ? 99.813  72.676  7.439   1.00   26.48  ? 231 THR A N   1 
ATOM   1694  C CA  . THR A  1 231 ? 100.482 71.398  7.510   1.00   25.09  ? 231 THR A CA  1 
ATOM   1695  C C   . THR A  1 231 ? 101.002 71.026  6.118   1.00   25.59  ? 231 THR A C   1 
ATOM   1696  O O   . THR A  1 231 ? 100.474 71.472  5.105   1.00   26.11  ? 231 THR A O   1 
ATOM   1697  C CB  . THR A  1 231 ? 99.573  70.300  8.060   1.00   26.60  ? 231 THR A CB  1 
ATOM   1698  O OG1 . THR A  1 231 ? 98.305  70.348  7.409   1.00   26.43  ? 231 THR A OG1 1 
ATOM   1699  C CG2 . THR A  1 231 ? 99.388  70.473  9.558   1.00   28.94  ? 231 THR A CG2 1 
ATOM   1700  N N   . ILE A  1 232 ? 102.058 70.215  6.107   1.00   27.90  ? 232 ILE A N   1 
ATOM   1701  C CA  . ILE A  1 232 ? 102.845 69.915  4.920   1.00   26.60  ? 232 ILE A CA  1 
ATOM   1702  C C   . ILE A  1 232 ? 102.924 68.422  4.713   1.00   26.54  ? 232 ILE A C   1 
ATOM   1703  O O   . ILE A  1 232 ? 103.270 67.705  5.626   1.00   29.08  ? 232 ILE A O   1 
ATOM   1704  C CB  . ILE A  1 232 ? 104.271 70.489  5.073   1.00   26.22  ? 232 ILE A CB  1 
ATOM   1705  C CG1 . ILE A  1 232 ? 104.210 71.992  5.388   1.00   21.58  ? 232 ILE A CG1 1 
ATOM   1706  C CG2 . ILE A  1 232 ? 105.097 70.223  3.822   1.00   27.65  ? 232 ILE A CG2 1 
ATOM   1707  C CD1 . ILE A  1 232 ? 103.602 72.824  4.264   1.00   18.23  ? 232 ILE A CD1 1 
ATOM   1708  N N   . SER A  1 233 ? 102.603 67.942  3.520   1.00   26.04  ? 233 SER A N   1 
ATOM   1709  C CA  . SER A  1 233 ? 102.693 66.510  3.264   1.00   27.84  ? 233 SER A CA  1 
ATOM   1710  C C   . SER A  1 233 ? 104.113 66.096  3.035   1.00   29.75  ? 233 SER A C   1 
ATOM   1711  O O   . SER A  1 233 ? 104.994 66.934  2.856   1.00   29.98  ? 233 SER A O   1 
ATOM   1712  C CB  . SER A  1 233 ? 101.846 66.119  2.062   1.00   29.72  ? 233 SER A CB  1 
ATOM   1713  O OG  . SER A  1 233 ? 102.424 66.624  0.880   1.00   30.91  ? 233 SER A OG  1 
ATOM   1714  N N   . LYS A  1 234 ? 104.328 64.792  3.009   1.00   33.08  ? 234 LYS A N   1 
ATOM   1715  C CA  . LYS A  1 234 ? 105.668 64.282  2.782   1.00   39.78  ? 234 LYS A CA  1 
ATOM   1716  C C   . LYS A  1 234 ? 106.169 64.648  1.403   1.00   37.48  ? 234 LYS A C   1 
ATOM   1717  O O   . LYS A  1 234 ? 107.367 64.628  1.179   1.00   35.75  ? 234 LYS A O   1 
ATOM   1718  C CB  . LYS A  1 234 ? 105.708 62.776  3.030   1.00   49.42  ? 234 LYS A CB  1 
ATOM   1719  C CG  . LYS A  1 234 ? 105.460 62.507  4.504   1.00   58.24  ? 234 LYS A CG  1 
ATOM   1720  C CD  . LYS A  1 234 ? 105.273 61.049  4.857   1.00   66.54  ? 234 LYS A CD  1 
ATOM   1721  C CE  . LYS A  1 234 ? 104.885 60.925  6.342   1.00   71.23  ? 234 LYS A CE  1 
ATOM   1722  N NZ  . LYS A  1 234 ? 103.660 61.729  6.697   1.00   71.17  ? 234 LYS A NZ  1 
ATOM   1723  N N   . GLN A  1 235 ? 105.273 65.071  0.511   1.00   37.32  ? 235 GLN A N   1 
ATOM   1724  C CA  . GLN A  1 235 ? 105.691 65.463  -0.820  1.00   36.91  ? 235 GLN A CA  1 
ATOM   1725  C C   . GLN A  1 235 ? 105.902 66.964  -0.921  1.00   32.95  ? 235 GLN A C   1 
ATOM   1726  O O   . GLN A  1 235 ? 106.298 67.464  -1.964  1.00   31.09  ? 235 GLN A O   1 
ATOM   1727  C CB  . GLN A  1 235 ? 104.637 65.051  -1.835  1.00   40.92  ? 235 GLN A CB  1 
ATOM   1728  C CG  . GLN A  1 235 ? 104.574 63.579  -2.084  1.00   51.41  ? 235 GLN A CG  1 
ATOM   1729  C CD  . GLN A  1 235 ? 105.861 63.032  -2.652  1.00   62.58  ? 235 GLN A CD  1 
ATOM   1730  O OE1 . GLN A  1 235 ? 106.522 63.673  -3.474  1.00   66.07  ? 235 GLN A OE1 1 
ATOM   1731  N NE2 . GLN A  1 235 ? 106.229 61.832  -2.217  1.00   67.84  ? 235 GLN A NE2 1 
ATOM   1732  N N   . GLY A  1 236 ? 105.712 67.672  0.186   1.00   31.75  ? 236 GLY A N   1 
ATOM   1733  C CA  . GLY A  1 236 ? 105.938 69.108  0.226   1.00   27.26  ? 236 GLY A CA  1 
ATOM   1734  C C   . GLY A  1 236 ? 104.770 70.007  -0.140  1.00   26.37  ? 236 GLY A C   1 
ATOM   1735  O O   . GLY A  1 236 ? 104.952 71.189  -0.421  1.00   26.49  ? 236 GLY A O   1 
ATOM   1736  N N   . GLU A  1 237 ? 103.561 69.461  -0.105  1.00   27.27  ? 237 GLU A N   1 
ATOM   1737  C CA  . GLU A  1 237 ? 102.354 70.213  -0.445  1.00   26.44  ? 237 GLU A CA  1 
ATOM   1738  C C   . GLU A  1 237 ? 101.715 70.933  0.739   1.00   26.03  ? 237 GLU A C   1 
ATOM   1739  O O   . GLU A  1 237 ? 101.810 70.488  1.881   1.00   26.47  ? 237 GLU A O   1 
ATOM   1740  C CB  . GLU A  1 237 ? 101.322 69.284  -1.063  1.00   27.83  ? 237 GLU A CB  1 
ATOM   1741  C CG  . GLU A  1 237 ? 101.788 68.537  -2.270  1.00   28.67  ? 237 GLU A CG  1 
ATOM   1742  C CD  . GLU A  1 237 ? 101.062 67.239  -2.380  1.00   35.06  ? 237 GLU A CD  1 
ATOM   1743  O OE1 . GLU A  1 237 ? 101.208 66.429  -1.443  1.00   38.76  ? 237 GLU A OE1 1 
ATOM   1744  O OE2 . GLU A  1 237 ? 100.353 67.015  -3.379  1.00   37.20  1 237 GLU A OE2 1 
ATOM   1745  N N   . TYR A  1 238 ? 101.020 72.024  0.430   1.00   24.48  ? 238 TYR A N   1 
ATOM   1746  C CA  . TYR A  1 238 ? 100.383 72.874  1.429   1.00   25.94  ? 238 TYR A CA  1 
ATOM   1747  C C   . TYR A  1 238 ? 98.962  72.444  1.711   1.00   26.43  ? 238 TYR A C   1 
ATOM   1748  O O   . TYR A  1 238 ? 98.169  72.333  0.786   1.00   24.88  ? 238 TYR A O   1 
ATOM   1749  C CB  . TYR A  1 238 ? 100.400 74.337  0.968   1.00   25.12  ? 238 TYR A CB  1 
ATOM   1750  C CG  . TYR A  1 238 ? 101.794 74.901  0.784   1.00   23.35  ? 238 TYR A CG  1 
ATOM   1751  C CD1 . TYR A  1 238 ? 102.553 75.268  1.881   1.00   23.79  ? 238 TYR A CD1 1 
ATOM   1752  C CD2 . TYR A  1 238 ? 102.350 75.065  -0.484  1.00   23.81  ? 238 TYR A CD2 1 
ATOM   1753  C CE1 . TYR A  1 238 ? 103.828 75.784  1.731   1.00   26.53  ? 238 TYR A CE1 1 
ATOM   1754  C CE2 . TYR A  1 238 ? 103.643 75.585  -0.644  1.00   22.13  ? 238 TYR A CE2 1 
ATOM   1755  C CZ  . TYR A  1 238 ? 104.371 75.933  0.469   1.00   25.40  ? 238 TYR A CZ  1 
ATOM   1756  O OH  . TYR A  1 238 ? 105.656 76.434  0.349   1.00   29.16  ? 238 TYR A OH  1 
ATOM   1757  N N   . PHE A  1 239 ? 98.670  72.201  2.996   1.00   27.22  ? 239 PHE A N   1 
ATOM   1758  C CA  . PHE A  1 239 ? 97.349  71.759  3.455   1.00   26.57  ? 239 PHE A CA  1 
ATOM   1759  C C   . PHE A  1 239 ? 96.824  72.612  4.584   1.00   25.46  ? 239 PHE A C   1 
ATOM   1760  O O   . PHE A  1 239 ? 97.581  73.016  5.458   1.00   26.84  ? 239 PHE A O   1 
ATOM   1761  C CB  . PHE A  1 239 ? 97.395  70.317  3.957   1.00   25.59  ? 239 PHE A CB  1 
ATOM   1762  C CG  . PHE A  1 239 ? 97.443  69.318  2.875   1.00   28.26  ? 239 PHE A CG  1 
ATOM   1763  C CD1 . PHE A  1 239 ? 98.648  68.940  2.330   1.00   29.01  ? 239 PHE A CD1 1 
ATOM   1764  C CD2 . PHE A  1 239 ? 96.284  68.790  2.352   1.00   30.43  ? 239 PHE A CD2 1 
ATOM   1765  C CE1 . PHE A  1 239 ? 98.700  68.034  1.296   1.00   28.69  ? 239 PHE A CE1 1 
ATOM   1766  C CE2 . PHE A  1 239 ? 96.336  67.880  1.312   1.00   29.54  ? 239 PHE A CE2 1 
ATOM   1767  C CZ  . PHE A  1 239 ? 97.552  67.506  0.787   1.00   27.70  ? 239 PHE A CZ  1 
ATOM   1768  N N   . ILE A  1 240 ? 95.517  72.838  4.598   1.00   27.27  ? 240 ILE A N   1 
ATOM   1769  C CA  . ILE A  1 240 ? 94.854  73.364  5.781   1.00   26.35  ? 240 ILE A CA  1 
ATOM   1770  C C   . ILE A  1 240 ? 93.712  72.454  6.162   1.00   29.58  ? 240 ILE A C   1 
ATOM   1771  O O   . ILE A  1 240 ? 93.314  71.589  5.391   1.00   31.30  ? 240 ILE A O   1 
ATOM   1772  C CB  . ILE A  1 240 ? 94.296  74.780  5.588   1.00   25.32  ? 240 ILE A CB  1 
ATOM   1773  C CG1 . ILE A  1 240 ? 93.323  74.805  4.404   1.00   24.09  ? 240 ILE A CG1 1 
ATOM   1774  C CG2 . ILE A  1 240 ? 95.430  75.773  5.443   1.00   25.90  ? 240 ILE A CG2 1 
ATOM   1775  C CD1 . ILE A  1 240 ? 92.524  76.069  4.262   1.00   22.90  ? 240 ILE A CD1 1 
ATOM   1776  N N   . GLN A  1 241 ? 93.169  72.681  7.352   1.00   29.06  ? 241 GLN A N   1 
ATOM   1777  C CA  . GLN A  1 241 ? 92.109  71.846  7.874   1.00   29.12  ? 241 GLN A CA  1 
ATOM   1778  C C   . GLN A  1 241 ? 90.733  72.505  7.756   1.00   29.87  ? 241 GLN A C   1 
ATOM   1779  O O   . GLN A  1 241 ? 90.501  73.577  8.313   1.00   29.22  ? 241 GLN A O   1 
ATOM   1780  C CB  . GLN A  1 241 ? 92.416  71.486  9.329   1.00   32.62  ? 241 GLN A CB  1 
ATOM   1781  C CG  . GLN A  1 241 ? 91.287  70.780  10.028  1.00   38.39  ? 241 GLN A CG  1 
ATOM   1782  C CD  . GLN A  1 241 ? 90.868  69.507  9.321   1.00   40.03  ? 241 GLN A CD  1 
ATOM   1783  O OE1 . GLN A  1 241 ? 91.652  68.905  8.597   1.00   39.68  ? 241 GLN A OE1 1 
ATOM   1784  N NE2 . GLN A  1 241 ? 89.624  69.089  9.530   1.00   41.89  ? 241 GLN A NE2 1 
ATOM   1785  N N   . VAL A  1 242 ? 89.838  71.866  7.002   1.00   28.76  ? 242 VAL A N   1 
ATOM   1786  C CA  . VAL A  1 242 ? 88.447  72.301  6.904   1.00   27.29  ? 242 VAL A CA  1 
ATOM   1787  C C   . VAL A  1 242 ? 87.475  71.342  7.629   1.00   30.32  ? 242 VAL A C   1 
ATOM   1788  O O   . VAL A  1 242 ? 87.311  70.202  7.201   1.00   32.07  ? 242 VAL A O   1 
ATOM   1789  C CB  . VAL A  1 242 ? 88.036  72.425  5.448   1.00   26.14  ? 242 VAL A CB  1 
ATOM   1790  C CG1 . VAL A  1 242 ? 86.574  72.775  5.348   1.00   27.42  ? 242 VAL A CG1 1 
ATOM   1791  C CG2 . VAL A  1 242 ? 88.878  73.477  4.757   1.00   25.35  ? 242 VAL A CG2 1 
ATOM   1792  N N   . ASN A  1 243 ? 86.837  71.794  8.709   1.00   27.00  ? 243 ASN A N   1 
ATOM   1793  C CA  . ASN A  1 243 ? 85.923  70.959  9.489   1.00   29.34  ? 243 ASN A CA  1 
ATOM   1794  C C   . ASN A  1 243 ? 84.559  70.765  8.820   1.00   30.26  ? 243 ASN A C   1 
ATOM   1795  O O   . ASN A  1 243 ? 83.898  69.740  8.991   1.00   28.95  ? 243 ASN A O   1 
ATOM   1796  C CB  . ASN A  1 243 ? 85.732  71.567  10.882  1.00   32.55  ? 243 ASN A CB  1 
ATOM   1797  C CG  . ASN A  1 243 ? 86.847  71.193  11.850  1.00   38.55  ? 243 ASN A CG  1 
ATOM   1798  O OD1 . ASN A  1 243 ? 87.802  70.495  11.505  1.00   40.11  ? 243 ASN A OD1 1 
ATOM   1799  N ND2 . ASN A  1 243 ? 86.720  71.654  13.075  1.00   42.04  ? 243 ASN A ND2 1 
ATOM   1800  N N   . ALA A  1 244 ? 84.147  71.780  8.062   1.00   32.56  ? 244 ALA A N   1 
ATOM   1801  C CA  . ALA A  1 244 ? 82.878  71.761  7.354   1.00   28.12  ? 244 ALA A CA  1 
ATOM   1802  C C   . ALA A  1 244 ? 82.835  72.779  6.233   1.00   30.73  ? 244 ALA A C   1 
ATOM   1803  O O   . ALA A  1 244 ? 83.514  73.804  6.260   1.00   24.93  ? 244 ALA A O   1 
ATOM   1804  C CB  . ALA A  1 244 ? 81.752  72.020  8.306   1.00   27.31  ? 244 ALA A CB  1 
ATOM   1805  N N   . ILE A  1 245 ? 82.009  72.492  5.236   1.00   34.08  ? 245 ILE A N   1 
ATOM   1806  C CA  . ILE A  1 245 ? 81.601  73.513  4.290   1.00   30.74  ? 245 ILE A CA  1 
ATOM   1807  C C   . ILE A  1 245 ? 80.169  73.894  4.616   1.00   33.20  ? 245 ILE A C   1 
ATOM   1808  O O   . ILE A  1 245 ? 79.254  73.084  4.501   1.00   30.43  ? 245 ILE A O   1 
ATOM   1809  C CB  . ILE A  1 245 ? 81.678  73.045  2.856   1.00   30.96  ? 245 ILE A CB  1 
ATOM   1810  C CG1 . ILE A  1 245 ? 83.068  72.462  2.572   1.00   32.29  ? 245 ILE A CG1 1 
ATOM   1811  C CG2 . ILE A  1 245 ? 81.332  74.200  1.920   1.00   28.15  ? 245 ILE A CG2 1 
ATOM   1812  C CD1 . ILE A  1 245 ? 83.165  71.651  1.280   1.00   33.79  ? 245 ILE A CD1 1 
ATOM   1813  N N   . ARG A  1 246 ? 79.971  75.155  4.976   1.00   33.79  ? 246 ARG A N   1 
ATOM   1814  C CA  . ARG A  1 246 ? 78.667  75.593  5.388   1.00   30.74  ? 246 ARG A CA  1 
ATOM   1815  C C   . ARG A  1 246 ? 77.930  76.297  4.259   1.00   31.18  ? 246 ARG A C   1 
ATOM   1816  O O   . ARG A  1 246 ? 78.468  77.175  3.610   1.00   34.01  ? 246 ARG A O   1 
ATOM   1817  C CB  . ARG A  1 246 ? 78.785  76.497  6.603   1.00   31.93  ? 246 ARG A CB  1 
ATOM   1818  C CG  . ARG A  1 246 ? 77.434  76.983  7.082   1.00   38.35  ? 246 ARG A CG  1 
ATOM   1819  C CD  . ARG A  1 246 ? 77.502  77.714  8.411   1.00   42.47  ? 246 ARG A CD  1 
ATOM   1820  N NE  . ARG A  1 246 ? 78.311  78.928  8.326   1.00   44.23  ? 246 ARG A NE  1 
ATOM   1821  C CZ  . ARG A  1 246 ? 79.008  79.428  9.344   1.00   45.61  ? 246 ARG A CZ  1 
ATOM   1822  N NH1 . ARG A  1 246 ? 79.727  80.528  9.195   1.00   42.87  ? 246 ARG A NH1 1 
ATOM   1823  N NH2 . ARG A  1 246 ? 78.986  78.824  10.521  1.00   49.32  ? 246 ARG A NH2 1 
ATOM   1824  N N   . VAL A  1 247 ? 76.690  75.885  4.037   1.00   31.90  ? 247 VAL A N   1 
ATOM   1825  C CA  . VAL A  1 247 ? 75.753  76.561  3.138   1.00   34.52  ? 247 VAL A CA  1 
ATOM   1826  C C   . VAL A  1 247 ? 74.527  76.999  3.922   1.00   33.45  ? 247 VAL A C   1 
ATOM   1827  O O   . VAL A  1 247 ? 73.709  76.164  4.298   1.00   35.59  ? 247 VAL A O   1 
ATOM   1828  C CB  . VAL A  1 247 ? 75.273  75.642  1.996   1.00   35.81  ? 247 VAL A CB  1 
ATOM   1829  C CG1 . VAL A  1 247 ? 74.289  76.392  1.126   1.00   33.47  ? 247 VAL A CG1 1 
ATOM   1830  C CG2 . VAL A  1 247 ? 76.455  75.067  1.197   1.00   30.09  ? 247 VAL A CG2 1 
ATOM   1831  N N   . ASN A  1 248 ? 74.385  78.297  4.158   1.00   33.73  ? 248 ASN A N   1 
ATOM   1832  C CA  . ASN A  1 248 ? 73.372  78.783  5.091   1.00   36.31  ? 248 ASN A CA  1 
ATOM   1833  C C   . ASN A  1 248 ? 73.467  78.070  6.451   1.00   36.53  ? 248 ASN A C   1 
ATOM   1834  O O   . ASN A  1 248 ? 74.448  78.247  7.165   1.00   36.45  ? 248 ASN A O   1 
ATOM   1835  C CB  . ASN A  1 248 ? 71.972  78.619  4.517   1.00   41.70  ? 248 ASN A CB  1 
ATOM   1836  C CG  . ASN A  1 248 ? 71.696  79.555  3.370   1.00   45.37  ? 248 ASN A CG  1 
ATOM   1837  O OD1 . ASN A  1 248 ? 72.361  80.582  3.198   1.00   44.10  ? 248 ASN A OD1 1 
ATOM   1838  N ND2 . ASN A  1 248 ? 70.702  79.205  2.568   1.00   48.70  ? 248 ASN A ND2 1 
ATOM   1839  N N   . LYS A  1 249 ? 72.471  77.258  6.809   1.00   38.82  ? 249 LYS A N   1 
ATOM   1840  C CA  . LYS A  1 249 ? 72.542  76.516  8.074   1.00   38.62  ? 249 LYS A CA  1 
ATOM   1841  C C   . LYS A  1 249 ? 72.751  75.014  7.928   1.00   37.11  ? 249 LYS A C   1 
ATOM   1842  O O   . LYS A  1 249 ? 72.543  74.251  8.873   1.00   35.84  ? 249 LYS A O   1 
ATOM   1843  C CB  . LYS A  1 249 ? 71.282  76.773  8.912   1.00   40.45  ? 249 LYS A CB  1 
ATOM   1844  C CG  . LYS A  1 249 ? 70.909  78.251  9.048   1.00   40.23  ? 249 LYS A CG  1 
ATOM   1845  C CD  . LYS A  1 249 ? 69.813  78.433  10.074  1.00   43.08  ? 249 LYS A CD  1 
ATOM   1846  C CE  . LYS A  1 249 ? 69.003  79.690  9.854   1.00   49.13  ? 249 LYS A CE  1 
ATOM   1847  N NZ  . LYS A  1 249 ? 68.023  79.884  10.983  1.00   53.60  ? 249 LYS A NZ  1 
ATOM   1848  N N   . HIS A  1 250 ? 73.218  74.609  6.757   1.00   36.63  ? 250 HIS A N   1 
ATOM   1849  C CA  . HIS A  1 250 ? 73.518  73.218  6.506   1.00   35.33  ? 250 HIS A CA  1 
ATOM   1850  C C   . HIS A  1 250 ? 75.038  73.032  6.471   1.00   34.81  ? 250 HIS A C   1 
ATOM   1851  O O   . HIS A  1 250 ? 75.707  73.608  5.617   1.00   33.35  ? 250 HIS A O   1 
ATOM   1852  C CB  . HIS A  1 250 ? 72.841  72.829  5.183   1.00   36.23  ? 250 HIS A CB  1 
ATOM   1853  C CG  . HIS A  1 250 ? 71.335  72.909  5.232   1.00   37.43  ? 250 HIS A CG  1 
ATOM   1854  N ND1 . HIS A  1 250 ? 70.538  72.791  4.112   1.00   38.77  ? 250 HIS A ND1 1 
ATOM   1855  C CD2 . HIS A  1 250 ? 70.487  73.117  6.271   1.00   37.63  ? 250 HIS A CD2 1 
ATOM   1856  C CE1 . HIS A  1 250 ? 69.269  72.911  4.458   1.00   39.88  ? 250 HIS A CE1 1 
ATOM   1857  N NE2 . HIS A  1 250 ? 69.211  73.114  5.762   1.00   39.56  ? 250 HIS A NE2 1 
ATOM   1858  N N   . LEU A  1 251 ? 75.581  72.154  7.322   1.00   35.29  ? 251 LEU A N   1 
ATOM   1859  C CA  . LEU A  1 251 ? 77.033  71.967  7.378   1.00   32.65  ? 251 LEU A CA  1 
ATOM   1860  C C   . LEU A  1 251 ? 77.471  70.606  6.875   1.00   32.43  ? 251 LEU A C   1 
ATOM   1861  O O   . LEU A  1 251 ? 77.131  69.578  7.446   1.00   35.76  ? 251 LEU A O   1 
ATOM   1862  C CB  . LEU A  1 251 ? 77.552  72.183  8.797   1.00   32.52  ? 251 LEU A CB  1 
ATOM   1863  C CG  . LEU A  1 251 ? 77.487  73.641  9.246   1.00   33.62  ? 251 LEU A CG  1 
ATOM   1864  C CD1 . LEU A  1 251 ? 76.220  73.915  10.000  1.00   34.13  ? 251 LEU A CD1 1 
ATOM   1865  C CD2 . LEU A  1 251 ? 78.664  73.991  10.096  1.00   33.25  ? 251 LEU A CD2 1 
ATOM   1866  N N   . VAL A  1 252 ? 78.293  70.646  5.834   1.00   29.76  ? 252 VAL A N   1 
ATOM   1867  C CA  . VAL A  1 252 ? 78.838  69.474  5.167   1.00   32.42  ? 252 VAL A CA  1 
ATOM   1868  C C   . VAL A  1 252 ? 80.177  69.164  5.765   1.00   31.49  ? 252 VAL A C   1 
ATOM   1869  O O   . VAL A  1 252 ? 81.072  69.980  5.701   1.00   31.64  ? 252 VAL A O   1 
ATOM   1870  C CB  . VAL A  1 252 ? 78.987  69.703  3.651   1.00   30.04  ? 252 VAL A CB  1 
ATOM   1871  C CG1 . VAL A  1 252 ? 79.474  68.456  2.956   1.00   31.07  ? 252 VAL A CG1 1 
ATOM   1872  C CG2 . VAL A  1 252 ? 77.665  70.108  3.071   1.00   31.26  ? 252 VAL A CG2 1 
ATOM   1873  N N   . ILE A  1 253 ? 80.297  67.983  6.366   1.00   35.09  ? 253 ILE A N   1 
ATOM   1874  C CA  . ILE A  1 253 ? 81.490  67.624  7.108   1.00   37.01  ? 253 ILE A CA  1 
ATOM   1875  C C   . ILE A  1 253 ? 82.337  66.711  6.249   1.00   42.11  ? 253 ILE A C   1 
ATOM   1876  O O   . ILE A  1 253 ? 81.952  65.581  6.001   1.00   46.20  ? 253 ILE A O   1 
ATOM   1877  C CB  . ILE A  1 253 ? 81.180  66.887  8.421   1.00   38.54  ? 253 ILE A CB  1 
ATOM   1878  C CG1 . ILE A  1 253 ? 80.060  67.565  9.223   1.00   38.39  ? 253 ILE A CG1 1 
ATOM   1879  C CG2 . ILE A  1 253 ? 82.461  66.716  9.222   1.00   40.78  ? 253 ILE A CG2 1 
ATOM   1880  C CD1 . ILE A  1 253 ? 80.259  69.018  9.477   1.00   37.49  ? 253 ILE A CD1 1 
ATOM   1881  N N   . PRO A  1 254 ? 83.476  67.217  5.748   1.00   42.79  ? 254 PRO A N   1 
ATOM   1882  C CA  . PRO A  1 254 ? 84.379  66.454  4.882   1.00   47.09  ? 254 PRO A CA  1 
ATOM   1883  C C   . PRO A  1 254 ? 85.059  65.287  5.597   1.00   54.03  ? 254 PRO A C   1 
ATOM   1884  O O   . PRO A  1 254 ? 85.029  65.237  6.823   1.00   54.46  ? 254 PRO A O   1 
ATOM   1885  C CB  . PRO A  1 254 ? 85.415  67.498  4.449   1.00   40.29  ? 254 PRO A CB  1 
ATOM   1886  C CG  . PRO A  1 254 ? 84.816  68.790  4.775   1.00   37.65  ? 254 PRO A CG  1 
ATOM   1887  C CD  . PRO A  1 254 ? 83.990  68.572  5.983   1.00   38.69  ? 254 PRO A CD  1 
ATOM   1888  N N   . THR A  1 255 ? 85.637  64.389  4.794   1.00   62.48  ? 255 THR A N   1 
ATOM   1889  C CA  . THR A  1 255 ? 86.460  63.202  5.143   1.00   69.17  ? 255 THR A CA  1 
ATOM   1890  C C   . THR A  1 255 ? 85.607  61.962  4.935   1.00   74.86  ? 255 THR A C   1 
ATOM   1891  O O   . THR A  1 255 ? 84.944  61.842  3.900   1.00   76.62  ? 255 THR A O   1 
ATOM   1892  C CB  . THR A  1 255 ? 87.074  63.196  6.595   1.00   95.97  ? 255 THR A CB  1 
ATOM   1893  O OG1 . THR A  1 255 ? 86.031  63.143  7.577   1.00   98.64  ? 255 THR A OG1 1 
ATOM   1894  C CG2 . THR A  1 255 ? 87.992  64.408  6.853   1.00   92.19  ? 255 THR A CG2 1 
ATOM   1895  N N   . GLU A  1 272 ? 97.910  65.517  12.824  1.00   67.31  ? 272 GLU A N   1 
ATOM   1896  C CA  . GLU A  1 272 ? 97.262  65.164  11.555  1.00   63.11  ? 272 GLU A CA  1 
ATOM   1897  C C   . GLU A  1 272 ? 97.318  66.255  10.464  1.00   56.46  ? 272 GLU A C   1 
ATOM   1898  O O   . GLU A  1 272 ? 97.124  67.439  10.756  1.00   53.82  ? 272 GLU A O   1 
ATOM   1899  C CB  . GLU A  1 272 ? 95.805  64.785  11.813  1.00   63.87  ? 272 GLU A CB  1 
ATOM   1900  C CG  . GLU A  1 272 ? 95.632  63.498  12.569  1.00   70.54  ? 272 GLU A CG  1 
ATOM   1901  C CD  . GLU A  1 272 ? 96.069  62.295  11.743  1.00   76.71  ? 272 GLU A CD  1 
ATOM   1902  O OE1 . GLU A  1 272 ? 96.217  62.436  10.508  1.00   76.38  ? 272 GLU A OE1 1 
ATOM   1903  O OE2 . GLU A  1 272 ? 96.226  61.196  12.312  1.00   82.28  ? 272 GLU A OE2 1 
ATOM   1904  N N   . ILE A  1 273 ? 97.581  65.835  9.219   1.00   52.66  ? 273 ILE A N   1 
ATOM   1905  C CA  . ILE A  1 273 ? 97.637  66.741  8.060   1.00   49.66  ? 273 ILE A CA  1 
ATOM   1906  C C   . ILE A  1 273 ? 96.238  67.234  7.740   1.00   45.82  ? 273 ILE A C   1 
ATOM   1907  O O   . ILE A  1 273 ? 95.286  66.469  7.819   1.00   46.42  ? 273 ILE A O   1 
ATOM   1908  C CB  . ILE A  1 273 ? 98.247  66.051  6.798   1.00   37.71  ? 273 ILE A CB  1 
ATOM   1909  C CG1 . ILE A  1 273 ? 99.680  65.620  7.076   1.00   43.91  ? 273 ILE A CG1 1 
ATOM   1910  C CG2 . ILE A  1 273 ? 98.344  66.996  5.615   1.00   33.20  ? 273 ILE A CG2 1 
ATOM   1911  C CD1 . ILE A  1 273 ? 100.407 65.063  5.866   1.00   47.01  ? 273 ILE A CD1 1 
ATOM   1912  N N   . GLY A  1 274 ? 96.126  68.503  7.365   1.00   40.17  ? 274 GLY A N   1 
ATOM   1913  C CA  . GLY A  1 274 ? 94.853  69.071  6.992   1.00   34.34  ? 274 GLY A CA  1 
ATOM   1914  C C   . GLY A  1 274 ? 94.269  68.332  5.811   1.00   31.22  ? 274 GLY A C   1 
ATOM   1915  O O   . GLY A  1 274 ? 94.982  67.669  5.080   1.00   31.88  ? 274 GLY A O   1 
ATOM   1916  N N   . GLY A  1 275 ? 92.967  68.470  5.608   1.00   30.47  ? 275 GLY A N   1 
ATOM   1917  C CA  . GLY A  1 275 ? 92.303  67.734  4.556   1.00   31.47  ? 275 GLY A CA  1 
ATOM   1918  C C   . GLY A  1 275 ? 92.118  68.505  3.271   1.00   32.52  ? 275 GLY A C   1 
ATOM   1919  O O   . GLY A  1 275 ? 91.756  67.916  2.253   1.00   33.32  ? 275 GLY A O   1 
ATOM   1920  N N   . ALA A  1 276 ? 92.385  69.808  3.305   1.00   27.82  ? 276 ALA A N   1 
ATOM   1921  C CA  . ALA A  1 276 ? 92.207  70.642  2.124   1.00   29.21  ? 276 ALA A CA  1 
ATOM   1922  C C   . ALA A  1 276 ? 93.563  71.093  1.524   1.00   27.16  ? 276 ALA A C   1 
ATOM   1923  O O   . ALA A  1 276 ? 94.345  71.808  2.151   1.00   27.25  ? 276 ALA A O   1 
ATOM   1924  C CB  . ALA A  1 276 ? 91.328  71.859  2.448   1.00   25.95  ? 276 ALA A CB  1 
ATOM   1925  N N   . LEU A  1 277 ? 93.814  70.651  0.297   1.00   26.31  ? 277 LEU A N   1 
ATOM   1926  C CA  . LEU A  1 277 ? 94.986  71.028  -0.444  1.00   24.86  ? 277 LEU A CA  1 
ATOM   1927  C C   . LEU A  1 277 ? 94.805  72.409  -0.980  1.00   25.94  ? 277 LEU A C   1 
ATOM   1928  O O   . LEU A  1 277 ? 93.712  72.775  -1.380  1.00   27.30  ? 277 LEU A O   1 
ATOM   1929  C CB  . LEU A  1 277 ? 95.227  70.049  -1.584  1.00   24.09  ? 277 LEU A CB  1 
ATOM   1930  C CG  . LEU A  1 277 ? 96.321  70.390  -2.603  1.00   25.01  ? 277 LEU A CG  1 
ATOM   1931  C CD1 . LEU A  1 277 ? 97.717  70.248  -2.044  1.00   22.03  ? 277 LEU A CD1 1 
ATOM   1932  C CD2 . LEU A  1 277 ? 96.189  69.505  -3.807  1.00   26.23  ? 277 LEU A CD2 1 
ATOM   1933  N N   . ILE A  1 278 ? 95.886  73.173  -0.981  1.00   27.10  ? 278 ILE A N   1 
ATOM   1934  C CA  . ILE A  1 278 ? 95.951  74.437  -1.699  1.00   23.67  ? 278 ILE A CA  1 
ATOM   1935  C C   . ILE A  1 278 ? 96.888  74.285  -2.880  1.00   25.69  ? 278 ILE A C   1 
ATOM   1936  O O   . ILE A  1 278 ? 98.015  73.803  -2.740  1.00   28.09  ? 278 ILE A O   1 
ATOM   1937  C CB  . ILE A  1 278 ? 96.418  75.560  -0.798  1.00   23.30  ? 278 ILE A CB  1 
ATOM   1938  C CG1 . ILE A  1 278 ? 95.548  75.625  0.465   1.00   23.87  ? 278 ILE A CG1 1 
ATOM   1939  C CG2 . ILE A  1 278 ? 96.371  76.869  -1.529  1.00   25.06  ? 278 ILE A CG2 1 
ATOM   1940  C CD1 . ILE A  1 278 ? 96.093  76.582  1.496   1.00   25.60  ? 278 ILE A CD1 1 
ATOM   1941  N N   . THR A  1 279 ? 96.415  74.652  -4.058  1.00   25.49  ? 279 THR A N   1 
ATOM   1942  C CA  . THR A  1 279 ? 97.203  74.421  -5.258  1.00   26.53  ? 279 THR A CA  1 
ATOM   1943  C C   . THR A  1 279 ? 96.914  75.465  -6.301  1.00   29.85  ? 279 THR A C   1 
ATOM   1944  O O   . THR A  1 279 ? 95.867  76.093  -6.267  1.00   31.64  ? 279 THR A O   1 
ATOM   1945  C CB  . THR A  1 279 ? 96.913  73.066  -5.831  1.00   27.13  ? 279 THR A CB  1 
ATOM   1946  O OG1 . THR A  1 279 ? 97.724  72.861  -6.987  1.00   28.72  ? 279 THR A OG1 1 
ATOM   1947  C CG2 . THR A  1 279 ? 95.465  72.997  -6.218  1.00   28.66  ? 279 THR A CG2 1 
ATOM   1948  N N   . THR A  1 280 ? 97.835  75.663  -7.233  1.00   31.16  ? 280 THR A N   1 
ATOM   1949  C CA  . THR A  1 280 ? 97.622  76.637  -8.303  1.00   29.60  ? 280 THR A CA  1 
ATOM   1950  C C   . THR A  1 280 ? 97.536  76.001  -9.677  1.00   29.77  ? 280 THR A C   1 
ATOM   1951  O O   . THR A  1 280 ? 97.454  76.708  -10.681 1.00   31.88  ? 280 THR A O   1 
ATOM   1952  C CB  . THR A  1 280 ? 98.738  77.712  -8.353  1.00   31.80  ? 280 THR A CB  1 
ATOM   1953  O OG1 . THR A  1 280 ? 100.020 77.079  -8.419  1.00   34.03  ? 280 THR A OG1 1 
ATOM   1954  C CG2 . THR A  1 280 ? 98.704  78.614  -7.134  1.00   27.70  ? 280 THR A CG2 1 
ATOM   1955  N N   . THR A  1 281 ? 97.537  74.677  -9.734  1.00   29.83  ? 281 THR A N   1 
ATOM   1956  C CA  . THR A  1 281 ? 97.654  73.999  -11.023 1.00   35.81  ? 281 THR A CA  1 
ATOM   1957  C C   . THR A  1 281 ? 96.332  73.458  -11.598 1.00   37.33  ? 281 THR A C   1 
ATOM   1958  O O   . THR A  1 281 ? 96.336  72.748  -12.612 1.00   36.82  ? 281 THR A O   1 
ATOM   1959  C CB  . THR A  1 281 ? 98.672  72.846  -10.945 1.00   39.25  ? 281 THR A CB  1 
ATOM   1960  O OG1 . THR A  1 281 ? 98.329  71.960  -9.870  1.00   41.05  ? 281 THR A OG1 1 
ATOM   1961  C CG2 . THR A  1 281 ? 100.048 73.420  -10.715 1.00   39.36  ? 281 THR A CG2 1 
ATOM   1962  N N   . HIS A  1 282 ? 95.206  73.806  -10.973 1.00   37.03  ? 282 HIS A N   1 
ATOM   1963  C CA  . HIS A  1 282 ? 93.907  73.731  -11.655 1.00   37.83  ? 282 HIS A CA  1 
ATOM   1964  C C   . HIS A  1 282 ? 93.075  74.919  -11.188 1.00   36.65  ? 282 HIS A C   1 
ATOM   1965  O O   . HIS A  1 282 ? 93.222  75.374  -10.053 1.00   36.13  ? 282 HIS A O   1 
ATOM   1966  C CB  . HIS A  1 282 ? 93.181  72.386  -11.426 1.00   36.24  ? 282 HIS A CB  1 
ATOM   1967  C CG  . HIS A  1 282 ? 92.984  72.007  -9.992  1.00   30.98  ? 282 HIS A CG  1 
ATOM   1968  N ND1 . HIS A  1 282 ? 92.133  72.684  -9.146  1.00   31.54  ? 282 HIS A ND1 1 
ATOM   1969  C CD2 . HIS A  1 282 ? 93.506  70.992  -9.264  1.00   30.03  ? 282 HIS A CD2 1 
ATOM   1970  C CE1 . HIS A  1 282 ? 92.158  72.116  -7.953  1.00   28.96  ? 282 HIS A CE1 1 
ATOM   1971  N NE2 . HIS A  1 282 ? 92.984  71.086  -7.999  1.00   27.10  ? 282 HIS A NE2 1 
ATOM   1972  N N   . PRO A  1 283 ? 92.235  75.463  -12.081 1.00   35.75  ? 283 PRO A N   1 
ATOM   1973  C CA  . PRO A  1 283 ? 91.551  76.707  -11.723 1.00   34.44  ? 283 PRO A CA  1 
ATOM   1974  C C   . PRO A  1 283 ? 90.456  76.513  -10.680 1.00   34.01  ? 283 PRO A C   1 
ATOM   1975  O O   . PRO A  1 283 ? 90.381  77.256  -9.699  1.00   35.43  ? 283 PRO A O   1 
ATOM   1976  C CB  . PRO A  1 283 ? 90.993  77.197  -13.070 1.00   38.33  ? 283 PRO A CB  1 
ATOM   1977  C CG  . PRO A  1 283 ? 90.943  75.994  -13.923 1.00   39.56  ? 283 PRO A CG  1 
ATOM   1978  C CD  . PRO A  1 283 ? 92.064  75.117  -13.499 1.00   34.96  ? 283 PRO A CD  1 
ATOM   1979  N N   . TYR A  1 284 ? 89.605  75.518  -10.882 1.00   33.82  ? 284 TYR A N   1 
ATOM   1980  C CA  . TYR A  1 284 ? 88.437  75.382  -10.023 1.00   32.63  ? 284 TYR A CA  1 
ATOM   1981  C C   . TYR A  1 284 ? 88.671  74.444  -8.857  1.00   33.23  ? 284 TYR A C   1 
ATOM   1982  O O   . TYR A  1 284 ? 89.611  73.649  -8.866  1.00   36.10  ? 284 TYR A O   1 
ATOM   1983  C CB  . TYR A  1 284 ? 87.226  74.951  -10.842 1.00   34.20  ? 284 TYR A CB  1 
ATOM   1984  C CG  . TYR A  1 284 ? 86.982  75.890  -11.995 1.00   35.04  ? 284 TYR A CG  1 
ATOM   1985  C CD1 . TYR A  1 284 ? 86.801  77.246  -11.769 1.00   37.47  ? 284 TYR A CD1 1 
ATOM   1986  C CD2 . TYR A  1 284 ? 86.924  75.432  -13.296 1.00   38.12  ? 284 TYR A CD2 1 
ATOM   1987  C CE1 . TYR A  1 284 ? 86.599  78.130  -12.812 1.00   40.95  ? 284 TYR A CE1 1 
ATOM   1988  C CE2 . TYR A  1 284 ? 86.701  76.310  -14.354 1.00   42.09  ? 284 TYR A CE2 1 
ATOM   1989  C CZ  . TYR A  1 284 ? 86.535  77.654  -14.106 1.00   43.48  ? 284 TYR A CZ  1 
ATOM   1990  O OH  . TYR A  1 284 ? 86.313  78.522  -15.151 1.00   46.45  ? 284 TYR A OH  1 
ATOM   1991  N N   . THR A  1 285 ? 87.831  74.583  -7.839  1.00   32.45  ? 285 THR A N   1 
ATOM   1992  C CA  . THR A  1 285 ? 87.943  73.780  -6.638  1.00   30.70  ? 285 THR A CA  1 
ATOM   1993  C C   . THR A  1 285 ? 87.394  72.380  -6.884  1.00   30.72  ? 285 THR A C   1 
ATOM   1994  O O   . THR A  1 285 ? 86.310  72.200  -7.426  1.00   31.72  ? 285 THR A O   1 
ATOM   1995  C CB  . THR A  1 285 ? 87.230  74.471  -5.478  1.00   30.12  ? 285 THR A CB  1 
ATOM   1996  O OG1 . THR A  1 285 ? 87.875  75.720  -5.230  1.00   30.76  ? 285 THR A OG1 1 
ATOM   1997  C CG2 . THR A  1 285 ? 87.301  73.627  -4.227  1.00   28.55  ? 285 THR A CG2 1 
ATOM   1998  N N   . VAL A  1 286 ? 88.189  71.387  -6.513  1.00   30.41  ? 286 VAL A N   1 
ATOM   1999  C CA  . VAL A  1 286 ? 87.879  70.003  -6.811  1.00   30.61  ? 286 VAL A CA  1 
ATOM   2000  C C   . VAL A  1 286 ? 87.522  69.339  -5.515  1.00   31.17  ? 286 VAL A C   1 
ATOM   2001  O O   . VAL A  1 286 ? 88.203  69.530  -4.510  1.00   31.04  ? 286 VAL A O   1 
ATOM   2002  C CB  . VAL A  1 286 ? 89.061  69.280  -7.517  1.00   29.62  ? 286 VAL A CB  1 
ATOM   2003  C CG1 . VAL A  1 286 ? 88.771  67.844  -7.718  1.00   29.37  ? 286 VAL A CG1 1 
ATOM   2004  C CG2 . VAL A  1 286 ? 89.324  69.903  -8.848  1.00   29.51  ? 286 VAL A CG2 1 
ATOM   2005  N N   . LEU A  1 287 ? 86.394  68.643  -5.529  1.00   32.99  ? 287 LEU A N   1 
ATOM   2006  C CA  . LEU A  1 287 ? 85.916  67.874  -4.379  1.00   32.78  ? 287 LEU A CA  1 
ATOM   2007  C C   . LEU A  1 287 ? 85.851  66.387  -4.726  1.00   34.64  ? 287 LEU A C   1 
ATOM   2008  O O   . LEU A  1 287 ? 85.520  66.007  -5.845  1.00   35.31  ? 287 LEU A O   1 
ATOM   2009  C CB  . LEU A  1 287 ? 84.549  68.360  -3.919  1.00   30.16  ? 287 LEU A CB  1 
ATOM   2010  C CG  . LEU A  1 287 ? 84.354  69.853  -3.642  1.00   28.50  ? 287 LEU A CG  1 
ATOM   2011  C CD1 . LEU A  1 287 ? 82.874  70.133  -3.407  1.00   29.11  ? 287 LEU A CD1 1 
ATOM   2012  C CD2 . LEU A  1 287 ? 85.169  70.274  -2.450  1.00   27.95  ? 287 LEU A CD2 1 
ATOM   2013  N N   . SER A  1 288 ? 86.185  65.546  -3.761  1.00   37.33  ? 288 SER A N   1 
ATOM   2014  C CA  . SER A  1 288 ? 86.101  64.111  -3.959  1.00   42.18  ? 288 SER A CA  1 
ATOM   2015  C C   . SER A  1 288 ? 84.658  63.780  -4.192  1.00   40.98  ? 288 SER A C   1 
ATOM   2016  O O   . SER A  1 288 ? 83.783  64.546  -3.810  1.00   41.09  ? 288 SER A O   1 
ATOM   2017  C CB  . SER A  1 288 ? 86.621  63.327  -2.753  1.00   47.19  ? 288 SER A CB  1 
ATOM   2018  O OG  . SER A  1 288 ? 85.789  63.514  -1.618  1.00   48.82  ? 288 SER A OG  1 
ATOM   2019  N N   . HIS A  1 289 ? 84.416  62.654  -4.843  1.00   41.21  ? 289 HIS A N   1 
ATOM   2020  C CA  . HIS A  1 289 ? 83.086  62.298  -5.290  1.00   45.50  ? 289 HIS A CA  1 
ATOM   2021  C C   . HIS A  1 289 ? 82.004  62.270  -4.188  1.00   48.77  ? 289 HIS A C   1 
ATOM   2022  O O   . HIS A  1 289 ? 80.889  62.762  -4.378  1.00   49.16  ? 289 HIS A O   1 
ATOM   2023  C CB  . HIS A  1 289 ? 83.137  60.947  -5.979  1.00   47.11  ? 289 HIS A CB  1 
ATOM   2024  C CG  . HIS A  1 289 ? 81.807  60.491  -6.466  1.00   48.47  ? 289 HIS A CG  1 
ATOM   2025  N ND1 . HIS A  1 289 ? 81.156  61.104  -7.510  1.00   48.92  ? 289 HIS A ND1 1 
ATOM   2026  C CD2 . HIS A  1 289 ? 80.981  59.519  -6.022  1.00   53.52  ? 289 HIS A CD2 1 
ATOM   2027  C CE1 . HIS A  1 289 ? 79.995  60.510  -7.711  1.00   52.87  ? 289 HIS A CE1 1 
ATOM   2028  N NE2 . HIS A  1 289 ? 79.862  59.547  -6.818  1.00   56.19  ? 289 HIS A NE2 1 
ATOM   2029  N N   . SER A  1 290 ? 82.310  61.664  -3.051  1.00   50.68  ? 290 SER A N   1 
ATOM   2030  C CA  . SER A  1 290 ? 81.320  61.581  -1.990  1.00   51.87  ? 290 SER A CA  1 
ATOM   2031  C C   . SER A  1 290 ? 80.995  62.977  -1.455  1.00   43.18  ? 290 SER A C   1 
ATOM   2032  O O   . SER A  1 290 ? 79.844  63.309  -1.238  1.00   42.84  ? 290 SER A O   1 
ATOM   2033  C CB  . SER A  1 290 ? 81.811  60.667  -0.864  1.00   58.53  ? 290 SER A CB  1 
ATOM   2034  O OG  . SER A  1 290 ? 82.989  61.181  -0.265  1.00   61.49  ? 290 SER A OG  1 
ATOM   2035  N N   . ILE A  1 291 ? 82.011  63.812  -1.285  1.00   39.81  ? 291 ILE A N   1 
ATOM   2036  C CA  . ILE A  1 291 ? 81.791  65.178  -0.822  1.00   35.79  ? 291 ILE A CA  1 
ATOM   2037  C C   . ILE A  1 291 ? 81.100  66.025  -1.889  1.00   38.00  ? 291 ILE A C   1 
ATOM   2038  O O   . ILE A  1 291 ? 80.230  66.853  -1.596  1.00   38.49  ? 291 ILE A O   1 
ATOM   2039  C CB  . ILE A  1 291 ? 83.094  65.847  -0.445  1.00   34.09  ? 291 ILE A CB  1 
ATOM   2040  C CG1 . ILE A  1 291 ? 83.783  65.071  0.667   1.00   33.27  ? 291 ILE A CG1 1 
ATOM   2041  C CG2 . ILE A  1 291 ? 82.860  67.288  -0.046  1.00   32.62  ? 291 ILE A CG2 1 
ATOM   2042  C CD1 . ILE A  1 291 ? 85.105  65.664  1.042   1.00   29.44  ? 291 ILE A CD1 1 
ATOM   2043  N N   . PHE A  1 292 ? 81.523  65.845  -3.133  1.00   35.76  ? 292 PHE A N   1 
ATOM   2044  C CA  . PHE A  1 292 ? 80.919  66.567  -4.236  1.00   35.59  ? 292 PHE A CA  1 
ATOM   2045  C C   . PHE A  1 292 ? 79.417  66.327  -4.311  1.00   42.00  ? 292 PHE A C   1 
ATOM   2046  O O   . PHE A  1 292 ? 78.612  67.264  -4.371  1.00   40.91  ? 292 PHE A O   1 
ATOM   2047  C CB  . PHE A  1 292 ? 81.579  66.153  -5.540  1.00   34.72  ? 292 PHE A CB  1 
ATOM   2048  C CG  . PHE A  1 292 ? 80.938  66.740  -6.742  1.00   34.74  ? 292 PHE A CG  1 
ATOM   2049  C CD1 . PHE A  1 292 ? 81.200  68.042  -7.106  1.00   34.60  ? 292 PHE A CD1 1 
ATOM   2050  C CD2 . PHE A  1 292 ? 80.120  65.982  -7.537  1.00   39.40  ? 292 PHE A CD2 1 
ATOM   2051  C CE1 . PHE A  1 292 ? 80.624  68.590  -8.223  1.00   37.39  ? 292 PHE A CE1 1 
ATOM   2052  C CE2 . PHE A  1 292 ? 79.532  66.523  -8.658  1.00   41.74  ? 292 PHE A CE2 1 
ATOM   2053  C CZ  . PHE A  1 292 ? 79.791  67.830  -9.003  1.00   39.43  ? 292 PHE A CZ  1 
ATOM   2054  N N   . GLU A  1 293 ? 79.037  65.061  -4.233  1.00   45.72  ? 293 GLU A N   1 
ATOM   2055  C CA  . GLU A  1 293 ? 77.646  64.702  -4.388  1.00   50.68  ? 293 GLU A CA  1 
ATOM   2056  C C   . GLU A  1 293 ? 76.824  65.315  -3.268  1.00   46.47  ? 293 GLU A C   1 
ATOM   2057  O O   . GLU A  1 293 ? 75.755  65.868  -3.509  1.00   45.70  ? 293 GLU A O   1 
ATOM   2058  C CB  . GLU A  1 293 ? 77.490  63.175  -4.439  1.00   60.56  ? 293 GLU A CB  1 
ATOM   2059  C CG  . GLU A  1 293 ? 76.522  62.744  -5.516  1.00   72.37  ? 293 GLU A CG  1 
ATOM   2060  C CD  . GLU A  1 293 ? 77.043  63.086  -6.901  1.00   81.20  ? 293 GLU A CD  1 
ATOM   2061  O OE1 . GLU A  1 293 ? 78.081  62.518  -7.282  1.00   84.08  ? 293 GLU A OE1 1 
ATOM   2062  O OE2 . GLU A  1 293 ? 76.450  63.951  -7.592  1.00   84.74  1 293 GLU A OE2 1 
ATOM   2063  N N   . VAL A  1 294 ? 77.351  65.271  -2.054  1.00   43.89  ? 294 VAL A N   1 
ATOM   2064  C CA  . VAL A  1 294 ? 76.629  65.804  -0.918  1.00   42.70  ? 294 VAL A CA  1 
ATOM   2065  C C   . VAL A  1 294 ? 76.551  67.322  -0.983  1.00   41.68  ? 294 VAL A C   1 
ATOM   2066  O O   . VAL A  1 294 ? 75.475  67.894  -0.851  1.00   45.50  ? 294 VAL A O   1 
ATOM   2067  C CB  . VAL A  1 294 ? 77.298  65.400  0.405   1.00   43.81  ? 294 VAL A CB  1 
ATOM   2068  C CG1 . VAL A  1 294 ? 76.625  66.079  1.566   1.00   42.25  ? 294 VAL A CG1 1 
ATOM   2069  C CG2 . VAL A  1 294 ? 77.234  63.918  0.583   1.00   46.05  ? 294 VAL A CG2 1 
ATOM   2070  N N   . PHE A  1 295 ? 77.677  67.967  -1.238  1.00   35.51  ? 295 PHE A N   1 
ATOM   2071  C CA  . PHE A  1 295 ? 77.713  69.409  -1.282  1.00   33.76  ? 295 PHE A CA  1 
ATOM   2072  C C   . PHE A  1 295 ? 76.828  69.988  -2.397  1.00   34.48  ? 295 PHE A C   1 
ATOM   2073  O O   . PHE A  1 295 ? 76.105  70.956  -2.167  1.00   35.01  ? 295 PHE A O   1 
ATOM   2074  C CB  . PHE A  1 295 ? 79.166  69.903  -1.427  1.00   33.92  ? 295 PHE A CB  1 
ATOM   2075  C CG  . PHE A  1 295 ? 79.275  71.385  -1.705  1.00   32.70  ? 295 PHE A CG  1 
ATOM   2076  C CD1 . PHE A  1 295 ? 79.111  72.311  -0.677  1.00   33.51  ? 295 PHE A CD1 1 
ATOM   2077  C CD2 . PHE A  1 295 ? 79.507  71.857  -2.979  1.00   31.10  ? 295 PHE A CD2 1 
ATOM   2078  C CE1 . PHE A  1 295 ? 79.189  73.684  -0.914  1.00   32.49  ? 295 PHE A CE1 1 
ATOM   2079  C CE2 . PHE A  1 295 ? 79.588  73.239  -3.213  1.00   31.87  ? 295 PHE A CE2 1 
ATOM   2080  C CZ  . PHE A  1 295 ? 79.425  74.143  -2.185  1.00   30.44  ? 295 PHE A CZ  1 
ATOM   2081  N N   . THR A  1 296 ? 76.876  69.436  -3.603  1.00   34.69  ? 296 THR A N   1 
ATOM   2082  C CA  . THR A  1 296 ? 76.088  70.036  -4.682  1.00   37.44  ? 296 THR A CA  1 
ATOM   2083  C C   . THR A  1 296 ? 74.573  69.906  -4.452  1.00   40.60  ? 296 THR A C   1 
ATOM   2084  O O   . THR A  1 296 ? 73.801  70.802  -4.832  1.00   39.88  ? 296 THR A O   1 
ATOM   2085  C CB  . THR A  1 296 ? 76.452  69.452  -6.066  1.00   40.28  ? 296 THR A CB  1 
ATOM   2086  O OG1 . THR A  1 296 ? 76.253  68.036  -6.070  1.00   46.40  ? 296 THR A OG1 1 
ATOM   2087  C CG2 . THR A  1 296 ? 77.890  69.753  -6.406  1.00   34.67  ? 296 THR A CG2 1 
ATOM   2088  N N   . GLN A  1 297 ? 74.124  68.810  -3.841  1.00   42.54  ? 297 GLN A N   1 
ATOM   2089  C CA  . GLN A  1 297 ? 72.690  68.697  -3.580  1.00   44.51  ? 297 GLN A CA  1 
ATOM   2090  C C   . GLN A  1 297 ? 72.261  69.657  -2.466  1.00   43.85  ? 297 GLN A C   1 
ATOM   2091  O O   . GLN A  1 297 ? 71.239  70.339  -2.591  1.00   46.29  ? 297 GLN A O   1 
ATOM   2092  C CB  . GLN A  1 297 ? 72.298  67.260  -3.232  1.00   47.58  ? 297 GLN A CB  1 
ATOM   2093  C CG  . GLN A  1 297 ? 70.767  67.019  -3.086  1.00   70.88  ? 297 GLN A CG  1 
ATOM   2094  C CD  . GLN A  1 297 ? 69.973  67.306  -4.367  1.00   74.05  ? 297 GLN A CD  1 
ATOM   2095  O OE1 . GLN A  1 297 ? 70.239  66.726  -5.417  1.00   76.24  ? 297 GLN A OE1 1 
ATOM   2096  N NE2 . GLN A  1 297 ? 68.979  68.187  -4.270  1.00   74.91  ? 297 GLN A NE2 1 
ATOM   2097  N N   . VAL A  1 298 ? 73.046  69.717  -1.387  1.00   42.82  ? 298 VAL A N   1 
ATOM   2098  C CA  . VAL A  1 298 ? 72.794  70.649  -0.279  1.00   41.59  ? 298 VAL A CA  1 
ATOM   2099  C C   . VAL A  1 298 ? 72.706  72.077  -0.818  1.00   41.82  ? 298 VAL A C   1 
ATOM   2100  O O   . VAL A  1 298 ? 71.851  72.859  -0.413  1.00   43.55  ? 298 VAL A O   1 
ATOM   2101  C CB  . VAL A  1 298 ? 73.894  70.560  0.802   1.00   39.01  ? 298 VAL A CB  1 
ATOM   2102  C CG1 . VAL A  1 298 ? 73.902  71.800  1.702   1.00   38.11  ? 298 VAL A CG1 1 
ATOM   2103  C CG2 . VAL A  1 298 ? 73.744  69.290  1.618   1.00   38.23  ? 298 VAL A CG2 1 
ATOM   2104  N N   . PHE A  1 299 ? 73.586  72.392  -1.760  1.00   41.18  ? 299 PHE A N   1 
ATOM   2105  C CA  . PHE A  1 299 ? 73.568  73.685  -2.409  1.00   39.12  ? 299 PHE A CA  1 
ATOM   2106  C C   . PHE A  1 299 ? 72.271  73.854  -3.189  1.00   40.05  ? 299 PHE A C   1 
ATOM   2107  O O   . PHE A  1 299 ? 71.629  74.891  -3.080  1.00   38.96  ? 299 PHE A O   1 
ATOM   2108  C CB  . PHE A  1 299 ? 74.774  73.843  -3.335  1.00   40.28  ? 299 PHE A CB  1 
ATOM   2109  C CG  . PHE A  1 299 ? 74.924  75.232  -3.895  1.00   42.60  ? 299 PHE A CG  1 
ATOM   2110  C CD1 . PHE A  1 299 ? 74.265  75.602  -5.063  1.00   43.96  ? 299 PHE A CD1 1 
ATOM   2111  C CD2 . PHE A  1 299 ? 75.708  76.169  -3.253  1.00   41.35  ? 299 PHE A CD2 1 
ATOM   2112  C CE1 . PHE A  1 299 ? 74.383  76.870  -5.582  1.00   42.51  ? 299 PHE A CE1 1 
ATOM   2113  C CE2 . PHE A  1 299 ? 75.839  77.447  -3.771  1.00   41.14  ? 299 PHE A CE2 1 
ATOM   2114  C CZ  . PHE A  1 299 ? 75.169  77.796  -4.938  1.00   42.33  ? 299 PHE A CZ  1 
ATOM   2115  N N   . ALA A  1 300 ? 71.888  72.843  -3.970  1.00   42.99  ? 300 ALA A N   1 
ATOM   2116  C CA  . ALA A  1 300 ? 70.659  72.904  -4.756  1.00   45.39  ? 300 ALA A CA  1 
ATOM   2117  C C   . ALA A  1 300 ? 69.455  73.104  -3.849  1.00   49.48  ? 300 ALA A C   1 
ATOM   2118  O O   . ALA A  1 300 ? 68.490  73.747  -4.242  1.00   56.10  ? 300 ALA A O   1 
ATOM   2119  C CB  . ALA A  1 300 ? 70.492  71.653  -5.599  1.00   45.55  ? 300 ALA A CB  1 
ATOM   2120  N N   . ASN A  1 301 ? 69.517  72.566  -2.632  1.00   48.04  ? 301 ASN A N   1 
ATOM   2121  C CA  . ASN A  1 301 ? 68.444  72.734  -1.643  1.00   48.65  ? 301 ASN A CA  1 
ATOM   2122  C C   . ASN A  1 301 ? 68.321  74.136  -1.061  1.00   50.23  ? 301 ASN A C   1 
ATOM   2123  O O   . ASN A  1 301 ? 67.295  74.477  -0.470  1.00   54.43  ? 301 ASN A O   1 
ATOM   2124  C CB  . ASN A  1 301 ? 68.624  71.781  -0.465  1.00   45.86  ? 301 ASN A CB  1 
ATOM   2125  C CG  . ASN A  1 301 ? 68.419  70.357  -0.839  1.00   46.01  ? 301 ASN A CG  1 
ATOM   2126  O OD1 . ASN A  1 301 ? 67.896  70.048  -1.913  1.00   46.09  ? 301 ASN A OD1 1 
ATOM   2127  N ND2 . ASN A  1 301 ? 68.822  69.462  0.051   1.00   45.28  ? 301 ASN A ND2 1 
ATOM   2128  N N   . ASN A  1 302 ? 69.376  74.930  -1.176  1.00   46.72  ? 302 ASN A N   1 
ATOM   2129  C CA  . ASN A  1 302 ? 69.333  76.290  -0.679  1.00   44.89  ? 302 ASN A CA  1 
ATOM   2130  C C   . ASN A  1 302 ? 69.173  77.298  -1.850  1.00   49.54  ? 302 ASN A C   1 
ATOM   2131  O O   . ASN A  1 302 ? 69.526  78.460  -1.736  1.00   51.77  ? 302 ASN A O   1 
ATOM   2132  C CB  . ASN A  1 302 ? 70.579  76.565  0.189   1.00   39.84  ? 302 ASN A CB  1 
ATOM   2133  C CG  . ASN A  1 302 ? 70.486  75.916  1.584   1.00   38.06  ? 302 ASN A CG  1 
ATOM   2134  O OD1 . ASN A  1 302 ? 70.056  76.545  2.559   1.00   39.10  ? 302 ASN A OD1 1 
ATOM   2135  N ND2 . ASN A  1 302 ? 70.882  74.651  1.673   1.00   37.23  ? 302 ASN A ND2 1 
ATOM   2136  N N   . MET A  1 303 ? 68.605  76.839  -2.962  1.00   47.73  ? 303 MET A N   1 
ATOM   2137  C CA  . MET A  1 303 ? 68.388  77.661  -4.155  1.00   48.99  ? 303 MET A CA  1 
ATOM   2138  C C   . MET A  1 303 ? 67.004  77.392  -4.733  1.00   51.72  ? 303 MET A C   1 
ATOM   2139  O O   . MET A  1 303 ? 66.426  76.357  -4.455  1.00   51.20  ? 303 MET A O   1 
ATOM   2140  C CB  . MET A  1 303 ? 69.443  77.372  -5.216  1.00   44.22  ? 303 MET A CB  1 
ATOM   2141  C CG  . MET A  1 303 ? 70.829  77.853  -4.879  1.00   56.19  ? 303 MET A CG  1 
ATOM   2142  S SD  . MET A  1 303 ? 70.985  79.644  -4.953  1.00   59.78  ? 303 MET A SD  1 
ATOM   2143  C CE  . MET A  1 303 ? 71.063  79.877  -6.719  1.00   49.85  ? 303 MET A CE  1 
ATOM   2144  N N   . PRO A  1 304 ? 66.480  78.305  -5.573  1.00   59.08  ? 304 PRO A N   1 
ATOM   2145  C CA  . PRO A  1 304 ? 65.215  77.951  -6.227  1.00   63.41  ? 304 PRO A CA  1 
ATOM   2146  C C   . PRO A  1 304 ? 65.407  76.755  -7.159  1.00   63.08  ? 304 PRO A C   1 
ATOM   2147  O O   . PRO A  1 304 ? 66.028  76.836  -8.212  1.00   59.89  ? 304 PRO A O   1 
ATOM   2148  C CB  . PRO A  1 304 ? 64.843  79.230  -6.995  1.00   66.10  ? 304 PRO A CB  1 
ATOM   2149  C CG  . PRO A  1 304 ? 66.115  79.978  -7.154  1.00   63.44  ? 304 PRO A CG  1 
ATOM   2150  C CD  . PRO A  1 304 ? 66.894  79.682  -5.895  1.00   60.99  ? 304 PRO A CD  1 
ATOM   2151  N N   . LYS A  1 305 ? 64.793  75.653  -6.763  1.00   65.49  ? 305 LYS A N   1 
ATOM   2152  C CA  . LYS A  1 305 ? 65.037  74.374  -7.384  1.00   65.20  ? 305 LYS A CA  1 
ATOM   2153  C C   . LYS A  1 305 ? 64.672  74.321  -8.862  1.00   67.76  ? 305 LYS A C   1 
ATOM   2154  O O   . LYS A  1 305 ? 65.158  73.442  -9.566  1.00   68.29  ? 305 LYS A O   1 
ATOM   2155  C CB  . LYS A  1 305 ? 64.266  73.290  -6.612  0.0000 63.88  ? 305 LYS A CB  1 
ATOM   2156  C CG  . LYS A  1 305 ? 62.789  73.296  -6.929  0.0000 65.28  ? 305 LYS A CG  1 
ATOM   2157  C CD  . LYS A  1 305 ? 62.036  72.250  -6.147  0.0000 64.44  ? 305 LYS A CD  1 
ATOM   2158  C CE  . LYS A  1 305 ? 60.608  72.688  -5.989  0.0000 66.51  ? 305 LYS A CE  1 
ATOM   2159  N NZ  . LYS A  1 305 ? 60.518  73.769  -4.983  0.0000 65.39  ? 305 LYS A NZ  1 
ATOM   2160  N N   . GLN A  1 306 ? 63.788  75.208  -9.315  1.00   69.11  ? 306 GLN A N   1 
ATOM   2161  C CA  . GLN A  1 306 ? 63.421  75.181  -10.715 1.00   69.00  ? 306 GLN A CA  1 
ATOM   2162  C C   . GLN A  1 306 ? 64.044  76.312  -11.511 1.00   66.40  ? 306 GLN A C   1 
ATOM   2163  O O   . GLN A  1 306 ? 63.442  76.815  -12.441 1.00   67.93  ? 306 GLN A O   1 
ATOM   2164  C CB  . GLN A  1 306 ? 61.921  75.132  -10.886 0.0000 70.85  ? 306 GLN A CB  1 
ATOM   2165  C CG  . GLN A  1 306 ? 61.589  74.399  -12.147 0.0000 72.35  ? 306 GLN A CG  1 
ATOM   2166  C CD  . GLN A  1 306 ? 61.390  72.921  -11.867 0.0000 70.53  ? 306 GLN A CD  1 
ATOM   2167  O OE1 . GLN A  1 306 ? 61.103  72.515  -10.738 0.0000 68.44  ? 306 GLN A OE1 1 
ATOM   2168  N NE2 . GLN A  1 306 ? 61.620  72.100  -12.883 0.0000 71.65  ? 306 GLN A NE2 1 
ATOM   2169  N N   . ALA A  1 307 ? 65.220  76.752  -11.095 1.00   65.24  ? 307 ALA A N   1 
ATOM   2170  C CA  . ALA A  1 307 ? 65.974  77.731  -11.859 1.00   68.05  ? 307 ALA A CA  1 
ATOM   2171  C C   . ALA A  1 307 ? 67.166  77.089  -12.548 1.00   66.86  ? 307 ALA A C   1 
ATOM   2172  O O   . ALA A  1 307 ? 67.932  77.768  -13.250 1.00   70.27  ? 307 ALA A O   1 
ATOM   2173  C CB  . ALA A  1 307 ? 66.433  78.863  -10.934 1.00   68.20  ? 307 ALA A CB  1 
ATOM   2174  N N   . GLN A  1 308 ? 67.339  75.802  -12.269 1.00   62.22  ? 308 GLN A N   1 
ATOM   2175  C CA  . GLN A  1 308 ? 68.443  75.047  -12.785 1.00   59.35  ? 308 GLN A CA  1 
ATOM   2176  C C   . GLN A  1 308 ? 68.301  74.842  -14.286 1.00   62.70  ? 308 GLN A C   1 
ATOM   2177  O O   . GLN A  1 308 ? 67.198  74.768  -14.818 1.00   64.35  ? 308 GLN A O   1 
ATOM   2178  C CB  . GLN A  1 308 ? 68.493  73.714  -12.065 1.00   57.01  ? 308 GLN A CB  1 
ATOM   2179  C CG  . GLN A  1 308 ? 68.458  73.895  -10.564 1.00   55.50  ? 308 GLN A CG  1 
ATOM   2180  C CD  . GLN A  1 308 ? 68.571  72.615  -9.786  1.00   57.44  ? 308 GLN A CD  1 
ATOM   2181  O OE1 . GLN A  1 308 ? 68.737  71.545  -10.362 1.00   61.11  ? 308 GLN A OE1 1 
ATOM   2182  N NE2 . GLN A  1 308 ? 68.498  72.717  -8.455  1.00   54.67  ? 308 GLN A NE2 1 
ATOM   2183  N N   . VAL A  1 309 ? 69.433  74.756  -14.968 1.00   64.11  ? 309 VAL A N   1 
ATOM   2184  C CA  . VAL A  1 309 ? 69.442  74.465  -16.389 1.00   67.71  ? 309 VAL A CA  1 
ATOM   2185  C C   . VAL A  1 309 ? 70.455  73.356  -16.532 1.00   68.02  ? 309 VAL A C   1 
ATOM   2186  O O   . VAL A  1 309 ? 71.237  73.106  -15.607 1.00   62.23  ? 309 VAL A O   1 
ATOM   2187  C CB  . VAL A  1 309 ? 69.839  75.663  -17.258 1.00   69.27  ? 309 VAL A CB  1 
ATOM   2188  C CG1 . VAL A  1 309 ? 68.926  76.842  -16.976 1.00   67.02  ? 309 VAL A CG1 1 
ATOM   2189  C CG2 . VAL A  1 309 ? 71.281  76.029  -16.994 1.00   68.52  ? 309 VAL A CG2 1 
ATOM   2190  N N   . LYS A  1 310 ? 70.437  72.692  -17.678 1.00   73.43  ? 310 LYS A N   1 
ATOM   2191  C CA  . LYS A  1 310 ? 71.424  71.666  -17.969 1.00   74.03  ? 310 LYS A CA  1 
ATOM   2192  C C   . LYS A  1 310 ? 72.840  72.165  -17.729 1.00   69.76  ? 310 LYS A C   1 
ATOM   2193  O O   . LYS A  1 310 ? 73.234  73.237  -18.217 1.00   69.01  ? 310 LYS A O   1 
ATOM   2194  C CB  . LYS A  1 310 ? 71.284  71.176  -19.405 1.00   79.47  ? 310 LYS A CB  1 
ATOM   2195  C CG  . LYS A  1 310 ? 72.135  69.976  -19.735 1.00   79.85  ? 310 LYS A CG  1 
ATOM   2196  C CD  . LYS A  1 310 ? 71.887  69.601  -21.166 1.00   85.92  ? 310 LYS A CD  1 
ATOM   2197  C CE  . LYS A  1 310 ? 72.183  70.773  -22.060 1.00   88.75  ? 310 LYS A CE  1 
ATOM   2198  N NZ  . LYS A  1 310 ? 72.147  70.394  -23.490 1.00   94.75  ? 310 LYS A NZ  1 
ATOM   2199  N N   . ALA A  1 311 ? 73.571  71.384  -16.937 1.00   66.76  ? 311 ALA A N   1 
ATOM   2200  C CA  . ALA A  1 311 ? 74.946  71.680  -16.582 1.00   63.76  ? 311 ALA A CA  1 
ATOM   2201  C C   . ALA A  1 311 ? 75.789  71.863  -17.819 1.00   69.04  ? 311 ALA A C   1 
ATOM   2202  O O   . ALA A  1 311 ? 75.634  71.166  -18.817 1.00   74.70  ? 311 ALA A O   1 
ATOM   2203  C CB  . ALA A  1 311 ? 75.518  70.593  -15.722 1.00   59.63  ? 311 ALA A CB  1 
ATOM   2204  N N   . VAL A  1 312 ? 76.719  72.790  -17.720 1.00   69.61  ? 312 VAL A N   1 
ATOM   2205  C CA  . VAL A  1 312 ? 77.496  73.207  -18.859 1.00   73.24  ? 312 VAL A CA  1 
ATOM   2206  C C   . VAL A  1 312 ? 78.947  73.150  -18.468 1.00   73.79  ? 312 VAL A C   1 
ATOM   2207  O O   . VAL A  1 312 ? 79.284  73.398  -17.314 1.00   73.24  ? 312 VAL A O   1 
ATOM   2208  C CB  . VAL A  1 312 ? 77.105  74.639  -19.266 1.00   74.22  ? 312 VAL A CB  1 
ATOM   2209  C CG1 . VAL A  1 312 ? 78.186  75.303  -20.102 1.00   77.05  ? 312 VAL A CG1 1 
ATOM   2210  C CG2 . VAL A  1 312 ? 75.736  74.647  -19.948 1.00   77.56  ? 312 VAL A CG2 1 
ATOM   2211  N N   . GLY A  1 313 ? 79.807  72.784  -19.409 1.00   75.66  ? 313 GLY A N   1 
ATOM   2212  C CA  . GLY A  1 313 ? 81.231  72.746  -19.136 1.00   72.57  ? 313 GLY A CA  1 
ATOM   2213  C C   . GLY A  1 313 ? 81.568  71.586  -18.218 1.00   67.06  ? 313 GLY A C   1 
ATOM   2214  O O   . GLY A  1 313 ? 80.966  70.515  -18.291 1.00   69.97  ? 313 GLY A O   1 
ATOM   2215  N N   . PRO A  1 314 ? 82.517  71.817  -17.308 1.00   59.52  ? 314 PRO A N   1 
ATOM   2216  C CA  . PRO A  1 314 ? 83.004  70.897  -16.276 1.00   54.45  ? 314 PRO A CA  1 
ATOM   2217  C C   . PRO A  1 314 ? 82.120  70.863  -15.045 1.00   52.53  ? 314 PRO A C   1 
ATOM   2218  O O   . PRO A  1 314 ? 82.414  70.123  -14.106 1.00   50.62  ? 314 PRO A O   1 
ATOM   2219  C CB  . PRO A  1 314 ? 84.358  71.476  -15.919 1.00   52.22  ? 314 PRO A CB  1 
ATOM   2220  C CG  . PRO A  1 314 ? 84.171  72.928  -16.124 1.00   51.76  ? 314 PRO A CG  1 
ATOM   2221  C CD  . PRO A  1 314 ? 83.249  73.091  -17.289 1.00   55.54  ? 314 PRO A CD  1 
ATOM   2222  N N   . PHE A  1 315 ? 81.080  71.691  -15.042 1.00   54.77  ? 315 PHE A N   1 
ATOM   2223  C CA  . PHE A  1 315 ? 80.240  71.896  -13.868 1.00   52.63  ? 315 PHE A CA  1 
ATOM   2224  C C   . PHE A  1 315 ? 79.023  70.962  -13.833 1.00   56.55  ? 315 PHE A C   1 
ATOM   2225  O O   . PHE A  1 315 ? 78.611  70.449  -14.868 1.00   62.53  ? 315 PHE A O   1 
ATOM   2226  C CB  . PHE A  1 315 ? 79.816  73.353  -13.820 1.00   51.41  ? 315 PHE A CB  1 
ATOM   2227  C CG  . PHE A  1 315 ? 80.979  74.311  -13.886 1.00   50.11  ? 315 PHE A CG  1 
ATOM   2228  C CD1 . PHE A  1 315 ? 81.943  74.327  -12.882 1.00   47.60  ? 315 PHE A CD1 1 
ATOM   2229  C CD2 . PHE A  1 315 ? 81.108  75.198  -14.949 1.00   52.72  ? 315 PHE A CD2 1 
ATOM   2230  C CE1 . PHE A  1 315 ? 83.022  75.198  -12.936 1.00   46.01  ? 315 PHE A CE1 1 
ATOM   2231  C CE2 . PHE A  1 315 ? 82.173  76.082  -15.008 1.00   50.76  ? 315 PHE A CE2 1 
ATOM   2232  C CZ  . PHE A  1 315 ? 83.134  76.082  -14.003 1.00   48.18  ? 315 PHE A CZ  1 
ATOM   2233  N N   . GLY A  1 316 ? 78.486  70.726  -12.632 1.00   54.07  ? 316 GLY A N   1 
ATOM   2234  C CA  . GLY A  1 316 ? 77.360  69.826  -12.410 1.00   54.68  ? 316 GLY A CA  1 
ATOM   2235  C C   . GLY A  1 316 ? 76.016  70.458  -12.056 1.00   57.56  ? 316 GLY A C   1 
ATOM   2236  O O   . GLY A  1 316 ? 74.951  69.839  -12.186 1.00   63.70  ? 316 GLY A O   1 
ATOM   2237  N N   . LEU A  1 317 ? 76.050  71.697  -11.597 1.00   51.73  ? 317 LEU A N   1 
ATOM   2238  C CA  . LEU A  1 317 ? 74.834  72.370  -11.177 1.00   47.91  ? 317 LEU A CA  1 
ATOM   2239  C C   . LEU A  1 317 ? 74.866  73.772  -11.739 1.00   49.72  ? 317 LEU A C   1 
ATOM   2240  O O   . LEU A  1 317 ? 75.612  74.619  -11.258 1.00   51.44  ? 317 LEU A O   1 
ATOM   2241  C CB  . LEU A  1 317 ? 74.757  72.381  -9.658  1.00   41.67  ? 317 LEU A CB  1 
ATOM   2242  C CG  . LEU A  1 317 ? 73.569  72.973  -8.928  1.00   42.41  ? 317 LEU A CG  1 
ATOM   2243  C CD1 . LEU A  1 317 ? 72.272  72.270  -9.308  1.00   44.91  ? 317 LEU A CD1 1 
ATOM   2244  C CD2 . LEU A  1 317 ? 73.842  72.872  -7.437  1.00   39.80  ? 317 LEU A CD2 1 
ATOM   2245  N N   . CYS A  1 318 ? 74.066  74.020  -12.761 1.00   51.77  ? 318 CYS A N   1 
ATOM   2246  C CA  . CYS A  1 318 ? 74.076  75.310  -13.421 1.00   53.79  ? 318 CYS A CA  1 
ATOM   2247  C C   . CYS A  1 318 ? 72.708  75.941  -13.390 1.00   59.99  ? 318 CYS A C   1 
ATOM   2248  O O   . CYS A  1 318 ? 71.693  75.243  -13.328 1.00   60.76  ? 318 CYS A O   1 
ATOM   2249  C CB  . CYS A  1 318 ? 74.537  75.147  -14.852 1.00   54.86  ? 318 CYS A CB  1 
ATOM   2250  S SG  . CYS A  1 318 ? 76.192  74.545  -14.897 1.00   61.39  ? 318 CYS A SG  1 
ATOM   2251  N N   . TYR A  1 319 ? 72.686  77.267  -13.419 1.00   64.24  ? 319 TYR A N   1 
ATOM   2252  C CA  . TYR A  1 319 ? 71.436  78.028  -13.351 1.00   67.19  ? 319 TYR A CA  1 
ATOM   2253  C C   . TYR A  1 319 ? 71.296  79.090  -14.451 1.00   70.76  ? 319 TYR A C   1 
ATOM   2254  O O   . TYR A  1 319 ? 72.297  79.486  -15.057 1.00   71.12  ? 319 TYR A O   1 
ATOM   2255  C CB  . TYR A  1 319 ? 71.340  78.722  -11.991 1.00   65.02  ? 319 TYR A CB  1 
ATOM   2256  C CG  . TYR A  1 319 ? 71.202  77.803  -10.790 1.00   61.84  ? 319 TYR A CG  1 
ATOM   2257  C CD1 . TYR A  1 319 ? 72.303  77.134  -10.270 1.00   60.35  ? 319 TYR A CD1 1 
ATOM   2258  C CD2 . TYR A  1 319 ? 69.978  77.640  -10.152 1.00   60.25  ? 319 TYR A CD2 1 
ATOM   2259  C CE1 . TYR A  1 319 ? 72.176  76.305  -9.159  1.00   59.04  ? 319 TYR A CE1 1 
ATOM   2260  C CE2 . TYR A  1 319 ? 69.841  76.818  -9.050  1.00   58.99  ? 319 TYR A CE2 1 
ATOM   2261  C CZ  . TYR A  1 319 ? 70.939  76.150  -8.553  1.00   59.55  ? 319 TYR A CZ  1 
ATOM   2262  O OH  . TYR A  1 319 ? 70.798  75.324  -7.451  1.00   59.40  ? 319 TYR A OH  1 
ATOM   2263  N N   . ASP A  1 320 ? 70.067  79.558  -14.705 1.00   73.15  ? 320 ASP A N   1 
ATOM   2264  C CA  . ASP A  1 320 ? 69.880  80.754  -15.538 1.00   76.88  ? 320 ASP A CA  1 
ATOM   2265  C C   . ASP A  1 320 ? 70.257  81.987  -14.722 1.00   74.59  ? 320 ASP A C   1 
ATOM   2266  O O   . ASP A  1 320 ? 69.836  82.133  -13.581 1.00   70.72  ? 320 ASP A O   1 
ATOM   2267  C CB  . ASP A  1 320 ? 68.449  80.882  -16.056 1.00   82.49  ? 320 ASP A CB  1 
ATOM   2268  C CG  . ASP A  1 320 ? 68.164  82.259  -16.658 1.00   87.17  ? 320 ASP A CG  1 
ATOM   2269  O OD1 . ASP A  1 320 ? 67.859  83.203  -15.897 1.00   84.99  ? 320 ASP A OD1 1 
ATOM   2270  O OD2 . ASP A  1 320 ? 68.268  82.406  -17.892 1.00   93.38  ? 320 ASP A OD2 1 
ATOM   2271  N N   . SER A  1 321 ? 71.023  82.883  -15.330 1.00   77.94  ? 321 SER A N   1 
ATOM   2272  C CA  . SER A  1 321 ? 71.559  84.064  -14.654 1.00   79.37  ? 321 SER A CA  1 
ATOM   2273  C C   . SER A  1 321 ? 70.519  85.118  -14.285 1.00   84.42  ? 321 SER A C   1 
ATOM   2274  O O   . SER A  1 321 ? 70.659  85.793  -13.263 1.00   86.48  ? 321 SER A O   1 
ATOM   2275  C CB  . SER A  1 321 ? 72.638  84.724  -15.515 1.00   81.07  ? 321 SER A CB  1 
ATOM   2276  O OG  . SER A  1 321 ? 73.575  83.776  -15.985 1.00   80.38  ? 321 SER A OG  1 
ATOM   2277  N N   . ARG A  1 322 ? 69.481  85.266  -15.101 1.00   85.37  ? 322 ARG A N   1 
ATOM   2278  C CA  . ARG A  1 322 ? 68.502  86.298  -14.825 1.00   86.03  ? 322 ARG A CA  1 
ATOM   2279  C C   . ARG A  1 322 ? 67.672  85.946  -13.601 1.00   85.29  ? 322 ARG A C   1 
ATOM   2280  O O   . ARG A  1 322 ? 67.358  86.827  -12.802 1.00   87.85  ? 322 ARG A O   1 
ATOM   2281  C CB  . ARG A  1 322 ? 67.585  86.518  -16.038 0.0000 88.68  ? 322 ARG A CB  1 
ATOM   2282  C CG  . ARG A  1 322 ? 66.131  86.095  -15.822 0.0000 88.12  ? 322 ARG A CG  1 
ATOM   2283  C CD  . ARG A  1 322 ? 65.336  86.145  -17.114 0.0000 91.97  ? 322 ARG A CD  1 
ATOM   2284  N NE  . ARG A  1 322 ? 64.134  85.317  -17.070 0.0000 91.62  ? 322 ARG A NE  1 
ATOM   2285  C CZ  . ARG A  1 322 ? 64.101  84.030  -17.398 0.0000 89.67  ? 322 ARG A CZ  1 
ATOM   2286  N NH1 . ARG A  1 322 ? 65.209  83.412  -17.783 0.0000 87.48  ? 322 ARG A NH1 1 
ATOM   2287  N NH2 . ARG A  1 322 ? 62.956  83.363  -17.341 0.0000 90.40  ? 322 ARG A NH2 1 
ATOM   2288  N N   . LYS A  1 323 ? 67.394  84.663  -13.396 1.00   82.56  ? 323 LYS A N   1 
ATOM   2289  C CA  . LYS A  1 323 ? 66.512  84.265  -12.300 1.00   81.06  ? 323 LYS A CA  1 
ATOM   2290  C C   . LYS A  1 323 ? 67.144  84.213  -10.901 1.00   80.55  ? 323 LYS A C   1 
ATOM   2291  O O   . LYS A  1 323 ? 66.489  84.522  -9.908  1.00   81.80  ? 323 LYS A O   1 
ATOM   2292  C CB  . LYS A  1 323 ? 65.880  82.898  -12.613 1.00   76.11  ? 323 LYS A CB  1 
ATOM   2293  C CG  . LYS A  1 323 ? 65.071  82.827  -13.897 0.0000 78.63  ? 323 LYS A CG  1 
ATOM   2294  C CD  . LYS A  1 323 ? 64.351  81.489  -13.981 0.0000 77.17  ? 323 LYS A CD  1 
ATOM   2295  C CE  . LYS A  1 323 ? 64.083  81.079  -15.417 0.0000 79.95  ? 323 LYS A CE  1 
ATOM   2296  N NZ  . LYS A  1 323 ? 64.117  79.602  -15.580 0.0000 78.25  ? 323 LYS A NZ  1 
ATOM   2297  N N   . ILE A  1 324 ? 68.427  83.895  -10.822 1.00   78.61  ? 324 ILE A N   1 
ATOM   2298  C CA  . ILE A  1 324 ? 69.094  83.759  -9.530  1.00   73.96  ? 324 ILE A CA  1 
ATOM   2299  C C   . ILE A  1 324 ? 69.801  85.012  -9.030  1.00   76.48  ? 324 ILE A C   1 
ATOM   2300  O O   . ILE A  1 324 ? 70.453  84.985  -7.986  1.00   70.86  ? 324 ILE A O   1 
ATOM   2301  C CB  . ILE A  1 324 ? 70.122  82.610  -9.597  0.0000 67.60  ? 324 ILE A CB  1 
ATOM   2302  C CG1 . ILE A  1 324 ? 71.250  82.964  -10.575 0.0000 66.68  ? 324 ILE A CG1 1 
ATOM   2303  C CG2 . ILE A  1 324 ? 69.475  81.379  -10.182 0.0000 67.02  ? 324 ILE A CG2 1 
ATOM   2304  C CD1 . ILE A  1 324 ? 72.531  83.458  -9.935  0.0000 63.75  ? 324 ILE A CD1 1 
ATOM   2305  N N   . SER A  1 325 ? 69.654  86.125  -9.739  1.00   85.23  ? 325 SER A N   1 
ATOM   2306  C CA  . SER A  1 325 ? 70.354  87.329  -9.306  1.00   89.68  ? 325 SER A CA  1 
ATOM   2307  C C   . SER A  1 325 ? 69.703  87.809  -8.010  1.00   91.30  ? 325 SER A C   1 
ATOM   2308  O O   . SER A  1 325 ? 70.283  88.615  -7.273  1.00   91.38  ? 325 SER A O   1 
ATOM   2309  C CB  . SER A  1 325 ? 70.345  88.410  -10.387 1.00   95.84  ? 325 SER A CB  1 
ATOM   2310  O OG  . SER A  1 325 ? 70.636  89.686  -9.841  1.00   98.35  ? 325 SER A OG  1 
ATOM   2311  N N   . GLY A  1 326 ? 68.479  87.333  -7.774  1.00   92.97  ? 326 GLY A N   1 
ATOM   2312  C CA  . GLY A  1 326 ? 67.836  87.401  -6.473  1.00   94.97  ? 326 GLY A CA  1 
ATOM   2313  C C   . GLY A  1 326 ? 68.787  87.358  -5.283  1.00   94.93  ? 326 GLY A C   1 
ATOM   2314  O O   . GLY A  1 326 ? 68.814  88.287  -4.474  1.00   100.64 ? 326 GLY A O   1 
ATOM   2315  N N   . GLY A  1 327 ? 69.527  86.250  -5.155  1.00   86.99  ? 327 GLY A N   1 
ATOM   2316  C CA  . GLY A  1 327 ? 70.368  86.000  -3.989  1.00   79.28  ? 327 GLY A CA  1 
ATOM   2317  C C   . GLY A  1 327 ? 71.073  84.644  -3.926  1.00   70.84  ? 327 GLY A C   1 
ATOM   2318  O O   . GLY A  1 327 ? 70.405  83.618  -3.923  1.00   70.45  ? 327 GLY A O   1 
ATOM   2319  N N   . ALA A  1 328 ? 72.400  84.610  -3.875  1.00   65.33  ? 328 ALA A N   1 
ATOM   2320  C CA  . ALA A  1 328 ? 73.107  83.332  -3.667  1.00   59.02  ? 328 ALA A CA  1 
ATOM   2321  C C   . ALA A  1 328 ? 73.328  83.074  -2.164  1.00   56.83  ? 328 ALA A C   1 
ATOM   2322  O O   . ALA A  1 328 ? 73.329  84.021  -1.373  1.00   60.80  ? 328 ALA A O   1 
ATOM   2323  C CB  . ALA A  1 328 ? 74.436  83.325  -4.407  1.00   57.52  ? 328 ALA A CB  1 
ATOM   2324  N N   . PRO A  1 329 ? 73.430  81.793  -1.742  1.00   51.10  ? 329 PRO A N   1 
ATOM   2325  C CA  . PRO A  1 329 ? 73.570  81.580  -0.293  1.00   49.05  ? 329 PRO A CA  1 
ATOM   2326  C C   . PRO A  1 329 ? 74.993  81.814  0.239   1.00   47.23  ? 329 PRO A C   1 
ATOM   2327  O O   . PRO A  1 329 ? 75.973  81.877  -0.522  1.00   42.79  ? 329 PRO A O   1 
ATOM   2328  C CB  . PRO A  1 329 ? 73.173  80.113  -0.110  1.00   46.30  ? 329 PRO A CB  1 
ATOM   2329  C CG  . PRO A  1 329 ? 73.452  79.472  -1.413  1.00   45.01  ? 329 PRO A CG  1 
ATOM   2330  C CD  . PRO A  1 329 ? 73.254  80.527  -2.471  1.00   47.98  ? 329 PRO A CD  1 
ATOM   2331  N N   . SER A  1 330 ? 75.081  81.969  1.558   1.00   51.21  ? 330 SER A N   1 
ATOM   2332  C CA  . SER A  1 330 ? 76.358  81.982  2.285   1.00   55.22  ? 330 SER A CA  1 
ATOM   2333  C C   . SER A  1 330 ? 77.141  80.659  2.189   1.00   52.13  ? 330 SER A C   1 
ATOM   2334  O O   . SER A  1 330 ? 76.647  79.624  2.636   1.00   53.61  ? 330 SER A O   1 
ATOM   2335  C CB  . SER A  1 330 ? 76.105  82.314  3.754   1.00   58.71  ? 330 SER A CB  1 
ATOM   2336  O OG  . SER A  1 330 ? 75.153  83.355  3.862   1.00   64.44  ? 330 SER A OG  1 
ATOM   2337  N N   . VAL A  1 331 ? 78.358  80.710  1.642   1.00   45.42  ? 331 VAL A N   1 
ATOM   2338  C CA  . VAL A  1 331 ? 79.287  79.571  1.622   1.00   40.18  ? 331 VAL A CA  1 
ATOM   2339  C C   . VAL A  1 331 ? 80.614  79.817  2.360   1.00   41.62  ? 331 VAL A C   1 
ATOM   2340  O O   . VAL A  1 331 ? 81.435  80.617  1.921   1.00   45.42  ? 331 VAL A O   1 
ATOM   2341  C CB  . VAL A  1 331 ? 79.615  79.174  0.171   1.00   34.88  ? 331 VAL A CB  1 
ATOM   2342  C CG1 . VAL A  1 331 ? 80.659  78.079  0.120   1.00   29.09  ? 331 VAL A CG1 1 
ATOM   2343  C CG2 . VAL A  1 331 ? 78.337  78.767  -0.545  1.00   36.95  ? 331 VAL A CG2 1 
ATOM   2344  N N   . ASP A  1 332 ? 80.824  79.132  3.480   1.00   38.27  ? 332 ASP A N   1 
ATOM   2345  C CA  . ASP A  1 332 ? 82.024  79.353  4.299   1.00   34.27  ? 332 ASP A CA  1 
ATOM   2346  C C   . ASP A  1 332 ? 82.772  78.090  4.585   1.00   28.40  ? 332 ASP A C   1 
ATOM   2347  O O   . ASP A  1 332 ? 82.159  77.076  4.864   1.00   28.39  ? 332 ASP A O   1 
ATOM   2348  C CB  . ASP A  1 332 ? 81.698  79.981  5.649   1.00   38.13  ? 332 ASP A CB  1 
ATOM   2349  C CG  . ASP A  1 332 ? 80.936  81.263  5.523   1.00   45.51  ? 332 ASP A CG  1 
ATOM   2350  O OD1 . ASP A  1 332 ? 81.054  81.929  4.471   1.00   48.28  ? 332 ASP A OD1 1 
ATOM   2351  O OD2 . ASP A  1 332 ? 80.252  81.625  6.500   1.00   48.27  ? 332 ASP A OD2 1 
ATOM   2352  N N   . LEU A  1 333 ? 84.098  78.162  4.560   1.00   27.00  ? 333 LEU A N   1 
ATOM   2353  C CA  . LEU A  1 333 ? 84.887  77.055  5.030   1.00   26.33  ? 333 LEU A CA  1 
ATOM   2354  C C   . LEU A  1 333 ? 85.106  77.247  6.527   1.00   28.66  ? 333 LEU A C   1 
ATOM   2355  O O   . LEU A  1 333 ? 85.711  78.224  6.946   1.00   29.61  ? 333 LEU A O   1 
ATOM   2356  C CB  . LEU A  1 333 ? 86.216  76.988  4.288   1.00   24.50  ? 333 LEU A CB  1 
ATOM   2357  C CG  . LEU A  1 333 ? 86.134  77.072  2.760   1.00   24.08  ? 333 LEU A CG  1 
ATOM   2358  C CD1 . LEU A  1 333 ? 87.504  76.910  2.133   1.00   22.67  ? 333 LEU A CD1 1 
ATOM   2359  C CD2 . LEU A  1 333 ? 85.147  76.079  2.211   1.00   24.60  ? 333 LEU A CD2 1 
ATOM   2360  N N   . ILE A  1 334 ? 84.603  76.310  7.322   1.00   28.37  ? 334 ILE A N   1 
ATOM   2361  C CA  . ILE A  1 334 ? 84.817  76.306  8.758   1.00   29.59  ? 334 ILE A CA  1 
ATOM   2362  C C   . ILE A  1 334 ? 86.111  75.578  9.013   1.00   32.93  ? 334 ILE A C   1 
ATOM   2363  O O   . ILE A  1 334 ? 86.271  74.445  8.589   1.00   31.93  ? 334 ILE A O   1 
ATOM   2364  C CB  . ILE A  1 334 ? 83.739  75.577  9.519   1.00   34.25  ? 334 ILE A CB  1 
ATOM   2365  C CG1 . ILE A  1 334 ? 82.335  75.909  9.001   1.00   35.74  ? 334 ILE A CG1 1 
ATOM   2366  C CG2 . ILE A  1 334 ? 83.894  75.879  11.006  1.00   38.13  ? 334 ILE A CG2 1 
ATOM   2367  C CD1 . ILE A  1 334 ? 81.959  77.346  9.101   1.00   35.43  ? 334 ILE A CD1 1 
ATOM   2368  N N   . LEU A  1 335 ? 87.044  76.240  9.667   1.00   35.37  ? 335 LEU A N   1 
ATOM   2369  C CA  . LEU A  1 335 ? 88.400  75.738  9.779   1.00   36.22  ? 335 LEU A CA  1 
ATOM   2370  C C   . LEU A  1 335 ? 88.735  75.085  11.093  1.00   38.34  ? 335 LEU A C   1 
ATOM   2371  O O   . LEU A  1 335 ? 87.914  74.992  11.994  1.00   38.26  ? 335 LEU A O   1 
ATOM   2372  C CB  . LEU A  1 335 ? 89.404  76.856  9.523   1.00   37.43  ? 335 LEU A CB  1 
ATOM   2373  C CG  . LEU A  1 335 ? 89.205  77.504  8.166   1.00   38.69  ? 335 LEU A CG  1 
ATOM   2374  C CD1 . LEU A  1 335 ? 90.214  78.574  8.009   1.00   41.52  ? 335 LEU A CD1 1 
ATOM   2375  C CD2 . LEU A  1 335 ? 89.378  76.467  7.081   1.00   38.99  ? 335 LEU A CD2 1 
ATOM   2376  N N   . ASP A  1 336 ? 89.995  74.656  11.142  1.00   42.28  ? 336 ASP A N   1 
ATOM   2377  C CA  . ASP A  1 336 ? 90.616  73.883  12.204  1.00   46.43  ? 336 ASP A CA  1 
ATOM   2378  C C   . ASP A  1 336 ? 90.145  74.465  13.529  1.00   46.83  ? 336 ASP A C   1 
ATOM   2379  O O   . ASP A  1 336 ? 90.144  75.679  13.718  1.00   46.36  ? 336 ASP A O   1 
ATOM   2380  C CB  . ASP A  1 336 ? 92.151  73.960  12.014  1.00   51.97  ? 336 ASP A CB  1 
ATOM   2381  C CG  . ASP A  1 336 ? 92.963  73.097  13.003  1.00   59.67  ? 336 ASP A CG  1 
ATOM   2382  O OD1 . ASP A  1 336 ? 93.228  71.915  12.677  1.00   63.08  ? 336 ASP A OD1 1 
ATOM   2383  O OD2 . ASP A  1 336 ? 93.395  73.616  14.067  1.00   61.38  ? 336 ASP A OD2 1 
ATOM   2384  N N   . LYS A  1 337 ? 89.624  73.609  14.393  1.00   50.30  ? 337 LYS A N   1 
ATOM   2385  C CA  . LYS A  1 337 ? 89.241  74.009  15.742  1.00   55.89  ? 337 LYS A CA  1 
ATOM   2386  C C   . LYS A  1 337 ? 88.148  75.055  15.725  1.00   56.01  ? 337 LYS A C   1 
ATOM   2387  O O   . LYS A  1 337 ? 87.875  75.670  16.740  1.00   58.85  ? 337 LYS A O   1 
ATOM   2388  C CB  . LYS A  1 337 ? 90.454  74.540  16.500  1.00   61.30  ? 337 LYS A CB  1 
ATOM   2389  C CG  . LYS A  1 337 ? 91.287  73.563  17.292  1.00   68.04  ? 337 LYS A CG  1 
ATOM   2390  C CD  . LYS A  1 337 ? 90.474  72.873  18.356  1.00   76.39  ? 337 LYS A CD  1 
ATOM   2391  C CE  . LYS A  1 337 ? 91.337  71.863  19.089  1.00   82.97  ? 337 LYS A CE  1 
ATOM   2392  N NZ  . LYS A  1 337 ? 91.566  72.333  20.497  1.00   88.58  ? 337 LYS A NZ  1 
ATOM   2393  N N   . ASN A  1 338 ? 87.490  75.205  14.580  1.00   56.48  ? 338 ASN A N   1 
ATOM   2394  C CA  . ASN A  1 338 ? 86.493  76.249  14.345  1.00   58.23  ? 338 ASN A CA  1 
ATOM   2395  C C   . ASN A  1 338 ? 86.937  77.645  14.823  1.00   64.39  ? 338 ASN A C   1 
ATOM   2396  O O   . ASN A  1 338 ? 86.090  78.462  15.215  1.00   67.92  ? 338 ASN A O   1 
ATOM   2397  C CB  . ASN A  1 338 ? 85.186  75.897  15.076  1.00   58.06  ? 338 ASN A CB  1 
ATOM   2398  C CG  . ASN A  1 338 ? 84.733  74.441  14.870  1.00   54.70  ? 338 ASN A CG  1 
ATOM   2399  O OD1 . ASN A  1 338 ? 84.803  73.876  13.774  1.00   47.61  ? 338 ASN A OD1 1 
ATOM   2400  N ND2 . ASN A  1 338 ? 84.275  73.830  15.959  1.00   58.37  ? 338 ASN A ND2 1 
ATOM   2401  N N   . ASP A  1 339 ? 88.238  77.943  14.781  1.00   63.74  ? 339 ASP A N   1 
ATOM   2402  C CA  . ASP A  1 339 ? 88.685  79.270  15.213  1.00   66.27  ? 339 ASP A CA  1 
ATOM   2403  C C   . ASP A  1 339 ? 88.486  80.268  14.126  1.00   63.35  ? 339 ASP A C   1 
ATOM   2404  O O   . ASP A  1 339 ? 88.393  81.460  14.371  1.00   68.19  ? 339 ASP A O   1 
ATOM   2405  C CB  . ASP A  1 339 ? 90.163  79.301  15.551  1.00   70.07  ? 339 ASP A CB  1 
ATOM   2406  C CG  . ASP A  1 339 ? 90.531  78.295  16.555  1.00   76.14  ? 339 ASP A CG  1 
ATOM   2407  O OD1 . ASP A  1 339 ? 90.858  78.660  17.704  1.00   78.73  ? 339 ASP A OD1 1 
ATOM   2408  O OD2 . ASP A  1 339 ? 90.482  77.121  16.163  1.00   78.45  1 339 ASP A OD2 1 
ATOM   2409  N N   . ALA A  1 340 ? 88.432  79.770  12.909  1.00   55.15  ? 340 ALA A N   1 
ATOM   2410  C CA  . ALA A  1 340 ? 88.486  80.657  11.788  1.00   49.73  ? 340 ALA A CA  1 
ATOM   2411  C C   . ALA A  1 340 ? 87.541  80.209  10.711  1.00   46.90  ? 340 ALA A C   1 
ATOM   2412  O O   . ALA A  1 340 ? 87.148  79.047  10.676  1.00   51.47  ? 340 ALA A O   1 
ATOM   2413  C CB  . ALA A  1 340 ? 89.921  80.719  11.257  1.00   47.21  ? 340 ALA A CB  1 
ATOM   2414  N N   . VAL A  1 341 ? 87.196  81.141  9.828   1.00   40.46  ? 341 VAL A N   1 
ATOM   2415  C CA  . VAL A  1 341 ? 86.244  80.916  8.754   1.00   35.42  ? 341 VAL A CA  1 
ATOM   2416  C C   . VAL A  1 341 ? 86.815  81.580  7.545   1.00   31.56  ? 341 VAL A C   1 
ATOM   2417  O O   . VAL A  1 341 ? 87.181  82.743  7.612   1.00   32.83  ? 341 VAL A O   1 
ATOM   2418  C CB  . VAL A  1 341 ? 84.847  81.512  9.055   1.00   38.33  ? 341 VAL A CB  1 
ATOM   2419  C CG1 . VAL A  1 341 ? 84.013  81.644  7.793   1.00   34.88  ? 341 VAL A CG1 1 
ATOM   2420  C CG2 . VAL A  1 341 ? 84.121  80.687  10.112  1.00   41.06  ? 341 VAL A CG2 1 
ATOM   2421  N N   . TRP A  1 342 ? 86.859  80.860  6.435   1.00   29.57  ? 342 TRP A N   1 
ATOM   2422  C CA  . TRP A  1 342 ? 87.231  81.439  5.166   1.00   26.46  ? 342 TRP A CA  1 
ATOM   2423  C C   . TRP A  1 342 ? 85.955  81.630  4.378   1.00   28.35  ? 342 TRP A C   1 
ATOM   2424  O O   . TRP A  1 342 ? 85.412  80.682  3.828   1.00   30.07  ? 342 TRP A O   1 
ATOM   2425  C CB  . TRP A  1 342 ? 88.201  80.560  4.392   1.00   27.13  ? 342 TRP A CB  1 
ATOM   2426  C CG  . TRP A  1 342 ? 88.977  81.344  3.400   1.00   27.29  ? 342 TRP A CG  1 
ATOM   2427  C CD1 . TRP A  1 342 ? 88.686  82.596  2.952   1.00   30.75  ? 342 TRP A CD1 1 
ATOM   2428  C CD2 . TRP A  1 342 ? 90.196  80.968  2.764   1.00   29.56  ? 342 TRP A CD2 1 
ATOM   2429  N NE1 . TRP A  1 342 ? 89.637  83.017  2.057   1.00   29.78  ? 342 TRP A NE1 1 
ATOM   2430  C CE2 . TRP A  1 342 ? 90.577  82.037  1.922   1.00   28.55  ? 342 TRP A CE2 1 
ATOM   2431  C CE3 . TRP A  1 342 ? 90.993  79.823  2.803   1.00   31.44  ? 342 TRP A CE3 1 
ATOM   2432  C CZ2 . TRP A  1 342 ? 91.726  82.004  1.138   1.00   28.35  ? 342 TRP A CZ2 1 
ATOM   2433  C CZ3 . TRP A  1 342 ? 92.129  79.788  2.026   1.00   30.04  ? 342 TRP A CZ3 1 
ATOM   2434  C CH2 . TRP A  1 342 ? 92.489  80.879  1.203   1.00   31.42  ? 342 TRP A CH2 1 
ATOM   2435  N N   . ARG A  1 343 ? 85.449  82.853  4.383   1.00   30.71  ? 343 ARG A N   1 
ATOM   2436  C CA  . ARG A  1 343 ? 84.234  83.182  3.665   1.00   30.97  ? 343 ARG A CA  1 
ATOM   2437  C C   . ARG A  1 343 ? 84.506  83.212  2.168   1.00   35.19  ? 343 ARG A C   1 
ATOM   2438  O O   . ARG A  1 343 ? 85.504  83.787  1.719   1.00   34.11  ? 343 ARG A O   1 
ATOM   2439  C CB  . ARG A  1 343 ? 83.683  84.523  4.143   1.00   32.21  ? 343 ARG A CB  1 
ATOM   2440  C CG  . ARG A  1 343 ? 82.397  84.927  3.475   1.00   33.74  ? 343 ARG A CG  1 
ATOM   2441  C CD  . ARG A  1 343 ? 81.622  85.797  4.392   1.00   39.05  ? 343 ARG A CD  1 
ATOM   2442  N NE  . ARG A  1 343 ? 81.122  84.997  5.502   1.00   42.15  ? 343 ARG A NE  1 
ATOM   2443  C CZ  . ARG A  1 343 ? 80.754  85.478  6.687   1.00   46.19  ? 343 ARG A CZ  1 
ATOM   2444  N NH1 . ARG A  1 343 ? 80.816  86.783  6.953   1.00   48.32  ? 343 ARG A NH1 1 
ATOM   2445  N NH2 . ARG A  1 343 ? 80.309  84.640  7.611   1.00   46.73  ? 343 ARG A NH2 1 
ATOM   2446  N N   . ILE A  1 344 ? 83.629  82.579  1.395   1.00   36.34  ? 344 ILE A N   1 
ATOM   2447  C CA  . ILE A  1 344 ? 83.779  82.575  -0.053  1.00   35.84  ? 344 ILE A CA  1 
ATOM   2448  C C   . ILE A  1 344 ? 82.666  83.422  -0.685  1.00   38.85  ? 344 ILE A C   1 
ATOM   2449  O O   . ILE A  1 344 ? 81.486  83.146  -0.523  1.00   39.20  ? 344 ILE A O   1 
ATOM   2450  C CB  . ILE A  1 344 ? 83.774  81.126  -0.602  1.00   31.53  ? 344 ILE A CB  1 
ATOM   2451  C CG1 . ILE A  1 344 ? 84.794  80.274  0.162   1.00   31.13  ? 344 ILE A CG1 1 
ATOM   2452  C CG2 . ILE A  1 344 ? 84.052  81.101  -2.089  1.00   29.84  ? 344 ILE A CG2 1 
ATOM   2453  C CD1 . ILE A  1 344 ? 84.765  78.837  -0.229  1.00   31.68  ? 344 ILE A CD1 1 
ATOM   2454  N N   . SER A  1 345 ? 83.065  84.466  -1.403  1.00   42.12  ? 345 SER A N   1 
ATOM   2455  C CA  . SER A  1 345 ? 82.126  85.386  -2.042  1.00   44.88  ? 345 SER A CA  1 
ATOM   2456  C C   . SER A  1 345 ? 81.422  84.703  -3.211  1.00   45.31  ? 345 SER A C   1 
ATOM   2457  O O   . SER A  1 345 ? 82.042  83.917  -3.925  1.00   47.33  ? 345 SER A O   1 
ATOM   2458  C CB  . SER A  1 345 ? 82.877  86.649  -2.508  1.00   44.86  ? 345 SER A CB  1 
ATOM   2459  O OG  . SER A  1 345 ? 82.210  87.328  -3.553  1.00   42.98  ? 345 SER A OG  1 
ATOM   2460  N N   . SER A  1 346 ? 80.145  85.017  -3.422  1.00   47.11  ? 346 SER A N   1 
ATOM   2461  C CA  . SER A  1 346 ? 79.363  84.420  -4.510  1.00   47.68  ? 346 SER A CA  1 
ATOM   2462  C C   . SER A  1 346 ? 79.866  84.902  -5.866  1.00   47.01  ? 346 SER A C   1 
ATOM   2463  O O   . SER A  1 346 ? 79.528  84.353  -6.910  1.00   46.22  ? 346 SER A O   1 
ATOM   2464  C CB  . SER A  1 346 ? 77.868  84.727  -4.344  1.00   50.95  ? 346 SER A CB  1 
ATOM   2465  O OG  . SER A  1 346 ? 77.549  86.066  -4.671  1.00   54.22  ? 346 SER A OG  1 
ATOM   2466  N N   . GLU A  1 347 ? 80.740  85.894  -5.831  1.00   48.28  ? 347 GLU A N   1 
ATOM   2467  C CA  . GLU A  1 347 ? 81.353  86.392  -7.040  1.00   52.37  ? 347 GLU A CA  1 
ATOM   2468  C C   . GLU A  1 347 ? 82.584  85.546  -7.331  1.00   48.74  ? 347 GLU A C   1 
ATOM   2469  O O   . GLU A  1 347 ? 83.093  85.559  -8.450  1.00   48.73  ? 347 GLU A O   1 
ATOM   2470  C CB  . GLU A  1 347 ? 81.737  87.856  -6.855  1.00   58.26  ? 347 GLU A CB  1 
ATOM   2471  C CG  . GLU A  1 347 ? 80.568  88.714  -6.424  1.00   67.36  ? 347 GLU A CG  1 
ATOM   2472  C CD  . GLU A  1 347 ? 80.973  90.132  -6.059  1.00   75.61  ? 347 GLU A CD  1 
ATOM   2473  O OE1 . GLU A  1 347 ? 82.054  90.582  -6.505  1.00   76.02  ? 347 GLU A OE1 1 
ATOM   2474  O OE2 . GLU A  1 347 ? 80.188  90.807  -5.346  1.00   81.10  ? 347 GLU A OE2 1 
ATOM   2475  N N   . ASN A  1 348 ? 83.033  84.782  -6.330  1.00   42.93  ? 348 ASN A N   1 
ATOM   2476  C CA  . ASN A  1 348 ? 84.108  83.820  -6.520  1.00   40.92  ? 348 ASN A CA  1 
ATOM   2477  C C   . ASN A  1 348 ? 83.574  82.470  -6.934  1.00   40.91  ? 348 ASN A C   1 
ATOM   2478  O O   . ASN A  1 348 ? 84.048  81.905  -7.912  1.00   44.90  ? 348 ASN A O   1 
ATOM   2479  C CB  . ASN A  1 348 ? 84.965  83.694  -5.250  1.00   41.35  ? 348 ASN A CB  1 
ATOM   2480  C CG  . ASN A  1 348 ? 86.183  82.764  -5.430  1.00   47.50  ? 348 ASN A CG  1 
ATOM   2481  O OD1 . ASN A  1 348 ? 86.049  81.572  -5.723  1.00   50.05  ? 348 ASN A OD1 1 
ATOM   2482  N ND2 . ASN A  1 348 ? 87.385  83.336  -5.311  1.00   49.51  ? 348 ASN A ND2 1 
ATOM   2483  N N   . PHE A  1 349 ? 82.566  81.955  -6.239  1.00   39.18  ? 349 PHE A N   1 
ATOM   2484  C CA  . PHE A  1 349 ? 82.204  80.567  -6.493  1.00   39.63  ? 349 PHE A CA  1 
ATOM   2485  C C   . PHE A  1 349 ? 81.131  80.363  -7.545  1.00   42.59  ? 349 PHE A C   1 
ATOM   2486  O O   . PHE A  1 349 ? 80.815  79.228  -7.882  1.00   43.55  ? 349 PHE A O   1 
ATOM   2487  C CB  . PHE A  1 349 ? 81.797  79.846  -5.197  1.00   38.45  ? 349 PHE A CB  1 
ATOM   2488  C CG  . PHE A  1 349 ? 80.543  80.353  -4.555  1.00   39.64  ? 349 PHE A CG  1 
ATOM   2489  C CD1 . PHE A  1 349 ? 79.300  80.101  -5.119  1.00   42.93  ? 349 PHE A CD1 1 
ATOM   2490  C CD2 . PHE A  1 349 ? 80.596  80.972  -3.329  1.00   39.68  ? 349 PHE A CD2 1 
ATOM   2491  C CE1 . PHE A  1 349 ? 78.133  80.538  -4.515  1.00   45.58  ? 349 PHE A CE1 1 
ATOM   2492  C CE2 . PHE A  1 349 ? 79.442  81.403  -2.709  1.00   42.32  ? 349 PHE A CE2 1 
ATOM   2493  C CZ  . PHE A  1 349 ? 78.202  81.188  -3.304  1.00   45.66  ? 349 PHE A CZ  1 
ATOM   2494  N N   . MET A  1 350 ? 80.533  81.440  -8.036  1.00   45.97  ? 350 MET A N   1 
ATOM   2495  C CA  . MET A  1 350 ? 79.641  81.311  -9.177  1.00   46.48  ? 350 MET A CA  1 
ATOM   2496  C C   . MET A  1 350 ? 80.423  81.626  -10.420 1.00   48.13  ? 350 MET A C   1 
ATOM   2497  O O   . MET A  1 350 ? 81.094  82.648  -10.479 1.00   47.69  ? 350 MET A O   1 
ATOM   2498  C CB  . MET A  1 350 ? 78.434  82.235  -9.068  1.00   48.11  ? 350 MET A CB  1 
ATOM   2499  C CG  . MET A  1 350 ? 77.498  81.928  -7.911  1.00   46.96  ? 350 MET A CG  1 
ATOM   2500  S SD  . MET A  1 350 ? 76.898  80.232  -7.800  1.00   43.45  ? 350 MET A SD  1 
ATOM   2501  C CE  . MET A  1 350 ? 76.070  80.007  -9.371  1.00   43.62  ? 350 MET A CE  1 
ATOM   2502  N N   . VAL A  1 351 ? 80.394  80.716  -11.384 1.00   52.06  ? 351 VAL A N   1 
ATOM   2503  C CA  . VAL A  1 351 ? 81.119  80.908  -12.630 1.00   55.21  ? 351 VAL A CA  1 
ATOM   2504  C C   . VAL A  1 351 ? 80.106  81.088  -13.751 1.00   64.71  ? 351 VAL A C   1 
ATOM   2505  O O   . VAL A  1 351 ? 79.072  80.427  -13.761 1.00   68.66  ? 351 VAL A O   1 
ATOM   2506  C CB  . VAL A  1 351 ? 82.057  79.730  -12.937 1.00   50.86  ? 351 VAL A CB  1 
ATOM   2507  C CG1 . VAL A  1 351 ? 82.876  80.011  -14.189 1.00   51.39  ? 351 VAL A CG1 1 
ATOM   2508  C CG2 . VAL A  1 351 ? 82.956  79.475  -11.761 1.00   46.63  ? 351 VAL A CG2 1 
ATOM   2509  N N   . GLN A  1 352 ? 80.428  81.945  -14.713 1.00   70.36  ? 352 GLN A N   1 
ATOM   2510  C CA  . GLN A  1 352 ? 79.545  82.269  -15.834 1.00   77.57  ? 352 GLN A CA  1 
ATOM   2511  C C   . GLN A  1 352 ? 79.875  81.365  -17.037 1.00   83.48  ? 352 GLN A C   1 
ATOM   2512  O O   . GLN A  1 352 ? 80.275  81.837  -18.096 1.00   89.37  ? 352 GLN A O   1 
ATOM   2513  C CB  . GLN A  1 352 ? 79.671  83.761  -16.187 1.00   79.00  ? 352 GLN A CB  1 
ATOM   2514  C CG  . GLN A  1 352 ? 78.728  84.297  -17.290 1.00   84.22  ? 352 GLN A CG  1 
ATOM   2515  C CD  . GLN A  1 352 ? 77.281  84.326  -16.883 1.00   84.92  ? 352 GLN A CD  1 
ATOM   2516  O OE1 . GLN A  1 352 ? 76.912  84.992  -15.918 1.00   82.05  ? 352 GLN A OE1 1 
ATOM   2517  N NE2 . GLN A  1 352 ? 76.444  83.615  -17.630 1.00   89.28  ? 352 GLN A NE2 1 
ATOM   2518  N N   . ALA A  1 353 ? 79.764  80.055  -16.826 1.00   83.29  ? 353 ALA A N   1 
ATOM   2519  C CA  . ALA A  1 353 ? 79.986  79.034  -17.860 1.00   85.10  ? 353 ALA A CA  1 
ATOM   2520  C C   . ALA A  1 353 ? 79.590  79.471  -19.270 1.00   87.36  ? 353 ALA A C   1 
ATOM   2521  O O   . ALA A  1 353 ? 80.338  79.266  -20.242 1.00   90.37  ? 353 ALA A O   1 
ATOM   2522  C CB  . ALA A  1 353 ? 79.226  77.752  -17.499 1.00   85.52  ? 353 ALA A CB  1 
ATOM   2523  N N   . GLN A  1 354 ? 78.399  80.034  -19.393 1.00   84.45  ? 354 GLN A N   1 
ATOM   2524  C CA  . GLN A  1 354 ? 77.925  80.441  -20.694 1.00   84.04  ? 354 GLN A CA  1 
ATOM   2525  C C   . GLN A  1 354 ? 77.118  81.716  -20.646 1.00   83.13  ? 354 GLN A C   1 
ATOM   2526  O O   . GLN A  1 354 ? 76.796  82.201  -19.566 1.00   77.86  ? 354 GLN A O   1 
ATOM   2527  C CB  . GLN A  1 354 ? 77.142  79.293  -21.313 1.00   86.07  ? 354 GLN A CB  1 
ATOM   2528  C CG  . GLN A  1 354 ? 77.904  78.658  -22.452 1.00   88.83  ? 354 GLN A CG  1 
ATOM   2529  C CD  . GLN A  1 354 ? 77.350  77.316  -22.819 1.00   90.57  ? 354 GLN A CD  1 
ATOM   2530  O OE1 . GLN A  1 354 ? 76.201  77.007  -22.509 1.00   91.66  ? 354 GLN A OE1 1 
ATOM   2531  N NE2 . GLN A  1 354 ? 78.153  76.509  -23.506 1.00   91.51  ? 354 GLN A NE2 1 
ATOM   2532  N N   . ASP A  1 355 ? 76.890  82.280  -21.831 1.00   88.86  ? 355 ASP A N   1 
ATOM   2533  C CA  . ASP A  1 355 ? 75.908  83.338  -22.094 1.00   96.09  ? 355 ASP A CA  1 
ATOM   2534  C C   . ASP A  1 355 ? 75.127  83.907  -20.895 1.00   95.98  ? 355 ASP A C   1 
ATOM   2535  O O   . ASP A  1 355 ? 75.373  85.030  -20.436 1.00   96.91  ? 355 ASP A O   1 
ATOM   2536  C CB  . ASP A  1 355 ? 74.893  82.787  -23.113 1.00   102.73 ? 355 ASP A CB  1 
ATOM   2537  C CG  . ASP A  1 355 ? 74.418  81.379  -22.749 1.00   103.51 ? 355 ASP A CG  1 
ATOM   2538  O OD1 . ASP A  1 355 ? 75.116  80.400  -23.091 1.00   104.39 ? 355 ASP A OD1 1 
ATOM   2539  O OD2 . ASP A  1 355 ? 73.383  81.241  -22.058 1.00   102.44 ? 355 ASP A OD2 1 
ATOM   2540  N N   . GLY A  1 356 ? 74.147  83.127  -20.450 1.00   94.23  ? 356 GLY A N   1 
ATOM   2541  C CA  . GLY A  1 356 ? 73.248  83.455  -19.363 1.00   89.92  ? 356 GLY A CA  1 
ATOM   2542  C C   . GLY A  1 356 ? 73.151  82.260  -18.430 1.00   82.44  ? 356 GLY A C   1 
ATOM   2543  O O   . GLY A  1 356 ? 72.106  82.028  -17.819 1.00   82.39  ? 356 GLY A O   1 
ATOM   2544  N N   . VAL A  1 357 ? 74.236  81.486  -18.355 1.00   75.50  ? 357 VAL A N   1 
ATOM   2545  C CA  . VAL A  1 357 ? 74.320  80.331  -17.469 1.00   68.43  ? 357 VAL A CA  1 
ATOM   2546  C C   . VAL A  1 357 ? 75.433  80.472  -16.453 1.00   64.20  ? 357 VAL A C   1 
ATOM   2547  O O   . VAL A  1 357 ? 76.595  80.630  -16.811 1.00   64.26  ? 357 VAL A O   1 
ATOM   2548  C CB  . VAL A  1 357 ? 74.591  79.031  -18.249 1.00   68.78  ? 357 VAL A CB  1 
ATOM   2549  C CG1 . VAL A  1 357 ? 74.744  77.868  -17.286 1.00   65.80  ? 357 VAL A CG1 1 
ATOM   2550  C CG2 . VAL A  1 357 ? 73.485  78.755  -19.265 1.00   72.18  ? 357 VAL A CG2 1 
ATOM   2551  N N   . SER A  1 358 ? 75.077  80.397  -15.179 1.00   61.16  ? 358 SER A N   1 
ATOM   2552  C CA  . SER A  1 358 ? 76.059  80.499  -14.110 1.00   59.10  ? 358 SER A CA  1 
ATOM   2553  C C   . SER A  1 358 ? 76.096  79.207  -13.345 1.00   55.70  ? 358 SER A C   1 
ATOM   2554  O O   . SER A  1 358 ? 75.075  78.689  -12.912 1.00   54.92  ? 358 SER A O   1 
ATOM   2555  C CB  . SER A  1 358 ? 75.779  81.657  -13.168 1.00   61.45  ? 358 SER A CB  1 
ATOM   2556  O OG  . SER A  1 358 ? 75.900  82.868  -13.873 1.00   67.91  ? 358 SER A OG  1 
ATOM   2557  N N   . CYS A  1 359 ? 77.287  78.649  -13.240 1.00   53.65  ? 359 CYS A N   1 
ATOM   2558  C CA  . CYS A  1 359 ? 77.436  77.335  -12.662 1.00   49.90  ? 359 CYS A CA  1 
ATOM   2559  C C   . CYS A  1 359 ? 78.131  77.438  -11.335 1.00   44.71  ? 359 CYS A C   1 
ATOM   2560  O O   . CYS A  1 359 ? 78.953  78.329  -11.110 1.00   42.68  ? 359 CYS A O   1 
ATOM   2561  C CB  . CYS A  1 359 ? 78.230  76.438  -13.591 1.00   49.65  ? 359 CYS A CB  1 
ATOM   2562  S SG  . CYS A  1 359 ? 77.400  76.155  -15.108 1.00   60.37  ? 359 CYS A SG  1 
ATOM   2563  N N   . LEU A  1 360 ? 77.791  76.518  -10.452 1.00   44.43  ? 360 LEU A N   1 
ATOM   2564  C CA  . LEU A  1 360 ? 78.504  76.393  -9.201  1.00   42.47  ? 360 LEU A CA  1 
ATOM   2565  C C   . LEU A  1 360 ? 79.911  75.881  -9.503  1.00   42.32  ? 360 LEU A C   1 
ATOM   2566  O O   . LEU A  1 360 ? 80.074  74.769  -10.009 1.00   46.99  ? 360 LEU A O   1 
ATOM   2567  C CB  . LEU A  1 360 ? 77.764  75.444  -8.265  1.00   41.43  ? 360 LEU A CB  1 
ATOM   2568  C CG  . LEU A  1 360 ? 78.428  75.119  -6.930  1.00   39.84  ? 360 LEU A CG  1 
ATOM   2569  C CD1 . LEU A  1 360 ? 78.596  76.355  -6.054  1.00   37.78  ? 360 LEU A CD1 1 
ATOM   2570  C CD2 . LEU A  1 360 ? 77.651  73.993  -6.231  1.00   42.61  ? 360 LEU A CD2 1 
ATOM   2571  N N   . GLY A  1 361 ? 80.920  76.699  -9.212  1.00   37.55  ? 361 GLY A N   1 
ATOM   2572  C CA  . GLY A  1 361 ? 82.284  76.437  -9.645  1.00   35.09  ? 361 GLY A CA  1 
ATOM   2573  C C   . GLY A  1 361 ? 83.116  75.478  -8.818  1.00   36.08  ? 361 GLY A C   1 
ATOM   2574  O O   . GLY A  1 361 ? 84.271  75.790  -8.491  1.00   36.04  ? 361 GLY A O   1 
ATOM   2575  N N   . PHE A  1 362 ? 82.536  74.317  -8.493  1.00   37.11  ? 362 PHE A N   1 
ATOM   2576  C CA  . PHE A  1 362 ? 83.227  73.201  -7.836  1.00   35.70  ? 362 PHE A CA  1 
ATOM   2577  C C   . PHE A  1 362 ? 83.146  71.987  -8.737  1.00   36.59  ? 362 PHE A C   1 
ATOM   2578  O O   . PHE A  1 362 ? 82.106  71.717  -9.326  1.00   42.25  ? 362 PHE A O   1 
ATOM   2579  C CB  . PHE A  1 362 ? 82.618  72.851  -6.495  1.00   32.08  ? 362 PHE A CB  1 
ATOM   2580  C CG  . PHE A  1 362 ? 82.728  73.923  -5.480  1.00   30.78  ? 362 PHE A CG  1 
ATOM   2581  C CD1 . PHE A  1 362 ? 81.935  75.042  -5.542  1.00   32.08  ? 362 PHE A CD1 1 
ATOM   2582  C CD2 . PHE A  1 362 ? 83.576  73.786  -4.421  1.00   30.14  ? 362 PHE A CD2 1 
ATOM   2583  C CE1 . PHE A  1 362 ? 82.023  76.022  -4.588  1.00   32.29  ? 362 PHE A CE1 1 
ATOM   2584  C CE2 . PHE A  1 362 ? 83.667  74.767  -3.461  1.00   30.71  ? 362 PHE A CE2 1 
ATOM   2585  C CZ  . PHE A  1 362 ? 82.884  75.883  -3.548  1.00   31.50  ? 362 PHE A CZ  1 
ATOM   2586  N N   . VAL A  1 363 ? 84.231  71.232  -8.827  1.00   35.66  ? 363 VAL A N   1 
ATOM   2587  C CA  . VAL A  1 363 ? 84.268  70.131  -9.781  1.00   37.06  ? 363 VAL A CA  1 
ATOM   2588  C C   . VAL A  1 363 ? 84.480  68.776  -9.074  1.00   36.81  ? 363 VAL A C   1 
ATOM   2589  O O   . VAL A  1 363 ? 85.021  68.722  -7.976  1.00   37.08  ? 363 VAL A O   1 
ATOM   2590  C CB  . VAL A  1 363 ? 85.356  70.414  -10.849 1.00   45.80  ? 363 VAL A CB  1 
ATOM   2591  C CG1 . VAL A  1 363 ? 85.472  69.285  -11.840 1.00   51.62  ? 363 VAL A CG1 1 
ATOM   2592  C CG2 . VAL A  1 363 ? 85.028  71.703  -11.587 1.00   42.70  ? 363 VAL A CG2 1 
ATOM   2593  N N   . ASP A  1 364 ? 83.951  67.708  -9.662  1.00   37.18  ? 364 ASP A N   1 
ATOM   2594  C CA  . ASP A  1 364 ? 84.050  66.366  -9.100  1.00   38.24  ? 364 ASP A CA  1 
ATOM   2595  C C   . ASP A  1 364 ? 85.403  65.734  -9.391  1.00   38.53  ? 364 ASP A C   1 
ATOM   2596  O O   . ASP A  1 364 ? 85.715  65.445  -10.542 1.00   39.08  ? 364 ASP A O   1 
ATOM   2597  C CB  . ASP A  1 364 ? 82.919  65.507  -9.664  1.00   40.66  ? 364 ASP A CB  1 
ATOM   2598  C CG  . ASP A  1 364 ? 82.722  64.197  -8.912  1.00   43.73  ? 364 ASP A CG  1 
ATOM   2599  O OD1 . ASP A  1 364 ? 83.622  63.764  -8.156  1.00   43.82  ? 364 ASP A OD1 1 
ATOM   2600  O OD2 . ASP A  1 364 ? 81.625  63.612  -9.071  1.00   45.22  1 364 ASP A OD2 1 
ATOM   2601  N N   . GLY A  1 365 ? 86.174  65.465  -8.339  1.00   38.02  ? 365 GLY A N   1 
ATOM   2602  C CA  . GLY A  1 365 ? 87.486  64.868  -8.479  1.00   35.92  ? 365 GLY A CA  1 
ATOM   2603  C C   . GLY A  1 365 ? 87.432  63.366  -8.623  1.00   41.49  ? 365 GLY A C   1 
ATOM   2604  O O   . GLY A  1 365 ? 88.462  62.707  -8.763  1.00   43.82  ? 365 GLY A O   1 
ATOM   2605  N N   . GLY A  1 366 ? 86.231  62.805  -8.584  1.00   42.15  ? 366 GLY A N   1 
ATOM   2606  C CA  . GLY A  1 366 ? 86.099  61.378  -8.732  1.00   44.50  ? 366 GLY A CA  1 
ATOM   2607  C C   . GLY A  1 366 ? 86.363  60.652  -7.438  1.00   47.81  ? 366 GLY A C   1 
ATOM   2608  O O   . GLY A  1 366 ? 86.461  61.265  -6.383  1.00   44.27  ? 366 GLY A O   1 
ATOM   2609  N N   . VAL A  1 367 ? 86.482  59.332  -7.540  1.00   55.97  ? 367 VAL A N   1 
ATOM   2610  C CA  . VAL A  1 367 ? 86.596  58.440  -6.390  1.00   59.68  ? 367 VAL A CA  1 
ATOM   2611  C C   . VAL A  1 367 ? 88.031  58.148  -5.985  1.00   65.09  ? 367 VAL A C   1 
ATOM   2612  O O   . VAL A  1 367 ? 88.281  57.565  -4.933  1.00   67.95  ? 367 VAL A O   1 
ATOM   2613  C CB  . VAL A  1 367 ? 85.902  57.118  -6.665  1.00   59.76  ? 367 VAL A CB  1 
ATOM   2614  C CG1 . VAL A  1 367 ? 84.421  57.353  -6.852  1.00   57.74  ? 367 VAL A CG1 1 
ATOM   2615  C CG2 . VAL A  1 367 ? 86.505  56.468  -7.900  1.00   62.41  ? 367 VAL A CG2 1 
ATOM   2616  N N   . HIS A  1 368 ? 88.976  58.504  -6.840  1.00   66.79  ? 368 HIS A N   1 
ATOM   2617  C CA  . HIS A  1 368 ? 90.378  58.386  -6.469  1.00   68.40  ? 368 HIS A CA  1 
ATOM   2618  C C   . HIS A  1 368 ? 90.998  59.763  -6.432  1.00   64.06  ? 368 HIS A C   1 
ATOM   2619  O O   . HIS A  1 368 ? 92.129  59.956  -6.856  1.00   67.50  ? 368 HIS A O   1 
ATOM   2620  C CB  . HIS A  1 368 ? 91.138  57.460  -7.427  1.00   73.88  ? 368 HIS A CB  1 
ATOM   2621  C CG  . HIS A  1 368 ? 90.643  56.048  -7.417  1.00   79.40  ? 368 HIS A CG  1 
ATOM   2622  N ND1 . HIS A  1 368 ? 90.776  55.228  -6.316  1.00   81.13  ? 368 HIS A ND1 1 
ATOM   2623  C CD2 . HIS A  1 368 ? 90.006  55.317  -8.361  1.00   84.00  ? 368 HIS A CD2 1 
ATOM   2624  C CE1 . HIS A  1 368 ? 90.246  54.048  -6.588  1.00   85.88  ? 368 HIS A CE1 1 
ATOM   2625  N NE2 . HIS A  1 368 ? 89.769  54.076  -7.820  1.00   86.94  ? 368 HIS A NE2 1 
ATOM   2626  N N   . ALA A  1 369 ? 90.250  60.723  -5.909  1.00   57.38  ? 369 ALA A N   1 
ATOM   2627  C CA  . ALA A  1 369 ? 90.773  62.059  -5.780  1.00   50.93  ? 369 ALA A CA  1 
ATOM   2628  C C   . ALA A  1 369 ? 91.918  62.060  -4.766  1.00   53.16  ? 369 ALA A C   1 
ATOM   2629  O O   . ALA A  1 369 ? 91.916  61.310  -3.781  1.00   53.78  ? 369 ALA A O   1 
ATOM   2630  C CB  . ALA A  1 369 ? 89.671  63.032  -5.374  1.00   44.57  ? 369 ALA A CB  1 
ATOM   2631  N N   . ARG A  1 370 ? 92.871  62.949  -5.014  1.00   54.14  ? 370 ARG A N   1 
ATOM   2632  C CA  . ARG A  1 370 ? 94.095  63.040  -4.253  1.00   56.19  ? 370 ARG A CA  1 
ATOM   2633  C C   . ARG A  1 370 ? 93.755  63.458  -2.816  1.00   51.12  ? 370 ARG A C   1 
ATOM   2634  O O   . ARG A  1 370 ? 94.244  62.864  -1.855  1.00   52.58  ? 370 ARG A O   1 
ATOM   2635  C CB  . ARG A  1 370 ? 95.025  64.034  -4.973  1.00   63.65  ? 370 ARG A CB  1 
ATOM   2636  C CG  . ARG A  1 370 ? 96.309  64.487  -4.280  1.00   71.08  ? 370 ARG A CG  1 
ATOM   2637  C CD  . ARG A  1 370 ? 97.264  63.320  -4.068  1.00   79.67  ? 370 ARG A CD  1 
ATOM   2638  N NE  . ARG A  1 370 ? 98.491  63.723  -3.379  1.00   82.39  ? 370 ARG A NE  1 
ATOM   2639  C CZ  . ARG A  1 370 ? 98.662  63.722  -2.059  1.00   83.48  ? 370 ARG A CZ  1 
ATOM   2640  N NH1 . ARG A  1 370 ? 97.677  63.359  -1.254  1.00   83.14  ? 370 ARG A NH1 1 
ATOM   2641  N NH2 . ARG A  1 370 ? 99.827  64.088  -1.544  1.00   84.00  ? 370 ARG A NH2 1 
ATOM   2642  N N   . ALA A  1 371 ? 92.854  64.431  -2.686  1.00   45.66  ? 371 ALA A N   1 
ATOM   2643  C CA  . ALA A  1 371 ? 92.348  64.904  -1.392  1.00   38.97  ? 371 ALA A CA  1 
ATOM   2644  C C   . ALA A  1 371 ? 90.838  65.165  -1.439  1.00   37.09  ? 371 ALA A C   1 
ATOM   2645  O O   . ALA A  1 371 ? 90.229  65.219  -2.508  1.00   40.39  ? 371 ALA A O   1 
ATOM   2646  C CB  . ALA A  1 371 ? 93.076  66.158  -0.955  1.00   36.44  ? 371 ALA A CB  1 
ATOM   2647  N N   . GLY A  1 372 ? 90.226  65.307  -0.271  1.00   34.21  ? 372 GLY A N   1 
ATOM   2648  C CA  . GLY A  1 372 ? 88.800  65.573  -0.202  1.00   33.37  ? 372 GLY A CA  1 
ATOM   2649  C C   . GLY A  1 372 ? 88.394  66.912  -0.781  1.00   32.34  ? 372 GLY A C   1 
ATOM   2650  O O   . GLY A  1 372 ? 87.352  67.007  -1.430  1.00   34.62  ? 372 GLY A O   1 
ATOM   2651  N N   . ILE A  1 373 ? 89.199  67.942  -0.512  1.00   31.98  ? 373 ILE A N   1 
ATOM   2652  C CA  . ILE A  1 373 ? 89.029  69.302  -1.041  1.00   29.78  ? 373 ILE A CA  1 
ATOM   2653  C C   . ILE A  1 373 ? 90.343  69.788  -1.618  1.00   30.36  ? 373 ILE A C   1 
ATOM   2654  O O   . ILE A  1 373 ? 91.357  69.726  -0.929  1.00   30.61  ? 373 ILE A O   1 
ATOM   2655  C CB  . ILE A  1 373 ? 88.581  70.310  0.052   1.00   27.07  ? 373 ILE A CB  1 
ATOM   2656  C CG1 . ILE A  1 373 ? 87.263  69.866  0.693   1.00   27.39  ? 373 ILE A CG1 1 
ATOM   2657  C CG2 . ILE A  1 373 ? 88.416  71.708  -0.543  1.00   24.97  ? 373 ILE A CG2 1 
ATOM   2658  C CD1 . ILE A  1 373 ? 86.849  70.677  1.897   1.00   27.32  ? 373 ILE A CD1 1 
ATOM   2659  N N   . ALA A  1 374 ? 90.347  70.282  -2.857  1.00   27.50  ? 374 ALA A N   1 
ATOM   2660  C CA  . ALA A  1 374 ? 91.551  70.933  -3.376  1.00   26.56  ? 374 ALA A CA  1 
ATOM   2661  C C   . ALA A  1 374 ? 91.230  72.344  -3.860  1.00   29.28  ? 374 ALA A C   1 
ATOM   2662  O O   . ALA A  1 374 ? 90.562  72.506  -4.871  1.00   32.60  ? 374 ALA A O   1 
ATOM   2663  C CB  . ALA A  1 374 ? 92.157  70.126  -4.473  1.00   26.86  ? 374 ALA A CB  1 
ATOM   2664  N N   . LEU A  1 375 ? 91.654  73.360  -3.112  1.00   27.70  ? 375 LEU A N   1 
ATOM   2665  C CA  . LEU A  1 375 ? 91.373  74.752  -3.475  1.00   28.97  ? 375 LEU A CA  1 
ATOM   2666  C C   . LEU A  1 375 ? 92.299  75.207  -4.581  1.00   31.11  ? 375 LEU A C   1 
ATOM   2667  O O   . LEU A  1 375 ? 93.495  75.146  -4.407  1.00   32.87  ? 375 LEU A O   1 
ATOM   2668  C CB  . LEU A  1 375 ? 91.519  75.677  -2.259  1.00   28.22  ? 375 LEU A CB  1 
ATOM   2669  C CG  . LEU A  1 375 ? 90.724  75.240  -1.032  1.00   28.25  ? 375 LEU A CG  1 
ATOM   2670  C CD1 . LEU A  1 375 ? 91.075  76.033  0.206   1.00   24.85  ? 375 LEU A CD1 1 
ATOM   2671  C CD2 . LEU A  1 375 ? 89.213  75.323  -1.320  1.00   26.80  ? 375 LEU A CD2 1 
ATOM   2672  N N   . GLY A  1 376 ? 91.762  75.704  -5.691  1.00   30.97  ? 376 GLY A N   1 
ATOM   2673  C CA  . GLY A  1 376 ? 92.579  75.994  -6.856  1.00   29.80  ? 376 GLY A CA  1 
ATOM   2674  C C   . GLY A  1 376 ? 92.797  77.484  -7.051  1.00   30.10  ? 376 GLY A C   1 
ATOM   2675  O O   . GLY A  1 376 ? 92.602  78.260  -6.118  1.00   29.66  ? 376 GLY A O   1 
ATOM   2676  N N   . ALA A  1 377 ? 93.212  77.878  -8.256  1.00   28.17  ? 377 ALA A N   1 
ATOM   2677  C CA  . ALA A  1 377 ? 93.570  79.271  -8.553  1.00   28.28  ? 377 ALA A CA  1 
ATOM   2678  C C   . ALA A  1 377 ? 92.392  80.218  -8.401  1.00   29.73  ? 377 ALA A C   1 
ATOM   2679  O O   . ALA A  1 377 ? 92.524  81.315  -7.874  1.00   31.78  ? 377 ALA A O   1 
ATOM   2680  C CB  . ALA A  1 377 ? 94.145  79.385  -9.969  1.00   29.25  ? 377 ALA A CB  1 
ATOM   2681  N N   . HIS A  1 378 ? 91.225  79.758  -8.822  1.00   29.14  ? 378 HIS A N   1 
ATOM   2682  C CA  . HIS A  1 378 ? 90.045  80.579  -8.797  1.00   28.03  ? 378 HIS A CA  1 
ATOM   2683  C C   . HIS A  1 378 ? 89.722  80.978  -7.383  1.00   27.80  ? 378 HIS A C   1 
ATOM   2684  O O   . HIS A  1 378 ? 89.336  82.108  -7.114  1.00   28.79  ? 378 HIS A O   1 
ATOM   2685  C CB  . HIS A  1 378 ? 88.886  79.799  -9.394  1.00   29.62  ? 378 HIS A CB  1 
ATOM   2686  C CG  . HIS A  1 378 ? 87.730  80.643  -9.794  1.00   33.94  ? 378 HIS A CG  1 
ATOM   2687  N ND1 . HIS A  1 378 ? 87.647  81.253  -11.024 1.00   37.04  ? 378 HIS A ND1 1 
ATOM   2688  C CD2 . HIS A  1 378 ? 86.601  80.986  -9.123  1.00   35.18  ? 378 HIS A CD2 1 
ATOM   2689  C CE1 . HIS A  1 378 ? 86.519  81.942  -11.092 1.00   37.55  ? 378 HIS A CE1 1 
ATOM   2690  N NE2 . HIS A  1 378 ? 85.866  81.793  -9.952  1.00   34.87  ? 378 HIS A NE2 1 
ATOM   2691  N N   . HIS A  1 379 ? 89.915  80.039  -6.473  1.00   27.78  ? 379 HIS A N   1 
ATOM   2692  C CA  . HIS A  1 379 ? 89.691  80.294  -5.073  1.00   26.64  ? 379 HIS A CA  1 
ATOM   2693  C C   . HIS A  1 379 ? 90.628  81.366  -4.571  1.00   30.15  ? 379 HIS A C   1 
ATOM   2694  O O   . HIS A  1 379 ? 90.240  82.248  -3.830  1.00   32.73  ? 379 HIS A O   1 
ATOM   2695  C CB  . HIS A  1 379 ? 89.883  79.030  -4.261  1.00   26.30  ? 379 HIS A CB  1 
ATOM   2696  C CG  . HIS A  1 379 ? 89.644  79.229  -2.800  1.00   27.27  ? 379 HIS A CG  1 
ATOM   2697  N ND1 . HIS A  1 379 ? 88.395  79.135  -2.231  1.00   28.94  ? 379 HIS A ND1 1 
ATOM   2698  C CD2 . HIS A  1 379 ? 90.491  79.524  -1.789  1.00   28.81  ? 379 HIS A CD2 1 
ATOM   2699  C CE1 . HIS A  1 379 ? 88.478  79.369  -0.935  1.00   26.03  ? 379 HIS A CE1 1 
ATOM   2700  N NE2 . HIS A  1 379 ? 89.739  79.608  -0.642  1.00   28.61  ? 379 HIS A NE2 1 
ATOM   2701  N N   . LEU A  1 380 ? 91.870  81.296  -5.005  1.00   31.62  ? 380 LEU A N   1 
ATOM   2702  C CA  . LEU A  1 380 ? 92.913  82.186  -4.516  1.00   31.00  ? 380 LEU A CA  1 
ATOM   2703  C C   . LEU A  1 380 ? 92.827  83.592  -5.048  1.00   29.66  ? 380 LEU A C   1 
ATOM   2704  O O   . LEU A  1 380 ? 93.270  84.521  -4.381  1.00   31.02  ? 380 LEU A O   1 
ATOM   2705  C CB  . LEU A  1 380 ? 94.278  81.617  -4.893  1.00   31.38  ? 380 LEU A CB  1 
ATOM   2706  C CG  . LEU A  1 380 ? 94.595  80.245  -4.344  1.00   29.65  ? 380 LEU A CG  1 
ATOM   2707  C CD1 . LEU A  1 380 ? 95.855  79.653  -5.002  1.00   29.19  ? 380 LEU A CD1 1 
ATOM   2708  C CD2 . LEU A  1 380 ? 94.751  80.386  -2.858  1.00   30.57  ? 380 LEU A CD2 1 
ATOM   2709  N N   . GLU A  1 381 ? 92.270  83.738  -6.252  1.00   31.40  ? 381 GLU A N   1 
ATOM   2710  C CA  . GLU A  1 381 ? 92.205  85.021  -6.959  1.00   30.52  ? 381 GLU A CA  1 
ATOM   2711  C C   . GLU A  1 381 ? 91.480  86.098  -6.178  1.00   32.05  ? 381 GLU A C   1 
ATOM   2712  O O   . GLU A  1 381 ? 90.434  85.844  -5.595  1.00   33.02  ? 381 GLU A O   1 
ATOM   2713  C CB  . GLU A  1 381 ? 91.527  84.844  -8.313  1.00   29.90  ? 381 GLU A CB  1 
ATOM   2714  C CG  . GLU A  1 381 ? 92.430  84.181  -9.322  1.00   30.93  ? 381 GLU A CG  1 
ATOM   2715  C CD  . GLU A  1 381 ? 91.701  83.654  -10.542 1.00   34.02  ? 381 GLU A CD  1 
ATOM   2716  O OE1 . GLU A  1 381 ? 90.469  83.828  -10.641 1.00   36.32  ? 381 GLU A OE1 1 
ATOM   2717  O OE2 . GLU A  1 381 ? 92.370  83.039  -11.397 1.00   33.81  1 381 GLU A OE2 1 
ATOM   2718  N N   . GLU A  1 382 ? 92.060  87.292  -6.187  1.00   27.60  ? 382 GLU A N   1 
ATOM   2719  C CA  . GLU A  1 382 ? 91.571  88.475  -5.474  1.00   32.98  ? 382 GLU A CA  1 
ATOM   2720  C C   . GLU A  1 382 ? 91.536  88.287  -3.972  1.00   31.56  ? 382 GLU A C   1 
ATOM   2721  O O   . GLU A  1 382 ? 90.820  88.970  -3.266  1.00   36.35  ? 382 GLU A O   1 
ATOM   2722  C CB  . GLU A  1 382 ? 90.197  88.906  -5.991  1.00   35.63  ? 382 GLU A CB  1 
ATOM   2723  C CG  . GLU A  1 382 ? 90.223  89.339  -7.444  1.00   37.04  ? 382 GLU A CG  1 
ATOM   2724  C CD  . GLU A  1 382 ? 91.276  90.403  -7.724  1.00   40.61  ? 382 GLU A CD  1 
ATOM   2725  O OE1 . GLU A  1 382 ? 91.473  91.309  -6.900  1.00   40.36  ? 382 GLU A OE1 1 
ATOM   2726  O OE2 . GLU A  1 382 ? 91.912  90.343  -8.786  1.00   44.35  1 382 GLU A OE2 1 
ATOM   2727  N N   . ASN A  1 383 ? 92.372  87.392  -3.484  1.00   30.16  ? 383 ASN A N   1 
ATOM   2728  C CA  . ASN A  1 383 ? 92.603  87.260  -2.059  1.00   30.53  ? 383 ASN A CA  1 
ATOM   2729  C C   . ASN A  1 383 ? 94.081  87.438  -1.781  1.00   30.07  ? 383 ASN A C   1 
ATOM   2730  O O   . ASN A  1 383 ? 94.906  87.084  -2.613  1.00   33.06  ? 383 ASN A O   1 
ATOM   2731  C CB  . ASN A  1 383 ? 92.142  85.892  -1.528  1.00   30.17  ? 383 ASN A CB  1 
ATOM   2732  C CG  . ASN A  1 383 ? 90.625  85.742  -1.493  1.00   32.31  ? 383 ASN A CG  1 
ATOM   2733  O OD1 . ASN A  1 383 ? 89.951  86.408  -0.711  1.00   32.42  ? 383 ASN A OD1 1 
ATOM   2734  N ND2 . ASN A  1 383 ? 90.089  84.844  -2.308  1.00   34.93  ? 383 ASN A ND2 1 
ATOM   2735  N N   . LEU A  1 384 ? 94.414  88.017  -0.636  1.00   29.41  ? 384 LEU A N   1 
ATOM   2736  C CA  . LEU A  1 384 ? 95.796  88.026  -0.187  1.00   27.75  ? 384 LEU A CA  1 
ATOM   2737  C C   . LEU A  1 384 ? 95.993  86.872  0.775   1.00   30.35  ? 384 LEU A C   1 
ATOM   2738  O O   . LEU A  1 384 ? 95.353  86.819  1.825   1.00   30.17  ? 384 LEU A O   1 
ATOM   2739  C CB  . LEU A  1 384 ? 96.174  89.334  0.483   1.00   30.15  ? 384 LEU A CB  1 
ATOM   2740  C CG  . LEU A  1 384 ? 97.602  89.341  1.046   1.00   31.11  ? 384 LEU A CG  1 
ATOM   2741  C CD1 . LEU A  1 384 ? 98.639  89.365  -0.075  1.00   28.83  ? 384 LEU A CD1 1 
ATOM   2742  C CD2 . LEU A  1 384 ? 97.819  90.521  2.002   1.00   33.02  ? 384 LEU A CD2 1 
ATOM   2743  N N   . VAL A  1 385 ? 96.877  85.945  0.386   1.00   29.78  ? 385 VAL A N   1 
ATOM   2744  C CA  . VAL A  1 385 ? 97.142  84.727  1.121   1.00   24.90  ? 385 VAL A CA  1 
ATOM   2745  C C   . VAL A  1 385 ? 98.602  84.644  1.549   1.00   24.66  ? 385 VAL A C   1 
ATOM   2746  O O   . VAL A  1 385 ? 99.484  84.533  0.721   1.00   23.85  ? 385 VAL A O   1 
ATOM   2747  C CB  . VAL A  1 385 ? 96.797  83.526  0.266   1.00   21.31  ? 385 VAL A CB  1 
ATOM   2748  C CG1 . VAL A  1 385 ? 96.976  82.277  1.067   1.00   20.54  ? 385 VAL A CG1 1 
ATOM   2749  C CG2 . VAL A  1 385 ? 95.356  83.658  -0.238  1.00   20.73  ? 385 VAL A CG2 1 
ATOM   2750  N N   . VAL A  1 386 ? 98.845  84.686  2.850   1.00   25.59  ? 386 VAL A N   1 
ATOM   2751  C CA  . VAL A  1 386 ? 100.211 84.710  3.389   1.00   24.71  ? 386 VAL A CA  1 
ATOM   2752  C C   . VAL A  1 386 ? 100.647 83.370  3.915   1.00   27.52  ? 386 VAL A C   1 
ATOM   2753  O O   . VAL A  1 386 ? 100.032 82.833  4.832   1.00   30.71  ? 386 VAL A O   1 
ATOM   2754  C CB  . VAL A  1 386 ? 100.355 85.691  4.526   1.00   24.31  ? 386 VAL A CB  1 
ATOM   2755  C CG1 . VAL A  1 386 ? 101.743 85.623  5.076   1.00   26.44  ? 386 VAL A CG1 1 
ATOM   2756  C CG2 . VAL A  1 386 ? 100.008 87.088  4.063   1.00   25.37  ? 386 VAL A CG2 1 
ATOM   2757  N N   . PHE A  1 387 ? 101.726 82.843  3.359   1.00   25.57  ? 387 PHE A N   1 
ATOM   2758  C CA  . PHE A  1 387 ? 102.255 81.587  3.825   1.00   23.70  ? 387 PHE A CA  1 
ATOM   2759  C C   . PHE A  1 387 ? 103.330 81.868  4.828   1.00   28.47  ? 387 PHE A C   1 
ATOM   2760  O O   . PHE A  1 387 ? 104.448 82.224  4.459   1.00   29.74  ? 387 PHE A O   1 
ATOM   2761  C CB  . PHE A  1 387 ? 102.781 80.784  2.660   1.00   22.52  ? 387 PHE A CB  1 
ATOM   2762  C CG  . PHE A  1 387 ? 101.711 80.349  1.727   1.00   25.84  ? 387 PHE A CG  1 
ATOM   2763  C CD1 . PHE A  1 387 ? 101.181 81.244  0.802   1.00   24.71  ? 387 PHE A CD1 1 
ATOM   2764  C CD2 . PHE A  1 387 ? 101.227 79.051  1.768   1.00   26.78  ? 387 PHE A CD2 1 
ATOM   2765  C CE1 . PHE A  1 387 ? 100.182 80.861  -0.053  1.00   24.16  ? 387 PHE A CE1 1 
ATOM   2766  C CE2 . PHE A  1 387 ? 100.229 78.657  0.909   1.00   27.91  ? 387 PHE A CE2 1 
ATOM   2767  C CZ  . PHE A  1 387 ? 99.705  79.575  -0.008  1.00   27.06  ? 387 PHE A CZ  1 
ATOM   2768  N N   . ASP A  1 388 ? 102.968 81.785  6.106   1.00   29.85  ? 388 ASP A N   1 
ATOM   2769  C CA  . ASP A  1 388 ? 103.917 82.079  7.165   1.00   29.70  ? 388 ASP A CA  1 
ATOM   2770  C C   . ASP A  1 388 ? 104.624 80.795  7.592   1.00   33.13  ? 388 ASP A C   1 
ATOM   2771  O O   . ASP A  1 388 ? 104.165 80.117  8.508   1.00   37.16  ? 388 ASP A O   1 
ATOM   2772  C CB  . ASP A  1 388 ? 103.202 82.732  8.341   1.00   31.82  ? 388 ASP A CB  1 
ATOM   2773  C CG  . ASP A  1 388 ? 104.160 83.275  9.385   1.00   36.73  ? 388 ASP A CG  1 
ATOM   2774  O OD1 . ASP A  1 388 ? 105.375 82.981  9.317   1.00   40.61  ? 388 ASP A OD1 1 
ATOM   2775  O OD2 . ASP A  1 388 ? 103.704 84.024  10.274  1.00   38.27  1 388 ASP A OD2 1 
ATOM   2776  N N   . LEU A  1 389 ? 105.764 80.497  6.961   1.00   28.82  ? 389 LEU A N   1 
ATOM   2777  C CA  . LEU A  1 389 ? 106.452 79.244  7.168   1.00   28.72  ? 389 LEU A CA  1 
ATOM   2778  C C   . LEU A  1 389 ? 107.123 79.225  8.515   1.00   32.64  ? 389 LEU A C   1 
ATOM   2779  O O   . LEU A  1 389 ? 107.364 78.174  9.091   1.00   36.30  ? 389 LEU A O   1 
ATOM   2780  C CB  . LEU A  1 389 ? 107.478 79.022  6.069   1.00   29.50  ? 389 LEU A CB  1 
ATOM   2781  C CG  . LEU A  1 389 ? 106.843 79.262  4.709   1.00   30.81  ? 389 LEU A CG  1 
ATOM   2782  C CD1 . LEU A  1 389 ? 107.908 79.364  3.682   1.00   33.99  ? 389 LEU A CD1 1 
ATOM   2783  C CD2 . LEU A  1 389 ? 105.918 78.102  4.404   1.00   28.29  ? 389 LEU A CD2 1 
ATOM   2784  N N   . GLU A  1 390 ? 107.423 80.401  9.017   1.00   31.11  ? 390 GLU A N   1 
ATOM   2785  C CA  . GLU A  1 390 ? 108.097 80.520  10.286  1.00   32.79  ? 390 GLU A CA  1 
ATOM   2786  C C   . GLU A  1 390 ? 107.195 80.155  11.483  1.00   33.52  ? 390 GLU A C   1 
ATOM   2787  O O   . GLU A  1 390 ? 107.672 79.660  12.510  1.00   34.71  ? 390 GLU A O   1 
ATOM   2788  C CB  . GLU A  1 390 ? 108.645 81.932  10.381  1.00   36.09  ? 390 GLU A CB  1 
ATOM   2789  C CG  . GLU A  1 390 ? 109.242 82.298  11.675  1.00   43.56  ? 390 GLU A CG  1 
ATOM   2790  C CD  . GLU A  1 390 ? 109.413 83.781  11.767  1.00   49.66  ? 390 GLU A CD  1 
ATOM   2791  O OE1 . GLU A  1 390 ? 108.781 84.380  12.663  1.00   57.03  ? 390 GLU A OE1 1 
ATOM   2792  O OE2 . GLU A  1 390 ? 110.139 84.345  10.917  1.00   45.48  ? 390 GLU A OE2 1 
ATOM   2793  N N   . ARG A  1 391 ? 105.892 80.375  11.349  1.00   33.42  ? 391 ARG A N   1 
ATOM   2794  C CA  . ARG A  1 391 ? 104.940 80.006  12.407  1.00   34.92  ? 391 ARG A CA  1 
ATOM   2795  C C   . ARG A  1 391 ? 104.054 78.839  11.962  1.00   34.11  ? 391 ARG A C   1 
ATOM   2796  O O   . ARG A  1 391 ? 103.142 78.448  12.689  1.00   35.63  ? 391 ARG A O   1 
ATOM   2797  C CB  . ARG A  1 391 ? 104.049 81.188  12.804  1.00   36.36  ? 391 ARG A CB  1 
ATOM   2798  C CG  . ARG A  1 391 ? 104.830 82.379  13.307  1.00   40.52  ? 391 ARG A CG  1 
ATOM   2799  C CD  . ARG A  1 391 ? 103.975 83.472  13.926  1.00   47.33  ? 391 ARG A CD  1 
ATOM   2800  N NE  . ARG A  1 391 ? 103.043 82.981  14.938  1.00   58.74  ? 391 ARG A NE  1 
ATOM   2801  C CZ  . ARG A  1 391 ? 102.333 83.770  15.750  1.00   67.78  ? 391 ARG A CZ  1 
ATOM   2802  N NH1 . ARG A  1 391 ? 102.469 85.099  15.690  1.00   69.02  ? 391 ARG A NH1 1 
ATOM   2803  N NH2 . ARG A  1 391 ? 101.496 83.229  16.636  1.00   71.48  ? 391 ARG A NH2 1 
ATOM   2804  N N   . SER A  1 392 ? 104.323 78.303  10.770  1.00   30.68  ? 392 SER A N   1 
ATOM   2805  C CA  . SER A  1 392 ? 103.547 77.214  10.190  1.00   29.00  ? 392 SER A CA  1 
ATOM   2806  C C   . SER A  1 392 ? 102.043 77.526  10.145  1.00   30.63  ? 392 SER A C   1 
ATOM   2807  O O   . SER A  1 392 ? 101.228 76.775  10.689  1.00   30.79  ? 392 SER A O   1 
ATOM   2808  C CB  . SER A  1 392 ? 103.790 75.915  10.962  1.00   29.20  ? 392 SER A CB  1 
ATOM   2809  O OG  . SER A  1 392 ? 103.362 74.778  10.227  1.00   28.49  ? 392 SER A OG  1 
ATOM   2810  N N   . ARG A  1 393 ? 101.676 78.631  9.500   1.00   29.76  ? 393 ARG A N   1 
ATOM   2811  C CA  . ARG A  1 393 ? 100.279 79.036  9.416   1.00   28.99  ? 393 ARG A CA  1 
ATOM   2812  C C   . ARG A  1 393 ? 100.047 79.749  8.110   1.00   27.58  ? 393 ARG A C   1 
ATOM   2813  O O   . ARG A  1 393 ? 100.978 80.266  7.505   1.00   26.29  ? 393 ARG A O   1 
ATOM   2814  C CB  . ARG A  1 393 ? 99.880  79.946  10.584  1.00   29.96  ? 393 ARG A CB  1 
ATOM   2815  C CG  . ARG A  1 393 ? 100.598 81.286  10.609  1.00   31.04  ? 393 ARG A CG  1 
ATOM   2816  C CD  . ARG A  1 393 ? 100.295 82.028  11.885  1.00   31.50  ? 393 ARG A CD  1 
ATOM   2817  N NE  . ARG A  1 393 ? 100.871 83.364  11.889  1.00   32.83  ? 393 ARG A NE  1 
ATOM   2818  C CZ  . ARG A  1 393 ? 100.529 84.338  12.724  1.00   33.71  ? 393 ARG A CZ  1 
ATOM   2819  N NH1 . ARG A  1 393 ? 99.615  84.138  13.667  1.00   35.33  ? 393 ARG A NH1 1 
ATOM   2820  N NH2 . ARG A  1 393 ? 101.128 85.512  12.636  1.00   34.46  ? 393 ARG A NH2 1 
ATOM   2821  N N   . VAL A  1 394 ? 98.785  79.761  7.691   1.00   28.36  ? 394 VAL A N   1 
ATOM   2822  C CA  . VAL A  1 394 ? 98.351  80.489  6.511   1.00   29.86  ? 394 VAL A CA  1 
ATOM   2823  C C   . VAL A  1 394 ? 97.449  81.636  6.963   1.00   30.26  ? 394 VAL A C   1 
ATOM   2824  O O   . VAL A  1 394 ? 96.562  81.428  7.798   1.00   29.80  ? 394 VAL A O   1 
ATOM   2825  C CB  . VAL A  1 394 ? 97.551  79.596  5.537   1.00   31.42  ? 394 VAL A CB  1 
ATOM   2826  C CG1 . VAL A  1 394 ? 97.151  80.397  4.329   1.00   33.30  ? 394 VAL A CG1 1 
ATOM   2827  C CG2 . VAL A  1 394 ? 98.351  78.458  5.072   1.00   32.31  ? 394 VAL A CG2 1 
ATOM   2828  N N   . GLY A  1 395 ? 97.666  82.834  6.420   1.00   29.62  ? 395 GLY A N   1 
ATOM   2829  C CA  . GLY A  1 395 ? 96.806  83.971  6.715   1.00   29.30  ? 395 GLY A CA  1 
ATOM   2830  C C   . GLY A  1 395 ? 96.034  84.436  5.491   1.00   27.25  ? 395 GLY A C   1 
ATOM   2831  O O   . GLY A  1 395 ? 96.506  84.280  4.380   1.00   24.18  ? 395 GLY A O   1 
ATOM   2832  N N   . PHE A  1 396 ? 94.841  84.990  5.688   1.00   29.45  ? 396 PHE A N   1 
ATOM   2833  C CA  . PHE A  1 396 ? 94.049  85.500  4.562   1.00   30.97  ? 396 PHE A CA  1 
ATOM   2834  C C   . PHE A  1 396 ? 93.217  86.705  4.980   1.00   31.07  ? 396 PHE A C   1 
ATOM   2835  O O   . PHE A  1 396 ? 92.954  86.915  6.165   1.00   33.35  ? 396 PHE A O   1 
ATOM   2836  C CB  . PHE A  1 396 ? 93.120  84.416  3.962   1.00   28.79  ? 396 PHE A CB  1 
ATOM   2837  C CG  . PHE A  1 396 ? 92.240  83.737  4.971   1.00   29.02  ? 396 PHE A CG  1 
ATOM   2838  C CD1 . PHE A  1 396 ? 91.034  84.297  5.356   1.00   30.03  ? 396 PHE A CD1 1 
ATOM   2839  C CD2 . PHE A  1 396 ? 92.612  82.532  5.527   1.00   28.36  ? 396 PHE A CD2 1 
ATOM   2840  C CE1 . PHE A  1 396 ? 90.245  83.683  6.287   1.00   29.41  ? 396 PHE A CE1 1 
ATOM   2841  C CE2 . PHE A  1 396 ? 91.822  81.916  6.457   1.00   26.54  ? 396 PHE A CE2 1 
ATOM   2842  C CZ  . PHE A  1 396 ? 90.641  82.486  6.836   1.00   26.47  ? 396 PHE A CZ  1 
ATOM   2843  N N   . ASN A  1 397 ? 92.811  87.503  3.998   1.00   30.93  ? 397 ASN A N   1 
ATOM   2844  C CA  . ASN A  1 397 ? 92.008  88.661  4.283   1.00   32.30  ? 397 ASN A CA  1 
ATOM   2845  C C   . ASN A  1 397 ? 90.630  88.248  4.795   1.00   32.17  ? 397 ASN A C   1 
ATOM   2846  O O   . ASN A  1 397 ? 89.959  87.405  4.195   1.00   32.89  ? 397 ASN A O   1 
ATOM   2847  C CB  . ASN A  1 397 ? 91.904  89.553  3.043   1.00   33.23  ? 397 ASN A CB  1 
ATOM   2848  C CG  . ASN A  1 397 ? 91.555  88.797  1.799   1.00   29.87  ? 397 ASN A CG  1 
ATOM   2849  O OD1 . ASN A  1 397 ? 92.320  87.988  1.327   1.00   28.53  ? 397 ASN A OD1 1 
ATOM   2850  N ND2 . ASN A  1 397 ? 90.381  89.080  1.244   1.00   32.60  ? 397 ASN A ND2 1 
ATOM   2851  N N   . SER A  1 398 ? 90.225  88.843  5.918   1.00   33.05  ? 398 SER A N   1 
ATOM   2852  C CA  . SER A  1 398 ? 88.960  88.509  6.576   1.00   36.53  ? 398 SER A CA  1 
ATOM   2853  C C   . SER A  1 398 ? 87.786  89.314  6.031   1.00   38.43  ? 398 SER A C   1 
ATOM   2854  O O   . SER A  1 398 ? 86.637  89.029  6.333   1.00   39.49  ? 398 SER A O   1 
ATOM   2855  C CB  . SER A  1 398 ? 89.071  88.703  8.093   1.00   36.53  ? 398 SER A CB  1 
ATOM   2856  O OG  . SER A  1 398 ? 89.486  90.011  8.438   1.00   38.57  ? 398 SER A OG  1 
ATOM   2857  N N   . ASN A  1 399 ? 88.090  90.328  5.235   1.00   36.75  ? 399 ASN A N   1 
ATOM   2858  C CA  . ASN A  1 399 ? 87.075  91.020  4.474   1.00   39.17  ? 399 ASN A CA  1 
ATOM   2859  C C   . ASN A  1 399 ? 87.550  91.018  3.018   1.00   40.44  ? 399 ASN A C   1 
ATOM   2860  O O   . ASN A  1 399 ? 88.734  90.822  2.761   1.00   41.28  ? 399 ASN A O   1 
ATOM   2861  C CB  . ASN A  1 399 ? 86.856  92.443  5.005   1.00   37.39  ? 399 ASN A CB  1 
ATOM   2862  C CG  . ASN A  1 399 ? 86.456  92.471  6.472   1.00   37.90  ? 399 ASN A CG  1 
ATOM   2863  O OD1 . ASN A  1 399 ? 85.323  92.154  6.842   1.00   38.06  ? 399 ASN A OD1 1 
ATOM   2864  N ND2 . ASN A  1 399 ? 87.392  92.863  7.319   1.00   39.55  ? 399 ASN A ND2 1 
ATOM   2865  N N   . SER A  1 400 ? 86.647  91.225  2.068   1.00   40.91  ? 400 SER A N   1 
ATOM   2866  C CA  . SER A  1 400 ? 87.024  91.223  0.657   1.00   38.52  ? 400 SER A CA  1 
ATOM   2867  C C   . SER A  1 400 ? 87.989  92.349  0.345   1.00   37.13  ? 400 SER A C   1 
ATOM   2868  O O   . SER A  1 400 ? 87.926  93.403  0.961   1.00   38.14  ? 400 SER A O   1 
ATOM   2869  C CB  . SER A  1 400 ? 85.781  91.328  -0.235  1.00   36.11  ? 400 SER A CB  1 
ATOM   2870  O OG  . SER A  1 400 ? 85.219  92.618  -0.176  1.00   40.02  ? 400 SER A OG  1 
ATOM   2871  N N   . LEU A  1 401 ? 88.879  92.132  -0.618  1.00   37.67  ? 401 LEU A N   1 
ATOM   2872  C CA  . LEU A  1 401 ? 89.814  93.189  -1.015  1.00   41.25  ? 401 LEU A CA  1 
ATOM   2873  C C   . LEU A  1 401 ? 89.054  94.398  -1.489  1.00   38.91  ? 401 LEU A C   1 
ATOM   2874  O O   . LEU A  1 401 ? 89.414  95.539  -1.203  1.00   39.00  ? 401 LEU A O   1 
ATOM   2875  C CB  . LEU A  1 401 ? 90.771  92.728  -2.122  1.00   41.74  ? 401 LEU A CB  1 
ATOM   2876  C CG  . LEU A  1 401 ? 91.803  91.655  -1.821  1.00   37.91  ? 401 LEU A CG  1 
ATOM   2877  C CD1 . LEU A  1 401 ? 92.779  91.613  -2.945  1.00   37.03  ? 401 LEU A CD1 1 
ATOM   2878  C CD2 . LEU A  1 401 ? 92.492  91.924  -0.499  1.00   36.49  ? 401 LEU A CD2 1 
ATOM   2879  N N   . LYS A  1 402 ? 87.979  94.106  -2.201  1.00   39.12  ? 402 LYS A N   1 
ATOM   2880  C CA  . LYS A  1 402 ? 87.109  95.105  -2.816  1.00   43.58  ? 402 LYS A CA  1 
ATOM   2881  C C   . LYS A  1 402 ? 86.420  95.949  -1.743  1.00   41.96  ? 402 LYS A C   1 
ATOM   2882  O O   . LYS A  1 402 ? 86.123  97.099  -1.980  1.00   45.84  ? 402 LYS A O   1 
ATOM   2883  C CB  . LYS A  1 402 ? 86.124  94.387  -3.739  1.00   46.93  ? 402 LYS A CB  1 
ATOM   2884  C CG  . LYS A  1 402 ? 85.049  95.159  -4.431  1.00   54.29  ? 402 LYS A CG  1 
ATOM   2885  C CD  . LYS A  1 402 ? 84.341  94.131  -5.321  1.00   59.64  ? 402 LYS A CD  1 
ATOM   2886  C CE  . LYS A  1 402 ? 83.088  94.632  -6.012  1.00   66.87  ? 402 LYS A CE  1 
ATOM   2887  N NZ  . LYS A  1 402 ? 82.978  93.966  -7.351  1.00   68.93  ? 402 LYS A NZ  1 
ATOM   2888  N N   . SER A  1 403 ? 86.201  95.395  -0.554  1.00   40.97  ? 403 SER A N   1 
ATOM   2889  C CA  . SER A  1 403 ? 85.676  96.182  0.563   1.00   44.84  ? 403 SER A CA  1 
ATOM   2890  C C   . SER A  1 403 ? 86.702  97.178  1.117   1.00   50.58  ? 403 SER A C   1 
ATOM   2891  O O   . SER A  1 403 ? 86.337  98.067  1.887   1.00   56.55  ? 403 SER A O   1 
ATOM   2892  C CB  . SER A  1 403 ? 85.198  95.284  1.699   1.00   42.57  ? 403 SER A CB  1 
ATOM   2893  O OG  . SER A  1 403 ? 86.250  94.930  2.580   1.00   39.69  ? 403 SER A OG  1 
ATOM   2894  N N   . TYR A  1 404 ? 87.980  97.014  0.762   1.00   47.70  ? 404 TYR A N   1 
ATOM   2895  C CA  . TYR A  1 404 ? 89.020  97.980  1.133   1.00   45.99  ? 404 TYR A CA  1 
ATOM   2896  C C   . TYR A  1 404 ? 89.278  98.972  0.014   1.00   48.18  ? 404 TYR A C   1 
ATOM   2897  O O   . TYR A  1 404 ? 90.090  99.884  0.154   1.00   49.27  ? 404 TYR A O   1 
ATOM   2898  C CB  . TYR A  1 404 ? 90.325  97.272  1.481   1.00   44.41  ? 404 TYR A CB  1 
ATOM   2899  C CG  . TYR A  1 404 ? 90.223  96.347  2.667   1.00   44.72  ? 404 TYR A CG  1 
ATOM   2900  C CD1 . TYR A  1 404 ? 90.351  96.825  3.963   1.00   45.65  ? 404 TYR A CD1 1 
ATOM   2901  C CD2 . TYR A  1 404 ? 89.998  94.993  2.492   1.00   43.99  ? 404 TYR A CD2 1 
ATOM   2902  C CE1 . TYR A  1 404 ? 90.255  95.970  5.054   1.00   46.02  ? 404 TYR A CE1 1 
ATOM   2903  C CE2 . TYR A  1 404 ? 89.915  94.127  3.572   1.00   44.10  ? 404 TYR A CE2 1 
ATOM   2904  C CZ  . TYR A  1 404 ? 90.035  94.617  4.856   1.00   45.37  ? 404 TYR A CZ  1 
ATOM   2905  O OH  . TYR A  1 404 ? 89.941  93.751  5.940   1.00   43.62  ? 404 TYR A OH  1 
ATOM   2906  N N   . GLY A  1 405 ? 88.567  98.788  -1.093  1.00   49.88  ? 405 GLY A N   1 
ATOM   2907  C CA  . GLY A  1 405 ? 88.786  99.556  -2.306  1.00   52.92  ? 405 GLY A CA  1 
ATOM   2908  C C   . GLY A  1 405 ? 89.988  99.064  -3.092  1.00   54.62  ? 405 GLY A C   1 
ATOM   2909  O O   . GLY A  1 405 ? 90.519  99.796  -3.932  1.00   56.18  ? 405 GLY A O   1 
ATOM   2910  N N   . LYS A  1 406 ? 90.393  97.812  -2.836  1.00   49.94  ? 406 LYS A N   1 
ATOM   2911  C CA  . LYS A  1 406 ? 91.596  97.239  -3.421  1.00   44.20  ? 406 LYS A CA  1 
ATOM   2912  C C   . LYS A  1 406 ? 91.298  96.062  -4.309  1.00   44.10  ? 406 LYS A C   1 
ATOM   2913  O O   . LYS A  1 406 ? 90.247  95.433  -4.192  1.00   39.06  ? 406 LYS A O   1 
ATOM   2914  C CB  . LYS A  1 406 ? 92.552  96.754  -2.333  1.00   41.99  ? 406 LYS A CB  1 
ATOM   2915  C CG  . LYS A  1 406 ? 92.808  97.742  -1.240  1.00   46.57  ? 406 LYS A CG  1 
ATOM   2916  C CD  . LYS A  1 406 ? 93.611  98.899  -1.735  1.00   53.62  ? 406 LYS A CD  1 
ATOM   2917  C CE  . LYS A  1 406 ? 93.643  100.005 -0.706  1.00   60.19  ? 406 LYS A CE  1 
ATOM   2918  N NZ  . LYS A  1 406 ? 93.894  99.446  0.644   1.00   60.38  ? 406 LYS A NZ  1 
ATOM   2919  N N   . THR A  1 407 ? 92.274  95.742  -5.156  1.00   44.40  ? 407 THR A N   1 
ATOM   2920  C CA  . THR A  1 407 ? 92.307  94.492  -5.912  1.00   42.79  ? 407 THR A CA  1 
ATOM   2921  C C   . THR A  1 407 ? 93.703  93.891  -5.778  1.00   40.50  ? 407 THR A C   1 
ATOM   2922  O O   . THR A  1 407 ? 94.601  94.519  -5.227  1.00   39.89  ? 407 THR A O   1 
ATOM   2923  C CB  . THR A  1 407 ? 91.977  94.672  -7.405  1.00   44.20  ? 407 THR A CB  1 
ATOM   2924  O OG1 . THR A  1 407 ? 93.055  95.343  -8.061  1.00   45.34  ? 407 THR A OG1 1 
ATOM   2925  C CG2 . THR A  1 407 ? 90.722  95.461  -7.573  1.00   42.90  ? 407 THR A CG2 1 
ATOM   2926  N N   . CYS A  1 408 ? 93.888  92.665  -6.246  1.00   36.39  ? 408 CYS A N   1 
ATOM   2927  C CA  . CYS A  1 408 ? 95.209  92.081  -6.205  1.00   35.62  ? 408 CYS A CA  1 
ATOM   2928  C C   . CYS A  1 408 ? 96.170  92.766  -7.168  1.00   37.46  ? 408 CYS A C   1 
ATOM   2929  O O   . CYS A  1 408 ? 97.368  92.646  -7.011  1.00   36.94  ? 408 CYS A O   1 
ATOM   2930  C CB  . CYS A  1 408 ? 95.143  90.579  -6.479  1.00   32.95  ? 408 CYS A CB  1 
ATOM   2931  S SG  . CYS A  1 408 ? 94.948  89.611  -4.983  1.00   36.57  ? 408 CYS A SG  1 
ATOM   2932  N N   . SER A  1 409 ? 95.656  93.510  -8.144  1.00   41.36  ? 409 SER A N   1 
ATOM   2933  C CA  . SER A  1 409 ? 96.518  94.237  -9.069  1.00   44.42  ? 409 SER A CA  1 
ATOM   2934  C C   . SER A  1 409 ? 97.058  95.533  -8.487  1.00   45.57  ? 409 SER A C   1 
ATOM   2935  O O   . SER A  1 409 ? 98.154  95.961  -8.833  1.00   45.18  ? 409 SER A O   1 
ATOM   2936  C CB  . SER A  1 409 ? 95.769  94.579  -10.354 1.00   48.08  ? 409 SER A CB  1 
ATOM   2937  O OG  . SER A  1 409 ? 95.305  93.419  -11.002 1.00   49.92  ? 409 SER A OG  1 
ATOM   2938  N N   . ASN A  1 410 ? 96.286  96.172  -7.614  1.00   46.33  ? 410 ASN A N   1 
ATOM   2939  C CA  . ASN A  1 410 ? 96.692  97.477  -7.114  1.00   46.47  ? 410 ASN A CA  1 
ATOM   2940  C C   . ASN A  1 410 ? 96.986  97.552  -5.615  1.00   44.70  ? 410 ASN A C   1 
ATOM   2941  O O   . ASN A  1 410 ? 97.323  98.619  -5.108  1.00   46.46  ? 410 ASN A O   1 
ATOM   2942  C CB  . ASN A  1 410 ? 95.627  98.522  -7.517  1.00   50.36  ? 410 ASN A CB  1 
ATOM   2943  C CG  . ASN A  1 410 ? 94.257  98.279  -6.878  1.00   51.54  ? 410 ASN A CG  1 
ATOM   2944  O OD1 . ASN A  1 410 ? 94.144  97.859  -5.727  1.00   51.84  ? 410 ASN A OD1 1 
ATOM   2945  N ND2 . ASN A  1 410 ? 93.207  98.501  -7.658  1.00   53.70  ? 410 ASN A ND2 1 
ATOM   2946  N N   . LEU A  1 411 ? 96.933  96.418  -4.925  1.00   42.98  ? 411 LEU A N   1 
ATOM   2947  C CA  . LEU A  1 411 ? 97.293  96.374  -3.507  1.00   42.67  ? 411 LEU A CA  1 
ATOM   2948  C C   . LEU A  1 411 ? 98.753  96.823  -3.340  1.00   46.46  ? 411 LEU A C   1 
ATOM   2949  O O   . LEU A  1 411 ? 99.106  97.541  -2.396  1.00   48.76  ? 411 LEU A O   1 
ATOM   2950  C CB  . LEU A  1 411 ? 97.064  94.976  -2.957  1.00   40.05  ? 411 LEU A CB  1 
ATOM   2951  C CG  . LEU A  1 411 ? 97.146  94.802  -1.447  1.00   37.77  ? 411 LEU A CG  1 
ATOM   2952  C CD1 . LEU A  1 411 ? 96.121  95.700  -0.790  1.00   39.64  ? 411 LEU A CD1 1 
ATOM   2953  C CD2 . LEU A  1 411 ? 96.916  93.331  -1.072  1.00   35.04  ? 411 LEU A CD2 1 
ATOM   2954  N N   . PHE A  1 412 ? 99.580  96.404  -4.290  1.00   45.65  ? 412 PHE A N   1 
ATOM   2955  C CA  . PHE A  1 412 ? 100.976 96.803  -4.343  1.00   43.90  ? 412 PHE A CA  1 
ATOM   2956  C C   . PHE A  1 412 ? 101.270 97.416  -5.706  1.00   44.39  ? 412 PHE A C   1 
ATOM   2957  O O   . PHE A  1 412 ? 100.609 97.097  -6.689  1.00   47.33  ? 412 PHE A O   1 
ATOM   2958  C CB  . PHE A  1 412 ? 101.885 95.597  -4.101  1.00   41.66  ? 412 PHE A CB  1 
ATOM   2959  C CG  . PHE A  1 412 ? 101.559 94.837  -2.851  1.00   37.57  ? 412 PHE A CG  1 
ATOM   2960  C CD1 . PHE A  1 412 ? 101.921 95.332  -1.614  1.00   38.07  ? 412 PHE A CD1 1 
ATOM   2961  C CD2 . PHE A  1 412 ? 100.888 93.631  -2.914  1.00   33.25  ? 412 PHE A CD2 1 
ATOM   2962  C CE1 . PHE A  1 412 ? 101.621 94.640  -0.460  1.00   33.41  ? 412 PHE A CE1 1 
ATOM   2963  C CE2 . PHE A  1 412 ? 100.584 92.934  -1.765  1.00   32.86  ? 412 PHE A CE2 1 
ATOM   2964  C CZ  . PHE A  1 412 ? 100.950 93.439  -0.536  1.00   33.08  ? 412 PHE A CZ  1 
ATOM   2965  N N   . ASP A  1 413 ? 102.261 98.297  -5.762  1.00   43.57  ? 413 ASP A N   1 
ATOM   2966  C CA  . ASP A  1 413 ? 102.650 98.919  -7.020  1.00   46.95  ? 413 ASP A CA  1 
ATOM   2967  C C   . ASP A  1 413 ? 103.471 97.953  -7.863  1.00   47.62  ? 413 ASP A C   1 
ATOM   2968  O O   . ASP A  1 413 ? 104.630 97.690  -7.562  1.00   47.45  ? 413 ASP A O   1 
ATOM   2969  C CB  . ASP A  1 413 ? 103.447 100.198 -6.760  1.00   50.09  ? 413 ASP A CB  1 
ATOM   2970  C CG  . ASP A  1 413 ? 103.600 101.055 -8.001  1.00   55.87  ? 413 ASP A CG  1 
ATOM   2971  O OD1 . ASP A  1 413 ? 103.746 100.493 -9.103  1.00   57.39  ? 413 ASP A OD1 1 
ATOM   2972  O OD2 . ASP A  1 413 ? 103.575 102.294 -7.872  1.00   60.06  1 413 ASP A OD2 1 
ATOM   2973  N N   . LEU A  1 414 ? 102.863 97.424  -8.918  1.00   49.38  ? 414 LEU A N   1 
ATOM   2974  C CA  . LEU A  1 414 ? 103.535 96.474  -9.795  1.00   48.85  ? 414 LEU A CA  1 
ATOM   2975  C C   . LEU A  1 414 ? 103.988 97.130  -11.092 1.00   56.57  ? 414 LEU A C   1 
ATOM   2976  O O   . LEU A  1 414 ? 104.325 96.449  -12.057 1.00   57.20  ? 414 LEU A O   1 
ATOM   2977  C CB  . LEU A  1 414 ? 102.619 95.291  -10.107 1.00   44.93  ? 414 LEU A CB  1 
ATOM   2978  C CG  . LEU A  1 414 ? 102.016 94.582  -8.896  1.00   41.82  ? 414 LEU A CG  1 
ATOM   2979  C CD1 . LEU A  1 414 ? 101.154 93.413  -9.337  1.00   40.01  ? 414 LEU A CD1 1 
ATOM   2980  C CD2 . LEU A  1 414 ? 103.113 94.124  -7.951  1.00   42.42  ? 414 LEU A CD2 1 
ATOM   2981  N N   . ASN A  1 415 ? 103.990 98.456  -11.111 1.00   64.79  ? 415 ASN A N   1 
ATOM   2982  C CA  . ASN A  1 415 ? 104.392 99.194  -12.298 1.00   72.08  ? 415 ASN A CA  1 
ATOM   2983  C C   . ASN A  1 415 ? 105.904 99.302  -12.433 1.00   74.05  ? 415 ASN A C   1 
ATOM   2984  O O   . ASN A  1 415 ? 106.611 99.534  -11.455 1.00   72.59  ? 415 ASN A O   1 
ATOM   2985  C CB  . ASN A  1 415 ? 103.763 100.585 -12.302 1.00   78.79  ? 415 ASN A CB  1 
ATOM   2986  C CG  . ASN A  1 415 ? 102.273 100.547 -12.565 1.00   82.57  ? 415 ASN A CG  1 
ATOM   2987  O OD1 . ASN A  1 415 ? 101.804 99.798  -13.420 1.00   85.69  ? 415 ASN A OD1 1 
ATOM   2988  N ND2 . ASN A  1 415 ? 101.521 101.353 -11.828 1.00   83.09  ? 415 ASN A ND2 1 
ATOM   2989  N N   . ASN A  1 416 ? 106.390 99.132  -13.656 1.00   78.72  ? 416 ASN A N   1 
ATOM   2990  C CA  . ASN A  1 416 ? 107.813 99.239  -13.944 1.00   86.13  ? 416 ASN A CA  1 
ATOM   2991  C C   . ASN A  1 416 ? 108.455 100.418 -13.225 1.00   85.83  ? 416 ASN A C   1 
ATOM   2992  O O   . ASN A  1 416 ? 107.994 101.553 -13.344 1.00   87.47  ? 416 ASN A O   1 
ATOM   2993  C CB  . ASN A  1 416 ? 108.039 99.367  -15.450 1.00   95.98  ? 416 ASN A CB  1 
ATOM   2994  C CG  . ASN A  1 416 ? 107.493 98.185  -16.224 1.00   99.48  ? 416 ASN A CG  1 
ATOM   2995  O OD1 . ASN A  1 416 ? 108.128 97.693  -17.155 1.00   105.47 ? 416 ASN A OD1 1 
ATOM   2996  N ND2 . ASN A  1 416 ? 106.309 97.722  -15.843 1.00   95.71  ? 416 ASN A ND2 1 
ATOM   2997  N N   . LYS B  1 11  ? 56.665  23.923  23.244  1.00   86.24  ? 11  LYS B N   1 
ATOM   2998  C CA  . LYS B  1 11  ? 57.710  24.644  22.500  1.00   82.21  ? 11  LYS B CA  1 
ATOM   2999  C C   . LYS B  1 11  ? 57.411  26.134  22.336  1.00   75.80  ? 11  LYS B C   1 
ATOM   3000  O O   . LYS B  1 11  ? 56.401  26.503  21.712  1.00   77.69  ? 11  LYS B O   1 
ATOM   3001  C CB  . LYS B  1 11  ? 57.959  24.021  21.127  1.00   85.48  ? 11  LYS B CB  1 
ATOM   3002  C CG  . LYS B  1 11  ? 59.042  24.778  20.347  1.00   82.84  ? 11  LYS B CG  1 
ATOM   3003  C CD  . LYS B  1 11  ? 60.106  23.868  19.713  1.00   81.02  ? 11  LYS B CD  1 
ATOM   3004  C CE  . LYS B  1 11  ? 61.069  23.289  20.755  1.00   74.68  ? 11  LYS B CE  1 
ATOM   3005  N NZ  . LYS B  1 11  ? 62.386  22.861  20.184  1.00   69.01  ? 11  LYS B NZ  1 
ATOM   3006  N N   . PRO B  1 12  ? 58.278  26.989  22.932  1.00   64.59  ? 12  PRO B N   1 
ATOM   3007  C CA  . PRO B  1 12  ? 58.087  28.441  23.024  1.00   61.16  ? 12  PRO B CA  1 
ATOM   3008  C C   . PRO B  1 12  ? 58.212  29.222  21.710  1.00   63.51  ? 12  PRO B C   1 
ATOM   3009  O O   . PRO B  1 12  ? 58.987  28.872  20.814  1.00   65.15  ? 12  PRO B O   1 
ATOM   3010  C CB  . PRO B  1 12  ? 59.194  28.862  23.995  1.00   49.47  ? 12  PRO B CB  1 
ATOM   3011  C CG  . PRO B  1 12  ? 60.217  27.883  23.825  1.00   46.09  ? 12  PRO B CG  1 
ATOM   3012  C CD  . PRO B  1 12  ? 59.561  26.586  23.532  1.00   53.56  ? 12  PRO B CD  1 
ATOM   3013  N N   . ASN B  1 13  ? 57.429  30.292  21.625  1.00   61.89  ? 13  ASN B N   1 
ATOM   3014  C CA  . ASN B  1 13  ? 57.471  31.190  20.499  1.00   59.34  ? 13  ASN B CA  1 
ATOM   3015  C C   . ASN B  1 13  ? 58.145  32.478  20.894  1.00   56.33  ? 13  ASN B C   1 
ATOM   3016  O O   . ASN B  1 13  ? 58.287  33.372  20.069  1.00   56.43  ? 13  ASN B O   1 
ATOM   3017  C CB  . ASN B  1 13  ? 56.083  31.484  19.959  1.00   61.94  ? 13  ASN B CB  1 
ATOM   3018  C CG  . ASN B  1 13  ? 55.744  30.627  18.777  1.00   69.48  ? 13  ASN B CG  1 
ATOM   3019  O OD1 . ASN B  1 13  ? 56.270  30.841  17.685  1.00   72.13  ? 13  ASN B OD1 1 
ATOM   3020  N ND2 . ASN B  1 13  ? 54.866  29.644  18.975  1.00   73.51  ? 13  ASN B ND2 1 
ATOM   3021  N N   . LEU B  1 14  ? 58.520  32.592  22.165  1.00   50.09  ? 14  LEU B N   1 
ATOM   3022  C CA  . LEU B  1 14  ? 59.159  33.809  22.643  1.00   45.14  ? 14  LEU B CA  1 
ATOM   3023  C C   . LEU B  1 14  ? 59.982  33.516  23.892  1.00   39.49  ? 14  LEU B C   1 
ATOM   3024  O O   . LEU B  1 14  ? 59.486  32.854  24.816  1.00   37.51  ? 14  LEU B O   1 
ATOM   3025  C CB  . LEU B  1 14  ? 58.116  34.892  22.925  1.00   45.74  ? 14  LEU B CB  1 
ATOM   3026  C CG  . LEU B  1 14  ? 58.615  36.335  23.080  1.00   42.73  ? 14  LEU B CG  1 
ATOM   3027  C CD1 . LEU B  1 14  ? 59.013  36.920  21.743  1.00   40.64  ? 14  LEU B CD1 1 
ATOM   3028  C CD2 . LEU B  1 14  ? 57.552  37.186  23.708  1.00   46.02  ? 14  LEU B CD2 1 
ATOM   3029  N N   . LEU B  1 15  ? 61.222  34.024  23.907  1.00   34.55  ? 15  LEU B N   1 
ATOM   3030  C CA  . LEU B  1 15  ? 62.175  33.853  25.010  1.00   31.42  ? 15  LEU B CA  1 
ATOM   3031  C C   . LEU B  1 15  ? 62.619  35.185  25.569  1.00   30.43  ? 15  LEU B C   1 
ATOM   3032  O O   . LEU B  1 15  ? 62.746  36.145  24.823  1.00   29.78  ? 15  LEU B O   1 
ATOM   3033  C CB  . LEU B  1 15  ? 63.399  33.082  24.526  1.00   28.48  ? 15  LEU B CB  1 
ATOM   3034  C CG  . LEU B  1 15  ? 63.050  31.804  23.765  1.00   31.57  ? 15  LEU B CG  1 
ATOM   3035  C CD1 . LEU B  1 15  ? 64.308  31.193  23.144  1.00   30.30  ? 15  LEU B CD1 1 
ATOM   3036  C CD2 . LEU B  1 15  ? 62.339  30.826  24.690  1.00   32.52  ? 15  LEU B CD2 1 
ATOM   3037  N N   . VAL B  1 16  ? 62.925  35.241  26.862  1.00   31.75  ? 16  VAL B N   1 
ATOM   3038  C CA  . VAL B  1 16  ? 63.230  36.523  27.495  1.00   27.87  ? 16  VAL B CA  1 
ATOM   3039  C C   . VAL B  1 16  ? 64.493  36.463  28.341  1.00   25.12  ? 16  VAL B C   1 
ATOM   3040  O O   . VAL B  1 16  ? 64.637  35.622  29.202  1.00   28.94  ? 16  VAL B O   1 
ATOM   3041  C CB  . VAL B  1 16  ? 62.042  37.032  28.396  1.00   34.56  ? 16  VAL B CB  1 
ATOM   3042  C CG1 . VAL B  1 16  ? 62.332  38.417  28.975  1.00   30.42  ? 16  VAL B CG1 1 
ATOM   3043  C CG2 . VAL B  1 16  ? 60.734  37.098  27.613  1.00   29.37  ? 16  VAL B CG2 1 
ATOM   3044  N N   . LEU B  1 17  ? 65.388  37.410  28.097  1.00   24.49  ? 17  LEU B N   1 
ATOM   3045  C CA  . LEU B  1 17  ? 66.620  37.567  28.861  1.00   27.93  ? 17  LEU B CA  1 
ATOM   3046  C C   . LEU B  1 17  ? 66.667  38.946  29.535  1.00   28.44  ? 17  LEU B C   1 
ATOM   3047  O O   . LEU B  1 17  ? 66.881  39.957  28.875  1.00   29.94  ? 17  LEU B O   1 
ATOM   3048  C CB  . LEU B  1 17  ? 67.848  37.403  27.946  1.00   26.93  ? 17  LEU B CB  1 
ATOM   3049  C CG  . LEU B  1 17  ? 69.254  37.529  28.558  1.00   28.91  ? 17  LEU B CG  1 
ATOM   3050  C CD1 . LEU B  1 17  ? 69.564  36.330  29.472  1.00   30.48  ? 17  LEU B CD1 1 
ATOM   3051  C CD2 . LEU B  1 17  ? 70.339  37.652  27.492  1.00   25.71  ? 17  LEU B CD2 1 
ATOM   3052  N N   . PRO B  1 18  ? 66.469  38.984  30.862  1.00   28.68  ? 18  PRO B N   1 
ATOM   3053  C CA  . PRO B  1 18  ? 66.605  40.233  31.612  1.00   30.57  ? 18  PRO B CA  1 
ATOM   3054  C C   . PRO B  1 18  ? 68.066  40.675  31.688  1.00   32.22  ? 18  PRO B C   1 
ATOM   3055  O O   . PRO B  1 18  ? 68.957  39.847  31.899  1.00   29.93  ? 18  PRO B O   1 
ATOM   3056  C CB  . PRO B  1 18  ? 66.067  39.875  33.000  1.00   29.97  ? 18  PRO B CB  1 
ATOM   3057  C CG  . PRO B  1 18  ? 65.228  38.649  32.790  1.00   32.10  ? 18  PRO B CG  1 
ATOM   3058  C CD  . PRO B  1 18  ? 65.935  37.900  31.707  1.00   31.25  ? 18  PRO B CD  1 
ATOM   3059  N N   . VAL B  1 19  ? 68.287  41.975  31.533  1.00   32.45  ? 19  VAL B N   1 
ATOM   3060  C CA  . VAL B  1 19  ? 69.608  42.558  31.523  1.00   30.72  ? 19  VAL B CA  1 
ATOM   3061  C C   . VAL B  1 19  ? 69.612  43.706  32.510  1.00   32.32  ? 19  VAL B C   1 
ATOM   3062  O O   . VAL B  1 19  ? 68.568  44.279  32.783  1.00   33.08  ? 19  VAL B O   1 
ATOM   3063  C CB  . VAL B  1 19  ? 70.008  43.060  30.119  1.00   30.33  ? 19  VAL B CB  1 
ATOM   3064  C CG1 . VAL B  1 19  ? 69.900  41.939  29.098  1.00   27.65  ? 19  VAL B CG1 1 
ATOM   3065  C CG2 . VAL B  1 19  ? 69.140  44.198  29.696  1.00   32.06  ? 19  VAL B CG2 1 
ATOM   3066  N N   . GLN B  1 20  ? 70.784  44.032  33.052  1.00   32.54  ? 20  GLN B N   1 
ATOM   3067  C CA  . GLN B  1 20  ? 70.896  45.073  34.064  1.00   32.40  ? 20  GLN B CA  1 
ATOM   3068  C C   . GLN B  1 20  ? 71.987  46.071  33.705  1.00   30.49  ? 20  GLN B C   1 
ATOM   3069  O O   . GLN B  1 20  ? 73.024  45.699  33.165  1.00   27.79  ? 20  GLN B O   1 
ATOM   3070  C CB  . GLN B  1 20  ? 71.197  44.461  35.420  1.00   35.33  ? 20  GLN B CB  1 
ATOM   3071  C CG  . GLN B  1 20  ? 71.092  45.428  36.583  1.00   40.97  ? 20  GLN B CG  1 
ATOM   3072  C CD  . GLN B  1 20  ? 71.279  44.716  37.920  1.00   46.54  ? 20  GLN B CD  1 
ATOM   3073  O OE1 . GLN B  1 20  ? 72.123  45.105  38.725  1.00   46.61  ? 20  GLN B OE1 1 
ATOM   3074  N NE2 . GLN B  1 20  ? 70.526  43.644  38.138  1.00   49.40  ? 20  GLN B NE2 1 
ATOM   3075  N N   . GLU B  1 21  ? 71.742  47.341  34.010  1.00   30.39  ? 21  GLU B N   1 
ATOM   3076  C CA  . GLU B  1 21  ? 72.733  48.386  33.805  1.00   30.67  ? 21  GLU B CA  1 
ATOM   3077  C C   . GLU B  1 21  ? 73.763  48.418  34.949  1.00   31.12  ? 21  GLU B C   1 
ATOM   3078  O O   . GLU B  1 21  ? 73.412  48.307  36.127  1.00   30.73  ? 21  GLU B O   1 
ATOM   3079  C CB  . GLU B  1 21  ? 72.037  49.747  33.669  1.00   29.26  ? 21  GLU B CB  1 
ATOM   3080  C CG  . GLU B  1 21  ? 72.879  50.806  32.969  1.00   30.71  ? 21  GLU B CG  1 
ATOM   3081  C CD  . GLU B  1 21  ? 73.533  51.755  33.941  1.00   35.01  ? 21  GLU B CD  1 
ATOM   3082  O OE1 . GLU B  1 21  ? 73.357  51.566  35.157  1.00   37.78  ? 21  GLU B OE1 1 
ATOM   3083  O OE2 . GLU B  1 21  ? 74.217  52.699  33.502  1.00   35.70  ? 21  GLU B OE2 1 
ATOM   3084  N N   . ASP B  1 22  ? 75.037  48.556  34.609  1.00   29.48  ? 22  ASP B N   1 
ATOM   3085  C CA  . ASP B  1 22  ? 76.030  48.726  35.638  1.00   30.61  ? 22  ASP B CA  1 
ATOM   3086  C C   . ASP B  1 22  ? 76.310  50.210  35.803  1.00   31.84  ? 22  ASP B C   1 
ATOM   3087  O O   . ASP B  1 22  ? 76.835  50.848  34.900  1.00   32.68  ? 22  ASP B O   1 
ATOM   3088  C CB  . ASP B  1 22  ? 77.293  47.976  35.292  1.00   31.56  ? 22  ASP B CB  1 
ATOM   3089  C CG  . ASP B  1 22  ? 78.353  48.205  36.294  1.00   35.71  ? 22  ASP B CG  1 
ATOM   3090  O OD1 . ASP B  1 22  ? 78.112  47.834  37.442  1.00   38.98  ? 22  ASP B OD1 1 
ATOM   3091  O OD2 . ASP B  1 22  ? 79.413  48.768  35.965  1.00   38.10  1 22  ASP B OD2 1 
ATOM   3092  N N   . ALA B  1 23  ? 75.963  50.756  36.966  1.00   34.12  ? 23  ALA B N   1 
ATOM   3093  C CA  . ALA B  1 23  ? 75.962  52.204  37.152  1.00   36.37  ? 23  ALA B CA  1 
ATOM   3094  C C   . ALA B  1 23  ? 77.345  52.782  36.959  1.00   40.26  ? 23  ALA B C   1 
ATOM   3095  O O   . ALA B  1 23  ? 77.514  53.857  36.378  1.00   42.17  ? 23  ALA B O   1 
ATOM   3096  C CB  . ALA B  1 23  ? 75.431  52.574  38.522  1.00   37.74  ? 23  ALA B CB  1 
ATOM   3097  N N   . SER B  1 24  ? 78.324  52.081  37.502  1.00   37.71  ? 24  SER B N   1 
ATOM   3098  C CA  . SER B  1 24  ? 79.693  52.510  37.419  1.00   42.52  ? 24  SER B CA  1 
ATOM   3099  C C   . SER B  1 24  ? 80.244  52.601  35.991  1.00   39.86  ? 24  SER B C   1 
ATOM   3100  O O   . SER B  1 24  ? 80.914  53.571  35.662  1.00   41.69  ? 24  SER B O   1 
ATOM   3101  C CB  . SER B  1 24  ? 80.561  51.593  38.236  1.00   49.87  ? 24  SER B CB  1 
ATOM   3102  O OG  . SER B  1 24  ? 81.896  51.944  38.023  1.00   56.43  ? 24  SER B OG  1 
ATOM   3103  N N   . THR B  1 25  ? 80.034  51.579  35.165  1.00   38.08  ? 25  THR B N   1 
ATOM   3104  C CA  . THR B  1 25  ? 80.610  51.576  33.821  1.00   38.02  ? 25  THR B CA  1 
ATOM   3105  C C   . THR B  1 25  ? 79.638  52.051  32.760  1.00   35.77  ? 25  THR B C   1 
ATOM   3106  O O   . THR B  1 25  ? 80.065  52.478  31.683  1.00   35.25  ? 25  THR B O   1 
ATOM   3107  C CB  . THR B  1 25  ? 81.116  50.171  33.381  1.00   35.78  ? 25  THR B CB  1 
ATOM   3108  O OG1 . THR B  1 25  ? 80.018  49.258  33.329  1.00   34.75  ? 25  THR B OG1 1 
ATOM   3109  C CG2 . THR B  1 25  ? 82.153  49.636  34.332  1.00   36.57  ? 25  THR B CG2 1 
ATOM   3110  N N   . GLY B  1 26  ? 78.342  51.986  33.052  1.00   32.47  ? 26  GLY B N   1 
ATOM   3111  C CA  . GLY B  1 26  ? 77.356  52.376  32.074  1.00   30.28  ? 26  GLY B CA  1 
ATOM   3112  C C   . GLY B  1 26  ? 77.109  51.282  31.059  1.00   30.24  ? 26  GLY B C   1 
ATOM   3113  O O   . GLY B  1 26  ? 76.463  51.486  30.034  1.00   29.63  ? 26  GLY B O   1 
ATOM   3114  N N   . LEU B  1 27  ? 77.672  50.119  31.328  1.00   29.10  ? 27  LEU B N   1 
ATOM   3115  C CA  . LEU B  1 27  ? 77.478  48.987  30.464  1.00   25.83  ? 27  LEU B CA  1 
ATOM   3116  C C   . LEU B  1 27  ? 76.403  48.110  31.033  1.00   27.18  ? 27  LEU B C   1 
ATOM   3117  O O   . LEU B  1 27  ? 75.983  48.273  32.173  1.00   28.67  ? 27  LEU B O   1 
ATOM   3118  C CB  . LEU B  1 27  ? 78.759  48.210  30.302  1.00   27.94  ? 27  LEU B CB  1 
ATOM   3119  C CG  . LEU B  1 27  ? 79.870  49.076  29.742  1.00   30.31  ? 27  LEU B CG  1 
ATOM   3120  C CD1 . LEU B  1 27  ? 81.147  48.300  29.686  1.00   33.18  ? 27  LEU B CD1 1 
ATOM   3121  C CD2 . LEU B  1 27  ? 79.496  49.595  28.377  1.00   29.11  ? 27  LEU B CD2 1 
ATOM   3122  N N   . HIS B  1 28  ? 75.956  47.179  30.215  1.00   28.79  ? 28  HIS B N   1 
ATOM   3123  C CA  . HIS B  1 28  ? 74.893  46.286  30.597  1.00   27.62  ? 28  HIS B CA  1 
ATOM   3124  C C   . HIS B  1 28  ? 75.393  44.880  30.605  1.00   27.98  ? 28  HIS B C   1 
ATOM   3125  O O   . HIS B  1 28  ? 76.273  44.541  29.843  1.00   27.64  ? 28  HIS B O   1 
ATOM   3126  C CB  . HIS B  1 28  ? 73.717  46.439  29.653  1.00   26.82  ? 28  HIS B CB  1 
ATOM   3127  C CG  . HIS B  1 28  ? 73.065  47.780  29.760  1.00   24.91  ? 28  HIS B CG  1 
ATOM   3128  N ND1 . HIS B  1 28  ? 71.817  47.960  30.309  1.00   25.50  ? 28  HIS B ND1 1 
ATOM   3129  C CD2 . HIS B  1 28  ? 73.522  49.013  29.443  1.00   24.70  ? 28  HIS B CD2 1 
ATOM   3130  C CE1 . HIS B  1 28  ? 71.521  49.248  30.300  1.00   24.48  ? 28  HIS B CE1 1 
ATOM   3131  N NE2 . HIS B  1 28  ? 72.541  49.906  29.788  1.00   24.73  ? 28  HIS B NE2 1 
ATOM   3132  N N   . TRP B  1 29  ? 74.841  44.078  31.503  1.00   28.37  ? 29  TRP B N   1 
ATOM   3133  C CA  . TRP B  1 29  ? 75.273  42.702  31.688  1.00   26.39  ? 29  TRP B CA  1 
ATOM   3134  C C   . TRP B  1 29  ? 74.065  41.809  32.005  1.00   30.64  ? 29  TRP B C   1 
ATOM   3135  O O   . TRP B  1 29  ? 73.003  42.297  32.373  1.00   30.66  ? 29  TRP B O   1 
ATOM   3136  C CB  . TRP B  1 29  ? 76.313  42.617  32.806  1.00   25.02  ? 29  TRP B CB  1 
ATOM   3137  C CG  . TRP B  1 29  ? 75.757  43.055  34.144  1.00   25.65  ? 29  TRP B CG  1 
ATOM   3138  C CD1 . TRP B  1 29  ? 75.642  44.338  34.616  1.00   26.80  ? 29  TRP B CD1 1 
ATOM   3139  C CD2 . TRP B  1 29  ? 75.223  42.208  35.169  1.00   28.81  ? 29  TRP B CD2 1 
ATOM   3140  N NE1 . TRP B  1 29  ? 75.077  44.330  35.869  1.00   28.62  ? 29  TRP B NE1 1 
ATOM   3141  C CE2 . TRP B  1 29  ? 74.803  43.033  36.220  1.00   28.61  ? 29  TRP B CE2 1 
ATOM   3142  C CE3 . TRP B  1 29  ? 75.060  40.829  35.296  1.00   29.71  ? 29  TRP B CE3 1 
ATOM   3143  C CZ2 . TRP B  1 29  ? 74.243  42.522  37.377  1.00   31.49  ? 29  TRP B CZ2 1 
ATOM   3144  C CZ3 . TRP B  1 29  ? 74.493  40.332  36.438  1.00   30.22  ? 29  TRP B CZ3 1 
ATOM   3145  C CH2 . TRP B  1 29  ? 74.100  41.169  37.464  1.00   31.61  ? 29  TRP B CH2 1 
ATOM   3146  N N   . ALA B  1 30  ? 74.219  40.496  31.865  1.00   32.50  ? 30  ALA B N   1 
ATOM   3147  C CA  . ALA B  1 30  ? 73.130  39.566  32.180  1.00   29.09  ? 30  ALA B CA  1 
ATOM   3148  C C   . ALA B  1 30  ? 73.638  38.324  32.903  1.00   29.75  ? 30  ALA B C   1 
ATOM   3149  O O   . ALA B  1 30  ? 74.782  37.914  32.708  1.00   30.21  ? 30  ALA B O   1 
ATOM   3150  C CB  . ALA B  1 30  ? 72.396  39.168  30.910  1.00   25.51  ? 30  ALA B CB  1 
ATOM   3151  N N   . ASN B  1 31  ? 72.804  37.745  33.761  1.00   30.16  ? 31  ASN B N   1 
ATOM   3152  C CA  . ASN B  1 31  ? 73.073  36.406  34.274  1.00   31.82  ? 31  ASN B CA  1 
ATOM   3153  C C   . ASN B  1 31  ? 72.639  35.357  33.257  1.00   32.70  ? 31  ASN B C   1 
ATOM   3154  O O   . ASN B  1 31  ? 71.455  35.253  32.960  1.00   35.68  ? 31  ASN B O   1 
ATOM   3155  C CB  . ASN B  1 31  ? 72.329  36.150  35.582  1.00   33.66  ? 31  ASN B CB  1 
ATOM   3156  C CG  . ASN B  1 31  ? 73.050  36.691  36.769  1.00   34.31  ? 31  ASN B CG  1 
ATOM   3157  O OD1 . ASN B  1 31  ? 74.259  36.567  36.870  1.00   37.24  ? 31  ASN B OD1 1 
ATOM   3158  N ND2 . ASN B  1 31  ? 72.310  37.259  37.705  1.00   33.64  ? 31  ASN B ND2 1 
ATOM   3159  N N   . ILE B  1 32  ? 73.579  34.580  32.731  1.00   30.15  ? 32  ILE B N   1 
ATOM   3160  C CA  . ILE B  1 32  ? 73.243  33.505  31.820  1.00   28.20  ? 32  ILE B CA  1 
ATOM   3161  C C   . ILE B  1 32  ? 73.249  32.208  32.595  1.00   28.21  ? 32  ILE B C   1 
ATOM   3162  O O   . ILE B  1 32  ? 74.157  31.940  33.370  1.00   29.18  ? 32  ILE B O   1 
ATOM   3163  C CB  . ILE B  1 32  ? 74.245  33.420  30.644  1.00   29.93  ? 32  ILE B CB  1 
ATOM   3164  C CG1 . ILE B  1 32  ? 74.278  34.737  29.888  1.00   29.38  ? 32  ILE B CG1 1 
ATOM   3165  C CG2 . ILE B  1 32  ? 73.840  32.351  29.650  1.00   28.11  ? 32  ILE B CG2 1 
ATOM   3166  C CD1 . ILE B  1 32  ? 73.030  34.983  29.105  1.00   31.84  ? 32  ILE B CD1 1 
ATOM   3167  N N   . HIS B  1 33  ? 72.227  31.398  32.393  1.00   28.31  ? 33  HIS B N   1 
ATOM   3168  C CA  . HIS B  1 33  ? 72.166  30.103  33.047  1.00   27.83  ? 33  HIS B CA  1 
ATOM   3169  C C   . HIS B  1 33  ? 72.822  29.059  32.171  1.00   30.35  ? 33  HIS B C   1 
ATOM   3170  O O   . HIS B  1 33  ? 72.446  28.903  31.003  1.00   30.60  ? 33  HIS B O   1 
ATOM   3171  C CB  . HIS B  1 33  ? 70.729  29.705  33.341  1.00   30.37  ? 33  HIS B CB  1 
ATOM   3172  C CG  . HIS B  1 33  ? 70.054  30.571  34.353  1.00   33.99  ? 33  HIS B CG  1 
ATOM   3173  N ND1 . HIS B  1 33  ? 69.708  31.882  34.101  1.00   37.19  ? 33  HIS B ND1 1 
ATOM   3174  C CD2 . HIS B  1 33  ? 69.629  30.303  35.609  1.00   35.35  ? 33  HIS B CD2 1 
ATOM   3175  C CE1 . HIS B  1 33  ? 69.107  32.385  35.165  1.00   35.80  ? 33  HIS B CE1 1 
ATOM   3176  N NE2 . HIS B  1 33  ? 69.047  31.448  36.092  1.00   35.86  ? 33  HIS B NE2 1 
ATOM   3177  N N   . LYS B  1 34  ? 73.818  28.362  32.718  1.00   29.86  ? 34  LYS B N   1 
ATOM   3178  C CA  . LYS B  1 34  ? 74.574  27.359  31.955  1.00   30.45  ? 34  LYS B CA  1 
ATOM   3179  C C   . LYS B  1 34  ? 74.917  26.109  32.758  1.00   28.44  ? 34  LYS B C   1 
ATOM   3180  O O   . LYS B  1 34  ? 74.799  26.107  33.975  1.00   32.49  ? 34  LYS B O   1 
ATOM   3181  C CB  . LYS B  1 34  ? 75.856  27.989  31.403  1.00   33.76  ? 34  LYS B CB  1 
ATOM   3182  C CG  . LYS B  1 34  ? 75.593  29.282  30.644  1.00   33.85  ? 34  LYS B CG  1 
ATOM   3183  C CD  . LYS B  1 34  ? 76.685  29.577  29.708  1.00   34.94  ? 34  LYS B CD  1 
ATOM   3184  C CE  . LYS B  1 34  ? 76.780  28.464  28.731  1.00   36.61  ? 34  LYS B CE  1 
ATOM   3185  N NZ  . LYS B  1 34  ? 78.147  28.474  28.256  1.00   37.52  ? 34  LYS B NZ  1 
ATOM   3186  N N   . ARG B  1 35  ? 75.293  25.041  32.061  1.00   27.20  ? 35  ARG B N   1 
ATOM   3187  C CA  . ARG B  1 35  ? 75.849  23.820  32.665  1.00   29.72  ? 35  ARG B CA  1 
ATOM   3188  C C   . ARG B  1 35  ? 74.859  22.882  33.310  1.00   30.04  ? 35  ARG B C   1 
ATOM   3189  O O   . ARG B  1 35  ? 73.693  23.212  33.481  1.00   35.73  ? 35  ARG B O   1 
ATOM   3190  C CB  . ARG B  1 35  ? 76.915  24.196  33.692  1.00   32.24  ? 35  ARG B CB  1 
ATOM   3191  C CG  . ARG B  1 35  ? 78.034  25.005  33.072  1.00   30.54  ? 35  ARG B CG  1 
ATOM   3192  C CD  . ARG B  1 35  ? 78.921  25.652  34.093  1.00   31.10  ? 35  ARG B CD  1 
ATOM   3193  N NE  . ARG B  1 35  ? 79.650  26.739  33.454  1.00   32.05  ? 35  ARG B NE  1 
ATOM   3194  C CZ  . ARG B  1 35  ? 80.587  27.473  34.044  1.00   34.63  ? 35  ARG B CZ  1 
ATOM   3195  N NH1 . ARG B  1 35  ? 80.902  27.247  35.315  1.00   37.98  ? 35  ARG B NH1 1 
ATOM   3196  N NH2 . ARG B  1 35  ? 81.209  28.431  33.362  1.00   33.01  ? 35  ARG B NH2 1 
ATOM   3197  N N   . THR B  1 36  ? 75.336  21.692  33.656  1.00   31.59  ? 36  THR B N   1 
ATOM   3198  C CA  . THR B  1 36  ? 74.552  20.755  34.459  1.00   35.98  ? 36  THR B CA  1 
ATOM   3199  C C   . THR B  1 36  ? 75.348  20.344  35.689  1.00   35.24  ? 36  THR B C   1 
ATOM   3200  O O   . THR B  1 36  ? 76.381  19.715  35.586  1.00   35.69  ? 36  THR B O   1 
ATOM   3201  C CB  . THR B  1 36  ? 74.140  19.492  33.679  1.00   34.98  ? 36  THR B CB  1 
ATOM   3202  O OG1 . THR B  1 36  ? 73.434  19.851  32.493  1.00   41.97  ? 36  THR B OG1 1 
ATOM   3203  C CG2 . THR B  1 36  ? 73.224  18.670  34.501  1.00   37.41  ? 36  THR B CG2 1 
ATOM   3204  N N   . PRO B  1 37  ? 74.880  20.727  36.871  1.00   36.26  ? 37  PRO B N   1 
ATOM   3205  C CA  . PRO B  1 37  ? 73.665  21.492  37.177  1.00   36.15  ? 37  PRO B CA  1 
ATOM   3206  C C   . PRO B  1 37  ? 73.723  22.941  36.741  1.00   37.88  ? 37  PRO B C   1 
ATOM   3207  O O   . PRO B  1 37  ? 74.768  23.559  36.636  1.00   37.28  ? 37  PRO B O   1 
ATOM   3208  C CB  . PRO B  1 37  ? 73.574  21.416  38.693  1.00   39.19  ? 37  PRO B CB  1 
ATOM   3209  C CG  . PRO B  1 37  ? 75.007  21.189  39.141  1.00   40.25  ? 37  PRO B CG  1 
ATOM   3210  C CD  . PRO B  1 37  ? 75.624  20.343  38.078  1.00   40.11  ? 37  PRO B CD  1 
ATOM   3211  N N   . LEU B  1 38  ? 72.555  23.481  36.479  1.00   37.69  ? 38  LEU B N   1 
ATOM   3212  C CA  . LEU B  1 38  ? 72.445  24.825  35.962  1.00   38.00  ? 38  LEU B CA  1 
ATOM   3213  C C   . LEU B  1 38  ? 72.901  25.877  36.989  1.00   37.11  ? 38  LEU B C   1 
ATOM   3214  O O   . LEU B  1 38  ? 72.618  25.772  38.176  1.00   37.75  ? 38  LEU B O   1 
ATOM   3215  C CB  . LEU B  1 38  ? 70.998  25.058  35.533  1.00   37.02  ? 38  LEU B CB  1 
ATOM   3216  C CG  . LEU B  1 38  ? 70.643  25.985  34.387  1.00   35.46  ? 38  LEU B CG  1 
ATOM   3217  C CD1 . LEU B  1 38  ? 71.235  25.514  33.080  1.00   28.93  ? 38  LEU B CD1 1 
ATOM   3218  C CD2 . LEU B  1 38  ? 69.141  26.003  34.317  1.00   40.26  ? 38  LEU B CD2 1 
ATOM   3219  N N   . MET B  1 39  ? 73.628  26.878  36.529  1.00   37.68  ? 39  MET B N   1 
ATOM   3220  C CA  . MET B  1 39  ? 74.018  27.997  37.382  1.00   39.09  ? 39  MET B CA  1 
ATOM   3221  C C   . MET B  1 39  ? 74.100  29.274  36.570  1.00   36.69  ? 39  MET B C   1 
ATOM   3222  O O   . MET B  1 39  ? 74.025  29.243  35.349  1.00   36.89  ? 39  MET B O   1 
ATOM   3223  C CB  . MET B  1 39  ? 75.356  27.716  38.086  1.00   42.48  ? 39  MET B CB  1 
ATOM   3224  C CG  . MET B  1 39  ? 76.469  27.173  37.192  1.00   40.97  ? 39  MET B CG  1 
ATOM   3225  S SD  . MET B  1 39  ? 77.245  28.440  36.197  1.00   54.51  ? 39  MET B SD  1 
ATOM   3226  C CE  . MET B  1 39  ? 78.106  29.346  37.484  1.00   53.47  ? 39  MET B CE  1 
ATOM   3227  N N   . GLN B  1 40  ? 74.291  30.390  37.253  1.00   36.27  ? 40  GLN B N   1 
ATOM   3228  C CA  . GLN B  1 40  ? 74.305  31.682  36.592  1.00   34.60  ? 40  GLN B CA  1 
ATOM   3229  C C   . GLN B  1 40  ? 75.690  32.218  36.371  1.00   33.55  ? 40  GLN B C   1 
ATOM   3230  O O   . GLN B  1 40  ? 76.495  32.281  37.302  1.00   35.88  ? 40  GLN B O   1 
ATOM   3231  C CB  . GLN B  1 40  ? 73.558  32.695  37.413  1.00   36.83  ? 40  GLN B CB  1 
ATOM   3232  C CG  . GLN B  1 40  ? 72.128  32.453  37.499  1.00   44.05  ? 40  GLN B CG  1 
ATOM   3233  C CD  . GLN B  1 40  ? 71.493  33.498  38.343  1.00   52.63  ? 40  GLN B CD  1 
ATOM   3234  O OE1 . GLN B  1 40  ? 70.734  34.321  37.851  1.00   54.77  ? 40  GLN B OE1 1 
ATOM   3235  N NE2 . GLN B  1 40  ? 71.821  33.499  39.633  1.00   57.21  ? 40  GLN B NE2 1 
ATOM   3236  N N   . VAL B  1 41  ? 75.942  32.668  35.153  1.00   30.83  ? 41  VAL B N   1 
ATOM   3237  C CA  . VAL B  1 41  ? 77.213  33.297  34.816  1.00   30.28  ? 41  VAL B CA  1 
ATOM   3238  C C   . VAL B  1 41  ? 76.949  34.746  34.427  1.00   27.19  ? 41  VAL B C   1 
ATOM   3239  O O   . VAL B  1 41  ? 76.203  34.979  33.493  1.00   27.64  ? 41  VAL B O   1 
ATOM   3240  C CB  . VAL B  1 41  ? 77.943  32.565  33.641  1.00   30.23  ? 41  VAL B CB  1 
ATOM   3241  C CG1 . VAL B  1 41  ? 79.325  33.079  33.496  1.00   28.16  ? 41  VAL B CG1 1 
ATOM   3242  C CG2 . VAL B  1 41  ? 77.957  31.057  33.852  1.00   32.48  ? 41  VAL B CG2 1 
ATOM   3243  N N   . PRO B  1 42  ? 77.530  35.727  35.165  1.00   27.94  ? 42  PRO B N   1 
ATOM   3244  C CA  . PRO B  1 42  ? 77.376  37.131  34.761  1.00   26.98  ? 42  PRO B CA  1 
ATOM   3245  C C   . PRO B  1 42  ? 78.262  37.479  33.554  1.00   28.30  ? 42  PRO B C   1 
ATOM   3246  O O   . PRO B  1 42  ? 79.478  37.268  33.612  1.00   28.51  ? 42  PRO B O   1 
ATOM   3247  C CB  . PRO B  1 42  ? 77.793  37.908  36.015  1.00   27.30  ? 42  PRO B CB  1 
ATOM   3248  C CG  . PRO B  1 42  ? 78.678  37.031  36.737  1.00   28.47  ? 42  PRO B CG  1 
ATOM   3249  C CD  . PRO B  1 42  ? 78.218  35.615  36.463  1.00   29.23  ? 42  PRO B CD  1 
ATOM   3250  N N   . LEU B  1 43  ? 77.636  37.962  32.475  1.00   27.49  ? 43  LEU B N   1 
ATOM   3251  C CA  . LEU B  1 43  ? 78.324  38.252  31.206  1.00   26.70  ? 43  LEU B CA  1 
ATOM   3252  C C   . LEU B  1 43  ? 77.960  39.614  30.630  1.00   25.23  ? 43  LEU B C   1 
ATOM   3253  O O   . LEU B  1 43  ? 76.837  40.075  30.741  1.00   24.21  ? 43  LEU B O   1 
ATOM   3254  C CB  . LEU B  1 43  ? 78.013  37.186  30.138  1.00   24.20  ? 43  LEU B CB  1 
ATOM   3255  C CG  . LEU B  1 43  ? 78.370  35.724  30.419  1.00   26.39  ? 43  LEU B CG  1 
ATOM   3256  C CD1 . LEU B  1 43  ? 77.867  34.813  29.310  1.00   26.47  ? 43  LEU B CD1 1 
ATOM   3257  C CD2 . LEU B  1 43  ? 79.869  35.531  30.666  1.00   26.19  ? 43  LEU B CD2 1 
ATOM   3258  N N   . LEU B  1 44  ? 78.921  40.248  29.989  1.00   27.12  ? 44  LEU B N   1 
ATOM   3259  C CA  . LEU B  1 44  ? 78.661  41.505  29.338  1.00   25.04  ? 44  LEU B CA  1 
ATOM   3260  C C   . LEU B  1 44  ? 77.778  41.346  28.119  1.00   24.60  ? 44  LEU B C   1 
ATOM   3261  O O   . LEU B  1 44  ? 77.954  40.428  27.328  1.00   25.46  ? 44  LEU B O   1 
ATOM   3262  C CB  . LEU B  1 44  ? 79.977  42.141  28.931  1.00   27.22  ? 44  LEU B CB  1 
ATOM   3263  C CG  . LEU B  1 44  ? 79.937  43.497  28.246  1.00   26.91  ? 44  LEU B CG  1 
ATOM   3264  C CD1 . LEU B  1 44  ? 79.776  44.589  29.290  1.00   26.11  ? 44  LEU B CD1 1 
ATOM   3265  C CD2 . LEU B  1 44  ? 81.211  43.675  27.424  1.00   26.29  ? 44  LEU B CD2 1 
ATOM   3266  N N   . LEU B  1 45  ? 76.823  42.255  27.975  1.00   24.94  ? 45  LEU B N   1 
ATOM   3267  C CA  . LEU B  1 45  ? 76.017  42.358  26.775  1.00   25.85  ? 45  LEU B CA  1 
ATOM   3268  C C   . LEU B  1 45  ? 76.776  43.083  25.655  1.00   24.65  ? 45  LEU B C   1 
ATOM   3269  O O   . LEU B  1 45  ? 77.072  44.286  25.750  1.00   24.99  ? 45  LEU B O   1 
ATOM   3270  C CB  . LEU B  1 45  ? 74.698  43.080  27.083  1.00   28.53  ? 45  LEU B CB  1 
ATOM   3271  C CG  . LEU B  1 45  ? 73.813  43.453  25.886  1.00   28.88  ? 45  LEU B CG  1 
ATOM   3272  C CD1 . LEU B  1 45  ? 73.309  42.213  25.142  1.00   29.56  ? 45  LEU B CD1 1 
ATOM   3273  C CD2 . LEU B  1 45  ? 72.646  44.340  26.329  1.00   28.55  ? 45  LEU B CD2 1 
ATOM   3274  N N   . ASP B  1 46  ? 77.089  42.332  24.603  1.00   24.40  ? 46  ASP B N   1 
ATOM   3275  C CA  . ASP B  1 46  ? 77.841  42.836  23.469  1.00   22.87  ? 46  ASP B CA  1 
ATOM   3276  C C   . ASP B  1 46  ? 77.040  42.632  22.193  1.00   24.50  ? 46  ASP B C   1 
ATOM   3277  O O   . ASP B  1 46  ? 77.063  41.560  21.581  1.00   23.85  ? 46  ASP B O   1 
ATOM   3278  C CB  . ASP B  1 46  ? 79.195  42.142  23.374  1.00   24.62  ? 46  ASP B CB  1 
ATOM   3279  C CG  . ASP B  1 46  ? 80.060  42.697  22.254  1.00   24.88  ? 46  ASP B CG  1 
ATOM   3280  O OD1 . ASP B  1 46  ? 79.674  43.699  21.615  1.00   26.91  ? 46  ASP B OD1 1 
ATOM   3281  O OD2 . ASP B  1 46  ? 81.142  42.132  22.031  1.00   27.08  1 46  ASP B OD2 1 
ATOM   3282  N N   . LEU B  1 47  ? 76.344  43.680  21.788  1.00   23.86  ? 47  LEU B N   1 
ATOM   3283  C CA  . LEU B  1 47  ? 75.421  43.577  20.680  1.00   23.40  ? 47  LEU B CA  1 
ATOM   3284  C C   . LEU B  1 47  ? 76.091  43.028  19.450  1.00   21.98  ? 47  LEU B C   1 
ATOM   3285  O O   . LEU B  1 47  ? 75.543  42.205  18.771  1.00   25.84  ? 47  LEU B O   1 
ATOM   3286  C CB  . LEU B  1 47  ? 74.819  44.939  20.362  1.00   25.47  ? 47  LEU B CB  1 
ATOM   3287  C CG  . LEU B  1 47  ? 73.845  44.989  19.189  1.00   23.24  ? 47  LEU B CG  1 
ATOM   3288  C CD1 . LEU B  1 47  ? 72.621  44.176  19.563  1.00   20.70  ? 47  LEU B CD1 1 
ATOM   3289  C CD2 . LEU B  1 47  ? 73.459  46.429  18.872  1.00   20.67  ? 47  LEU B CD2 1 
ATOM   3290  N N   . ASN B  1 48  ? 77.291  43.476  19.159  1.00   22.02  ? 48  ASN B N   1 
ATOM   3291  C CA  . ASN B  1 48  ? 77.944  43.047  17.936  1.00   22.84  ? 48  ASN B CA  1 
ATOM   3292  C C   . ASN B  1 48  ? 78.899  41.856  18.109  1.00   21.69  ? 48  ASN B C   1 
ATOM   3293  O O   . ASN B  1 48  ? 79.584  41.463  17.179  1.00   20.50  ? 48  ASN B O   1 
ATOM   3294  C CB  . ASN B  1 48  ? 78.697  44.222  17.350  1.00   26.10  ? 48  ASN B CB  1 
ATOM   3295  C CG  . ASN B  1 48  ? 77.791  45.314  16.917  1.00   26.35  ? 48  ASN B CG  1 
ATOM   3296  O OD1 . ASN B  1 48  ? 76.842  45.099  16.165  1.00   27.22  ? 48  ASN B OD1 1 
ATOM   3297  N ND2 . ASN B  1 48  ? 78.039  46.499  17.427  1.00   27.33  ? 48  ASN B ND2 1 
ATOM   3298  N N   . GLY B  1 49  ? 78.962  41.302  19.310  1.00   22.38  ? 49  GLY B N   1 
ATOM   3299  C CA  . GLY B  1 49  ? 79.871  40.202  19.573  1.00   21.53  ? 49  GLY B CA  1 
ATOM   3300  C C   . GLY B  1 49  ? 79.539  38.970  18.756  1.00   21.55  ? 49  GLY B C   1 
ATOM   3301  O O   . GLY B  1 49  ? 78.374  38.622  18.564  1.00   23.88  ? 49  GLY B O   1 
ATOM   3302  N N   . LYS B  1 50  ? 80.573  38.297  18.272  1.00   20.72  ? 50  LYS B N   1 
ATOM   3303  C CA  . LYS B  1 50  ? 80.381  37.179  17.381  1.00   22.84  ? 50  LYS B CA  1 
ATOM   3304  C C   . LYS B  1 50  ? 79.971  35.899  18.089  1.00   21.84  ? 50  LYS B C   1 
ATOM   3305  O O   . LYS B  1 50  ? 79.419  35.009  17.468  1.00   23.98  ? 50  LYS B O   1 
ATOM   3306  C CB  . LYS B  1 50  ? 81.639  36.926  16.592  1.00   23.51  ? 50  LYS B CB  1 
ATOM   3307  C CG  . LYS B  1 50  ? 81.954  38.019  15.604  1.00   25.25  ? 50  LYS B CG  1 
ATOM   3308  C CD  . LYS B  1 50  ? 83.147  37.598  14.773  1.00   28.99  ? 50  LYS B CD  1 
ATOM   3309  C CE  . LYS B  1 50  ? 83.676  38.695  13.901  1.00   32.41  ? 50  LYS B CE  1 
ATOM   3310  N NZ  . LYS B  1 50  ? 84.898  38.179  13.243  1.00   37.12  ? 50  LYS B NZ  1 
ATOM   3311  N N   . HIS B  1 51  ? 80.254  35.801  19.383  1.00   20.69  ? 51  HIS B N   1 
ATOM   3312  C CA  . HIS B  1 51  ? 79.888  34.624  20.145  1.00   19.45  ? 51  HIS B CA  1 
ATOM   3313  C C   . HIS B  1 51  ? 79.845  34.913  21.634  1.00   20.89  ? 51  HIS B C   1 
ATOM   3314  O O   . HIS B  1 51  ? 80.228  35.998  22.084  1.00   21.52  ? 51  HIS B O   1 
ATOM   3315  C CB  . HIS B  1 51  ? 80.873  33.473  19.847  1.00   22.17  ? 51  HIS B CB  1 
ATOM   3316  C CG  . HIS B  1 51  ? 82.300  33.789  20.188  1.00   24.10  ? 51  HIS B CG  1 
ATOM   3317  N ND1 . HIS B  1 51  ? 83.239  34.111  19.232  1.00   21.88  ? 51  HIS B ND1 1 
ATOM   3318  C CD2 . HIS B  1 51  ? 82.948  33.823  21.376  1.00   22.62  ? 51  HIS B CD2 1 
ATOM   3319  C CE1 . HIS B  1 51  ? 84.396  34.342  19.816  1.00   24.20  ? 51  HIS B CE1 1 
ATOM   3320  N NE2 . HIS B  1 51  ? 84.245  34.180  21.118  1.00   23.95  ? 51  HIS B NE2 1 
ATOM   3321  N N   . LEU B  1 52  ? 79.359  33.936  22.393  1.00   19.58  ? 52  LEU B N   1 
ATOM   3322  C CA  . LEU B  1 52  ? 79.434  33.996  23.841  1.00   20.68  ? 52  LEU B CA  1 
ATOM   3323  C C   . LEU B  1 52  ? 80.774  33.441  24.286  1.00   24.47  ? 52  LEU B C   1 
ATOM   3324  O O   . LEU B  1 52  ? 81.186  32.384  23.822  1.00   28.29  ? 52  LEU B O   1 
ATOM   3325  C CB  . LEU B  1 52  ? 78.279  33.221  24.468  1.00   21.11  ? 52  LEU B CB  1 
ATOM   3326  C CG  . LEU B  1 52  ? 78.115  33.251  25.988  1.00   23.20  ? 52  LEU B CG  1 
ATOM   3327  C CD1 . LEU B  1 52  ? 76.673  33.098  26.282  1.00   24.74  ? 52  LEU B CD1 1 
ATOM   3328  C CD2 . LEU B  1 52  ? 78.853  32.133  26.637  1.00   24.67  ? 52  LEU B CD2 1 
ATOM   3329  N N   . TRP B  1 53  ? 81.472  34.145  25.170  1.00   22.43  ? 53  TRP B N   1 
ATOM   3330  C CA  . TRP B  1 53  ? 82.683  33.579  25.715  1.00   22.10  ? 53  TRP B CA  1 
ATOM   3331  C C   . TRP B  1 53  ? 82.731  33.740  27.220  1.00   27.36  ? 53  TRP B C   1 
ATOM   3332  O O   . TRP B  1 53  ? 82.151  34.667  27.774  1.00   28.46  ? 53  TRP B O   1 
ATOM   3333  C CB  . TRP B  1 53  ? 83.920  34.182  25.067  1.00   21.90  ? 53  TRP B CB  1 
ATOM   3334  C CG  . TRP B  1 53  ? 84.114  35.664  25.176  1.00   24.41  ? 53  TRP B CG  1 
ATOM   3335  C CD1 . TRP B  1 53  ? 83.706  36.604  24.282  1.00   25.54  ? 53  TRP B CD1 1 
ATOM   3336  C CD2 . TRP B  1 53  ? 84.833  36.373  26.194  1.00   24.07  ? 53  TRP B CD2 1 
ATOM   3337  N NE1 . TRP B  1 53  ? 84.100  37.841  24.687  1.00   24.06  ? 53  TRP B NE1 1 
ATOM   3338  C CE2 . TRP B  1 53  ? 84.800  37.725  25.858  1.00   25.09  ? 53  TRP B CE2 1 
ATOM   3339  C CE3 . TRP B  1 53  ? 85.488  35.989  27.371  1.00   22.88  ? 53  TRP B CE3 1 
ATOM   3340  C CZ2 . TRP B  1 53  ? 85.397  38.704  26.654  1.00   28.14  ? 53  TRP B CZ2 1 
ATOM   3341  C CZ3 . TRP B  1 53  ? 86.069  36.955  28.158  1.00   25.40  ? 53  TRP B CZ3 1 
ATOM   3342  C CH2 . TRP B  1 53  ? 86.021  38.297  27.798  1.00   28.48  ? 53  TRP B CH2 1 
ATOM   3343  N N   . VAL B  1 54  ? 83.399  32.794  27.874  1.00   27.81  ? 54  VAL B N   1 
ATOM   3344  C CA  . VAL B  1 54  ? 83.541  32.760  29.330  1.00   28.12  ? 54  VAL B CA  1 
ATOM   3345  C C   . VAL B  1 54  ? 84.956  32.328  29.744  1.00   29.84  ? 54  VAL B C   1 
ATOM   3346  O O   . VAL B  1 54  ? 85.655  31.663  28.990  1.00   29.94  ? 54  VAL B O   1 
ATOM   3347  C CB  A VAL B  1 54  ? 82.575  31.772  30.020  0.50   26.74  ? 54  VAL B CB  1 
ATOM   3348  C CB  B VAL B  1 54  ? 82.506  31.800  29.989  0.50   26.08  ? 54  VAL B CB  1 
ATOM   3349  C CG1 A VAL B  1 54  ? 82.095  32.358  31.329  0.50   27.55  ? 54  VAL B CG1 1 
ATOM   3350  C CG1 B VAL B  1 54  ? 81.075  32.248  29.703  0.50   26.55  ? 54  VAL B CG1 1 
ATOM   3351  C CG2 A VAL B  1 54  ? 81.417  31.388  29.123  0.50   25.53  ? 54  VAL B CG2 1 
ATOM   3352  C CG2 B VAL B  1 54  ? 82.709  30.378  29.510  0.50   21.41  ? 54  VAL B CG2 1 
ATOM   3353  N N   . THR B  1 55  ? 85.375  32.732  30.937  1.00   34.89  ? 55  THR B N   1 
ATOM   3354  C CA  . THR B  1 55  ? 86.569  32.170  31.564  1.00   40.96  ? 55  THR B CA  1 
ATOM   3355  C C   . THR B  1 55  ? 86.219  30.772  32.089  1.00   45.61  ? 55  THR B C   1 
ATOM   3356  O O   . THR B  1 55  ? 85.310  30.639  32.916  1.00   48.63  ? 55  THR B O   1 
ATOM   3357  C CB  . THR B  1 55  ? 87.033  33.024  32.726  1.00   41.57  ? 55  THR B CB  1 
ATOM   3358  O OG1 . THR B  1 55  ? 87.254  34.356  32.271  1.00   40.26  ? 55  THR B OG1 1 
ATOM   3359  C CG2 . THR B  1 55  ? 88.298  32.457  33.320  1.00   46.54  ? 55  THR B CG2 1 
ATOM   3360  N N   . CYS B  1 56  ? 86.950  29.739  31.668  1.00   45.46  ? 56  CYS B N   1 
ATOM   3361  C CA  . CYS B  1 56  ? 86.599  28.376  32.078  1.00   45.84  ? 56  CYS B CA  1 
ATOM   3362  C C   . CYS B  1 56  ? 87.572  27.785  33.060  1.00   51.78  ? 56  CYS B C   1 
ATOM   3363  O O   . CYS B  1 56  ? 87.247  26.838  33.771  1.00   56.54  ? 56  CYS B O   1 
ATOM   3364  C CB  . CYS B  1 56  ? 86.492  27.448  30.872  1.00   37.63  ? 56  CYS B CB  1 
ATOM   3365  S SG  . CYS B  1 56  ? 85.120  27.820  29.885  1.00   36.47  ? 56  CYS B SG  1 
ATOM   3366  N N   . SER B  1 57  ? 88.761  28.353  33.110  1.00   53.88  ? 57  SER B N   1 
ATOM   3367  C CA  . SER B  1 57  ? 89.799  27.831  33.966  1.00   63.58  ? 57  SER B CA  1 
ATOM   3368  C C   . SER B  1 57  ? 89.402  27.749  35.458  1.00   69.72  ? 57  SER B C   1 
ATOM   3369  O O   . SER B  1 57  ? 90.125  27.159  36.264  1.00   73.85  ? 57  SER B O   1 
ATOM   3370  C CB  . SER B  1 57  ? 91.041  28.696  33.793  1.00   67.25  ? 57  SER B CB  1 
ATOM   3371  O OG  . SER B  1 57  ? 90.804  29.990  34.305  1.00   69.26  ? 57  SER B OG  1 
ATOM   3372  N N   . GLN B  1 58  ? 88.261  28.338  35.813  1.00   70.89  ? 58  GLN B N   1 
ATOM   3373  C CA  . GLN B  1 58  ? 87.679  28.277  37.161  1.00   77.55  ? 58  GLN B CA  1 
ATOM   3374  C C   . GLN B  1 58  ? 87.210  26.968  37.799  1.00   81.51  ? 58  GLN B C   1 
ATOM   3375  O O   . GLN B  1 58  ? 87.872  25.927  37.780  1.00   87.33  ? 58  GLN B O   1 
ATOM   3376  C CB  . GLN B  1 58  ? 86.468  29.205  37.188  1.00   80.39  ? 58  GLN B CB  1 
ATOM   3377  C CG  . GLN B  1 58  ? 86.404  30.181  36.046  1.00   82.80  ? 58  GLN B CG  1 
ATOM   3378  C CD  . GLN B  1 58  ? 85.313  31.205  36.266  1.00   87.85  ? 58  GLN B CD  1 
ATOM   3379  O OE1 . GLN B  1 58  ? 85.239  31.829  37.334  1.00   91.91  ? 58  GLN B OE1 1 
ATOM   3380  N NE2 . GLN B  1 58  ? 84.436  31.367  35.270  1.00   87.03  ? 58  GLN B NE2 1 
ATOM   3381  N N   . HIS B  1 59  ? 86.035  27.095  38.408  1.00   77.69  ? 59  HIS B N   1 
ATOM   3382  C CA  . HIS B  1 59  ? 85.336  26.056  39.147  1.00   74.43  ? 59  HIS B CA  1 
ATOM   3383  C C   . HIS B  1 59  ? 84.376  25.376  38.187  1.00   67.99  ? 59  HIS B C   1 
ATOM   3384  O O   . HIS B  1 59  ? 83.232  25.113  38.548  1.00   73.87  ? 59  HIS B O   1 
ATOM   3385  C CB  . HIS B  1 59  ? 84.526  26.636  40.313  1.00   74.86  ? 59  HIS B CB  1 
ATOM   3386  C CG  . HIS B  1 59  ? 85.286  27.548  41.218  1.00   75.99  ? 59  HIS B CG  1 
ATOM   3387  N ND1 . HIS B  1 59  ? 86.318  27.107  42.018  1.00   79.80  ? 59  HIS B ND1 1 
ATOM   3388  C CD2 . HIS B  1 59  ? 85.124  28.861  41.496  1.00   75.77  ? 59  HIS B CD2 1 
ATOM   3389  C CE1 . HIS B  1 59  ? 86.777  28.120  42.731  1.00   82.63  ? 59  HIS B CE1 1 
ATOM   3390  N NE2 . HIS B  1 59  ? 86.071  29.196  42.435  1.00   80.10  ? 59  HIS B NE2 1 
ATOM   3391  N N   . TYR B  1 60  ? 84.794  25.147  36.952  1.00   54.80  ? 60  TYR B N   1 
ATOM   3392  C CA  . TYR B  1 60  ? 83.829  24.685  35.981  1.00   43.80  ? 60  TYR B CA  1 
ATOM   3393  C C   . TYR B  1 60  ? 83.386  23.279  36.343  1.00   40.71  ? 60  TYR B C   1 
ATOM   3394  O O   . TYR B  1 60  ? 84.114  22.305  36.144  1.00   38.76  ? 60  TYR B O   1 
ATOM   3395  C CB  . TYR B  1 60  ? 84.439  24.731  34.586  1.00   39.62  ? 60  TYR B CB  1 
ATOM   3396  C CG  . TYR B  1 60  ? 83.439  24.646  33.459  1.00   35.11  ? 60  TYR B CG  1 
ATOM   3397  C CD1 . TYR B  1 60  ? 82.662  23.521  33.266  1.00   32.95  ? 60  TYR B CD1 1 
ATOM   3398  C CD2 . TYR B  1 60  ? 83.269  25.725  32.599  1.00   29.67  ? 60  TYR B CD2 1 
ATOM   3399  C CE1 . TYR B  1 60  ? 81.746  23.466  32.248  1.00   33.41  ? 60  TYR B CE1 1 
ATOM   3400  C CE2 . TYR B  1 60  ? 82.373  25.674  31.572  1.00   28.94  ? 60  TYR B CE2 1 
ATOM   3401  C CZ  . TYR B  1 60  ? 81.615  24.543  31.393  1.00   31.12  ? 60  TYR B CZ  1 
ATOM   3402  O OH  . TYR B  1 60  ? 80.705  24.501  30.370  1.00   33.70  ? 60  TYR B OH  1 
ATOM   3403  N N   . SER B  1 61  ? 82.161  23.180  36.846  1.00   37.69  ? 61  SER B N   1 
ATOM   3404  C CA  . SER B  1 61  ? 81.621  21.902  37.262  1.00   37.96  ? 61  SER B CA  1 
ATOM   3405  C C   . SER B  1 61  ? 80.392  21.591  36.403  1.00   41.23  ? 61  SER B C   1 
ATOM   3406  O O   . SER B  1 61  ? 79.401  22.301  36.452  1.00   42.13  ? 61  SER B O   1 
ATOM   3407  C CB  . SER B  1 61  ? 81.277  21.927  38.750  1.00   41.38  ? 61  SER B CB  1 
ATOM   3408  O OG  . SER B  1 61  ? 82.418  22.111  39.575  1.00   45.79  ? 61  SER B OG  1 
ATOM   3409  N N   . SER B  1 62  ? 80.454  20.523  35.617  1.00   38.86  ? 62  SER B N   1 
ATOM   3410  C CA  . SER B  1 62  ? 79.343  20.195  34.742  1.00   35.85  ? 62  SER B CA  1 
ATOM   3411  C C   . SER B  1 62  ? 79.453  18.760  34.229  1.00   36.76  ? 62  SER B C   1 
ATOM   3412  O O   . SER B  1 62  ? 80.524  18.291  33.821  1.00   38.56  ? 62  SER B O   1 
ATOM   3413  C CB  . SER B  1 62  ? 79.275  21.191  33.578  1.00   32.36  ? 62  SER B CB  1 
ATOM   3414  O OG  . SER B  1 62  ? 78.219  20.888  32.695  1.00   33.15  ? 62  SER B OG  1 
ATOM   3415  N N   . SER B  1 63  ? 78.333  18.054  34.295  1.00   36.06  ? 63  SER B N   1 
ATOM   3416  C CA  . SER B  1 63  ? 78.256  16.714  33.752  1.00   38.07  ? 63  SER B CA  1 
ATOM   3417  C C   . SER B  1 63  ? 77.885  16.770  32.277  1.00   38.31  ? 63  SER B C   1 
ATOM   3418  O O   . SER B  1 63  ? 77.767  15.741  31.620  1.00   38.15  ? 63  SER B O   1 
ATOM   3419  C CB  . SER B  1 63  ? 77.245  15.874  34.522  1.00   41.09  ? 63  SER B CB  1 
ATOM   3420  O OG  . SER B  1 63  ? 75.937  16.375  34.346  1.00   43.71  ? 63  SER B OG  1 
ATOM   3421  N N   . THR B  1 64  ? 77.710  17.974  31.751  1.00   37.94  ? 64  THR B N   1 
ATOM   3422  C CA  . THR B  1 64  ? 77.314  18.105  30.358  1.00   38.85  ? 64  THR B CA  1 
ATOM   3423  C C   . THR B  1 64  ? 78.337  18.820  29.486  1.00   37.68  ? 64  THR B C   1 
ATOM   3424  O O   . THR B  1 64  ? 78.036  19.156  28.353  1.00   39.91  ? 64  THR B O   1 
ATOM   3425  C CB  . THR B  1 64  ? 75.951  18.852  30.195  1.00   32.47  ? 64  THR B CB  1 
ATOM   3426  O OG1 . THR B  1 64  ? 75.891  19.998  31.052  1.00   34.49  ? 64  THR B OG1 1 
ATOM   3427  C CG2 . THR B  1 64  ? 74.812  17.936  30.504  1.00   37.79  ? 64  THR B CG2 1 
ATOM   3428  N N   . TYR B  1 65  ? 79.538  19.054  29.993  1.00   33.30  ? 65  TYR B N   1 
ATOM   3429  C CA  . TYR B  1 65  ? 80.544  19.757  29.212  1.00   28.02  ? 65  TYR B CA  1 
ATOM   3430  C C   . TYR B  1 65  ? 81.230  18.918  28.161  1.00   28.73  ? 65  TYR B C   1 
ATOM   3431  O O   . TYR B  1 65  ? 81.541  17.766  28.411  1.00   32.93  ? 65  TYR B O   1 
ATOM   3432  C CB  . TYR B  1 65  ? 81.621  20.318  30.127  1.00   28.19  ? 65  TYR B CB  1 
ATOM   3433  C CG  . TYR B  1 65  ? 82.827  20.827  29.367  1.00   27.94  ? 65  TYR B CG  1 
ATOM   3434  C CD1 . TYR B  1 65  ? 82.817  22.088  28.792  1.00   27.79  ? 65  TYR B CD1 1 
ATOM   3435  C CD2 . TYR B  1 65  ? 83.977  20.055  29.234  1.00   26.26  ? 65  TYR B CD2 1 
ATOM   3436  C CE1 . TYR B  1 65  ? 83.910  22.558  28.105  1.00   30.12  ? 65  TYR B CE1 1 
ATOM   3437  C CE2 . TYR B  1 65  ? 85.053  20.504  28.542  1.00   25.27  ? 65  TYR B CE2 1 
ATOM   3438  C CZ  . TYR B  1 65  ? 85.033  21.756  27.983  1.00   31.03  ? 65  TYR B CZ  1 
ATOM   3439  O OH  . TYR B  1 65  ? 86.142  22.216  27.294  1.00   34.77  ? 65  TYR B OH  1 
ATOM   3440  N N   . GLN B  1 66  ? 81.484  19.499  26.993  1.00   30.72  ? 66  GLN B N   1 
ATOM   3441  C CA  . GLN B  1 66  ? 82.362  18.874  25.996  1.00   35.62  ? 66  GLN B CA  1 
ATOM   3442  C C   . GLN B  1 66  ? 83.179  19.904  25.233  1.00   33.97  ? 66  GLN B C   1 
ATOM   3443  O O   . GLN B  1 66  ? 82.695  20.998  24.956  1.00   31.29  ? 66  GLN B O   1 
ATOM   3444  C CB  . GLN B  1 66  ? 81.574  18.031  24.993  1.00   42.56  ? 66  GLN B CB  1 
ATOM   3445  C CG  . GLN B  1 66  ? 81.043  16.739  25.559  1.00   52.70  ? 66  GLN B CG  1 
ATOM   3446  C CD  . GLN B  1 66  ? 80.146  15.992  24.599  1.00   59.04  ? 66  GLN B CD  1 
ATOM   3447  O OE1 . GLN B  1 66  ? 80.471  15.828  23.424  1.00   61.93  ? 66  GLN B OE1 1 
ATOM   3448  N NE2 . GLN B  1 66  ? 79.005  15.533  25.098  1.00   61.54  ? 66  GLN B NE2 1 
ATOM   3449  N N   . ALA B  1 67  ? 84.411  19.538  24.869  1.00   34.81  ? 67  ALA B N   1 
ATOM   3450  C CA  . ALA B  1 67  ? 85.216  20.340  23.946  1.00   34.81  ? 67  ALA B CA  1 
ATOM   3451  C C   . ALA B  1 67  ? 85.297  19.642  22.585  1.00   32.51  ? 67  ALA B C   1 
ATOM   3452  O O   . ALA B  1 67  ? 85.937  18.591  22.482  1.00   31.61  ? 67  ALA B O   1 
ATOM   3453  C CB  . ALA B  1 67  ? 86.614  20.573  24.509  1.00   37.30  ? 67  ALA B CB  1 
ATOM   3454  N N   . PRO B  1 68  ? 84.615  20.192  21.552  1.00   27.13  ? 68  PRO B N   1 
ATOM   3455  C CA  . PRO B  1 68  ? 84.599  19.533  20.242  1.00   26.47  ? 68  PRO B CA  1 
ATOM   3456  C C   . PRO B  1 68  ? 85.997  19.295  19.644  1.00   28.55  ? 68  PRO B C   1 
ATOM   3457  O O   . PRO B  1 68  ? 86.881  20.115  19.827  1.00   29.29  ? 68  PRO B O   1 
ATOM   3458  C CB  . PRO B  1 68  ? 83.791  20.494  19.388  1.00   21.98  ? 68  PRO B CB  1 
ATOM   3459  C CG  . PRO B  1 68  ? 82.897  21.184  20.335  1.00   21.98  ? 68  PRO B CG  1 
ATOM   3460  C CD  . PRO B  1 68  ? 83.700  21.343  21.588  1.00   22.72  ? 68  PRO B CD  1 
ATOM   3461  N N   . PHE B  1 69  ? 86.179  18.196  18.915  1.00   28.74  ? 69  PHE B N   1 
ATOM   3462  C CA  . PHE B  1 69  ? 87.479  17.899  18.361  1.00   30.51  ? 69  PHE B CA  1 
ATOM   3463  C C   . PHE B  1 69  ? 87.692  18.710  17.109  1.00   31.32  ? 69  PHE B C   1 
ATOM   3464  O O   . PHE B  1 69  ? 86.737  19.163  16.480  1.00   31.77  ? 69  PHE B O   1 
ATOM   3465  C CB  . PHE B  1 69  ? 87.661  16.381  18.088  1.00   33.63  ? 69  PHE B CB  1 
ATOM   3466  C CG  . PHE B  1 69  ? 86.650  15.760  17.130  1.00   32.39  ? 69  PHE B CG  1 
ATOM   3467  C CD1 . PHE B  1 69  ? 86.812  15.861  15.752  1.00   32.31  ? 69  PHE B CD1 1 
ATOM   3468  C CD2 . PHE B  1 69  ? 85.600  14.992  17.609  1.00   29.85  ? 69  PHE B CD2 1 
ATOM   3469  C CE1 . PHE B  1 69  ? 85.902  15.259  14.882  1.00   32.48  ? 69  PHE B CE1 1 
ATOM   3470  C CE2 . PHE B  1 69  ? 84.691  14.387  16.734  1.00   30.08  ? 69  PHE B CE2 1 
ATOM   3471  C CZ  . PHE B  1 69  ? 84.847  14.524  15.378  1.00   31.11  ? 69  PHE B CZ  1 
ATOM   3472  N N   . CYS B  1 70  ? 88.956  18.916  16.768  1.00   29.26  ? 70  CYS B N   1 
ATOM   3473  C CA  . CYS B  1 70  ? 89.306  19.698  15.601  1.00   29.96  ? 70  CYS B CA  1 
ATOM   3474  C C   . CYS B  1 70  ? 88.769  19.058  14.328  1.00   28.84  ? 70  CYS B C   1 
ATOM   3475  O O   . CYS B  1 70  ? 88.852  17.855  14.167  1.00   31.53  ? 70  CYS B O   1 
ATOM   3476  C CB  . CYS B  1 70  ? 90.819  19.865  15.509  1.00   33.38  ? 70  CYS B CB  1 
ATOM   3477  S SG  . CYS B  1 70  ? 91.316  21.295  14.504  1.00   37.02  ? 70  CYS B SG  1 
ATOM   3478  N N   . HIS B  1 71  ? 88.246  19.897  13.439  1.00   24.17  ? 71  HIS B N   1 
ATOM   3479  C CA  . HIS B  1 71  ? 87.624  19.496  12.179  1.00   27.79  ? 71  HIS B CA  1 
ATOM   3480  C C   . HIS B  1 71  ? 86.279  18.816  12.380  1.00   27.34  ? 71  HIS B C   1 
ATOM   3481  O O   . HIS B  1 71  ? 85.740  18.254  11.430  1.00   29.12  ? 71  HIS B O   1 
ATOM   3482  C CB  . HIS B  1 71  ? 88.530  18.588  11.354  1.00   29.89  ? 71  HIS B CB  1 
ATOM   3483  C CG  . HIS B  1 71  ? 89.928  19.100  11.189  1.00   31.48  ? 71  HIS B CG  1 
ATOM   3484  N ND1 . HIS B  1 71  ? 91.032  18.447  11.706  1.00   32.54  ? 71  HIS B ND1 1 
ATOM   3485  C CD2 . HIS B  1 71  ? 90.406  20.191  10.549  1.00   31.52  ? 71  HIS B CD2 1 
ATOM   3486  C CE1 . HIS B  1 71  ? 92.124  19.111  11.387  1.00   30.60  ? 71  HIS B CE1 1 
ATOM   3487  N NE2 . HIS B  1 71  ? 91.773  20.169  10.680  1.00   33.82  ? 71  HIS B NE2 1 
ATOM   3488  N N   . SER B  1 72  ? 85.717  18.916  13.589  1.00   25.21  ? 72  SER B N   1 
ATOM   3489  C CA  . SER B  1 72  ? 84.394  18.376  13.870  1.00   23.09  ? 72  SER B CA  1 
ATOM   3490  C C   . SER B  1 72  ? 83.349  19.215  13.190  1.00   26.68  ? 72  SER B C   1 
ATOM   3491  O O   . SER B  1 72  ? 83.650  20.267  12.649  1.00   29.77  ? 72  SER B O   1 
ATOM   3492  C CB  . SER B  1 72  ? 84.097  18.342  15.367  1.00   22.22  ? 72  SER B CB  1 
ATOM   3493  O OG  . SER B  1 72  ? 84.087  19.640  15.917  1.00   23.95  ? 72  SER B OG  1 
ATOM   3494  N N   . THR B  1 73  ? 82.122  18.723  13.168  1.00   27.21  ? 73  THR B N   1 
ATOM   3495  C CA  . THR B  1 73  ? 81.007  19.491  12.654  1.00   24.80  ? 73  THR B CA  1 
ATOM   3496  C C   . THR B  1 73  ? 80.715  20.709  13.535  1.00   22.98  ? 73  THR B C   1 
ATOM   3497  O O   . THR B  1 73  ? 80.329  21.755  13.044  1.00   22.18  ? 73  THR B O   1 
ATOM   3498  C CB  . THR B  1 73  ? 79.776  18.603  12.526  1.00   25.32  ? 73  THR B CB  1 
ATOM   3499  O OG1 . THR B  1 73  ? 79.538  17.949  13.777  1.00   26.61  ? 73  THR B OG1 1 
ATOM   3500  C CG2 . THR B  1 73  ? 80.004  17.553  11.443  1.00   22.54  ? 73  THR B CG2 1 
ATOM   3501  N N   . GLN B  1 74  ? 80.925  20.590  14.838  1.00   23.82  ? 74  GLN B N   1 
ATOM   3502  C CA  . GLN B  1 74  ? 80.757  21.748  15.700  1.00   23.18  ? 74  GLN B CA  1 
ATOM   3503  C C   . GLN B  1 74  ? 81.726  22.861  15.338  1.00   24.19  ? 74  GLN B C   1 
ATOM   3504  O O   . GLN B  1 74  ? 81.369  24.044  15.353  1.00   25.27  ? 74  GLN B O   1 
ATOM   3505  C CB  . GLN B  1 74  ? 80.952  21.379  17.166  1.00   23.76  ? 74  GLN B CB  1 
ATOM   3506  C CG  . GLN B  1 74  ? 79.909  20.438  17.761  1.00   23.79  ? 74  GLN B CG  1 
ATOM   3507  C CD  . GLN B  1 74  ? 80.394  19.027  17.764  1.00   29.42  ? 74  GLN B CD  1 
ATOM   3508  O OE1 . GLN B  1 74  ? 81.145  18.640  16.892  1.00   32.69  ? 74  GLN B OE1 1 
ATOM   3509  N NE2 . GLN B  1 74  ? 80.033  18.263  18.787  1.00   34.93  ? 74  GLN B NE2 1 
ATOM   3510  N N   . CYS B  1 75  ? 82.964  22.491  15.030  1.00   27.32  ? 75  CYS B N   1 
ATOM   3511  C CA  . CYS B  1 75  ? 83.985  23.473  14.636  1.00   27.25  ? 75  CYS B CA  1 
ATOM   3512  C C   . CYS B  1 75  ? 83.702  24.136  13.272  1.00   25.37  ? 75  CYS B C   1 
ATOM   3513  O O   . CYS B  1 75  ? 83.993  25.312  13.068  1.00   24.40  ? 75  CYS B O   1 
ATOM   3514  C CB  . CYS B  1 75  ? 85.368  22.813  14.654  1.00   29.54  ? 75  CYS B CB  1 
ATOM   3515  S SG  . CYS B  1 75  ? 85.831  22.291  16.340  1.00   35.57  ? 75  CYS B SG  1 
ATOM   3516  N N   . SER B  1 76  ? 83.148  23.382  12.334  1.00   25.69  ? 76  SER B N   1 
ATOM   3517  C CA  . SER B  1 76  ? 82.726  23.955  11.070  1.00   25.05  ? 76  SER B CA  1 
ATOM   3518  C C   . SER B  1 76  ? 81.640  25.020  11.290  1.00   24.00  ? 76  SER B C   1 
ATOM   3519  O O   . SER B  1 76  ? 81.701  26.112  10.731  1.00   27.09  ? 76  SER B O   1 
ATOM   3520  C CB  . SER B  1 76  ? 82.233  22.859  10.144  1.00   26.83  ? 76  SER B CB  1 
ATOM   3521  O OG  . SER B  1 76  ? 81.841  23.395  8.899   1.00   32.33  ? 76  SER B OG  1 
ATOM   3522  N N   . ARG B  1 77  ? 80.651  24.706  12.115  1.00   24.60  ? 77  ARG B N   1 
ATOM   3523  C CA  . ARG B  1 77  ? 79.554  25.640  12.383  1.00   24.76  ? 77  ARG B CA  1 
ATOM   3524  C C   . ARG B  1 77  ? 80.026  26.954  13.003  1.00   25.22  ? 77  ARG B C   1 
ATOM   3525  O O   . ARG B  1 77  ? 79.548  28.031  12.656  1.00   26.93  ? 77  ARG B O   1 
ATOM   3526  C CB  . ARG B  1 77  ? 78.532  24.961  13.293  1.00   24.31  ? 77  ARG B CB  1 
ATOM   3527  C CG  . ARG B  1 77  ? 77.271  25.734  13.469  1.00   27.82  ? 77  ARG B CG  1 
ATOM   3528  C CD  . ARG B  1 77  ? 76.239  25.048  14.359  1.00   29.72  ? 77  ARG B CD  1 
ATOM   3529  N NE  . ARG B  1 77  ? 75.099  25.962  14.471  1.00   32.88  ? 77  ARG B NE  1 
ATOM   3530  C CZ  . ARG B  1 77  ? 74.154  25.924  15.400  1.00   31.81  ? 77  ARG B CZ  1 
ATOM   3531  N NH1 . ARG B  1 77  ? 74.177  25.007  16.349  1.00   34.60  ? 77  ARG B NH1 1 
ATOM   3532  N NH2 . ARG B  1 77  ? 73.196  26.835  15.380  1.00   33.41  ? 77  ARG B NH2 1 
ATOM   3533  N N   . ALA B  1 78  ? 80.989  26.848  13.906  1.00   23.28  ? 78  ALA B N   1 
ATOM   3534  C CA  . ALA B  1 78  ? 81.593  27.980  14.593  1.00   21.15  ? 78  ALA B CA  1 
ATOM   3535  C C   . ALA B  1 78  ? 82.576  28.741  13.697  1.00   24.81  ? 78  ALA B C   1 
ATOM   3536  O O   . ALA B  1 78  ? 83.111  29.773  14.088  1.00   25.16  ? 78  ALA B O   1 
ATOM   3537  C CB  . ALA B  1 78  ? 82.300  27.495  15.858  1.00   19.03  ? 78  ALA B CB  1 
ATOM   3538  N N   . ASN B  1 79  ? 82.843  28.174  12.522  1.00   28.76  ? 79  ASN B N   1 
ATOM   3539  C CA  . ASN B  1 79  ? 83.709  28.741  11.495  1.00   30.57  ? 79  ASN B CA  1 
ATOM   3540  C C   . ASN B  1 79  ? 85.164  28.905  11.990  1.00   32.82  ? 79  ASN B C   1 
ATOM   3541  O O   . ASN B  1 79  ? 85.832  29.916  11.758  1.00   32.54  ? 79  ASN B O   1 
ATOM   3542  C CB  . ASN B  1 79  ? 83.136  30.061  10.992  1.00   33.24  ? 79  ASN B CB  1 
ATOM   3543  C CG  . ASN B  1 79  ? 83.735  30.488  9.652   1.00   40.97  ? 79  ASN B CG  1 
ATOM   3544  O OD1 . ASN B  1 79  ? 84.175  29.660  8.845   1.00   44.17  ? 79  ASN B OD1 1 
ATOM   3545  N ND2 . ASN B  1 79  ? 83.751  31.788  9.412   1.00   43.20  ? 79  ASN B ND2 1 
ATOM   3546  N N   . THR B  1 80  ? 85.659  27.894  12.684  1.00   33.20  ? 80  THR B N   1 
ATOM   3547  C CA  . THR B  1 80  ? 87.057  27.884  13.070  1.00   35.82  ? 80  THR B CA  1 
ATOM   3548  C C   . THR B  1 80  ? 87.654  26.594  12.559  1.00   44.39  ? 80  THR B C   1 
ATOM   3549  O O   . THR B  1 80  ? 87.128  25.529  12.852  1.00   45.56  ? 80  THR B O   1 
ATOM   3550  C CB  . THR B  1 80  ? 87.240  27.999  14.598  1.00   31.30  ? 80  THR B CB  1 
ATOM   3551  O OG1 . THR B  1 80  ? 88.588  27.696  14.913  1.00   36.66  ? 80  THR B OG1 1 
ATOM   3552  C CG2 . THR B  1 80  ? 86.365  27.053  15.359  1.00   25.24  ? 80  THR B CG2 1 
ATOM   3553  N N   . HIS B  1 81  ? 88.722  26.661  11.769  1.00   48.20  ? 81  HIS B N   1 
ATOM   3554  C CA  . HIS B  1 81  ? 89.332  25.420  11.285  1.00   52.68  ? 81  HIS B CA  1 
ATOM   3555  C C   . HIS B  1 81  ? 90.785  25.368  11.743  1.00   57.13  ? 81  HIS B C   1 
ATOM   3556  O O   . HIS B  1 81  ? 91.598  24.598  11.223  1.00   60.84  ? 81  HIS B O   1 
ATOM   3557  C CB  . HIS B  1 81  ? 89.205  25.297  9.756   1.00   57.61  ? 81  HIS B CB  1 
ATOM   3558  C CG  . HIS B  1 81  ? 87.782  25.147  9.274   1.00   64.06  ? 81  HIS B CG  1 
ATOM   3559  N ND1 . HIS B  1 81  ? 86.944  26.227  9.057   1.00   67.80  ? 81  HIS B ND1 1 
ATOM   3560  C CD2 . HIS B  1 81  ? 87.038  24.042  9.008   1.00   63.35  ? 81  HIS B CD2 1 
ATOM   3561  C CE1 . HIS B  1 81  ? 85.759  25.796  8.655   1.00   67.20  ? 81  HIS B CE1 1 
ATOM   3562  N NE2 . HIS B  1 81  ? 85.791  24.474  8.620   1.00   65.35  ? 81  HIS B NE2 1 
ATOM   3563  N N   . GLN B  1 82  ? 91.077  26.196  12.747  1.00   55.90  ? 82  GLN B N   1 
ATOM   3564  C CA  . GLN B  1 82  ? 92.371  26.278  13.414  1.00   52.36  ? 82  GLN B CA  1 
ATOM   3565  C C   . GLN B  1 82  ? 92.417  25.436  14.684  1.00   43.62  ? 82  GLN B C   1 
ATOM   3566  O O   . GLN B  1 82  ? 91.595  25.633  15.568  1.00   41.49  ? 82  GLN B O   1 
ATOM   3567  C CB  . GLN B  1 82  ? 92.677  27.724  13.784  1.00   57.32  ? 82  GLN B CB  1 
ATOM   3568  C CG  . GLN B  1 82  ? 93.714  27.806  14.883  1.00   63.44  ? 82  GLN B CG  1 
ATOM   3569  C CD  . GLN B  1 82  ? 94.026  29.215  15.339  1.00   67.57  ? 82  GLN B CD  1 
ATOM   3570  O OE1 . GLN B  1 82  ? 93.527  30.201  14.785  1.00   70.08  ? 82  GLN B OE1 1 
ATOM   3571  N NE2 . GLN B  1 82  ? 94.867  29.316  16.361  1.00   67.50  ? 82  GLN B NE2 1 
ATOM   3572  N N   . CYS B  1 83  ? 93.371  24.511  14.783  1.00   40.62  ? 83  CYS B N   1 
ATOM   3573  C CA  . CYS B  1 83  ? 93.458  23.610  15.944  1.00   37.83  ? 83  CYS B CA  1 
ATOM   3574  C C   . CYS B  1 83  ? 94.066  24.248  17.192  1.00   38.25  ? 83  CYS B C   1 
ATOM   3575  O O   . CYS B  1 83  ? 94.889  25.143  17.120  1.00   40.69  ? 83  CYS B O   1 
ATOM   3576  C CB  . CYS B  1 83  ? 94.241  22.346  15.583  1.00   36.81  ? 83  CYS B CB  1 
ATOM   3577  S SG  . CYS B  1 83  ? 93.353  21.325  14.387  1.00   43.20  ? 83  CYS B SG  1 
ATOM   3578  N N   . PHE B  1 84  ? 93.653  23.741  18.340  1.00   34.99  ? 84  PHE B N   1 
ATOM   3579  C CA  . PHE B  1 84  ? 94.009  24.316  19.609  1.00   32.27  ? 84  PHE B CA  1 
ATOM   3580  C C   . PHE B  1 84  ? 95.007  23.429  20.335  1.00   38.12  ? 84  PHE B C   1 
ATOM   3581  O O   . PHE B  1 84  ? 94.885  22.206  20.364  1.00   38.71  ? 84  PHE B O   1 
ATOM   3582  C CB  . PHE B  1 84  ? 92.733  24.518  20.432  1.00   29.81  ? 84  PHE B CB  1 
ATOM   3583  C CG  . PHE B  1 84  ? 92.933  25.258  21.725  1.00   31.69  ? 84  PHE B CG  1 
ATOM   3584  C CD1 . PHE B  1 84  ? 93.193  24.578  22.898  1.00   32.93  ? 84  PHE B CD1 1 
ATOM   3585  C CD2 . PHE B  1 84  ? 92.827  26.631  21.767  1.00   31.23  ? 84  PHE B CD2 1 
ATOM   3586  C CE1 . PHE B  1 84  ? 93.376  25.257  24.088  1.00   33.64  ? 84  PHE B CE1 1 
ATOM   3587  C CE2 . PHE B  1 84  ? 92.996  27.311  22.947  1.00   31.76  ? 84  PHE B CE2 1 
ATOM   3588  C CZ  . PHE B  1 84  ? 93.262  26.627  24.110  1.00   34.87  ? 84  PHE B CZ  1 
ATOM   3589  N N   . THR B  1 85  ? 96.017  24.062  20.904  1.00   44.21  ? 85  THR B N   1 
ATOM   3590  C CA  . THR B  1 85  ? 96.989  23.382  21.718  1.00   49.56  ? 85  THR B CA  1 
ATOM   3591  C C   . THR B  1 85  ? 97.120  24.082  23.049  1.00   49.06  ? 85  THR B C   1 
ATOM   3592  O O   . THR B  1 85  ? 97.322  25.295  23.105  1.00   50.03  ? 85  THR B O   1 
ATOM   3593  C CB  . THR B  1 85  ? 98.345  23.311  21.019  1.00   55.83  ? 85  THR B CB  1 
ATOM   3594  O OG1 . THR B  1 85  ? 98.196  22.563  19.809  1.00   54.55  ? 85  THR B OG1 1 
ATOM   3595  C CG2 . THR B  1 85  ? 99.381  22.619  21.907  1.00   62.23  ? 85  THR B CG2 1 
ATOM   3596  N N   . CYS B  1 86  ? 96.941  23.310  24.115  1.00   50.29  ? 86  CYS B N   1 
ATOM   3597  C CA  . CYS B  1 86  ? 97.057  23.828  25.469  1.00   56.28  ? 86  CYS B CA  1 
ATOM   3598  C C   . CYS B  1 86  ? 98.499  23.818  25.990  1.00   62.93  ? 86  CYS B C   1 
ATOM   3599  O O   . CYS B  1 86  ? 99.139  22.766  26.133  1.00   60.22  ? 86  CYS B O   1 
ATOM   3600  C CB  . CYS B  1 86  ? 96.180  23.046  26.432  1.00   57.59  ? 86  CYS B CB  1 
ATOM   3601  S SG  . CYS B  1 86  ? 95.989  23.901  28.012  1.00   51.84  ? 86  CYS B SG  1 
ATOM   3602  N N   . THR B  1 87  ? 98.975  25.019  26.295  1.00   71.43  ? 87  THR B N   1 
ATOM   3603  C CA  . THR B  1 87  ? 100.321 25.257  26.810  1.00   79.83  ? 87  THR B CA  1 
ATOM   3604  C C   . THR B  1 87  ? 100.331 25.768  28.267  1.00   85.98  ? 87  THR B C   1 
ATOM   3605  O O   . THR B  1 87  ? 101.354 26.279  28.746  1.00   93.92  ? 87  THR B O   1 
ATOM   3606  C CB  . THR B  1 87  ? 101.063 26.288  25.930  1.00   79.70  ? 87  THR B CB  1 
ATOM   3607  O OG1 . THR B  1 87  ? 100.311 27.513  25.885  1.00   78.06  ? 87  THR B OG1 1 
ATOM   3608  C CG2 . THR B  1 87  ? 101.244 25.758  24.506  1.00   76.62  ? 87  THR B CG2 1 
ATOM   3609  N N   . ASP B  1 88  ? 99.202  25.644  28.969  1.00   82.14  ? 88  ASP B N   1 
ATOM   3610  C CA  . ASP B  1 88  ? 99.108  26.021  30.389  1.00   83.76  ? 88  ASP B CA  1 
ATOM   3611  C C   . ASP B  1 88  ? 99.232  24.805  31.295  1.00   85.85  ? 88  ASP B C   1 
ATOM   3612  O O   . ASP B  1 88  ? 100.339 24.436  31.693  1.00   92.01  ? 88  ASP B O   1 
ATOM   3613  C CB  . ASP B  1 88  ? 97.792  26.758  30.672  1.00   81.04  ? 88  ASP B CB  1 
ATOM   3614  C CG  . ASP B  1 88  ? 97.738  28.132  30.024  1.00   80.66  ? 88  ASP B CG  1 
ATOM   3615  O OD1 . ASP B  1 88  ? 98.820  28.723  29.819  1.00   85.66  ? 88  ASP B OD1 1 
ATOM   3616  O OD2 . ASP B  1 88  ? 96.622  28.618  29.718  1.00   75.72  ? 88  ASP B OD2 1 
ATOM   3617  N N   . SER B  1 89  ? 98.105  24.221  31.683  1.00   82.22  ? 89  SER B N   1 
ATOM   3618  C CA  . SER B  1 89  ? 98.144  23.009  32.486  1.00   87.62  ? 89  SER B CA  1 
ATOM   3619  C C   . SER B  1 89  ? 98.753  21.927  31.577  1.00   90.03  ? 89  SER B C   1 
ATOM   3620  O O   . SER B  1 89  ? 98.733  22.099  30.355  1.00   89.74  ? 89  SER B O   1 
ATOM   3621  C CB  . SER B  1 89  ? 96.727  22.642  32.962  1.00   85.78  ? 89  SER B CB  1 
ATOM   3622  O OG  . SER B  1 89  ? 96.611  21.285  33.349  1.00   87.73  ? 89  SER B OG  1 
ATOM   3623  N N   . THR B  1 90  ? 99.326  20.848  32.121  1.00   92.02  ? 90  THR B N   1 
ATOM   3624  C CA  . THR B  1 90  ? 99.685  19.720  31.245  1.00   91.14  ? 90  THR B CA  1 
ATOM   3625  C C   . THR B  1 90  ? 98.723  18.561  31.494  1.00   89.48  ? 90  THR B C   1 
ATOM   3626  O O   . THR B  1 90  ? 98.934  17.456  30.992  1.00   89.92  ? 90  THR B O   1 
ATOM   3627  C CB  . THR B  1 90  ? 101.167 19.241  31.375  1.00   89.72  ? 90  THR B CB  1 
ATOM   3628  O OG1 . THR B  1 90  ? 101.524 18.488  30.199  1.00   87.33  ? 90  THR B OG1 1 
ATOM   3629  C CG2 . THR B  1 90  ? 101.400 18.415  32.634  1.00   93.93  ? 90  THR B CG2 1 
ATOM   3630  N N   . THR B  1 91  ? 97.676  18.831  32.278  1.00   87.54  ? 91  THR B N   1 
ATOM   3631  C CA  . THR B  1 91  ? 96.552  17.901  32.412  1.00   83.61  ? 91  THR B CA  1 
ATOM   3632  C C   . THR B  1 91  ? 95.235  18.545  31.918  1.00   75.45  ? 91  THR B C   1 
ATOM   3633  O O   . THR B  1 91  ? 95.096  19.771  31.927  1.00   73.02  ? 91  THR B O   1 
ATOM   3634  C CB  . THR B  1 91  ? 96.397  17.431  33.868  1.00   87.96  ? 91  THR B CB  1 
ATOM   3635  O OG1 . THR B  1 91  ? 95.287  16.529  33.959  1.00   85.45  ? 91  THR B OG1 1 
ATOM   3636  C CG2 . THR B  1 91  ? 96.151  18.617  34.804  1.00   89.13  ? 91  THR B CG2 1 
ATOM   3637  N N   . THR B  1 92  ? 94.257  17.722  31.534  1.00   70.62  ? 92  THR B N   1 
ATOM   3638  C CA  . THR B  1 92  ? 93.054  18.247  30.889  1.00   64.66  ? 92  THR B CA  1 
ATOM   3639  C C   . THR B  1 92  ? 91.940  18.755  31.799  1.00   61.17  ? 92  THR B C   1 
ATOM   3640  O O   . THR B  1 92  ? 91.682  18.221  32.884  1.00   62.34  ? 92  THR B O   1 
ATOM   3641  C CB  . THR B  1 92  ? 92.425  17.189  29.961  1.00   63.45  ? 92  THR B CB  1 
ATOM   3642  O OG1 . THR B  1 92  ? 91.810  16.153  30.743  1.00   65.90  ? 92  THR B OG1 1 
ATOM   3643  C CG2 . THR B  1 92  ? 93.475  16.615  29.025  1.00   64.37  ? 92  THR B CG2 1 
ATOM   3644  N N   . ARG B  1 93  ? 91.241  19.758  31.269  1.00   54.43  ? 93  ARG B N   1 
ATOM   3645  C CA  . ARG B  1 93  ? 90.151  20.454  31.937  1.00   50.39  ? 93  ARG B CA  1 
ATOM   3646  C C   . ARG B  1 93  ? 89.442  21.308  30.904  1.00   44.23  ? 93  ARG B C   1 
ATOM   3647  O O   . ARG B  1 93  ? 89.982  21.456  29.814  1.00   38.44  ? 93  ARG B O   1 
ATOM   3648  C CB  . ARG B  1 93  ? 90.696  21.322  33.060  1.00   56.87  ? 93  ARG B CB  1 
ATOM   3649  C CG  . ARG B  1 93  ? 91.733  22.271  32.570  1.00   60.73  ? 93  ARG B CG  1 
ATOM   3650  C CD  . ARG B  1 93  ? 91.920  23.429  33.490  1.00   67.90  ? 93  ARG B CD  1 
ATOM   3651  N NE  . ARG B  1 93  ? 92.905  24.333  32.912  1.00   73.62  ? 93  ARG B NE  1 
ATOM   3652  C CZ  . ARG B  1 93  ? 92.592  25.419  32.211  1.00   75.24  ? 93  ARG B CZ  1 
ATOM   3653  N NH1 . ARG B  1 93  ? 91.319  25.709  31.965  1.00   69.78  ? 93  ARG B NH1 1 
ATOM   3654  N NH2 . ARG B  1 93  ? 93.554  26.175  31.697  1.00   79.89  ? 93  ARG B NH2 1 
ATOM   3655  N N   . PRO B  1 94  ? 88.242  21.875  31.231  1.00   43.08  ? 94  PRO B N   1 
ATOM   3656  C CA  . PRO B  1 94  ? 87.562  22.831  30.337  1.00   35.80  ? 94  PRO B CA  1 
ATOM   3657  C C   . PRO B  1 94  ? 88.454  23.998  29.936  1.00   35.82  ? 94  PRO B C   1 
ATOM   3658  O O   . PRO B  1 94  ? 88.993  24.666  30.816  1.00   38.36  ? 94  PRO B O   1 
ATOM   3659  C CB  . PRO B  1 94  ? 86.395  23.329  31.188  1.00   36.18  ? 94  PRO B CB  1 
ATOM   3660  C CG  . PRO B  1 94  ? 86.103  22.186  32.091  1.00   38.30  ? 94  PRO B CG  1 
ATOM   3661  C CD  . PRO B  1 94  ? 87.427  21.597  32.432  1.00   41.99  ? 94  PRO B CD  1 
ATOM   3662  N N   . GLY B  1 95  ? 88.603  24.243  28.641  1.00   33.40  ? 95  GLY B N   1 
ATOM   3663  C CA  . GLY B  1 95  ? 89.448  25.324  28.167  1.00   35.86  ? 95  GLY B CA  1 
ATOM   3664  C C   . GLY B  1 95  ? 90.872  24.909  27.843  1.00   36.63  ? 95  GLY B C   1 
ATOM   3665  O O   . GLY B  1 95  ? 91.635  25.671  27.247  1.00   38.79  ? 95  GLY B O   1 
ATOM   3666  N N   . CYS B  1 96  ? 91.233  23.692  28.235  1.00   39.18  ? 96  CYS B N   1 
ATOM   3667  C CA  . CYS B  1 96  ? 92.589  23.197  28.038  1.00   41.02  ? 96  CYS B CA  1 
ATOM   3668  C C   . CYS B  1 96  ? 92.631  21.756  27.532  1.00   40.19  ? 96  CYS B C   1 
ATOM   3669  O O   . CYS B  1 96  ? 92.591  20.816  28.327  1.00   40.01  ? 96  CYS B O   1 
ATOM   3670  C CB  . CYS B  1 96  ? 93.365  23.316  29.349  1.00   43.67  ? 96  CYS B CB  1 
ATOM   3671  S SG  . CYS B  1 96  ? 95.059  22.684  29.335  1.00   82.11  ? 96  CYS B SG  1 
ATOM   3672  N N   . HIS B  1 97  ? 92.694  21.592  26.211  1.00   36.02  ? 97  HIS B N   1 
ATOM   3673  C CA  . HIS B  1 97  ? 92.946  20.292  25.606  1.00   41.61  ? 97  HIS B CA  1 
ATOM   3674  C C   . HIS B  1 97  ? 93.873  20.442  24.398  1.00   41.64  ? 97  HIS B C   1 
ATOM   3675  O O   . HIS B  1 97  ? 94.189  21.552  23.958  1.00   37.63  ? 97  HIS B O   1 
ATOM   3676  C CB  . HIS B  1 97  ? 91.646  19.601  25.168  1.00   38.46  ? 97  HIS B CB  1 
ATOM   3677  C CG  . HIS B  1 97  ? 90.557  19.626  26.196  1.00   36.13  ? 97  HIS B CG  1 
ATOM   3678  N ND1 . HIS B  1 97  ? 89.681  20.681  26.321  1.00   33.75  ? 97  HIS B ND1 1 
ATOM   3679  C CD2 . HIS B  1 97  ? 90.210  18.736  27.156  1.00   38.02  ? 97  HIS B CD2 1 
ATOM   3680  C CE1 . HIS B  1 97  ? 88.834  20.437  27.306  1.00   32.34  ? 97  HIS B CE1 1 
ATOM   3681  N NE2 . HIS B  1 97  ? 89.136  19.265  27.833  1.00   36.88  ? 97  HIS B NE2 1 
ATOM   3682  N N   . ASN B  1 98  ? 94.314  19.303  23.874  1.00   46.07  ? 98  ASN B N   1 
ATOM   3683  C CA  . ASN B  1 98  ? 94.986  19.251  22.581  1.00   50.50  ? 98  ASN B CA  1 
ATOM   3684  C C   . ASN B  1 98  ? 93.988  18.626  21.602  1.00   45.38  ? 98  ASN B C   1 
ATOM   3685  O O   . ASN B  1 98  ? 93.023  17.974  22.022  1.00   38.72  ? 98  ASN B O   1 
ATOM   3686  C CB  . ASN B  1 98  ? 96.275  18.447  22.660  1.00   61.06  ? 98  ASN B CB  1 
ATOM   3687  C CG  . ASN B  1 98  ? 97.381  19.199  23.350  1.00   70.17  ? 98  ASN B CG  1 
ATOM   3688  O OD1 . ASN B  1 98  ? 97.415  20.417  23.322  1.00   62.64  ? 98  ASN B OD1 1 
ATOM   3689  N ND2 . ASN B  1 98  ? 98.286  18.471  24.003  1.00   88.67  ? 98  ASN B ND2 1 
ATOM   3690  N N   . ASN B  1 99  ? 94.188  18.854  20.313  1.00   47.47  ? 99  ASN B N   1 
ATOM   3691  C CA  . ASN B  1 99  ? 93.243  18.371  19.312  1.00   50.39  ? 99  ASN B CA  1 
ATOM   3692  C C   . ASN B  1 99  ? 91.813  18.934  19.451  1.00   43.24  ? 99  ASN B C   1 
ATOM   3693  O O   . ASN B  1 99  ? 90.848  18.275  19.065  1.00   40.18  ? 99  ASN B O   1 
ATOM   3694  C CB  . ASN B  1 99  ? 93.170  16.834  19.366  1.00   62.46  ? 99  ASN B CB  1 
ATOM   3695  C CG  . ASN B  1 99  ? 92.506  16.233  18.139  1.00   72.44  ? 99  ASN B CG  1 
ATOM   3696  O OD1 . ASN B  1 99  ? 92.598  16.795  17.051  1.00   76.47  ? 99  ASN B OD1 1 
ATOM   3697  N ND2 . ASN B  1 99  ? 91.770  15.124  18.324  1.00   75.05  ? 99  ASN B ND2 1 
ATOM   3698  N N   . THR B  1 100 ? 91.681  20.160  19.963  1.00   38.64  ? 100 THR B N   1 
ATOM   3699  C CA  . THR B  1 100 ? 90.409  20.865  19.981  1.00   32.44  ? 100 THR B CA  1 
ATOM   3700  C C   . THR B  1 100 ? 90.502  21.980  18.945  1.00   28.84  ? 100 THR B C   1 
ATOM   3701  O O   . THR B  1 100 ? 91.419  21.960  18.130  1.00   26.88  ? 100 THR B O   1 
ATOM   3702  C CB  . THR B  1 100 ? 90.096  21.417  21.370  1.00   32.11  ? 100 THR B CB  1 
ATOM   3703  O OG1 . THR B  1 100 ? 91.275  22.009  21.911  1.00   31.11  ? 100 THR B OG1 1 
ATOM   3704  C CG2 . THR B  1 100 ? 89.657  20.294  22.305  1.00   30.75  ? 100 THR B CG2 1 
ATOM   3705  N N   . CYS B  1 101 ? 89.570  22.938  18.930  1.00   32.03  ? 101 CYS B N   1 
ATOM   3706  C CA  . CYS B  1 101 ? 89.731  24.057  17.989  1.00   31.33  ? 101 CYS B CA  1 
ATOM   3707  C C   . CYS B  1 101 ? 89.730  25.423  18.649  1.00   27.56  ? 101 CYS B C   1 
ATOM   3708  O O   . CYS B  1 101 ? 89.101  25.655  19.670  1.00   27.31  ? 101 CYS B O   1 
ATOM   3709  C CB  A CYS B  1 101 ? 88.685  24.007  16.867  0.50   31.75  ? 101 CYS B CB  1 
ATOM   3710  C CB  B CYS B  1 101 ? 88.626  24.032  16.933  0.50   31.67  ? 101 CYS B CB  1 
ATOM   3711  S SG  A CYS B  1 101 ? 87.028  23.575  17.324  0.50   32.07  ? 101 CYS B SG  1 
ATOM   3712  S SG  B CYS B  1 101 ? 87.759  22.481  16.809  0.50   28.15  ? 101 CYS B SG  1 
ATOM   3713  N N   . GLY B  1 102 ? 90.470  26.326  18.033  1.00   29.25  ? 102 GLY B N   1 
ATOM   3714  C CA  . GLY B  1 102 ? 90.666  27.641  18.590  1.00   31.11  ? 102 GLY B CA  1 
ATOM   3715  C C   . GLY B  1 102 ? 89.727  28.680  18.023  1.00   29.47  ? 102 GLY B C   1 
ATOM   3716  O O   . GLY B  1 102 ? 89.388  28.708  16.855  1.00   28.01  ? 102 GLY B O   1 
ATOM   3717  N N   . LEU B  1 103 ? 89.322  29.561  18.897  1.00   29.83  ? 103 LEU B N   1 
ATOM   3718  C CA  . LEU B  1 103 ? 88.396  30.585  18.559  1.00   32.88  ? 103 LEU B CA  1 
ATOM   3719  C C   . LEU B  1 103 ? 88.887  31.871  19.187  1.00   30.98  ? 103 LEU B C   1 
ATOM   3720  O O   . LEU B  1 103 ? 89.158  31.923  20.384  1.00   29.52  ? 103 LEU B O   1 
ATOM   3721  C CB  . LEU B  1 103 ? 87.010  30.199  19.063  1.00   37.55  ? 103 LEU B CB  1 
ATOM   3722  C CG  . LEU B  1 103 ? 85.824  30.970  18.526  1.00   41.99  ? 103 LEU B CG  1 
ATOM   3723  C CD1 . LEU B  1 103 ? 85.863  31.007  17.017  1.00   46.56  ? 103 LEU B CD1 1 
ATOM   3724  C CD2 . LEU B  1 103 ? 84.583  30.283  19.011  1.00   41.22  ? 103 LEU B CD2 1 
ATOM   3725  N N   . LEU B  1 104 ? 89.005  32.912  18.381  1.00   30.11  ? 104 LEU B N   1 
ATOM   3726  C CA  . LEU B  1 104 ? 89.441  34.189  18.893  1.00   28.68  ? 104 LEU B CA  1 
ATOM   3727  C C   . LEU B  1 104 ? 88.305  34.989  19.549  1.00   28.31  ? 104 LEU B C   1 
ATOM   3728  O O   . LEU B  1 104 ? 87.307  35.288  18.902  1.00   29.43  ? 104 LEU B O   1 
ATOM   3729  C CB  . LEU B  1 104 ? 90.028  34.996  17.762  1.00   32.11  ? 104 LEU B CB  1 
ATOM   3730  C CG  . LEU B  1 104 ? 90.983  36.076  18.224  1.00   41.78  ? 104 LEU B CG  1 
ATOM   3731  C CD1 . LEU B  1 104 ? 92.299  35.472  18.770  1.00   44.54  ? 104 LEU B CD1 1 
ATOM   3732  C CD2 . LEU B  1 104 ? 91.196  37.091  17.126  1.00   46.35  ? 104 LEU B CD2 1 
ATOM   3733  N N   . SER B  1 105 ? 88.464  35.322  20.833  1.00   30.22  ? 105 SER B N   1 
ATOM   3734  C CA  . SER B  1 105 ? 87.494  36.123  21.583  1.00   27.23  ? 105 SER B CA  1 
ATOM   3735  C C   . SER B  1 105 ? 88.036  37.505  21.881  1.00   29.34  ? 105 SER B C   1 
ATOM   3736  O O   . SER B  1 105 ? 89.200  37.634  22.219  1.00   32.13  ? 105 SER B O   1 
ATOM   3737  C CB  . SER B  1 105 ? 87.156  35.451  22.902  1.00   27.35  ? 105 SER B CB  1 
ATOM   3738  O OG  . SER B  1 105 ? 86.637  34.163  22.687  1.00   31.84  ? 105 SER B OG  1 
ATOM   3739  N N   . SER B  1 106 ? 87.179  38.529  21.857  1.00   32.96  ? 106 SER B N   1 
ATOM   3740  C CA  . SER B  1 106 ? 87.623  39.906  22.089  1.00   33.58  ? 106 SER B CA  1 
ATOM   3741  C C   . SER B  1 106 ? 86.919  40.572  23.270  1.00   33.46  ? 106 SER B C   1 
ATOM   3742  O O   . SER B  1 106 ? 85.721  40.414  23.442  1.00   33.22  ? 106 SER B O   1 
ATOM   3743  C CB  A SER B  1 106 ? 87.394  40.756  20.837  0.50   36.24  ? 106 SER B CB  1 
ATOM   3744  C CB  B SER B  1 106 ? 87.426  40.743  20.829  0.50   36.28  ? 106 SER B CB  1 
ATOM   3745  O OG  A SER B  1 106 ? 88.180  40.325  19.738  0.50   38.07  ? 106 SER B OG  1 
ATOM   3746  O OG  B SER B  1 106 ? 86.316  41.606  20.955  0.50   38.68  ? 106 SER B OG  1 
ATOM   3747  N N   . ASN B  1 107 ? 87.681  41.283  24.097  1.00   27.15  ? 107 ASN B N   1 
ATOM   3748  C CA  . ASN B  1 107 ? 87.119  42.185  25.086  1.00   26.18  ? 107 ASN B CA  1 
ATOM   3749  C C   . ASN B  1 107 ? 86.846  43.476  24.339  1.00   29.64  ? 107 ASN B C   1 
ATOM   3750  O O   . ASN B  1 107 ? 87.788  44.111  23.888  1.00   27.78  ? 107 ASN B O   1 
ATOM   3751  C CB  . ASN B  1 107 ? 88.087  42.395  26.244  1.00   27.90  ? 107 ASN B CB  1 
ATOM   3752  C CG  . ASN B  1 107 ? 87.528  43.308  27.342  1.00   32.48  ? 107 ASN B CG  1 
ATOM   3753  O OD1 . ASN B  1 107 ? 86.797  44.238  27.082  1.00   29.22  ? 107 ASN B OD1 1 
ATOM   3754  N ND2 . ASN B  1 107 ? 87.925  43.056  28.567  1.00   29.49  ? 107 ASN B ND2 1 
ATOM   3755  N N   . PRO B  1 108 ? 85.554  43.833  24.139  1.00   29.82  ? 108 PRO B N   1 
ATOM   3756  C CA  . PRO B  1 108 ? 85.135  44.956  23.287  1.00   29.84  ? 108 PRO B CA  1 
ATOM   3757  C C   . PRO B  1 108 ? 85.397  46.324  23.930  1.00   34.31  ? 108 PRO B C   1 
ATOM   3758  O O   . PRO B  1 108 ? 85.397  47.361  23.258  1.00   35.66  ? 108 PRO B O   1 
ATOM   3759  C CB  . PRO B  1 108 ? 83.643  44.716  23.109  1.00   30.73  ? 108 PRO B CB  1 
ATOM   3760  C CG  . PRO B  1 108 ? 83.231  44.008  24.337  1.00   28.93  ? 108 PRO B CG  1 
ATOM   3761  C CD  . PRO B  1 108 ? 84.395  43.122  24.703  1.00   28.46  ? 108 PRO B CD  1 
ATOM   3762  N N   . VAL B  1 109 ? 85.627  46.302  25.237  1.00   32.31  ? 109 VAL B N   1 
ATOM   3763  C CA  . VAL B  1 109 ? 85.931  47.490  25.997  1.00   32.06  ? 109 VAL B CA  1 
ATOM   3764  C C   . VAL B  1 109 ? 87.403  47.811  25.889  1.00   34.14  ? 109 VAL B C   1 
ATOM   3765  O O   . VAL B  1 109 ? 87.779  48.944  25.637  1.00   37.77  ? 109 VAL B O   1 
ATOM   3766  C CB  . VAL B  1 109 ? 85.542  47.303  27.461  1.00   34.71  ? 109 VAL B CB  1 
ATOM   3767  C CG1 . VAL B  1 109 ? 86.043  48.477  28.306  1.00   38.66  ? 109 VAL B CG1 1 
ATOM   3768  C CG2 . VAL B  1 109 ? 84.025  47.126  27.581  1.00   30.65  ? 109 VAL B CG2 1 
ATOM   3769  N N   . THR B  1 110 ? 88.250  46.816  26.121  1.00   35.16  ? 110 THR B N   1 
ATOM   3770  C CA  . THR B  1 110 ? 89.682  47.031  26.065  1.00   35.27  ? 110 THR B CA  1 
ATOM   3771  C C   . THR B  1 110 ? 90.213  46.771  24.670  1.00   38.56  ? 110 THR B C   1 
ATOM   3772  O O   . THR B  1 110 ? 91.357  47.113  24.386  1.00   40.36  ? 110 THR B O   1 
ATOM   3773  C CB  . THR B  1 110 ? 90.438  46.136  27.049  1.00   35.39  ? 110 THR B CB  1 
ATOM   3774  O OG1 . THR B  1 110 ? 90.274  44.769  26.649  1.00   35.02  ? 110 THR B OG1 1 
ATOM   3775  C CG2 . THR B  1 110 ? 89.903  46.318  28.418  1.00   34.32  ? 110 THR B CG2 1 
ATOM   3776  N N   . GLN B  1 111 ? 89.401  46.144  23.822  1.00   37.96  ? 111 GLN B N   1 
ATOM   3777  C CA  . GLN B  1 111 ? 89.811  45.773  22.472  1.00   42.97  ? 111 GLN B CA  1 
ATOM   3778  C C   . GLN B  1 111 ? 90.901  44.679  22.463  1.00   45.50  ? 111 GLN B C   1 
ATOM   3779  O O   . GLN B  1 111 ? 91.490  44.405  21.418  1.00   44.54  ? 111 GLN B O   1 
ATOM   3780  C CB  . GLN B  1 111 ? 90.292  47.021  21.714  1.00   48.71  ? 111 GLN B CB  1 
ATOM   3781  C CG  . GLN B  1 111 ? 89.224  48.065  21.368  1.00   55.73  ? 111 GLN B CG  1 
ATOM   3782  C CD  . GLN B  1 111 ? 88.221  47.563  20.371  1.00   67.20  ? 111 GLN B CD  1 
ATOM   3783  O OE1 . GLN B  1 111 ? 87.093  47.198  20.716  1.00   69.03  ? 111 GLN B OE1 1 
ATOM   3784  N NE2 . GLN B  1 111 ? 88.645  47.478  19.127  1.00   73.11  ? 111 GLN B NE2 1 
ATOM   3785  N N   . GLU B  1 112 ? 91.174  44.080  23.631  1.00   45.49  ? 112 GLU B N   1 
ATOM   3786  C CA  . GLU B  1 112 ? 92.038  42.890  23.766  1.00   43.15  ? 112 GLU B CA  1 
ATOM   3787  C C   . GLU B  1 112 ? 91.417  41.674  23.108  1.00   34.88  ? 112 GLU B C   1 
ATOM   3788  O O   . GLU B  1 112 ? 90.215  41.517  23.124  1.00   31.50  ? 112 GLU B O   1 
ATOM   3789  C CB  . GLU B  1 112 ? 92.255  42.524  25.235  1.00   47.39  ? 112 GLU B CB  1 
ATOM   3790  C CG  . GLU B  1 112 ? 93.173  43.387  26.068  1.00   52.89  ? 112 GLU B CG  1 
ATOM   3791  C CD  . GLU B  1 112 ? 92.951  43.147  27.566  1.00   56.88  ? 112 GLU B CD  1 
ATOM   3792  O OE1 . GLU B  1 112 ? 91.770  42.944  27.981  1.00   53.18  ? 112 GLU B OE1 1 
ATOM   3793  O OE2 . GLU B  1 112 ? 93.959  43.115  28.315  1.00   61.20  1 112 GLU B OE2 1 
ATOM   3794  N N   . SER B  1 113 ? 92.239  40.787  22.570  1.00   31.21  ? 113 SER B N   1 
ATOM   3795  C CA  . SER B  1 113 ? 91.720  39.503  22.148  1.00   38.84  ? 113 SER B CA  1 
ATOM   3796  C C   . SER B  1 113 ? 92.634  38.375  22.604  1.00   34.73  ? 113 SER B C   1 
ATOM   3797  O O   . SER B  1 113 ? 93.780  38.594  22.965  1.00   33.70  ? 113 SER B O   1 
ATOM   3798  C CB  . SER B  1 113 ? 91.527  39.457  20.639  1.00   38.13  ? 113 SER B CB  1 
ATOM   3799  O OG  . SER B  1 113 ? 92.772  39.544  20.005  1.00   42.51  ? 113 SER B OG  1 
ATOM   3800  N N   . GLY B  1 114 ? 92.094  37.169  22.633  1.00   31.74  ? 114 GLY B N   1 
ATOM   3801  C CA  . GLY B  1 114 ? 92.861  36.010  23.041  1.00   34.20  ? 114 GLY B CA  1 
ATOM   3802  C C   . GLY B  1 114 ? 92.317  34.748  22.403  1.00   31.96  ? 114 GLY B C   1 
ATOM   3803  O O   . GLY B  1 114 ? 91.138  34.689  22.095  1.00   32.34  ? 114 GLY B O   1 
ATOM   3804  N N   . LEU B  1 115 ? 93.147  33.727  22.233  1.00   33.96  ? 115 LEU B N   1 
ATOM   3805  C CA  . LEU B  1 115 ? 92.670  32.488  21.622  1.00   36.40  ? 115 LEU B CA  1 
ATOM   3806  C C   . LEU B  1 115 ? 92.010  31.572  22.654  1.00   37.01  ? 115 LEU B C   1 
ATOM   3807  O O   . LEU B  1 115 ? 92.661  31.105  23.582  1.00   40.10  ? 115 LEU B O   1 
ATOM   3808  C CB  . LEU B  1 115 ? 93.816  31.751  20.919  1.00   36.35  ? 115 LEU B CB  1 
ATOM   3809  C CG  . LEU B  1 115 ? 93.364  30.599  20.022  1.00   34.55  ? 115 LEU B CG  1 
ATOM   3810  C CD1 . LEU B  1 115 ? 92.789  31.114  18.714  1.00   33.54  ? 115 LEU B CD1 1 
ATOM   3811  C CD2 . LEU B  1 115 ? 94.544  29.715  19.770  1.00   37.12  ? 115 LEU B CD2 1 
ATOM   3812  N N   . GLY B  1 116 ? 90.717  31.329  22.483  1.00   33.28  ? 116 GLY B N   1 
ATOM   3813  C CA  . GLY B  1 116 ? 89.989  30.464  23.383  1.00   31.95  ? 116 GLY B CA  1 
ATOM   3814  C C   . GLY B  1 116 ? 89.759  29.129  22.728  1.00   31.38  ? 116 GLY B C   1 
ATOM   3815  O O   . GLY B  1 116 ? 90.156  28.902  21.587  1.00   30.55  ? 116 GLY B O   1 
ATOM   3816  N N   . GLU B  1 117 ? 89.125  28.236  23.468  1.00   31.88  ? 117 GLU B N   1 
ATOM   3817  C CA  . GLU B  1 117 ? 88.833  26.903  22.997  1.00   26.58  ? 117 GLU B CA  1 
ATOM   3818  C C   . GLU B  1 117 ? 87.335  26.773  22.828  1.00   25.88  ? 117 GLU B C   1 
ATOM   3819  O O   . GLU B  1 117 ? 86.571  27.161  23.715  1.00   26.18  ? 117 GLU B O   1 
ATOM   3820  C CB  . GLU B  1 117 ? 89.352  25.883  23.998  1.00   28.00  ? 117 GLU B CB  1 
ATOM   3821  C CG  . GLU B  1 117 ? 89.320  24.446  23.545  1.00   28.65  ? 117 GLU B CG  1 
ATOM   3822  C CD  . GLU B  1 117 ? 89.653  23.477  24.656  1.00   30.12  ? 117 GLU B CD  1 
ATOM   3823  O OE1 . GLU B  1 117 ? 89.006  23.561  25.708  1.00   36.54  ? 117 GLU B OE1 1 
ATOM   3824  O OE2 . GLU B  1 117 ? 90.559  22.628  24.496  1.00   36.73  1 117 GLU B OE2 1 
ATOM   3825  N N   . LEU B  1 118 ? 86.896  26.231  21.697  1.00   26.06  ? 118 LEU B N   1 
ATOM   3826  C CA  . LEU B  1 118 ? 85.459  26.005  21.495  1.00   26.12  ? 118 LEU B CA  1 
ATOM   3827  C C   . LEU B  1 118 ? 84.895  25.012  22.537  1.00   27.11  ? 118 LEU B C   1 
ATOM   3828  O O   . LEU B  1 118 ? 85.509  23.986  22.860  1.00   28.76  ? 118 LEU B O   1 
ATOM   3829  C CB  . LEU B  1 118 ? 85.176  25.509  20.071  1.00   26.06  ? 118 LEU B CB  1 
ATOM   3830  C CG  . LEU B  1 118 ? 83.705  25.389  19.691  1.00   25.98  ? 118 LEU B CG  1 
ATOM   3831  C CD1 . LEU B  1 118 ? 83.050  26.748  19.652  1.00   24.19  ? 118 LEU B CD1 1 
ATOM   3832  C CD2 . LEU B  1 118 ? 83.512  24.640  18.400  1.00   23.09  ? 118 LEU B CD2 1 
ATOM   3833  N N   . ALA B  1 119 ? 83.727  25.333  23.070  1.00   23.03  ? 119 ALA B N   1 
ATOM   3834  C CA  . ALA B  1 119 ? 83.136  24.525  24.108  1.00   23.52  ? 119 ALA B CA  1 
ATOM   3835  C C   . ALA B  1 119 ? 81.672  24.273  23.801  1.00   26.97  ? 119 ALA B C   1 
ATOM   3836  O O   . ALA B  1 119 ? 81.062  24.990  23.026  1.00   25.93  ? 119 ALA B O   1 
ATOM   3837  C CB  . ALA B  1 119 ? 83.287  25.191  25.441  1.00   23.73  ? 119 ALA B CB  1 
ATOM   3838  N N   . GLN B  1 120 ? 81.122  23.256  24.445  1.00   27.56  ? 120 GLN B N   1 
ATOM   3839  C CA  . GLN B  1 120 ? 79.747  22.879  24.281  1.00   28.32  ? 120 GLN B CA  1 
ATOM   3840  C C   . GLN B  1 120 ? 79.156  22.505  25.636  1.00   27.53  ? 120 GLN B C   1 
ATOM   3841  O O   . GLN B  1 120 ? 79.775  21.757  26.352  1.00   30.54  ? 120 GLN B O   1 
ATOM   3842  C CB  . GLN B  1 120 ? 79.690  21.717  23.303  1.00   32.93  ? 120 GLN B CB  1 
ATOM   3843  C CG  . GLN B  1 120 ? 78.344  21.197  23.033  1.00   37.67  ? 120 GLN B CG  1 
ATOM   3844  C CD  . GLN B  1 120 ? 78.376  19.998  22.147  1.00   41.54  ? 120 GLN B CD  1 
ATOM   3845  O OE1 . GLN B  1 120 ? 78.654  20.108  20.955  1.00   39.79  ? 120 GLN B OE1 1 
ATOM   3846  N NE2 . GLN B  1 120 ? 78.073  18.837  22.709  1.00   46.20  ? 120 GLN B NE2 1 
ATOM   3847  N N   . ASP B  1 121 ? 77.998  23.049  26.007  1.00   26.87  ? 121 ASP B N   1 
ATOM   3848  C CA  . ASP B  1 121 ? 77.334  22.719  27.284  1.00   29.03  ? 121 ASP B CA  1 
ATOM   3849  C C   . ASP B  1 121 ? 75.888  23.205  27.249  1.00   28.58  ? 121 ASP B C   1 
ATOM   3850  O O   . ASP B  1 121 ? 75.452  23.792  26.272  1.00   26.46  ? 121 ASP B O   1 
ATOM   3851  C CB  . ASP B  1 121 ? 78.077  23.352  28.473  1.00   28.71  ? 121 ASP B CB  1 
ATOM   3852  C CG  . ASP B  1 121 ? 77.929  22.562  29.772  1.00   31.05  ? 121 ASP B CG  1 
ATOM   3853  O OD1 . ASP B  1 121 ? 76.918  21.867  29.986  1.00   32.22  ? 121 ASP B OD1 1 
ATOM   3854  O OD2 . ASP B  1 121 ? 78.855  22.631  30.602  1.00   33.80  1 121 ASP B OD2 1 
ATOM   3855  N N   . VAL B  1 122 ? 75.160  22.999  28.336  1.00   29.59  ? 122 VAL B N   1 
ATOM   3856  C CA  . VAL B  1 122 ? 73.791  23.493  28.440  1.00   28.37  ? 122 VAL B CA  1 
ATOM   3857  C C   . VAL B  1 122 ? 73.728  25.000  28.627  1.00   30.44  ? 122 VAL B C   1 
ATOM   3858  O O   . VAL B  1 122 ? 74.450  25.570  29.438  1.00   30.75  ? 122 VAL B O   1 
ATOM   3859  C CB  . VAL B  1 122 ? 73.038  22.841  29.623  1.00   27.25  ? 122 VAL B CB  1 
ATOM   3860  C CG1 . VAL B  1 122 ? 71.690  23.466  29.803  1.00   26.67  ? 122 VAL B CG1 1 
ATOM   3861  C CG2 . VAL B  1 122 ? 72.864  21.371  29.409  1.00   29.09  ? 122 VAL B CG2 1 
ATOM   3862  N N   . LEU B  1 123 ? 72.871  25.651  27.852  1.00   30.53  ? 123 LEU B N   1 
ATOM   3863  C CA  . LEU B  1 123 ? 72.443  27.011  28.163  1.00   27.74  ? 123 LEU B CA  1 
ATOM   3864  C C   . LEU B  1 123 ? 70.933  26.957  28.347  1.00   27.51  ? 123 LEU B C   1 
ATOM   3865  O O   . LEU B  1 123 ? 70.263  26.226  27.626  1.00   27.59  ? 123 LEU B O   1 
ATOM   3866  C CB  . LEU B  1 123 ? 72.846  27.980  27.054  1.00   25.61  ? 123 LEU B CB  1 
ATOM   3867  C CG  . LEU B  1 123 ? 72.416  29.441  27.188  1.00   28.21  ? 123 LEU B CG  1 
ATOM   3868  C CD1 . LEU B  1 123 ? 73.474  30.383  26.634  1.00   26.49  ? 123 LEU B CD1 1 
ATOM   3869  C CD2 . LEU B  1 123 ? 71.132  29.654  26.449  1.00   29.51  ? 123 LEU B CD2 1 
ATOM   3870  N N   . ALA B  1 124 ? 70.409  27.686  29.332  1.00   28.54  ? 124 ALA B N   1 
ATOM   3871  C CA  . ALA B  1 124 ? 68.959  27.787  29.567  1.00   28.40  ? 124 ALA B CA  1 
ATOM   3872  C C   . ALA B  1 124 ? 68.474  29.240  29.550  1.00   27.51  ? 124 ALA B C   1 
ATOM   3873  O O   . ALA B  1 124 ? 69.238  30.144  29.860  1.00   27.99  ? 124 ALA B O   1 
ATOM   3874  C CB  . ALA B  1 124 ? 68.580  27.123  30.890  1.00   28.78  ? 124 ALA B CB  1 
ATOM   3875  N N   . ILE B  1 125 ? 67.209  29.457  29.186  1.00   26.20  ? 125 ILE B N   1 
ATOM   3876  C CA  . ILE B  1 125 ? 66.627  30.803  29.085  1.00   26.40  ? 125 ILE B CA  1 
ATOM   3877  C C   . ILE B  1 125 ? 65.113  30.740  29.344  1.00   29.22  ? 125 ILE B C   1 
ATOM   3878  O O   . ILE B  1 125 ? 64.480  29.714  29.072  1.00   30.64  ? 125 ILE B O   1 
ATOM   3879  C CB  . ILE B  1 125 ? 66.897  31.457  27.689  1.00   26.14  ? 125 ILE B CB  1 
ATOM   3880  C CG1 . ILE B  1 125 ? 66.561  32.968  27.702  1.00   26.49  ? 125 ILE B CG1 1 
ATOM   3881  C CG2 . ILE B  1 125 ? 66.194  30.669  26.578  1.00   24.60  ? 125 ILE B CG2 1 
ATOM   3882  C CD1 . ILE B  1 125 ? 66.891  33.750  26.412  1.00   24.24  ? 125 ILE B CD1 1 
ATOM   3883  N N   . HIS B  1 126 ? 64.544  31.822  29.884  1.00   27.73  ? 126 HIS B N   1 
ATOM   3884  C CA  . HIS B  1 126 ? 63.124  31.856  30.211  1.00   29.37  ? 126 HIS B CA  1 
ATOM   3885  C C   . HIS B  1 126 ? 62.270  31.811  28.975  1.00   29.05  ? 126 HIS B C   1 
ATOM   3886  O O   . HIS B  1 126 ? 62.545  32.496  27.993  1.00   26.00  ? 126 HIS B O   1 
ATOM   3887  C CB  . HIS B  1 126 ? 62.763  33.118  31.011  1.00   25.87  ? 126 HIS B CB  1 
ATOM   3888  C CG  . HIS B  1 126 ? 63.067  33.034  32.476  1.00   31.18  ? 126 HIS B CG  1 
ATOM   3889  N ND1 . HIS B  1 126 ? 62.268  32.347  33.367  1.00   36.05  ? 126 HIS B ND1 1 
ATOM   3890  C CD2 . HIS B  1 126 ? 64.101  33.530  33.200  1.00   28.73  ? 126 HIS B CD2 1 
ATOM   3891  C CE1 . HIS B  1 126 ? 62.789  32.434  34.579  1.00   36.04  ? 126 HIS B CE1 1 
ATOM   3892  N NE2 . HIS B  1 126 ? 63.902  33.144  34.504  1.00   32.76  ? 126 HIS B NE2 1 
ATOM   3893  N N   . SER B  1 127 ? 61.220  31.007  29.049  1.00   33.37  ? 127 SER B N   1 
ATOM   3894  C CA  . SER B  1 127 ? 60.101  31.135  28.133  1.00   34.01  ? 127 SER B CA  1 
ATOM   3895  C C   . SER B  1 127 ? 59.075  32.094  28.764  1.00   34.39  ? 127 SER B C   1 
ATOM   3896  O O   . SER B  1 127 ? 59.376  32.828  29.717  1.00   31.94  ? 127 SER B O   1 
ATOM   3897  C CB  . SER B  1 127 ? 59.481  29.764  27.845  1.00   33.53  ? 127 SER B CB  1 
ATOM   3898  O OG  . SER B  1 127 ? 59.118  29.107  29.048  1.00   36.95  ? 127 SER B OG  1 
ATOM   3899  N N   . THR B  1 128 ? 57.871  32.120  28.204  1.00   38.54  ? 128 THR B N   1 
ATOM   3900  C CA  . THR B  1 128 ? 56.770  32.873  28.800  1.00   38.68  ? 128 THR B CA  1 
ATOM   3901  C C   . THR B  1 128 ? 55.543  31.990  29.090  1.00   37.99  ? 128 THR B C   1 
ATOM   3902  O O   . THR B  1 128 ? 55.321  30.949  28.466  1.00   37.01  ? 128 THR B O   1 
ATOM   3903  C CB  . THR B  1 128 ? 56.354  34.060  27.897  1.00   36.63  ? 128 THR B CB  1 
ATOM   3904  O OG1 . THR B  1 128 ? 55.803  33.579  26.666  1.00   34.12  ? 128 THR B OG1 1 
ATOM   3905  C CG2 . THR B  1 128 ? 57.555  34.903  27.583  1.00   28.72  ? 128 THR B CG2 1 
ATOM   3906  N N   . HIS B  1 129 ? 54.758  32.408  30.066  1.00   40.60  ? 129 HIS B N   1 
ATOM   3907  C CA  . HIS B  1 129 ? 53.534  31.705  30.378  1.00   44.61  ? 129 HIS B CA  1 
ATOM   3908  C C   . HIS B  1 129 ? 52.446  32.734  30.611  1.00   44.41  ? 129 HIS B C   1 
ATOM   3909  O O   . HIS B  1 129 ? 52.412  33.391  31.657  1.00   42.02  ? 129 HIS B O   1 
ATOM   3910  C CB  . HIS B  1 129 ? 53.672  30.799  31.595  1.00   50.70  ? 129 HIS B CB  1 
ATOM   3911  C CG  . HIS B  1 129 ? 52.469  29.937  31.812  1.00   57.44  ? 129 HIS B CG  1 
ATOM   3912  N ND1 . HIS B  1 129 ? 52.006  29.064  30.849  1.00   60.18  ? 129 HIS B ND1 1 
ATOM   3913  C CD2 . HIS B  1 129 ? 51.598  29.855  32.843  1.00   62.32  ? 129 HIS B CD2 1 
ATOM   3914  C CE1 . HIS B  1 129 ? 50.917  28.461  31.290  1.00   65.07  ? 129 HIS B CE1 1 
ATOM   3915  N NE2 . HIS B  1 129 ? 50.646  28.923  32.498  1.00   66.07  ? 129 HIS B NE2 1 
ATOM   3916  N N   . GLY B  1 130 ? 51.566  32.883  29.626  1.00   47.19  ? 130 GLY B N   1 
ATOM   3917  C CA  . GLY B  1 130 ? 50.582  33.947  29.657  1.00   52.50  ? 130 GLY B CA  1 
ATOM   3918  C C   . GLY B  1 130 ? 51.311  35.276  29.618  1.00   54.55  ? 130 GLY B C   1 
ATOM   3919  O O   . GLY B  1 130 ? 52.118  35.498  28.716  1.00   56.38  ? 130 GLY B O   1 
ATOM   3920  N N   . SER B  1 131 ? 51.045  36.148  30.595  1.00   51.65  ? 131 SER B N   1 
ATOM   3921  C CA  . SER B  1 131 ? 51.698  37.452  30.676  1.00   47.63  ? 131 SER B CA  1 
ATOM   3922  C C   . SER B  1 131 ? 52.959  37.484  31.545  1.00   44.38  ? 131 SER B C   1 
ATOM   3923  O O   . SER B  1 131 ? 53.584  38.528  31.671  1.00   41.51  ? 131 SER B O   1 
ATOM   3924  C CB  . SER B  1 131 ? 50.711  38.489  31.202  1.00   48.51  ? 131 SER B CB  1 
ATOM   3925  O OG  . SER B  1 131 ? 50.525  38.328  32.601  1.00   49.84  ? 131 SER B OG  1 
ATOM   3926  N N   . LYS B  1 132 ? 53.342  36.356  32.134  1.00   45.21  ? 132 LYS B N   1 
ATOM   3927  C CA  . LYS B  1 132 ? 54.505  36.340  33.021  1.00   44.03  ? 132 LYS B CA  1 
ATOM   3928  C C   . LYS B  1 132 ? 55.661  35.579  32.396  1.00   40.74  ? 132 LYS B C   1 
ATOM   3929  O O   . LYS B  1 132 ? 55.526  35.005  31.321  1.00   38.32  ? 132 LYS B O   1 
ATOM   3930  C CB  . LYS B  1 132 ? 54.155  35.742  34.391  1.00   46.88  ? 132 LYS B CB  1 
ATOM   3931  C CG  . LYS B  1 132 ? 53.134  36.552  35.204  1.00   52.16  ? 132 LYS B CG  1 
ATOM   3932  C CD  . LYS B  1 132 ? 53.360  36.456  36.732  1.00   56.48  ? 132 LYS B CD  1 
ATOM   3933  C CE  . LYS B  1 132 ? 52.201  35.730  37.483  1.00   76.57  ? 132 LYS B CE  1 
ATOM   3934  N NZ  . LYS B  1 132 ? 51.372  36.499  38.492  1.00   77.41  ? 132 LYS B NZ  1 
ATOM   3935  N N   . LEU B  1 133 ? 56.813  35.606  33.050  1.00   42.11  ? 133 LEU B N   1 
ATOM   3936  C CA  . LEU B  1 133 ? 57.893  34.700  32.669  1.00   42.81  ? 133 LEU B CA  1 
ATOM   3937  C C   . LEU B  1 133 ? 57.497  33.248  32.924  1.00   46.21  ? 133 LEU B C   1 
ATOM   3938  O O   . LEU B  1 133 ? 56.906  32.919  33.958  1.00   47.87  ? 133 LEU B O   1 
ATOM   3939  C CB  . LEU B  1 133 ? 59.171  35.026  33.433  1.00   40.62  ? 133 LEU B CB  1 
ATOM   3940  C CG  . LEU B  1 133 ? 59.861  36.327  33.067  1.00   36.97  ? 133 LEU B CG  1 
ATOM   3941  C CD1 . LEU B  1 133 ? 61.109  36.493  33.912  1.00   36.47  ? 133 LEU B CD1 1 
ATOM   3942  C CD2 . LEU B  1 133 ? 60.201  36.350  31.591  1.00   34.98  ? 133 LEU B CD2 1 
ATOM   3943  N N   . GLY B  1 134 ? 57.849  32.376  31.990  1.00   44.41  ? 134 GLY B N   1 
ATOM   3944  C CA  . GLY B  1 134 ? 57.510  30.982  32.116  1.00   43.92  ? 134 GLY B CA  1 
ATOM   3945  C C   . GLY B  1 134 ? 58.758  30.230  32.469  1.00   43.44  ? 134 GLY B C   1 
ATOM   3946  O O   . GLY B  1 134 ? 59.779  30.834  32.786  1.00   40.44  ? 134 GLY B O   1 
ATOM   3947  N N   . PRO B  1 135 ? 58.691  28.904  32.392  1.00   44.42  ? 135 PRO B N   1 
ATOM   3948  C CA  . PRO B  1 135 ? 59.798  28.016  32.746  1.00   42.77  ? 135 PRO B CA  1 
ATOM   3949  C C   . PRO B  1 135 ? 61.020  28.180  31.848  1.00   37.87  ? 135 PRO B C   1 
ATOM   3950  O O   . PRO B  1 135 ? 60.928  28.594  30.699  1.00   36.53  ? 135 PRO B O   1 
ATOM   3951  C CB  . PRO B  1 135 ? 59.193  26.625  32.575  1.00   44.42  ? 135 PRO B CB  1 
ATOM   3952  C CG  . PRO B  1 135 ? 58.050  26.821  31.664  1.00   45.64  ? 135 PRO B CG  1 
ATOM   3953  C CD  . PRO B  1 135 ? 57.506  28.166  31.942  1.00   45.35  ? 135 PRO B CD  1 
ATOM   3954  N N   . MET B  1 136 ? 62.178  27.863  32.395  1.00   35.92  ? 136 MET B N   1 
ATOM   3955  C CA  . MET B  1 136 ? 63.393  27.833  31.607  1.00   34.90  ? 136 MET B CA  1 
ATOM   3956  C C   . MET B  1 136 ? 63.302  26.767  30.559  1.00   32.44  ? 136 MET B C   1 
ATOM   3957  O O   . MET B  1 136 ? 62.747  25.711  30.801  1.00   35.41  ? 136 MET B O   1 
ATOM   3958  C CB  . MET B  1 136 ? 64.618  27.559  32.471  1.00   37.59  ? 136 MET B CB  1 
ATOM   3959  C CG  . MET B  1 136 ? 64.781  28.444  33.676  1.00   40.25  ? 136 MET B CG  1 
ATOM   3960  S SD  . MET B  1 136 ? 65.487  30.056  33.287  1.00   46.39  ? 136 MET B SD  1 
ATOM   3961  C CE  . MET B  1 136 ? 67.165  29.668  32.912  1.00   47.48  ? 136 MET B CE  1 
ATOM   3962  N N   . VAL B  1 137 ? 63.823  27.048  29.382  1.00   28.69  ? 137 VAL B N   1 
ATOM   3963  C CA  . VAL B  1 137 ? 63.978  26.005  28.387  1.00   29.65  ? 137 VAL B CA  1 
ATOM   3964  C C   . VAL B  1 137 ? 65.467  25.889  28.009  1.00   27.94  ? 137 VAL B C   1 
ATOM   3965  O O   . VAL B  1 137 ? 66.196  26.860  28.118  1.00   27.92  ? 137 VAL B O   1 
ATOM   3966  C CB  . VAL B  1 137 ? 63.123  26.286  27.159  1.00   30.15  ? 137 VAL B CB  1 
ATOM   3967  C CG1 . VAL B  1 137 ? 61.643  26.092  27.505  1.00   32.79  ? 137 VAL B CG1 1 
ATOM   3968  C CG2 . VAL B  1 137 ? 63.384  27.680  26.641  1.00   28.26  ? 137 VAL B CG2 1 
ATOM   3969  N N   . LYS B  1 138 ? 65.926  24.718  27.586  1.00   27.65  ? 138 LYS B N   1 
ATOM   3970  C CA  . LYS B  1 138 ? 67.354  24.508  27.388  1.00   26.51  ? 138 LYS B CA  1 
ATOM   3971  C C   . LYS B  1 138 ? 67.768  24.305  25.933  1.00   27.47  ? 138 LYS B C   1 
ATOM   3972  O O   . LYS B  1 138 ? 67.033  23.702  25.168  1.00   29.19  ? 138 LYS B O   1 
ATOM   3973  C CB  . LYS B  1 138 ? 67.823  23.290  28.176  1.00   30.75  ? 138 LYS B CB  1 
ATOM   3974  C CG  . LYS B  1 138 ? 67.642  23.350  29.677  1.00   35.86  ? 138 LYS B CG  1 
ATOM   3975  C CD  . LYS B  1 138 ? 68.114  22.034  30.322  1.00   40.82  ? 138 LYS B CD  1 
ATOM   3976  C CE  . LYS B  1 138 ? 67.913  22.053  31.826  1.00   44.70  ? 138 LYS B CE  1 
ATOM   3977  N NZ  . LYS B  1 138 ? 68.449  20.830  32.459  1.00   48.81  ? 138 LYS B NZ  1 
ATOM   3978  N N   . VAL B  1 139 ? 68.962  24.799  25.590  1.00   26.95  ? 139 VAL B N   1 
ATOM   3979  C CA  . VAL B  1 139 ? 69.747  24.369  24.421  1.00   26.39  ? 139 VAL B CA  1 
ATOM   3980  C C   . VAL B  1 139 ? 70.860  23.490  24.966  1.00   28.49  ? 139 VAL B C   1 
ATOM   3981  O O   . VAL B  1 139 ? 71.816  23.992  25.525  1.00   30.60  ? 139 VAL B O   1 
ATOM   3982  C CB  . VAL B  1 139 ? 70.393  25.529  23.651  1.00   24.01  ? 139 VAL B CB  1 
ATOM   3983  C CG1 . VAL B  1 139 ? 71.151  25.005  22.415  1.00   23.45  ? 139 VAL B CG1 1 
ATOM   3984  C CG2 . VAL B  1 139 ? 69.366  26.570  23.267  1.00   23.37  ? 139 VAL B CG2 1 
ATOM   3985  N N   . PRO B  1 140 ? 70.732  22.173  24.837  1.00   29.51  ? 140 PRO B N   1 
ATOM   3986  C CA  . PRO B  1 140 ? 71.649  21.308  25.563  1.00   29.21  ? 140 PRO B CA  1 
ATOM   3987  C C   . PRO B  1 140 ? 73.069  21.335  25.038  1.00   31.87  ? 140 PRO B C   1 
ATOM   3988  O O   . PRO B  1 140 ? 74.004  21.059  25.780  1.00   33.04  ? 140 PRO B O   1 
ATOM   3989  C CB  . PRO B  1 140 ? 71.059  19.927  25.345  1.00   31.95  ? 140 PRO B CB  1 
ATOM   3990  C CG  . PRO B  1 140 ? 69.691  20.146  24.804  1.00   32.64  ? 140 PRO B CG  1 
ATOM   3991  C CD  . PRO B  1 140 ? 69.763  21.403  24.052  1.00   30.64  ? 140 PRO B CD  1 
ATOM   3992  N N   . GLN B  1 141 ? 73.236  21.634  23.761  1.00   30.99  ? 141 GLN B N   1 
ATOM   3993  C CA  . GLN B  1 141 ? 74.572  21.700  23.188  1.00   30.65  ? 141 GLN B CA  1 
ATOM   3994  C C   . GLN B  1 141 ? 74.898  23.052  22.630  1.00   29.26  ? 141 GLN B C   1 
ATOM   3995  O O   . GLN B  1 141 ? 75.217  23.176  21.451  1.00   31.72  ? 141 GLN B O   1 
ATOM   3996  C CB  . GLN B  1 141 ? 74.733  20.659  22.096  1.00   37.36  ? 141 GLN B CB  1 
ATOM   3997  C CG  . GLN B  1 141 ? 74.686  19.248  22.633  1.00   49.05  ? 141 GLN B CG  1 
ATOM   3998  C CD  . GLN B  1 141 ? 73.885  18.343  21.749  1.00   59.39  ? 141 GLN B CD  1 
ATOM   3999  O OE1 . GLN B  1 141 ? 72.727  18.637  21.429  1.00   61.85  ? 141 GLN B OE1 1 
ATOM   4000  N NE2 . GLN B  1 141 ? 74.495  17.233  21.331  1.00   64.76  ? 141 GLN B NE2 1 
ATOM   4001  N N   . PHE B  1 142 ? 74.831  24.055  23.493  1.00   27.59  ? 142 PHE B N   1 
ATOM   4002  C CA  . PHE B  1 142 ? 75.122  25.428  23.139  1.00   24.04  ? 142 PHE B CA  1 
ATOM   4003  C C   . PHE B  1 142 ? 76.617  25.600  22.898  1.00   23.23  ? 142 PHE B C   1 
ATOM   4004  O O   . PHE B  1 142 ? 77.418  25.212  23.729  1.00   25.02  ? 142 PHE B O   1 
ATOM   4005  C CB  . PHE B  1 142 ? 74.645  26.365  24.257  1.00   25.20  ? 142 PHE B CB  1 
ATOM   4006  C CG  . PHE B  1 142 ? 74.796  27.809  23.923  1.00   25.67  ? 142 PHE B CG  1 
ATOM   4007  C CD1 . PHE B  1 142 ? 73.844  28.460  23.159  1.00   23.61  ? 142 PHE B CD1 1 
ATOM   4008  C CD2 . PHE B  1 142 ? 75.910  28.511  24.338  1.00   25.72  ? 142 PHE B CD2 1 
ATOM   4009  C CE1 . PHE B  1 142 ? 73.993  29.780  22.824  1.00   22.81  ? 142 PHE B CE1 1 
ATOM   4010  C CE2 . PHE B  1 142 ? 76.072  29.827  24.003  1.00   23.46  ? 142 PHE B CE2 1 
ATOM   4011  C CZ  . PHE B  1 142 ? 75.119  30.467  23.245  1.00   23.60  ? 142 PHE B CZ  1 
ATOM   4012  N N   . LEU B  1 143 ? 76.995  26.203  21.778  1.00   21.23  ? 143 LEU B N   1 
ATOM   4013  C CA  . LEU B  1 143 ? 78.403  26.419  21.467  1.00   20.82  ? 143 LEU B CA  1 
ATOM   4014  C C   . LEU B  1 143 ? 78.926  27.766  21.926  1.00   21.26  ? 143 LEU B C   1 
ATOM   4015  O O   . LEU B  1 143 ? 78.275  28.779  21.775  1.00   24.65  ? 143 LEU B O   1 
ATOM   4016  C CB  . LEU B  1 143 ? 78.629  26.269  19.970  1.00   22.49  ? 143 LEU B CB  1 
ATOM   4017  C CG  . LEU B  1 143 ? 78.263  24.888  19.429  1.00   22.63  ? 143 LEU B CG  1 
ATOM   4018  C CD1 . LEU B  1 143 ? 78.377  24.857  17.915  1.00   22.18  ? 143 LEU B CD1 1 
ATOM   4019  C CD2 . LEU B  1 143 ? 79.159  23.863  20.063  1.00   23.08  ? 143 LEU B CD2 1 
ATOM   4020  N N   . PHE B  1 144 ? 80.109  27.769  22.518  1.00   22.42  ? 144 PHE B N   1 
ATOM   4021  C CA  . PHE B  1 144 ? 80.677  28.988  23.055  1.00   22.78  ? 144 PHE B CA  1 
ATOM   4022  C C   . PHE B  1 144 ? 82.184  28.843  23.195  1.00   22.83  ? 144 PHE B C   1 
ATOM   4023  O O   . PHE B  1 144 ? 82.727  27.802  22.883  1.00   26.62  ? 144 PHE B O   1 
ATOM   4024  C CB  . PHE B  1 144 ? 80.068  29.334  24.406  1.00   24.23  ? 144 PHE B CB  1 
ATOM   4025  C CG  . PHE B  1 144 ? 80.425  28.369  25.513  1.00   28.16  ? 144 PHE B CG  1 
ATOM   4026  C CD1 . PHE B  1 144 ? 79.712  27.186  25.691  1.00   27.66  ? 144 PHE B CD1 1 
ATOM   4027  C CD2 . PHE B  1 144 ? 81.474  28.653  26.392  1.00   28.00  ? 144 PHE B CD2 1 
ATOM   4028  C CE1 . PHE B  1 144 ? 80.034  26.304  26.731  1.00   27.07  ? 144 PHE B CE1 1 
ATOM   4029  C CE2 . PHE B  1 144 ? 81.804  27.777  27.415  1.00   29.27  ? 144 PHE B CE2 1 
ATOM   4030  C CZ  . PHE B  1 144 ? 81.083  26.602  27.584  1.00   28.90  ? 144 PHE B CZ  1 
ATOM   4031  N N   . SER B  1 145 ? 82.856  29.872  23.685  1.00   22.99  ? 145 SER B N   1 
ATOM   4032  C CA  . SER B  1 145 ? 84.291  29.813  23.832  1.00   23.91  ? 145 SER B CA  1 
ATOM   4033  C C   . SER B  1 145 ? 84.736  29.867  25.275  1.00   26.68  ? 145 SER B C   1 
ATOM   4034  O O   . SER B  1 145 ? 84.216  30.643  26.064  1.00   26.49  ? 145 SER B O   1 
ATOM   4035  C CB  . SER B  1 145 ? 84.945  30.944  23.052  1.00   26.28  ? 145 SER B CB  1 
ATOM   4036  O OG  . SER B  1 145 ? 86.330  30.974  23.299  1.00   29.00  ? 145 SER B OG  1 
ATOM   4037  N N   . CYS B  1 146 ? 85.663  28.986  25.624  1.00   27.82  ? 146 CYS B N   1 
ATOM   4038  C CA  . CYS B  1 146 ? 86.419  29.087  26.866  1.00   30.79  ? 146 CYS B CA  1 
ATOM   4039  C C   . CYS B  1 146 ? 87.621  29.959  26.617  1.00   30.29  ? 146 CYS B C   1 
ATOM   4040  O O   . CYS B  1 146 ? 88.611  29.494  26.046  1.00   32.24  ? 146 CYS B O   1 
ATOM   4041  C CB  . CYS B  1 146 ? 86.888  27.715  27.352  1.00   33.76  ? 146 CYS B CB  1 
ATOM   4042  S SG  . CYS B  1 146 ? 85.639  26.748  28.215  1.00   85.02  ? 146 CYS B SG  1 
ATOM   4043  N N   . ALA B  1 147 ? 87.540  31.208  27.057  1.00   29.14  ? 147 ALA B N   1 
ATOM   4044  C CA  . ALA B  1 147 ? 88.561  32.217  26.764  1.00   32.02  ? 147 ALA B CA  1 
ATOM   4045  C C   . ALA B  1 147 ? 89.660  32.261  27.816  1.00   35.98  ? 147 ALA B C   1 
ATOM   4046  O O   . ALA B  1 147 ? 89.439  31.848  28.957  1.00   37.88  ? 147 ALA B O   1 
ATOM   4047  C CB  . ALA B  1 147 ? 87.916  33.566  26.648  1.00   31.73  ? 147 ALA B CB  1 
ATOM   4048  N N   . PRO B  1 148 ? 90.857  32.754  27.443  1.00   36.90  ? 148 PRO B N   1 
ATOM   4049  C CA  . PRO B  1 148 ? 91.918  32.917  28.444  1.00   39.32  ? 148 PRO B CA  1 
ATOM   4050  C C   . PRO B  1 148 ? 91.515  33.910  29.531  1.00   41.45  ? 148 PRO B C   1 
ATOM   4051  O O   . PRO B  1 148 ? 90.834  34.895  29.248  1.00   38.07  ? 148 PRO B O   1 
ATOM   4052  C CB  . PRO B  1 148 ? 93.122  33.413  27.625  1.00   39.52  ? 148 PRO B CB  1 
ATOM   4053  C CG  . PRO B  1 148 ? 92.582  33.858  26.339  1.00   39.59  ? 148 PRO B CG  1 
ATOM   4054  C CD  . PRO B  1 148 ? 91.339  33.051  26.086  1.00   36.80  ? 148 PRO B CD  1 
ATOM   4055  N N   . SER B  1 149 ? 91.919  33.626  30.765  1.00   44.91  ? 149 SER B N   1 
ATOM   4056  C CA  . SER B  1 149 ? 91.506  34.389  31.938  1.00   47.55  ? 149 SER B CA  1 
ATOM   4057  C C   . SER B  1 149 ? 91.771  35.877  31.883  1.00   45.88  ? 149 SER B C   1 
ATOM   4058  O O   . SER B  1 149 ? 90.993  36.663  32.405  1.00   47.41  ? 149 SER B O   1 
ATOM   4059  C CB  . SER B  1 149 ? 92.200  33.835  33.175  1.00   56.60  ? 149 SER B CB  1 
ATOM   4060  O OG  . SER B  1 149 ? 91.854  32.483  33.386  1.00   60.75  ? 149 SER B OG  1 
ATOM   4061  N N   . PHE B  1 150 ? 92.878  36.271  31.270  1.00   45.69  ? 150 PHE B N   1 
ATOM   4062  C CA  . PHE B  1 150 ? 93.266  37.672  31.273  1.00   46.88  ? 150 PHE B CA  1 
ATOM   4063  C C   . PHE B  1 150 ? 92.231  38.548  30.584  1.00   48.03  ? 150 PHE B C   1 
ATOM   4064  O O   . PHE B  1 150 ? 92.148  39.750  30.848  1.00   50.41  ? 150 PHE B O   1 
ATOM   4065  C CB  . PHE B  1 150 ? 94.623  37.843  30.596  1.00   45.52  ? 150 PHE B CB  1 
ATOM   4066  C CG  . PHE B  1 150 ? 94.561  37.823  29.086  1.00   43.00  ? 150 PHE B CG  1 
ATOM   4067  C CD1 . PHE B  1 150 ? 94.322  38.985  28.360  1.00   41.19  ? 150 PHE B CD1 1 
ATOM   4068  C CD2 . PHE B  1 150 ? 94.764  36.643  28.392  1.00   40.08  ? 150 PHE B CD2 1 
ATOM   4069  C CE1 . PHE B  1 150 ? 94.260  38.966  26.977  1.00   38.58  ? 150 PHE B CE1 1 
ATOM   4070  C CE2 . PHE B  1 150 ? 94.711  36.625  27.008  1.00   39.23  ? 150 PHE B CE2 1 
ATOM   4071  C CZ  . PHE B  1 150 ? 94.453  37.788  26.302  1.00   37.32  ? 150 PHE B CZ  1 
ATOM   4072  N N   . LEU B  1 151 ? 91.443  37.941  29.702  1.00   43.90  ? 151 LEU B N   1 
ATOM   4073  C CA  . LEU B  1 151 ? 90.627  38.711  28.772  1.00   39.42  ? 151 LEU B CA  1 
ATOM   4074  C C   . LEU B  1 151 ? 89.528  39.434  29.500  1.00   37.87  ? 151 LEU B C   1 
ATOM   4075  O O   . LEU B  1 151 ? 89.138  40.506  29.077  1.00   38.90  ? 151 LEU B O   1 
ATOM   4076  C CB  . LEU B  1 151 ? 90.049  37.806  27.662  1.00   35.79  ? 151 LEU B CB  1 
ATOM   4077  C CG  . LEU B  1 151 ? 89.512  38.467  26.383  1.00   31.70  ? 151 LEU B CG  1 
ATOM   4078  C CD1 . LEU B  1 151 ? 90.583  39.346  25.731  1.00   29.27  ? 151 LEU B CD1 1 
ATOM   4079  C CD2 . LEU B  1 151 ? 88.946  37.444  25.389  1.00   28.17  ? 151 LEU B CD2 1 
ATOM   4080  N N   . ALA B  1 152 ? 89.046  38.855  30.602  1.00   37.86  ? 152 ALA B N   1 
ATOM   4081  C CA  . ALA B  1 152 ? 87.944  39.439  31.370  1.00   37.15  ? 152 ALA B CA  1 
ATOM   4082  C C   . ALA B  1 152 ? 88.391  40.184  32.627  1.00   40.23  ? 152 ALA B C   1 
ATOM   4083  O O   . ALA B  1 152 ? 87.557  40.667  33.388  1.00   41.63  ? 152 ALA B O   1 
ATOM   4084  C CB  . ALA B  1 152 ? 86.952  38.357  31.747  1.00   33.12  ? 152 ALA B CB  1 
ATOM   4085  N N   . GLN B  1 153 ? 89.698  40.286  32.841  1.00   44.09  ? 153 GLN B N   1 
ATOM   4086  C CA  . GLN B  1 153 ? 90.228  40.872  34.074  1.00   50.31  ? 153 GLN B CA  1 
ATOM   4087  C C   . GLN B  1 153 ? 90.213  42.387  34.070  1.00   47.60  ? 153 GLN B C   1 
ATOM   4088  O O   . GLN B  1 153 ? 90.452  43.007  35.100  1.00   47.06  ? 153 GLN B O   1 
ATOM   4089  C CB  . GLN B  1 153 ? 91.653  40.405  34.337  1.00   58.80  ? 153 GLN B CB  1 
ATOM   4090  C CG  . GLN B  1 153 ? 91.732  39.053  34.996  1.00   66.74  ? 153 GLN B CG  1 
ATOM   4091  C CD  . GLN B  1 153 ? 93.151  38.586  35.131  1.00   74.97  ? 153 GLN B CD  1 
ATOM   4092  O OE1 . GLN B  1 153 ? 94.068  39.189  34.573  1.00   78.75  ? 153 GLN B OE1 1 
ATOM   4093  N NE2 . GLN B  1 153 ? 93.350  37.504  35.866  1.00   77.53  ? 153 GLN B NE2 1 
ATOM   4094  N N   . LYS B  1 154 ? 89.924  42.979  32.917  1.00   45.54  ? 154 LYS B N   1 
ATOM   4095  C CA  . LYS B  1 154 ? 89.957  44.416  32.791  1.00   45.46  ? 154 LYS B CA  1 
ATOM   4096  C C   . LYS B  1 154 ? 88.760  44.956  32.006  1.00   42.08  ? 154 LYS B C   1 
ATOM   4097  O O   . LYS B  1 154 ? 88.417  44.451  30.948  1.00   41.90  ? 154 LYS B O   1 
ATOM   4098  C CB  . LYS B  1 154 ? 91.270  44.810  32.118  1.00   49.21  ? 154 LYS B CB  1 
ATOM   4099  C CG  . LYS B  1 154 ? 92.473  44.737  33.059  1.00   57.68  ? 154 LYS B CG  1 
ATOM   4100  C CD  . LYS B  1 154 ? 93.816  44.870  32.331  1.00   62.32  ? 154 LYS B CD  1 
ATOM   4101  C CE  . LYS B  1 154 ? 94.958  45.393  33.234  1.00   66.67  ? 154 LYS B CE  1 
ATOM   4102  N NZ  . LYS B  1 154 ? 94.571  46.001  34.550  1.00   67.71  ? 154 LYS B NZ  1 
ATOM   4103  N N   . GLY B  1 155 ? 88.130  45.996  32.537  1.00   43.91  ? 155 GLY B N   1 
ATOM   4104  C CA  . GLY B  1 155 ? 87.166  46.777  31.786  1.00   43.32  ? 155 GLY B CA  1 
ATOM   4105  C C   . GLY B  1 155 ? 85.701  46.424  31.914  1.00   43.85  ? 155 GLY B C   1 
ATOM   4106  O O   . GLY B  1 155 ? 84.848  47.210  31.523  1.00   45.81  ? 155 GLY B O   1 
ATOM   4107  N N   . LEU B  1 156 ? 85.397  45.256  32.464  1.00   41.68  ? 156 LEU B N   1 
ATOM   4108  C CA  . LEU B  1 156 ? 84.024  44.759  32.496  1.00   36.68  ? 156 LEU B CA  1 
ATOM   4109  C C   . LEU B  1 156 ? 83.400  45.143  33.824  1.00   39.45  ? 156 LEU B C   1 
ATOM   4110  O O   . LEU B  1 156 ? 84.135  45.475  34.751  1.00   47.02  ? 156 LEU B O   1 
ATOM   4111  C CB  . LEU B  1 156 ? 84.012  43.239  32.325  1.00   36.13  ? 156 LEU B CB  1 
ATOM   4112  C CG  . LEU B  1 156 ? 84.845  42.635  31.196  1.00   33.39  ? 156 LEU B CG  1 
ATOM   4113  C CD1 . LEU B  1 156 ? 84.629  41.142  31.131  1.00   30.98  ? 156 LEU B CD1 1 
ATOM   4114  C CD2 . LEU B  1 156 ? 84.460  43.285  29.889  1.00   32.67  ? 156 LEU B CD2 1 
ATOM   4115  N N   . PRO B  1 157 ? 82.058  45.108  33.939  1.00   35.99  ? 157 PRO B N   1 
ATOM   4116  C CA  . PRO B  1 157 ? 81.451  45.331  35.258  1.00   38.53  ? 157 PRO B CA  1 
ATOM   4117  C C   . PRO B  1 157 ? 82.000  44.355  36.298  1.00   45.13  ? 157 PRO B C   1 
ATOM   4118  O O   . PRO B  1 157 ? 82.547  43.303  35.937  1.00   46.77  ? 157 PRO B O   1 
ATOM   4119  C CB  . PRO B  1 157 ? 79.970  45.101  35.006  1.00   35.77  ? 157 PRO B CB  1 
ATOM   4120  C CG  . PRO B  1 157 ? 79.791  45.420  33.568  1.00   33.75  ? 157 PRO B CG  1 
ATOM   4121  C CD  . PRO B  1 157 ? 81.038  44.972  32.887  1.00   32.96  ? 157 PRO B CD  1 
ATOM   4122  N N   . ASN B  1 158 ? 81.864  44.695  37.573  1.00   47.73  ? 158 ASN B N   1 
ATOM   4123  C CA  . ASN B  1 158 ? 82.587  43.942  38.577  1.00   49.72  ? 158 ASN B CA  1 
ATOM   4124  C C   . ASN B  1 158 ? 82.068  42.524  38.558  1.00   44.27  ? 158 ASN B C   1 
ATOM   4125  O O   . ASN B  1 158 ? 80.874  42.316  38.395  1.00   37.92  ? 158 ASN B O   1 
ATOM   4126  C CB  . ASN B  1 158 ? 82.438  44.590  39.955  1.00   56.28  ? 158 ASN B CB  1 
ATOM   4127  C CG  . ASN B  1 158 ? 83.511  44.145  40.916  1.00   65.14  ? 158 ASN B CG  1 
ATOM   4128  O OD1 . ASN B  1 158 ? 84.613  44.699  40.912  1.00   68.54  ? 158 ASN B OD1 1 
ATOM   4129  N ND2 . ASN B  1 158 ? 83.210  43.153  41.743  1.00   68.09  ? 158 ASN B ND2 1 
ATOM   4130  N N   . ASN B  1 159 ? 82.992  41.569  38.623  1.00   45.23  ? 159 ASN B N   1 
ATOM   4131  C CA  . ASN B  1 159 ? 82.691  40.138  38.647  1.00   46.32  ? 159 ASN B CA  1 
ATOM   4132  C C   . ASN B  1 159 ? 82.141  39.572  37.343  1.00   40.64  ? 159 ASN B C   1 
ATOM   4133  O O   . ASN B  1 159 ? 81.785  38.392  37.282  1.00   38.24  ? 159 ASN B O   1 
ATOM   4134  C CB  . ASN B  1 159 ? 81.737  39.803  39.787  1.00   52.42  ? 159 ASN B CB  1 
ATOM   4135  C CG  . ASN B  1 159 ? 82.430  39.812  41.117  1.00   60.99  ? 159 ASN B CG  1 
ATOM   4136  O OD1 . ASN B  1 159 ? 82.174  40.666  41.967  1.00   65.16  ? 159 ASN B OD1 1 
ATOM   4137  N ND2 . ASN B  1 159 ? 83.369  38.900  41.283  1.00   63.67  ? 159 ASN B ND2 1 
ATOM   4138  N N   . VAL B  1 160 ? 82.053  40.399  36.306  1.00   37.68  ? 160 VAL B N   1 
ATOM   4139  C CA  . VAL B  1 160 ? 81.601  39.899  35.008  1.00   36.14  ? 160 VAL B CA  1 
ATOM   4140  C C   . VAL B  1 160 ? 82.724  39.087  34.404  1.00   40.13  ? 160 VAL B C   1 
ATOM   4141  O O   . VAL B  1 160 ? 83.878  39.499  34.451  1.00   40.54  ? 160 VAL B O   1 
ATOM   4142  C CB  . VAL B  1 160 ? 81.191  41.025  34.067  1.00   31.25  ? 160 VAL B CB  1 
ATOM   4143  C CG1 . VAL B  1 160 ? 81.117  40.543  32.652  1.00   25.61  ? 160 VAL B CG1 1 
ATOM   4144  C CG2 . VAL B  1 160 ? 79.852  41.521  34.482  1.00   30.13  ? 160 VAL B CG2 1 
ATOM   4145  N N   . GLN B  1 161 ? 82.391  37.920  33.858  1.00   43.41  ? 161 GLN B N   1 
ATOM   4146  C CA  . GLN B  1 161 ? 83.405  36.919  33.500  1.00   44.23  ? 161 GLN B CA  1 
ATOM   4147  C C   . GLN B  1 161 ? 83.471  36.558  32.020  1.00   33.93  ? 161 GLN B C   1 
ATOM   4148  O O   . GLN B  1 161 ? 84.032  35.536  31.673  1.00   34.42  ? 161 GLN B O   1 
ATOM   4149  C CB  . GLN B  1 161 ? 83.141  35.654  34.306  1.00   52.40  ? 161 GLN B CB  1 
ATOM   4150  C CG  . GLN B  1 161 ? 83.657  35.773  35.736  1.00   63.13  ? 161 GLN B CG  1 
ATOM   4151  C CD  . GLN B  1 161 ? 82.930  34.849  36.699  1.00   69.22  ? 161 GLN B CD  1 
ATOM   4152  O OE1 . GLN B  1 161 ? 82.279  33.887  36.279  1.00   68.10  ? 161 GLN B OE1 1 
ATOM   4153  N NE2 . GLN B  1 161 ? 83.005  35.162  38.002  1.00   73.70  ? 161 GLN B NE2 1 
ATOM   4154  N N   . GLY B  1 162 ? 82.903  37.394  31.160  1.00   24.90  ? 162 GLY B N   1 
ATOM   4155  C CA  . GLY B  1 162 ? 82.876  37.146  29.737  1.00   23.24  ? 162 GLY B CA  1 
ATOM   4156  C C   . GLY B  1 162 ? 81.844  38.042  29.111  1.00   24.36  ? 162 GLY B C   1 
ATOM   4157  O O   . GLY B  1 162 ? 81.438  39.032  29.699  1.00   25.00  ? 162 GLY B O   1 
ATOM   4158  N N   . ALA B  1 163 ? 81.427  37.685  27.907  1.00   24.23  ? 163 ALA B N   1 
ATOM   4159  C CA  . ALA B  1 163 ? 80.465  38.477  27.166  1.00   24.30  ? 163 ALA B CA  1 
ATOM   4160  C C   . ALA B  1 163 ? 79.530  37.567  26.388  1.00   26.67  ? 163 ALA B C   1 
ATOM   4161  O O   . ALA B  1 163 ? 79.914  36.484  25.967  1.00   24.89  ? 163 ALA B O   1 
ATOM   4162  C CB  . ALA B  1 163 ? 81.190  39.429  26.209  1.00   23.28  ? 163 ALA B CB  1 
ATOM   4163  N N   . LEU B  1 164 ? 78.300  38.007  26.196  1.00   25.89  ? 164 LEU B N   1 
ATOM   4164  C CA  . LEU B  1 164 ? 77.416  37.324  25.287  1.00   24.69  ? 164 LEU B CA  1 
ATOM   4165  C C   . LEU B  1 164 ? 77.267  38.186  24.055  1.00   24.13  ? 164 LEU B C   1 
ATOM   4166  O O   . LEU B  1 164 ? 77.030  39.374  24.151  1.00   28.57  ? 164 LEU B O   1 
ATOM   4167  C CB  . LEU B  1 164 ? 76.079  37.021  25.966  1.00   28.75  ? 164 LEU B CB  1 
ATOM   4168  C CG  . LEU B  1 164 ? 75.260  38.199  26.471  1.00   34.55  ? 164 LEU B CG  1 
ATOM   4169  C CD1 . LEU B  1 164 ? 74.011  38.355  25.678  1.00   35.88  ? 164 LEU B CD1 1 
ATOM   4170  C CD2 . LEU B  1 164 ? 74.969  38.080  27.944  1.00   39.61  ? 164 LEU B CD2 1 
ATOM   4171  N N   . GLY B  1 165 ? 77.462  37.599  22.890  1.00   22.80  ? 165 GLY B N   1 
ATOM   4172  C CA  . GLY B  1 165 ? 77.448  38.363  21.675  1.00   22.18  ? 165 GLY B CA  1 
ATOM   4173  C C   . GLY B  1 165 ? 76.180  38.126  20.902  1.00   23.32  ? 165 GLY B C   1 
ATOM   4174  O O   . GLY B  1 165 ? 75.697  37.006  20.844  1.00   21.96  ? 165 GLY B O   1 
ATOM   4175  N N   . LEU B  1 166 ? 75.628  39.193  20.337  1.00   19.62  ? 166 LEU B N   1 
ATOM   4176  C CA  . LEU B  1 166 ? 74.407  39.110  19.553  1.00   20.79  ? 166 LEU B CA  1 
ATOM   4177  C C   . LEU B  1 166 ? 74.671  39.542  18.118  1.00   20.31  ? 166 LEU B C   1 
ATOM   4178  O O   . LEU B  1 166 ? 73.761  39.972  17.419  1.00   22.11  ? 166 LEU B O   1 
ATOM   4179  C CB  A LEU B  1 166 ? 73.285  39.982  20.140  0.40   17.37  ? 166 LEU B CB  1 
ATOM   4180  C CB  B LEU B  1 166 ? 73.302  39.973  20.188  0.60   17.36  ? 166 LEU B CB  1 
ATOM   4181  C CG  A LEU B  1 166 ? 72.525  39.655  21.428  0.40   18.91  ? 166 LEU B CG  1 
ATOM   4182  C CG  B LEU B  1 166 ? 72.287  39.399  21.188  0.60   19.99  ? 166 LEU B CG  1 
ATOM   4183  C CD1 A LEU B  1 166 ? 71.836  38.292  21.397  0.40   18.67  ? 166 LEU B CD1 1 
ATOM   4184  C CD1 B LEU B  1 166 ? 72.883  38.422  22.169  0.60   19.43  ? 166 LEU B CD1 1 
ATOM   4185  C CD2 A LEU B  1 166 ? 73.454  39.733  22.585  0.40   19.19  ? 166 LEU B CD2 1 
ATOM   4186  C CD2 B LEU B  1 166 ? 71.603  40.501  21.944  0.60   17.60  ? 166 LEU B CD2 1 
ATOM   4187  N N   . GLY B  1 167 ? 75.917  39.431  17.681  1.00   21.50  ? 167 GLY B N   1 
ATOM   4188  C CA  . GLY B  1 167 ? 76.281  39.899  16.356  1.00   23.83  ? 167 GLY B CA  1 
ATOM   4189  C C   . GLY B  1 167 ? 75.815  38.993  15.218  1.00   23.81  ? 167 GLY B C   1 
ATOM   4190  O O   . GLY B  1 167 ? 75.286  37.906  15.421  1.00   22.86  ? 167 GLY B O   1 
ATOM   4191  N N   . GLN B  1 168 ? 76.013  39.453  13.993  1.00   24.91  ? 168 GLN B N   1 
ATOM   4192  C CA  . GLN B  1 168 ? 75.663  38.654  12.824  1.00   26.06  ? 168 GLN B CA  1 
ATOM   4193  C C   . GLN B  1 168 ? 76.757  37.666  12.482  1.00   27.31  ? 168 GLN B C   1 
ATOM   4194  O O   . GLN B  1 168 ? 77.571  37.917  11.586  1.00   30.28  ? 168 GLN B O   1 
ATOM   4195  C CB  . GLN B  1 168 ? 75.382  39.557  11.625  1.00   25.74  ? 168 GLN B CB  1 
ATOM   4196  C CG  . GLN B  1 168 ? 74.058  40.262  11.730  1.00   25.66  ? 168 GLN B CG  1 
ATOM   4197  C CD  . GLN B  1 168 ? 72.912  39.295  11.704  1.00   25.03  ? 168 GLN B CD  1 
ATOM   4198  O OE1 . GLN B  1 168 ? 72.677  38.625  10.696  1.00   28.19  ? 168 GLN B OE1 1 
ATOM   4199  N NE2 . GLN B  1 168 ? 72.206  39.186  12.823  1.00   23.80  ? 168 GLN B NE2 1 
ATOM   4200  N N   . ALA B  1 169 ? 76.729  36.520  13.167  1.00   26.09  ? 169 ALA B N   1 
ATOM   4201  C CA  . ALA B  1 169 ? 77.770  35.507  13.069  1.00   23.08  ? 169 ALA B CA  1 
ATOM   4202  C C   . ALA B  1 169 ? 77.155  34.177  13.477  1.00   21.89  ? 169 ALA B C   1 
ATOM   4203  O O   . ALA B  1 169 ? 76.218  34.163  14.254  1.00   23.73  ? 169 ALA B O   1 
ATOM   4204  C CB  . ALA B  1 169 ? 78.954  35.872  13.956  1.00   21.41  ? 169 ALA B CB  1 
ATOM   4205  N N   . PRO B  1 170 ? 77.671  33.057  12.946  1.00   24.29  ? 170 PRO B N   1 
ATOM   4206  C CA  . PRO B  1 170 ? 76.972  31.759  13.022  1.00   24.60  ? 170 PRO B CA  1 
ATOM   4207  C C   . PRO B  1 170 ? 76.732  31.166  14.407  1.00   23.10  ? 170 PRO B C   1 
ATOM   4208  O O   . PRO B  1 170 ? 75.764  30.434  14.544  1.00   23.23  ? 170 PRO B O   1 
ATOM   4209  C CB  . PRO B  1 170 ? 77.865  30.828  12.197  1.00   24.58  ? 170 PRO B CB  1 
ATOM   4210  C CG  . PRO B  1 170 ? 79.178  31.542  12.083  1.00   27.12  ? 170 PRO B CG  1 
ATOM   4211  C CD  . PRO B  1 170 ? 78.837  32.989  12.052  1.00   25.72  ? 170 PRO B CD  1 
ATOM   4212  N N   . ILE B  1 171 ? 77.569  31.424  15.405  1.00   23.00  ? 171 ILE B N   1 
ATOM   4213  C CA  . ILE B  1 171 ? 77.214  30.909  16.719  1.00   22.49  ? 171 ILE B CA  1 
ATOM   4214  C C   . ILE B  1 171 ? 76.943  32.023  17.719  1.00   22.28  ? 171 ILE B C   1 
ATOM   4215  O O   . ILE B  1 171 ? 77.187  31.872  18.923  1.00   22.45  ? 171 ILE B O   1 
ATOM   4216  C CB  . ILE B  1 171 ? 78.290  29.912  17.265  1.00   22.73  ? 171 ILE B CB  1 
ATOM   4217  C CG1 . ILE B  1 171 ? 79.682  30.517  17.355  1.00   21.85  ? 171 ILE B CG1 1 
ATOM   4218  C CG2 . ILE B  1 171 ? 78.346  28.680  16.376  1.00   24.21  ? 171 ILE B CG2 1 
ATOM   4219  C CD1 . ILE B  1 171 ? 80.608  29.765  18.297  1.00   21.04  ? 171 ILE B CD1 1 
ATOM   4220  N N   . SER B  1 172 ? 76.384  33.124  17.228  1.00   22.32  ? 172 SER B N   1 
ATOM   4221  C CA  . SER B  1 172 ? 75.892  34.149  18.119  1.00   22.73  ? 172 SER B CA  1 
ATOM   4222  C C   . SER B  1 172 ? 74.761  33.584  18.961  1.00   22.09  ? 172 SER B C   1 
ATOM   4223  O O   . SER B  1 172 ? 74.166  32.570  18.620  1.00   22.40  ? 172 SER B O   1 
ATOM   4224  C CB  . SER B  1 172 ? 75.422  35.364  17.352  1.00   23.26  ? 172 SER B CB  1 
ATOM   4225  O OG  . SER B  1 172 ? 74.350  35.040  16.511  1.00   25.45  ? 172 SER B OG  1 
ATOM   4226  N N   . LEU B  1 173 ? 74.462  34.240  20.068  1.00   22.05  ? 173 LEU B N   1 
ATOM   4227  C CA  . LEU B  1 173 ? 73.432  33.753  20.960  1.00   24.69  ? 173 LEU B CA  1 
ATOM   4228  C C   . LEU B  1 173 ? 72.086  33.689  20.281  1.00   26.97  ? 173 LEU B C   1 
ATOM   4229  O O   . LEU B  1 173 ? 71.403  32.677  20.345  1.00   27.58  ? 173 LEU B O   1 
ATOM   4230  C CB  . LEU B  1 173 ? 73.330  34.643  22.191  1.00   23.74  ? 173 LEU B CB  1 
ATOM   4231  C CG  . LEU B  1 173 ? 72.099  34.413  23.060  1.00   23.16  ? 173 LEU B CG  1 
ATOM   4232  C CD1 . LEU B  1 173 ? 72.109  33.026  23.614  1.00   20.39  ? 173 LEU B CD1 1 
ATOM   4233  C CD2 . LEU B  1 173 ? 72.085  35.417  24.215  1.00   23.71  ? 173 LEU B CD2 1 
ATOM   4234  N N   . GLN B  1 174 ? 71.704  34.765  19.613  1.00   25.84  ? 174 GLN B N   1 
ATOM   4235  C CA  . GLN B  1 174 ? 70.377  34.779  19.027  1.00   24.85  ? 174 GLN B CA  1 
ATOM   4236  C C   . GLN B  1 174 ? 70.291  33.750  17.900  1.00   26.06  ? 174 GLN B C   1 
ATOM   4237  O O   . GLN B  1 174 ? 69.310  33.045  17.817  1.00   27.90  ? 174 GLN B O   1 
ATOM   4238  C CB  . GLN B  1 174 ? 69.994  36.194  18.535  1.00   22.65  ? 174 GLN B CB  1 
ATOM   4239  C CG  . GLN B  1 174 ? 70.470  36.594  17.149  1.00   22.29  ? 174 GLN B CG  1 
ATOM   4240  C CD  . GLN B  1 174 ? 71.901  37.003  17.148  1.00   21.65  ? 174 GLN B CD  1 
ATOM   4241  O OE1 . GLN B  1 174 ? 72.535  37.008  18.184  1.00   23.78  ? 174 GLN B OE1 1 
ATOM   4242  N NE2 . GLN B  1 174 ? 72.422  37.349  15.990  1.00   20.99  ? 174 GLN B NE2 1 
ATOM   4243  N N   . ASN B  1 175 ? 71.327  33.595  17.080  1.00   27.52  ? 175 ASN B N   1 
ATOM   4244  C CA  . ASN B  1 175 ? 71.259  32.641  15.977  1.00   27.42  ? 175 ASN B CA  1 
ATOM   4245  C C   . ASN B  1 175 ? 71.052  31.214  16.507  1.00   25.57  ? 175 ASN B C   1 
ATOM   4246  O O   . ASN B  1 175 ? 70.274  30.438  15.957  1.00   24.44  ? 175 ASN B O   1 
ATOM   4247  C CB  A ASN B  1 175 ? 72.492  32.768  15.077  0.50   28.83  ? 175 ASN B CB  1 
ATOM   4248  C CB  B ASN B  1 175 ? 72.552  32.724  15.150  0.50   29.49  ? 175 ASN B CB  1 
ATOM   4249  C CG  A ASN B  1 175 ? 72.386  33.967  14.139  0.50   26.37  ? 175 ASN B CG  1 
ATOM   4250  C CG  B ASN B  1 175 ? 72.420  32.121  13.769  0.50   34.61  ? 175 ASN B CG  1 
ATOM   4251  O OD1 A ASN B  1 175 ? 71.280  34.351  13.760  0.50   27.78  ? 175 ASN B OD1 1 
ATOM   4252  O OD1 B ASN B  1 175 ? 71.596  31.240  13.536  0.50   41.26  ? 175 ASN B OD1 1 
ATOM   4253  N ND2 A ASN B  1 175 ? 73.518  34.572  13.774  0.50   19.53  ? 175 ASN B ND2 1 
ATOM   4254  N ND2 B ASN B  1 175 ? 73.244  32.594  12.838  0.50   36.38  ? 175 ASN B ND2 1 
ATOM   4255  N N   . GLN B  1 176 ? 71.682  30.892  17.629  1.00   27.30  ? 176 GLN B N   1 
ATOM   4256  C CA  . GLN B  1 176 ? 71.556  29.550  18.184  1.00   26.06  ? 176 GLN B CA  1 
ATOM   4257  C C   . GLN B  1 176 ? 70.177  29.361  18.827  1.00   26.16  ? 176 GLN B C   1 
ATOM   4258  O O   . GLN B  1 176 ? 69.628  28.271  18.795  1.00   25.48  ? 176 GLN B O   1 
ATOM   4259  C CB  . GLN B  1 176 ? 72.686  29.248  19.201  1.00   18.17  ? 176 GLN B CB  1 
ATOM   4260  C CG  . GLN B  1 176 ? 74.106  29.069  18.576  1.00   21.97  ? 176 GLN B CG  1 
ATOM   4261  C CD  . GLN B  1 176 ? 75.150  28.497  19.533  1.00   21.13  ? 176 GLN B CD  1 
ATOM   4262  O OE1 . GLN B  1 176 ? 75.180  27.299  19.812  1.00   21.10  ? 176 GLN B OE1 1 
ATOM   4263  N NE2 . GLN B  1 176 ? 75.998  29.362  20.050  1.00   20.07  ? 176 GLN B NE2 1 
ATOM   4264  N N   . LEU B  1 177 ? 69.627  30.401  19.436  1.00   25.15  ? 177 LEU B N   1 
ATOM   4265  C CA  . LEU B  1 177 ? 68.284  30.286  19.978  1.00   24.99  ? 177 LEU B CA  1 
ATOM   4266  C C   . LEU B  1 177 ? 67.242  30.146  18.860  1.00   23.56  ? 177 LEU B C   1 
ATOM   4267  O O   . LEU B  1 177 ? 66.340  29.328  18.954  1.00   26.24  ? 177 LEU B O   1 
ATOM   4268  C CB  . LEU B  1 177 ? 67.953  31.487  20.862  1.00   23.65  ? 177 LEU B CB  1 
ATOM   4269  C CG  . LEU B  1 177 ? 68.756  31.671  22.150  1.00   21.34  ? 177 LEU B CG  1 
ATOM   4270  C CD1 . LEU B  1 177 ? 68.352  32.961  22.830  1.00   18.46  ? 177 LEU B CD1 1 
ATOM   4271  C CD2 . LEU B  1 177 ? 68.534  30.494  23.075  1.00   20.01  ? 177 LEU B CD2 1 
ATOM   4272  N N   . PHE B  1 178 ? 67.371  30.951  17.811  1.00   22.31  ? 178 PHE B N   1 
ATOM   4273  C CA  . PHE B  1 178 ? 66.476  30.878  16.655  1.00   24.83  ? 178 PHE B CA  1 
ATOM   4274  C C   . PHE B  1 178 ? 66.439  29.445  16.097  1.00   26.25  ? 178 PHE B C   1 
ATOM   4275  O O   . PHE B  1 178 ? 65.384  28.876  15.840  1.00   26.77  ? 178 PHE B O   1 
ATOM   4276  C CB  . PHE B  1 178 ? 66.915  31.815  15.499  1.00   24.71  ? 178 PHE B CB  1 
ATOM   4277  C CG  . PHE B  1 178 ? 66.845  33.321  15.780  1.00   25.42  ? 178 PHE B CG  1 
ATOM   4278  C CD1 . PHE B  1 178 ? 66.048  33.858  16.781  1.00   28.31  ? 178 PHE B CD1 1 
ATOM   4279  C CD2 . PHE B  1 178 ? 67.612  34.201  15.004  1.00   21.48  ? 178 PHE B CD2 1 
ATOM   4280  C CE1 . PHE B  1 178 ? 66.024  35.245  17.017  1.00   26.69  ? 178 PHE B CE1 1 
ATOM   4281  C CE2 . PHE B  1 178 ? 67.585  35.578  15.230  1.00   20.20  ? 178 PHE B CE2 1 
ATOM   4282  C CZ  . PHE B  1 178 ? 66.790  36.097  16.226  1.00   20.11  ? 178 PHE B CZ  1 
ATOM   4283  N N   . SER B  1 179 ? 67.614  28.873  15.873  1.00   27.20  ? 179 SER B N   1 
ATOM   4284  C CA  . SER B  1 179 ? 67.682  27.625  15.143  1.00   25.24  ? 179 SER B CA  1 
ATOM   4285  C C   . SER B  1 179 ? 67.265  26.465  16.018  1.00   26.43  ? 179 SER B C   1 
ATOM   4286  O O   . SER B  1 179 ? 66.665  25.520  15.536  1.00   28.40  ? 179 SER B O   1 
ATOM   4287  C CB  . SER B  1 179 ? 69.077  27.389  14.568  1.00   27.74  ? 179 SER B CB  1 
ATOM   4288  O OG  . SER B  1 179 ? 69.980  26.977  15.559  1.00   33.88  ? 179 SER B OG  1 
ATOM   4289  N N   . HIS B  1 180 ? 67.542  26.527  17.310  1.00   26.02  ? 180 HIS B N   1 
ATOM   4290  C CA  . HIS B  1 180 ? 67.156  25.424  18.170  1.00   25.74  ? 180 HIS B CA  1 
ATOM   4291  C C   . HIS B  1 180 ? 65.640  25.330  18.374  1.00   28.48  ? 180 HIS B C   1 
ATOM   4292  O O   . HIS B  1 180 ? 65.057  24.240  18.402  1.00   28.97  ? 180 HIS B O   1 
ATOM   4293  C CB  . HIS B  1 180 ? 67.855  25.539  19.502  1.00   22.19  ? 180 HIS B CB  1 
ATOM   4294  C CG  . HIS B  1 180 ? 67.692  24.328  20.353  1.00   24.74  ? 180 HIS B CG  1 
ATOM   4295  N ND1 . HIS B  1 180 ? 66.805  24.264  21.402  1.00   29.82  ? 180 HIS B ND1 1 
ATOM   4296  C CD2 . HIS B  1 180 ? 68.269  23.114  20.277  1.00   23.85  ? 180 HIS B CD2 1 
ATOM   4297  C CE1 . HIS B  1 180 ? 66.870  23.075  21.962  1.00   24.78  ? 180 HIS B CE1 1 
ATOM   4298  N NE2 . HIS B  1 180 ? 67.746  22.355  21.293  1.00   28.71  ? 180 HIS B NE2 1 
ATOM   4299  N N   . PHE B  1 181 ? 65.001  26.482  18.500  1.00   28.44  ? 181 PHE B N   1 
ATOM   4300  C CA  . PHE B  1 181 ? 63.591  26.524  18.825  1.00   25.86  ? 181 PHE B CA  1 
ATOM   4301  C C   . PHE B  1 181 ? 62.730  26.837  17.612  1.00   27.68  ? 181 PHE B C   1 
ATOM   4302  O O   . PHE B  1 181 ? 61.520  26.885  17.719  1.00   32.35  ? 181 PHE B O   1 
ATOM   4303  C CB  . PHE B  1 181 ? 63.349  27.544  19.946  1.00   25.26  ? 181 PHE B CB  1 
ATOM   4304  C CG  . PHE B  1 181 ? 63.935  27.131  21.283  1.00   27.00  ? 181 PHE B CG  1 
ATOM   4305  C CD1 . PHE B  1 181 ? 63.309  26.180  22.066  1.00   28.40  ? 181 PHE B CD1 1 
ATOM   4306  C CD2 . PHE B  1 181 ? 65.115  27.673  21.741  1.00   29.36  ? 181 PHE B CD2 1 
ATOM   4307  C CE1 . PHE B  1 181 ? 63.842  25.790  23.291  1.00   27.50  ? 181 PHE B CE1 1 
ATOM   4308  C CE2 . PHE B  1 181 ? 65.646  27.277  22.967  1.00   28.23  ? 181 PHE B CE2 1 
ATOM   4309  C CZ  . PHE B  1 181 ? 65.003  26.328  23.725  1.00   27.88  ? 181 PHE B CZ  1 
ATOM   4310  N N   . GLY B  1 182 ? 63.331  27.068  16.456  1.00   26.66  ? 182 GLY B N   1 
ATOM   4311  C CA  . GLY B  1 182 ? 62.529  27.373  15.279  1.00   28.46  ? 182 GLY B CA  1 
ATOM   4312  C C   . GLY B  1 182 ? 61.801  28.712  15.368  1.00   28.36  ? 182 GLY B C   1 
ATOM   4313  O O   . GLY B  1 182 ? 60.684  28.855  14.878  1.00   29.34  ? 182 GLY B O   1 
ATOM   4314  N N   . LEU B  1 183 ? 62.451  29.707  15.971  1.00   30.97  ? 183 LEU B N   1 
ATOM   4315  C CA  . LEU B  1 183 ? 61.862  31.042  16.178  1.00   29.03  ? 183 LEU B CA  1 
ATOM   4316  C C   . LEU B  1 183 ? 61.906  31.902  14.914  1.00   30.39  ? 183 LEU B C   1 
ATOM   4317  O O   . LEU B  1 183 ? 62.697  31.626  14.013  1.00   32.24  ? 183 LEU B O   1 
ATOM   4318  C CB  . LEU B  1 183 ? 62.594  31.776  17.318  1.00   27.13  ? 183 LEU B CB  1 
ATOM   4319  C CG  . LEU B  1 183 ? 62.699  31.098  18.688  1.00   30.63  ? 183 LEU B CG  1 
ATOM   4320  C CD1 . LEU B  1 183 ? 63.594  31.864  19.646  1.00   29.19  ? 183 LEU B CD1 1 
ATOM   4321  C CD2 . LEU B  1 183 ? 61.334  30.932  19.296  1.00   32.77  ? 183 LEU B CD2 1 
ATOM   4322  N N   . LYS B  1 184 ? 61.052  32.926  14.831  1.00   31.35  ? 184 LYS B N   1 
ATOM   4323  C CA  . LYS B  1 184 ? 61.242  33.991  13.838  1.00   30.84  ? 184 LYS B CA  1 
ATOM   4324  C C   . LYS B  1 184 ? 62.566  34.706  14.123  1.00   26.04  ? 184 LYS B C   1 
ATOM   4325  O O   . LYS B  1 184 ? 62.955  34.863  15.273  1.00   24.88  ? 184 LYS B O   1 
ATOM   4326  C CB  . LYS B  1 184 ? 60.074  35.011  13.831  1.00   50.28  ? 184 LYS B CB  1 
ATOM   4327  C CG  . LYS B  1 184 ? 60.353  36.326  13.005  1.00   62.90  ? 184 LYS B CG  1 
ATOM   4328  C CD  . LYS B  1 184 ? 59.094  37.161  12.681  1.00   65.15  ? 184 LYS B CD  1 
ATOM   4329  C CE  . LYS B  1 184 ? 59.379  38.487  11.925  1.00   50.98  ? 184 LYS B CE  1 
ATOM   4330  N NZ  . LYS B  1 184 ? 60.456  39.368  12.478  1.00   48.25  ? 184 LYS B NZ  1 
ATOM   4331  N N   . ARG B  1 185 ? 63.266  35.104  13.069  1.00   26.27  ? 185 ARG B N   1 
ATOM   4332  C CA  . ARG B  1 185 ? 64.546  35.775  13.198  1.00   23.69  ? 185 ARG B CA  1 
ATOM   4333  C C   . ARG B  1 185 ? 64.357  37.266  13.492  1.00   24.33  ? 185 ARG B C   1 
ATOM   4334  O O   . ARG B  1 185 ? 64.437  38.102  12.596  1.00   24.45  ? 185 ARG B O   1 
ATOM   4335  C CB  . ARG B  1 185 ? 65.348  35.567  11.920  1.00   26.01  ? 185 ARG B CB  1 
ATOM   4336  C CG  . ARG B  1 185 ? 65.474  34.080  11.587  1.00   29.66  ? 185 ARG B CG  1 
ATOM   4337  C CD  . ARG B  1 185 ? 66.412  33.749  10.403  1.00   36.25  ? 185 ARG B CD  1 
ATOM   4338  N NE  . ARG B  1 185 ? 67.820  33.901  10.760  1.00   37.66  ? 185 ARG B NE  1 
ATOM   4339  C CZ  . ARG B  1 185 ? 68.580  32.960  11.320  1.00   35.23  ? 185 ARG B CZ  1 
ATOM   4340  N NH1 . ARG B  1 185 ? 69.838  33.236  11.607  1.00   34.19  ? 185 ARG B NH1 1 
ATOM   4341  N NH2 . ARG B  1 185 ? 68.097  31.748  11.582  1.00   35.70  ? 185 ARG B NH2 1 
ATOM   4342  N N   . GLN B  1 186 ? 64.140  37.583  14.763  1.00   22.94  ? 186 GLN B N   1 
ATOM   4343  C CA  . GLN B  1 186 ? 63.854  38.930  15.214  1.00   26.96  ? 186 GLN B CA  1 
ATOM   4344  C C   . GLN B  1 186 ? 64.239  38.946  16.667  1.00   27.69  ? 186 GLN B C   1 
ATOM   4345  O O   . GLN B  1 186 ? 63.958  37.990  17.369  1.00   29.42  ? 186 GLN B O   1 
ATOM   4346  C CB  . GLN B  1 186 ? 62.376  39.259  15.025  1.00   28.70  ? 186 GLN B CB  1 
ATOM   4347  C CG  . GLN B  1 186 ? 61.938  40.624  15.435  1.00   29.50  ? 186 GLN B CG  1 
ATOM   4348  C CD  . GLN B  1 186 ? 60.432  40.734  15.486  1.00   30.95  ? 186 GLN B CD  1 
ATOM   4349  O OE1 . GLN B  1 186 ? 59.739  40.553  14.489  1.00   33.57  ? 186 GLN B OE1 1 
ATOM   4350  N NE2 . GLN B  1 186 ? 59.916  40.998  16.659  1.00   32.00  ? 186 GLN B NE2 1 
ATOM   4351  N N   . PHE B  1 187 ? 64.939  39.979  17.122  1.00   26.90  ? 187 PHE B N   1 
ATOM   4352  C CA  . PHE B  1 187 ? 65.080  40.146  18.553  1.00   24.79  ? 187 PHE B CA  1 
ATOM   4353  C C   . PHE B  1 187 ? 64.928  41.605  18.860  1.00   26.28  ? 187 PHE B C   1 
ATOM   4354  O O   . PHE B  1 187 ? 65.141  42.454  18.004  1.00   27.26  ? 187 PHE B O   1 
ATOM   4355  C CB  . PHE B  1 187 ? 66.403  39.576  19.103  1.00   24.46  ? 187 PHE B CB  1 
ATOM   4356  C CG  . PHE B  1 187 ? 67.654  40.307  18.659  1.00   25.00  ? 187 PHE B CG  1 
ATOM   4357  C CD1 . PHE B  1 187 ? 68.310  39.950  17.491  1.00   23.94  ? 187 PHE B CD1 1 
ATOM   4358  C CD2 . PHE B  1 187 ? 68.193  41.334  19.437  1.00   24.63  ? 187 PHE B CD2 1 
ATOM   4359  C CE1 . PHE B  1 187 ? 69.482  40.602  17.111  1.00   23.76  ? 187 PHE B CE1 1 
ATOM   4360  C CE2 . PHE B  1 187 ? 69.327  42.013  19.046  1.00   23.03  ? 187 PHE B CE2 1 
ATOM   4361  C CZ  . PHE B  1 187 ? 69.988  41.639  17.884  1.00   23.14  ? 187 PHE B CZ  1 
ATOM   4362  N N   . SER B  1 188 ? 64.524  41.888  20.091  1.00   26.42  ? 188 SER B N   1 
ATOM   4363  C CA  . SER B  1 188 ? 64.174  43.236  20.519  1.00   27.85  ? 188 SER B CA  1 
ATOM   4364  C C   . SER B  1 188 ? 64.915  43.653  21.778  1.00   30.27  ? 188 SER B C   1 
ATOM   4365  O O   . SER B  1 188 ? 65.048  42.872  22.710  1.00   30.21  ? 188 SER B O   1 
ATOM   4366  C CB  . SER B  1 188 ? 62.675  43.333  20.770  1.00   30.31  ? 188 SER B CB  1 
ATOM   4367  O OG  . SER B  1 188 ? 61.955  43.011  19.597  1.00   30.95  ? 188 SER B OG  1 
ATOM   4368  N N   . VAL B  1 189 ? 65.392  44.890  21.812  1.00   29.27  ? 189 VAL B N   1 
ATOM   4369  C CA  . VAL B  1 189 ? 66.182  45.336  22.953  1.00   27.84  ? 189 VAL B CA  1 
ATOM   4370  C C   . VAL B  1 189 ? 65.495  46.470  23.716  1.00   25.70  ? 189 VAL B C   1 
ATOM   4371  O O   . VAL B  1 189 ? 65.183  47.504  23.142  1.00   26.01  ? 189 VAL B O   1 
ATOM   4372  C CB  . VAL B  1 189 ? 67.576  45.804  22.488  1.00   24.36  ? 189 VAL B CB  1 
ATOM   4373  C CG1 . VAL B  1 189 ? 68.454  46.057  23.662  1.00   23.89  ? 189 VAL B CG1 1 
ATOM   4374  C CG2 . VAL B  1 189 ? 68.202  44.755  21.616  1.00   22.50  ? 189 VAL B CG2 1 
ATOM   4375  N N   . CYS B  1 190 ? 65.251  46.271  25.004  1.00   23.21  ? 190 CYS B N   1 
ATOM   4376  C CA  . CYS B  1 190 ? 64.741  47.359  25.831  1.00   24.49  ? 190 CYS B CA  1 
ATOM   4377  C C   . CYS B  1 190 ? 65.596  47.513  27.073  1.00   24.55  ? 190 CYS B C   1 
ATOM   4378  O O   . CYS B  1 190 ? 65.323  46.926  28.119  1.00   28.31  ? 190 CYS B O   1 
ATOM   4379  C CB  . CYS B  1 190 ? 63.284  47.118  26.219  1.00   32.81  ? 190 CYS B CB  1 
ATOM   4380  S SG  . CYS B  1 190 ? 62.324  48.659  26.481  1.00   36.15  ? 190 CYS B SG  1 
ATOM   4381  N N   . LEU B  1 191 ? 66.651  48.309  26.951  1.00   32.21  ? 191 LEU B N   1 
ATOM   4382  C CA  . LEU B  1 191 ? 67.565  48.503  28.068  1.00   29.22  ? 191 LEU B CA  1 
ATOM   4383  C C   . LEU B  1 191 ? 67.010  49.491  29.076  1.00   26.50  ? 191 LEU B C   1 
ATOM   4384  O O   . LEU B  1 191 ? 66.376  50.468  28.725  1.00   28.74  ? 191 LEU B O   1 
ATOM   4385  C CB  . LEU B  1 191 ? 68.932  48.963  27.564  1.00   26.50  ? 191 LEU B CB  1 
ATOM   4386  C CG  . LEU B  1 191 ? 69.669  48.114  26.521  1.00   24.24  ? 191 LEU B CG  1 
ATOM   4387  C CD1 . LEU B  1 191 ? 71.022  48.738  26.175  1.00   25.21  ? 191 LEU B CD1 1 
ATOM   4388  C CD2 . LEU B  1 191 ? 69.834  46.653  26.958  1.00   25.18  ? 191 LEU B CD2 1 
ATOM   4389  N N   . SER B  1 192 ? 67.240  49.210  30.345  1.00   33.45  ? 192 SER B N   1 
ATOM   4390  C CA  . SER B  1 192 ? 66.845  50.100  31.414  1.00   28.74  ? 192 SER B CA  1 
ATOM   4391  C C   . SER B  1 192 ? 67.967  51.090  31.798  1.00   33.03  ? 192 SER B C   1 
ATOM   4392  O O   . SER B  1 192 ? 69.122  50.710  31.973  1.00   32.20  ? 192 SER B O   1 
ATOM   4393  C CB  . SER B  1 192 ? 66.434  49.268  32.619  1.00   29.21  ? 192 SER B CB  1 
ATOM   4394  O OG  . SER B  1 192 ? 66.119  50.088  33.726  1.00   31.40  ? 192 SER B OG  1 
ATOM   4395  N N   . ARG B  1 193 ? 67.611  52.366  31.909  1.00   33.97  ? 193 ARG B N   1 
ATOM   4396  C CA  . ARG B  1 193 ? 68.502  53.430  32.337  1.00   32.44  ? 193 ARG B CA  1 
ATOM   4397  C C   . ARG B  1 193 ? 68.967  53.287  33.788  1.00   37.28  ? 193 ARG B C   1 
ATOM   4398  O O   . ARG B  1 193 ? 70.012  53.787  34.174  1.00   38.39  ? 193 ARG B O   1 
ATOM   4399  C CB  . ARG B  1 193 ? 67.785  54.767  32.092  1.00   43.62  ? 193 ARG B CB  1 
ATOM   4400  C CG  . ARG B  1 193 ? 68.438  55.990  32.673  1.00   51.21  ? 193 ARG B CG  1 
ATOM   4401  C CD  . ARG B  1 193 ? 67.799  57.317  32.227  1.00   61.09  ? 193 ARG B CD  1 
ATOM   4402  N NE  . ARG B  1 193 ? 67.784  57.418  30.761  1.00   73.41  ? 193 ARG B NE  1 
ATOM   4403  C CZ  . ARG B  1 193 ? 66.936  58.146  30.030  1.00   82.67  ? 193 ARG B CZ  1 
ATOM   4404  N NH1 . ARG B  1 193 ? 66.010  58.903  30.613  1.00   87.36  ? 193 ARG B NH1 1 
ATOM   4405  N NH2 . ARG B  1 193 ? 67.038  58.137  28.702  1.00   83.54  ? 193 ARG B NH2 1 
ATOM   4406  N N   . TYR B  1 194 ? 68.198  52.569  34.588  1.00   39.45  ? 194 TYR B N   1 
ATOM   4407  C CA  . TYR B  1 194 ? 68.433  52.516  36.026  1.00   41.46  ? 194 TYR B CA  1 
ATOM   4408  C C   . TYR B  1 194 ? 69.117  51.233  36.450  1.00   37.92  ? 194 TYR B C   1 
ATOM   4409  O O   . TYR B  1 194 ? 68.754  50.163  35.991  1.00   35.09  ? 194 TYR B O   1 
ATOM   4410  C CB  . TYR B  1 194 ? 67.111  52.646  36.761  1.00   46.81  ? 194 TYR B CB  1 
ATOM   4411  C CG  . TYR B  1 194 ? 66.201  53.665  36.125  1.00   52.27  ? 194 TYR B CG  1 
ATOM   4412  C CD1 . TYR B  1 194 ? 66.417  55.026  36.303  1.00   56.85  ? 194 TYR B CD1 1 
ATOM   4413  C CD2 . TYR B  1 194 ? 65.123  53.266  35.350  1.00   53.45  ? 194 TYR B CD2 1 
ATOM   4414  C CE1 . TYR B  1 194 ? 65.590  55.961  35.720  1.00   60.03  ? 194 TYR B CE1 1 
ATOM   4415  C CE2 . TYR B  1 194 ? 64.287  54.191  34.768  1.00   56.94  ? 194 TYR B CE2 1 
ATOM   4416  C CZ  . TYR B  1 194 ? 64.527  55.540  34.954  1.00   61.79  ? 194 TYR B CZ  1 
ATOM   4417  O OH  . TYR B  1 194 ? 63.696  56.475  34.372  1.00   66.44  ? 194 TYR B OH  1 
ATOM   4418  N N   . SER B  1 195 ? 70.098  51.324  37.332  1.00   37.67  ? 195 SER B N   1 
ATOM   4419  C CA  . SER B  1 195 ? 70.750  50.112  37.819  1.00   37.45  ? 195 SER B CA  1 
ATOM   4420  C C   . SER B  1 195 ? 69.839  49.273  38.728  1.00   37.59  ? 195 SER B C   1 
ATOM   4421  O O   . SER B  1 195 ? 70.092  48.098  38.953  1.00   37.76  ? 195 SER B O   1 
ATOM   4422  C CB  . SER B  1 195 ? 72.019  50.460  38.585  1.00   38.17  ? 195 SER B CB  1 
ATOM   4423  O OG  . SER B  1 195 ? 71.714  51.313  39.674  1.00   42.49  ? 195 SER B OG  1 
ATOM   4424  N N   . THR B  1 196 ? 68.781  49.888  39.238  1.00   40.53  ? 196 THR B N   1 
ATOM   4425  C CA  . THR B  1 196 ? 67.900  49.270  40.232  1.00   42.38  ? 196 THR B CA  1 
ATOM   4426  C C   . THR B  1 196 ? 66.717  48.469  39.682  1.00   45.28  ? 196 THR B C   1 
ATOM   4427  O O   . THR B  1 196 ? 65.959  47.856  40.447  1.00   46.76  ? 196 THR B O   1 
ATOM   4428  C CB  . THR B  1 196 ? 67.343  50.336  41.184  1.00   42.89  ? 196 THR B CB  1 
ATOM   4429  O OG1 . THR B  1 196 ? 66.700  51.347  40.411  1.00   40.85  ? 196 THR B OG1 1 
ATOM   4430  C CG2 . THR B  1 196 ? 68.459  51.008  41.949  1.00   44.16  ? 196 THR B CG2 1 
ATOM   4431  N N   . SER B  1 197 ? 66.562  48.470  38.363  1.00   43.58  ? 197 SER B N   1 
ATOM   4432  C CA  . SER B  1 197 ? 65.539  47.666  37.711  1.00   39.86  ? 197 SER B CA  1 
ATOM   4433  C C   . SER B  1 197 ? 66.032  47.192  36.344  1.00   36.88  ? 197 SER B C   1 
ATOM   4434  O O   . SER B  1 197 ? 66.760  47.905  35.652  1.00   41.17  ? 197 SER B O   1 
ATOM   4435  C CB  . SER B  1 197 ? 64.238  48.470  37.613  1.00   40.15  ? 197 SER B CB  1 
ATOM   4436  O OG  . SER B  1 197 ? 64.434  49.676  36.907  1.00   39.58  ? 197 SER B OG  1 
ATOM   4437  N N   . ASN B  1 198 ? 65.623  45.991  35.957  1.00   31.22  ? 198 ASN B N   1 
ATOM   4438  C CA  . ASN B  1 198 ? 66.114  45.356  34.743  1.00   28.79  ? 198 ASN B CA  1 
ATOM   4439  C C   . ASN B  1 198 ? 65.430  45.803  33.488  1.00   28.05  ? 198 ASN B C   1 
ATOM   4440  O O   . ASN B  1 198 ? 64.297  46.229  33.512  1.00   35.98  ? 198 ASN B O   1 
ATOM   4441  C CB  . ASN B  1 198 ? 65.950  43.852  34.831  1.00   41.22  ? 198 ASN B CB  1 
ATOM   4442  C CG  . ASN B  1 198 ? 66.908  43.218  35.791  1.00   41.00  ? 198 ASN B CG  1 
ATOM   4443  O OD1 . ASN B  1 198 ? 67.898  43.819  36.194  1.00   41.63  ? 198 ASN B OD1 1 
ATOM   4444  N ND2 . ASN B  1 198 ? 66.623  41.987  36.163  1.00   40.12  ? 198 ASN B ND2 1 
ATOM   4445  N N   . GLY B  1 199 ? 66.131  45.682  32.379  1.00   26.88  ? 199 GLY B N   1 
ATOM   4446  C CA  . GLY B  1 199 ? 65.517  45.783  31.073  1.00   25.31  ? 199 GLY B CA  1 
ATOM   4447  C C   . GLY B  1 199 ? 65.535  44.380  30.521  1.00   27.17  ? 199 GLY B C   1 
ATOM   4448  O O   . GLY B  1 199 ? 65.771  43.425  31.256  1.00   26.23  ? 199 GLY B O   1 
ATOM   4449  N N   . ALA B  1 200 ? 65.285  44.228  29.232  1.00   29.16  ? 200 ALA B N   1 
ATOM   4450  C CA  . ALA B  1 200 ? 65.233  42.881  28.673  1.00   29.48  ? 200 ALA B CA  1 
ATOM   4451  C C   . ALA B  1 200 ? 65.600  42.797  27.206  1.00   29.47  ? 200 ALA B C   1 
ATOM   4452  O O   . ALA B  1 200 ? 65.579  43.792  26.478  1.00   29.38  ? 200 ALA B O   1 
ATOM   4453  C CB  . ALA B  1 200 ? 63.871  42.302  28.869  1.00   31.05  ? 200 ALA B CB  1 
ATOM   4454  N N   . ILE B  1 201 ? 65.970  41.589  26.801  1.00   27.80  ? 201 ILE B N   1 
ATOM   4455  C CA  . ILE B  1 201 ? 66.040  41.223  25.406  1.00   27.86  ? 201 ILE B CA  1 
ATOM   4456  C C   . ILE B  1 201 ? 65.046  40.122  25.133  1.00   29.39  ? 201 ILE B C   1 
ATOM   4457  O O   . ILE B  1 201 ? 64.946  39.182  25.891  1.00   30.88  ? 201 ILE B O   1 
ATOM   4458  C CB  . ILE B  1 201 ? 67.426  40.795  25.028  1.00   27.06  ? 201 ILE B CB  1 
ATOM   4459  C CG1 . ILE B  1 201 ? 68.363  41.925  25.452  1.00   30.38  ? 201 ILE B CG1 1 
ATOM   4460  C CG2 . ILE B  1 201 ? 67.500  40.565  23.538  1.00   24.65  ? 201 ILE B CG2 1 
ATOM   4461  C CD1 . ILE B  1 201 ? 69.769  41.721  25.099  1.00   31.79  ? 201 ILE B CD1 1 
ATOM   4462  N N   . LEU B  1 202 ? 64.300  40.268  24.047  1.00   29.33  ? 202 LEU B N   1 
ATOM   4463  C CA  . LEU B  1 202 ? 63.267  39.318  23.642  1.00   28.24  ? 202 LEU B CA  1 
ATOM   4464  C C   . LEU B  1 202 ? 63.666  38.655  22.339  1.00   25.85  ? 202 LEU B C   1 
ATOM   4465  O O   . LEU B  1 202 ? 64.109  39.315  21.419  1.00   26.90  ? 202 LEU B O   1 
ATOM   4466  C CB  . LEU B  1 202 ? 61.912  40.034  23.477  1.00   30.64  ? 202 LEU B CB  1 
ATOM   4467  C CG  . LEU B  1 202 ? 60.950  40.195  24.651  1.00   35.77  ? 202 LEU B CG  1 
ATOM   4468  C CD1 . LEU B  1 202 ? 61.536  41.033  25.738  1.00   36.90  ? 202 LEU B CD1 1 
ATOM   4469  C CD2 . LEU B  1 202 ? 59.684  40.864  24.137  1.00   37.57  ? 202 LEU B CD2 1 
ATOM   4470  N N   . PHE B  1 203 ? 63.507  37.351  22.257  1.00   26.56  ? 203 PHE B N   1 
ATOM   4471  C CA  . PHE B  1 203 ? 63.885  36.617  21.067  1.00   24.05  ? 203 PHE B CA  1 
ATOM   4472  C C   . PHE B  1 203 ? 62.659  35.965  20.438  1.00   24.49  ? 203 PHE B C   1 
ATOM   4473  O O   . PHE B  1 203 ? 61.960  35.210  21.078  1.00   27.51  ? 203 PHE B O   1 
ATOM   4474  C CB  . PHE B  1 203 ? 64.924  35.553  21.408  1.00   24.62  ? 203 PHE B CB  1 
ATOM   4475  C CG  . PHE B  1 203 ? 66.156  36.094  22.066  1.00   24.19  ? 203 PHE B CG  1 
ATOM   4476  C CD1 . PHE B  1 203 ? 67.222  36.529  21.306  1.00   23.24  ? 203 PHE B CD1 1 
ATOM   4477  C CD2 . PHE B  1 203 ? 66.241  36.156  23.443  1.00   23.78  ? 203 PHE B CD2 1 
ATOM   4478  C CE1 . PHE B  1 203 ? 68.335  37.022  21.907  1.00   27.24  ? 203 PHE B CE1 1 
ATOM   4479  C CE2 . PHE B  1 203 ? 67.348  36.643  24.047  1.00   23.82  ? 203 PHE B CE2 1 
ATOM   4480  C CZ  . PHE B  1 203 ? 68.396  37.079  23.290  1.00   27.55  ? 203 PHE B CZ  1 
ATOM   4481  N N   . GLY B  1 204 ? 62.391  36.267  19.180  1.00   24.61  ? 204 GLY B N   1 
ATOM   4482  C CA  . GLY B  1 204 ? 61.221  35.736  18.521  1.00   26.09  ? 204 GLY B CA  1 
ATOM   4483  C C   . GLY B  1 204 ? 60.281  36.844  18.076  1.00   28.60  ? 204 GLY B C   1 
ATOM   4484  O O   . GLY B  1 204 ? 60.563  38.010  18.289  1.00   26.70  ? 204 GLY B O   1 
ATOM   4485  N N   . ASP B  1 205 ? 59.171  36.471  17.450  1.00   33.70  ? 205 ASP B N   1 
ATOM   4486  C CA  . ASP B  1 205 ? 58.223  37.429  16.876  1.00   37.37  ? 205 ASP B CA  1 
ATOM   4487  C C   . ASP B  1 205 ? 57.312  38.046  17.905  1.00   36.99  ? 205 ASP B C   1 
ATOM   4488  O O   . ASP B  1 205 ? 56.499  37.330  18.481  1.00   37.16  ? 205 ASP B O   1 
ATOM   4489  C CB  . ASP B  1 205 ? 57.371  36.732  15.827  1.00   40.62  ? 205 ASP B CB  1 
ATOM   4490  C CG  . ASP B  1 205 ? 56.529  37.685  15.026  1.00   42.86  ? 205 ASP B CG  1 
ATOM   4491  O OD1 . ASP B  1 205 ? 56.716  38.926  15.100  1.00   44.57  ? 205 ASP B OD1 1 
ATOM   4492  O OD2 . ASP B  1 205 ? 55.707  37.166  14.264  1.00   45.28  1 205 ASP B OD2 1 
ATOM   4493  N N   . ILE B  1 206 ? 57.324  39.368  18.032  1.00   38.93  ? 206 ILE B N   1 
ATOM   4494  C CA  . ILE B  1 206 ? 56.472  40.002  19.035  1.00   44.04  ? 206 ILE B CA  1 
ATOM   4495  C C   . ILE B  1 206 ? 55.087  40.276  18.498  1.00   48.85  ? 206 ILE B C   1 
ATOM   4496  O O   . ILE B  1 206 ? 54.196  40.641  19.249  1.00   53.63  ? 206 ILE B O   1 
ATOM   4497  C CB  . ILE B  1 206 ? 57.037  41.355  19.468  1.00   41.74  ? 206 ILE B CB  1 
ATOM   4498  C CG1 . ILE B  1 206 ? 57.282  42.203  18.226  1.00   40.79  ? 206 ILE B CG1 1 
ATOM   4499  C CG2 . ILE B  1 206 ? 58.302  41.190  20.280  1.00   40.18  ? 206 ILE B CG2 1 
ATOM   4500  C CD1 . ILE B  1 206 ? 57.784  43.542  18.526  1.00   40.27  ? 206 ILE B CD1 1 
ATOM   4501  N N   . ASN B  1 207 ? 54.895  39.982  17.217  1.00   50.94  ? 207 ASN B N   1 
ATOM   4502  C CA  . ASN B  1 207 ? 53.650  40.238  16.503  1.00   52.80  ? 207 ASN B CA  1 
ATOM   4503  C C   . ASN B  1 207 ? 52.945  38.908  16.222  1.00   53.00  ? 207 ASN B C   1 
ATOM   4504  O O   . ASN B  1 207 ? 52.168  38.777  15.282  1.00   56.63  ? 207 ASN B O   1 
ATOM   4505  C CB  . ASN B  1 207 ? 53.920  40.976  15.180  1.00   56.59  ? 207 ASN B CB  1 
ATOM   4506  C CG  . ASN B  1 207 ? 54.630  42.316  15.372  1.00   59.38  ? 207 ASN B CG  1 
ATOM   4507  O OD1 . ASN B  1 207 ? 54.240  43.115  16.223  1.00   59.82  ? 207 ASN B OD1 1 
ATOM   4508  N ND2 . ASN B  1 207 ? 55.668  42.571  14.565  1.00   59.84  ? 207 ASN B ND2 1 
ATOM   4509  N N   . ASP B  1 208 ? 53.202  37.928  17.070  1.00   50.68  ? 208 ASP B N   1 
ATOM   4510  C CA  . ASP B  1 208 ? 52.669  36.587  16.914  1.00   53.37  ? 208 ASP B CA  1 
ATOM   4511  C C   . ASP B  1 208 ? 51.572  36.453  17.917  1.00   57.30  ? 208 ASP B C   1 
ATOM   4512  O O   . ASP B  1 208 ? 51.815  36.576  19.115  1.00   56.68  ? 208 ASP B O   1 
ATOM   4513  C CB  . ASP B  1 208 ? 53.736  35.520  17.148  1.00   55.02  ? 208 ASP B CB  1 
ATOM   4514  C CG  . ASP B  1 208 ? 53.197  34.094  17.009  1.00   59.22  ? 208 ASP B CG  1 
ATOM   4515  O OD1 . ASP B  1 208 ? 51.989  33.908  16.754  1.00   63.36  ? 208 ASP B OD1 1 
ATOM   4516  O OD2 . ASP B  1 208 ? 53.986  33.142  17.195  1.00   58.10  ? 208 ASP B OD2 1 
ATOM   4517  N N   . PRO B  1 209 ? 50.340  36.292  17.421  1.00   61.85  ? 209 PRO B N   1 
ATOM   4518  C CA  . PRO B  1 209 ? 49.142  36.163  18.250  1.00   63.76  ? 209 PRO B CA  1 
ATOM   4519  C C   . PRO B  1 209 ? 49.333  35.195  19.421  1.00   62.77  ? 209 PRO B C   1 
ATOM   4520  O O   . PRO B  1 209 ? 48.729  35.402  20.470  1.00   65.64  ? 209 PRO B O   1 
ATOM   4521  C CB  . PRO B  1 209 ? 48.086  35.651  17.254  1.00   68.53  ? 209 PRO B CB  1 
ATOM   4522  C CG  . PRO B  1 209 ? 48.861  35.162  16.059  1.00   67.42  ? 209 PRO B CG  1 
ATOM   4523  C CD  . PRO B  1 209 ? 50.046  36.058  15.998  1.00   63.37  ? 209 PRO B CD  1 
ATOM   4524  N N   . ASN B  1 210 ? 50.172  34.176  19.262  1.00   61.79  ? 210 ASN B N   1 
ATOM   4525  C CA  . ASN B  1 210 ? 50.471  33.260  20.362  1.00   62.50  ? 210 ASN B CA  1 
ATOM   4526  C C   . ASN B  1 210 ? 51.157  33.988  21.497  1.00   59.49  ? 210 ASN B C   1 
ATOM   4527  O O   . ASN B  1 210 ? 51.093  33.554  22.649  1.00   59.21  ? 210 ASN B O   1 
ATOM   4528  C CB  . ASN B  1 210 ? 51.371  32.112  19.921  1.00   64.63  ? 210 ASN B CB  1 
ATOM   4529  C CG  . ASN B  1 210 ? 50.680  31.158  18.995  1.00   70.49  ? 210 ASN B CG  1 
ATOM   4530  O OD1 . ASN B  1 210 ? 51.129  30.937  17.877  1.00   71.84  ? 210 ASN B OD1 1 
ATOM   4531  N ND2 . ASN B  1 210 ? 49.561  30.604  19.440  1.00   74.63  ? 210 ASN B ND2 1 
ATOM   4532  N N   . ASN B  1 211 ? 51.841  35.083  21.162  1.00   57.92  ? 211 ASN B N   1 
ATOM   4533  C CA  . ASN B  1 211 ? 52.560  35.860  22.160  1.00   55.19  ? 211 ASN B CA  1 
ATOM   4534  C C   . ASN B  1 211 ? 51.803  37.089  22.612  1.00   55.25  ? 211 ASN B C   1 
ATOM   4535  O O   . ASN B  1 211 ? 52.347  37.900  23.346  1.00   54.58  ? 211 ASN B O   1 
ATOM   4536  C CB  . ASN B  1 211 ? 53.913  36.312  21.619  1.00   50.78  ? 211 ASN B CB  1 
ATOM   4537  C CG  . ASN B  1 211 ? 54.756  35.169  21.206  1.00   47.18  ? 211 ASN B CG  1 
ATOM   4538  O OD1 . ASN B  1 211 ? 54.742  34.120  21.854  1.00   48.26  ? 211 ASN B OD1 1 
ATOM   4539  N ND2 . ASN B  1 211 ? 55.522  35.351  20.134  1.00   42.52  ? 211 ASN B ND2 1 
ATOM   4540  N N   . ASN B  1 212 ? 50.547  37.209  22.208  1.00   54.96  ? 212 ASN B N   1 
ATOM   4541  C CA  . ASN B  1 212 ? 49.777  38.398  22.535  1.00   57.39  ? 212 ASN B CA  1 
ATOM   4542  C C   . ASN B  1 212 ? 49.629  38.704  24.012  1.00   54.21  ? 212 ASN B C   1 
ATOM   4543  O O   . ASN B  1 212 ? 49.549  39.865  24.411  1.00   54.59  ? 212 ASN B O   1 
ATOM   4544  C CB  . ASN B  1 212 ? 48.370  38.309  21.965  1.00   64.66  ? 212 ASN B CB  1 
ATOM   4545  C CG  . ASN B  1 212 ? 47.581  39.563  22.242  1.00   66.65  ? 212 ASN B CG  1 
ATOM   4546  O OD1 . ASN B  1 212 ? 48.011  40.677  21.929  1.00   63.47  ? 212 ASN B OD1 1 
ATOM   4547  N ND2 . ASN B  1 212 ? 46.451  39.394  22.916  1.00   71.53  ? 212 ASN B ND2 1 
ATOM   4548  N N   . ASN B  1 213 ? 49.568  37.661  24.816  1.00   50.92  ? 213 ASN B N   1 
ATOM   4549  C CA  . ASN B  1 213 ? 49.319  37.834  26.220  1.00   50.52  ? 213 ASN B CA  1 
ATOM   4550  C C   . ASN B  1 213 ? 50.536  38.400  26.953  1.00   47.36  ? 213 ASN B C   1 
ATOM   4551  O O   . ASN B  1 213 ? 50.393  39.157  27.919  1.00   47.66  ? 213 ASN B O   1 
ATOM   4552  C CB  . ASN B  1 213 ? 48.930  36.493  26.772  1.00   56.77  ? 213 ASN B CB  1 
ATOM   4553  C CG  . ASN B  1 213 ? 47.613  36.050  26.237  1.00   66.80  ? 213 ASN B CG  1 
ATOM   4554  O OD1 . ASN B  1 213 ? 47.562  35.189  25.358  1.00   72.11  ? 213 ASN B OD1 1 
ATOM   4555  N ND2 . ASN B  1 213 ? 46.537  36.659  26.717  1.00   68.41  ? 213 ASN B ND2 1 
ATOM   4556  N N   . TYR B  1 214 ? 51.731  38.005  26.506  1.00   42.90  ? 214 TYR B N   1 
ATOM   4557  C CA  . TYR B  1 214 ? 52.963  38.510  27.106  1.00   39.46  ? 214 TYR B CA  1 
ATOM   4558  C C   . TYR B  1 214 ? 53.270  39.952  26.657  1.00   38.08  ? 214 TYR B C   1 
ATOM   4559  O O   . TYR B  1 214 ? 53.768  40.778  27.436  1.00   35.45  ? 214 TYR B O   1 
ATOM   4560  C CB  . TYR B  1 214 ? 54.155  37.585  26.792  1.00   35.24  ? 214 TYR B CB  1 
ATOM   4561  C CG  . TYR B  1 214 ? 55.375  38.006  27.581  1.00   35.46  ? 214 TYR B CG  1 
ATOM   4562  C CD1 . TYR B  1 214 ? 55.476  37.703  28.929  1.00   37.51  ? 214 TYR B CD1 1 
ATOM   4563  C CD2 . TYR B  1 214 ? 56.396  38.743  27.003  1.00   34.01  ? 214 TYR B CD2 1 
ATOM   4564  C CE1 . TYR B  1 214 ? 56.557  38.117  29.676  1.00   35.04  ? 214 TYR B CE1 1 
ATOM   4565  C CE2 . TYR B  1 214 ? 57.488  39.157  27.755  1.00   33.23  ? 214 TYR B CE2 1 
ATOM   4566  C CZ  . TYR B  1 214 ? 57.547  38.838  29.096  1.00   32.91  ? 214 TYR B CZ  1 
ATOM   4567  O OH  . TYR B  1 214 ? 58.604  39.230  29.874  1.00   32.97  ? 214 TYR B OH  1 
ATOM   4568  N N   . ILE B  1 215 ? 52.980  40.247  25.394  1.00   39.20  ? 215 ILE B N   1 
ATOM   4569  C CA  . ILE B  1 215 ? 53.325  41.546  24.847  1.00   41.96  ? 215 ILE B CA  1 
ATOM   4570  C C   . ILE B  1 215 ? 52.135  42.494  24.863  1.00   46.02  ? 215 ILE B C   1 
ATOM   4571  O O   . ILE B  1 215 ? 52.213  43.579  24.309  1.00   47.91  ? 215 ILE B O   1 
ATOM   4572  C CB  . ILE B  1 215 ? 53.916  41.441  23.404  1.00   48.88  ? 215 ILE B CB  1 
ATOM   4573  C CG1 . ILE B  1 215 ? 52.984  40.721  22.443  1.00   51.53  ? 215 ILE B CG1 1 
ATOM   4574  C CG2 . ILE B  1 215 ? 55.229  40.702  23.416  1.00   46.20  ? 215 ILE B CG2 1 
ATOM   4575  C CD1 . ILE B  1 215 ? 52.218  41.629  21.542  1.00   54.49  ? 215 ILE B CD1 1 
ATOM   4576  N N   . HIS B  1 216 ? 51.041  42.081  25.503  1.00   49.09  ? 216 HIS B N   1 
ATOM   4577  C CA  . HIS B  1 216 ? 49.808  42.864  25.528  1.00   49.82  ? 216 HIS B CA  1 
ATOM   4578  C C   . HIS B  1 216 ? 49.980  44.265  26.073  1.00   48.71  ? 216 HIS B C   1 
ATOM   4579  O O   . HIS B  1 216 ? 49.468  45.225  25.515  1.00   48.54  ? 216 HIS B O   1 
ATOM   4580  C CB  . HIS B  1 216 ? 48.755  42.164  26.371  1.00   55.57  ? 216 HIS B CB  1 
ATOM   4581  C CG  . HIS B  1 216 ? 47.463  42.901  26.410  1.00   63.34  ? 216 HIS B CG  1 
ATOM   4582  N ND1 . HIS B  1 216 ? 47.152  43.793  27.415  1.00   67.22  ? 216 HIS B ND1 1 
ATOM   4583  C CD2 . HIS B  1 216 ? 46.424  42.931  25.542  1.00   66.79  ? 216 HIS B CD2 1 
ATOM   4584  C CE1 . HIS B  1 216 ? 45.966  44.325  27.176  1.00   69.94  ? 216 HIS B CE1 1 
ATOM   4585  N NE2 . HIS B  1 216 ? 45.503  43.819  26.045  1.00   69.54  ? 216 HIS B NE2 1 
ATOM   4586  N N   . ASN B  1 217 ? 50.744  44.390  27.143  1.00   50.29  ? 217 ASN B N   1 
ATOM   4587  C CA  . ASN B  1 217 ? 50.966  45.684  27.753  1.00   53.36  ? 217 ASN B CA  1 
ATOM   4588  C C   . ASN B  1 217 ? 51.813  46.664  26.913  1.00   54.92  ? 217 ASN B C   1 
ATOM   4589  O O   . ASN B  1 217 ? 51.848  47.856  27.203  1.00   60.31  ? 217 ASN B O   1 
ATOM   4590  C CB  . ASN B  1 217 ? 51.614  45.479  29.119  1.00   52.90  ? 217 ASN B CB  1 
ATOM   4591  C CG  . ASN B  1 217 ? 51.813  46.773  29.862  1.00   53.78  ? 217 ASN B CG  1 
ATOM   4592  O OD1 . ASN B  1 217 ? 50.846  47.430  30.262  1.00   56.73  ? 217 ASN B OD1 1 
ATOM   4593  N ND2 . ASN B  1 217 ? 53.073  47.170  30.029  1.00   50.74  ? 217 ASN B ND2 1 
ATOM   4594  N N   . SER B  1 218 ? 52.477  46.182  25.865  1.00   49.14  ? 218 SER B N   1 
ATOM   4595  C CA  . SER B  1 218 ? 53.349  47.032  25.055  1.00   38.46  ? 218 SER B CA  1 
ATOM   4596  C C   . SER B  1 218 ? 52.718  47.459  23.733  1.00   37.85  ? 218 SER B C   1 
ATOM   4597  O O   . SER B  1 218 ? 53.382  48.032  22.874  1.00   37.37  ? 218 SER B O   1 
ATOM   4598  C CB  . SER B  1 218 ? 54.637  46.309  24.755  1.00   35.77  ? 218 SER B CB  1 
ATOM   4599  O OG  . SER B  1 218 ? 54.450  45.393  23.701  1.00   35.63  ? 218 SER B OG  1 
ATOM   4600  N N   . LEU B  1 219 ? 51.437  47.161  23.567  1.00   38.76  ? 219 LEU B N   1 
ATOM   4601  C CA  . LEU B  1 219 ? 50.787  47.282  22.273  1.00   42.98  ? 219 LEU B CA  1 
ATOM   4602  C C   . LEU B  1 219 ? 50.690  48.708  21.718  1.00   42.92  ? 219 LEU B C   1 
ATOM   4603  O O   . LEU B  1 219 ? 50.825  48.897  20.513  1.00   42.39  ? 219 LEU B O   1 
ATOM   4604  C CB  . LEU B  1 219 ? 49.387  46.643  22.360  1.00   47.28  ? 219 LEU B CB  1 
ATOM   4605  C CG  . LEU B  1 219 ? 49.409  45.107  22.292  1.00   44.88  ? 219 LEU B CG  1 
ATOM   4606  C CD1 . LEU B  1 219 ? 48.045  44.494  22.541  1.00   46.64  ? 219 LEU B CD1 1 
ATOM   4607  C CD2 . LEU B  1 219 ? 49.977  44.640  20.957  1.00   43.23  ? 219 LEU B CD2 1 
ATOM   4608  N N   . ASP B  1 220 ? 50.520  49.709  22.576  1.00   44.23  ? 220 ASP B N   1 
ATOM   4609  C CA  . ASP B  1 220 ? 50.426  51.087  22.091  1.00   48.67  ? 220 ASP B CA  1 
ATOM   4610  C C   . ASP B  1 220 ? 51.760  51.516  21.515  1.00   47.22  ? 220 ASP B C   1 
ATOM   4611  O O   . ASP B  1 220 ? 51.809  52.242  20.527  1.00   48.96  ? 220 ASP B O   1 
ATOM   4612  C CB  . ASP B  1 220 ? 50.003  52.053  23.197  1.00   55.17  ? 220 ASP B CB  1 
ATOM   4613  C CG  . ASP B  1 220 ? 48.585  51.808  23.683  1.00   65.06  ? 220 ASP B CG  1 
ATOM   4614  O OD1 . ASP B  1 220 ? 47.689  51.543  22.855  1.00   64.87  ? 220 ASP B OD1 1 
ATOM   4615  O OD2 . ASP B  1 220 ? 48.354  51.900  24.902  1.00   71.38  ? 220 ASP B OD2 1 
ATOM   4616  N N   . VAL B  1 221 ? 52.841  51.069  22.141  1.00   43.38  ? 221 VAL B N   1 
ATOM   4617  C CA  . VAL B  1 221 ? 54.181  51.333  21.639  1.00   37.94  ? 221 VAL B CA  1 
ATOM   4618  C C   . VAL B  1 221 ? 54.438  50.695  20.277  1.00   36.07  ? 221 VAL B C   1 
ATOM   4619  O O   . VAL B  1 221 ? 54.987  51.322  19.375  1.00   34.76  ? 221 VAL B O   1 
ATOM   4620  C CB  . VAL B  1 221 ? 55.232  50.818  22.629  1.00   39.84  ? 221 VAL B CB  1 
ATOM   4621  C CG1 . VAL B  1 221 ? 56.642  51.111  22.130  1.00   37.88  ? 221 VAL B CG1 1 
ATOM   4622  C CG2 . VAL B  1 221 ? 55.006  51.439  23.983  1.00   42.60  ? 221 VAL B CG2 1 
ATOM   4623  N N   . LEU B  1 222 ? 54.043  49.436  20.133  1.00   38.23  ? 222 LEU B N   1 
ATOM   4624  C CA  . LEU B  1 222 ? 54.300  48.696  18.906  1.00   39.57  ? 222 LEU B CA  1 
ATOM   4625  C C   . LEU B  1 222 ? 53.596  49.277  17.690  1.00   45.03  ? 222 LEU B C   1 
ATOM   4626  O O   . LEU B  1 222 ? 54.112  49.183  16.573  1.00   44.95  ? 222 LEU B O   1 
ATOM   4627  C CB  . LEU B  1 222 ? 53.884  47.233  19.060  1.00   39.13  ? 222 LEU B CB  1 
ATOM   4628  C CG  . LEU B  1 222 ? 54.606  46.376  20.096  1.00   37.82  ? 222 LEU B CG  1 
ATOM   4629  C CD1 . LEU B  1 222 ? 54.140  44.935  20.070  1.00   35.96  ? 222 LEU B CD1 1 
ATOM   4630  C CD2 . LEU B  1 222 ? 56.093  46.458  19.905  1.00   36.31  ? 222 LEU B CD2 1 
ATOM   4631  N N   . HIS B  1 223 ? 52.398  49.812  17.904  1.00   49.44  ? 223 HIS B N   1 
ATOM   4632  C CA  . HIS B  1 223 ? 51.596  50.427  16.849  1.00   52.89  ? 223 HIS B CA  1 
ATOM   4633  C C   . HIS B  1 223 ? 52.258  51.654  16.250  1.00   51.94  ? 223 HIS B C   1 
ATOM   4634  O O   . HIS B  1 223 ? 51.943  52.037  15.125  1.00   54.17  ? 223 HIS B O   1 
ATOM   4635  C CB  . HIS B  1 223 ? 50.210  50.781  17.369  1.00   57.41  ? 223 HIS B CB  1 
ATOM   4636  C CG  . HIS B  1 223 ? 49.404  49.584  17.780  1.00   60.25  ? 223 HIS B CG  1 
ATOM   4637  N ND1 . HIS B  1 223 ? 48.264  49.686  18.549  0.0000 61.81  ? 223 HIS B ND1 1 
ATOM   4638  C CD2 . HIS B  1 223 ? 49.581  48.264  17.541  0.0000 58.52  ? 223 HIS B CD2 1 
ATOM   4639  C CE1 . HIS B  1 223 ? 47.771  48.479  18.760  0.0000 61.96  ? 223 HIS B CE1 1 
ATOM   4640  N NE2 . HIS B  1 223 ? 48.550  47.598  18.159  0.0000 60.01  ? 223 HIS B NE2 1 
ATOM   4641  N N   . ASP B  1 224 ? 53.099  52.314  17.042  1.00   49.98  ? 224 ASP B N   1 
ATOM   4642  C CA  . ASP B  1 224 ? 53.758  53.554  16.624  1.00   47.94  ? 224 ASP B CA  1 
ATOM   4643  C C   . ASP B  1 224 ? 55.221  53.369  16.264  1.00   42.04  ? 224 ASP B C   1 
ATOM   4644  O O   . ASP B  1 224 ? 55.956  54.337  16.168  1.00   39.15  ? 224 ASP B O   1 
ATOM   4645  C CB  . ASP B  1 224 ? 53.674  54.619  17.706  1.00   48.15  ? 224 ASP B CB  1 
ATOM   4646  C CG  . ASP B  1 224 ? 52.280  55.032  17.986  1.00   49.08  ? 224 ASP B CG  1 
ATOM   4647  O OD1 . ASP B  1 224 ? 51.433  54.851  17.094  1.00   48.88  ? 224 ASP B OD1 1 
ATOM   4648  O OD2 . ASP B  1 224 ? 52.040  55.556  19.087  1.00   49.06  1 224 ASP B OD2 1 
ATOM   4649  N N   . LEU B  1 225 ? 55.660  52.127  16.130  1.00   41.07  ? 225 LEU B N   1 
ATOM   4650  C CA  . LEU B  1 225 ? 57.045  51.855  15.740  1.00   37.46  ? 225 LEU B CA  1 
ATOM   4651  C C   . LEU B  1 225 ? 57.369  52.436  14.375  1.00   34.84  ? 225 LEU B C   1 
ATOM   4652  O O   . LEU B  1 225 ? 56.540  52.439  13.472  1.00   37.26  ? 225 LEU B O   1 
ATOM   4653  C CB  . LEU B  1 225 ? 57.328  50.354  15.737  1.00   36.29  ? 225 LEU B CB  1 
ATOM   4654  C CG  . LEU B  1 225 ? 57.555  49.588  17.038  1.00   35.85  ? 225 LEU B CG  1 
ATOM   4655  C CD1 . LEU B  1 225 ? 58.052  48.211  16.701  1.00   38.41  ? 225 LEU B CD1 1 
ATOM   4656  C CD2 . LEU B  1 225 ? 58.560  50.266  17.956  1.00   33.10  ? 225 LEU B CD2 1 
ATOM   4657  N N   . VAL B  1 226 ? 58.583  52.942  14.250  1.00   35.08  ? 226 VAL B N   1 
ATOM   4658  C CA  . VAL B  1 226 ? 59.095  53.496  13.005  1.00   35.86  ? 226 VAL B CA  1 
ATOM   4659  C C   . VAL B  1 226 ? 60.274  52.628  12.547  1.00   33.32  ? 226 VAL B C   1 
ATOM   4660  O O   . VAL B  1 226 ? 61.048  52.172  13.385  1.00   35.04  ? 226 VAL B O   1 
ATOM   4661  C CB  . VAL B  1 226 ? 59.543  54.965  13.204  1.00   37.08  ? 226 VAL B CB  1 
ATOM   4662  C CG1 . VAL B  1 226 ? 60.350  55.443  12.020  1.00   39.67  ? 226 VAL B CG1 1 
ATOM   4663  C CG2 . VAL B  1 226 ? 58.354  55.847  13.357  1.00   40.91  ? 226 VAL B CG2 1 
ATOM   4664  N N   . TYR B  1 227 ? 60.405  52.375  11.244  1.00   32.28  ? 227 TYR B N   1 
ATOM   4665  C CA  . TYR B  1 227 ? 61.448  51.487  10.725  1.00   30.97  ? 227 TYR B CA  1 
ATOM   4666  C C   . TYR B  1 227 ? 62.471  52.163  9.811   1.00   30.63  ? 227 TYR B C   1 
ATOM   4667  O O   . TYR B  1 227 ? 62.151  53.141  9.153   1.00   34.55  ? 227 TYR B O   1 
ATOM   4668  C CB  . TYR B  1 227 ? 60.801  50.300  9.988   1.00   34.22  ? 227 TYR B CB  1 
ATOM   4669  C CG  . TYR B  1 227 ? 60.079  49.359  10.927  1.00   37.07  ? 227 TYR B CG  1 
ATOM   4670  C CD1 . TYR B  1 227 ? 60.769  48.351  11.574  1.00   39.67  ? 227 TYR B CD1 1 
ATOM   4671  C CD2 . TYR B  1 227 ? 58.736  49.513  11.211  1.00   42.95  ? 227 TYR B CD2 1 
ATOM   4672  C CE1 . TYR B  1 227 ? 60.151  47.513  12.451  1.00   45.08  ? 227 TYR B CE1 1 
ATOM   4673  C CE2 . TYR B  1 227 ? 58.104  48.667  12.085  1.00   48.04  ? 227 TYR B CE2 1 
ATOM   4674  C CZ  . TYR B  1 227 ? 58.819  47.672  12.700  1.00   51.79  ? 227 TYR B CZ  1 
ATOM   4675  O OH  . TYR B  1 227 ? 58.200  46.816  13.573  1.00   60.79  ? 227 TYR B OH  1 
ATOM   4676  N N   . THR B  1 228 ? 63.698  51.629  9.788   1.00   29.45  ? 228 THR B N   1 
ATOM   4677  C CA  . THR B  1 228 ? 64.751  52.074  8.871   1.00   29.80  ? 228 THR B CA  1 
ATOM   4678  C C   . THR B  1 228 ? 65.607  50.857  8.478   1.00   29.36  ? 228 THR B C   1 
ATOM   4679  O O   . THR B  1 228 ? 65.741  49.919  9.261   1.00   30.30  ? 228 THR B O   1 
ATOM   4680  C CB  . THR B  1 228 ? 65.633  53.212  9.502   1.00   32.93  ? 228 THR B CB  1 
ATOM   4681  O OG1 . THR B  1 228 ? 66.493  53.801  8.513   1.00   32.09  ? 228 THR B OG1 1 
ATOM   4682  C CG2 . THR B  1 228 ? 66.481  52.681  10.627  1.00   29.58  ? 228 THR B CG2 1 
ATOM   4683  N N   . PRO B  1 229 ? 66.177  50.857  7.253   1.00   28.04  ? 229 PRO B N   1 
ATOM   4684  C CA  . PRO B  1 229 ? 66.940  49.685  6.796   1.00   29.14  ? 229 PRO B CA  1 
ATOM   4685  C C   . PRO B  1 229 ? 68.188  49.386  7.630   1.00   27.40  ? 229 PRO B C   1 
ATOM   4686  O O   . PRO B  1 229 ? 68.871  50.273  8.112   1.00   25.50  ? 229 PRO B O   1 
ATOM   4687  C CB  . PRO B  1 229 ? 67.319  50.059  5.351   1.00   27.23  ? 229 PRO B CB  1 
ATOM   4688  C CG  . PRO B  1 229 ? 66.290  51.012  4.938   1.00   25.41  ? 229 PRO B CG  1 
ATOM   4689  C CD  . PRO B  1 229 ? 65.995  51.828  6.162   1.00   25.06  ? 229 PRO B CD  1 
ATOM   4690  N N   . LEU B  1 230 ? 68.445  48.098  7.817   1.00   29.47  ? 230 LEU B N   1 
ATOM   4691  C CA  . LEU B  1 230 ? 69.578  47.629  8.581   1.00   26.71  ? 230 LEU B CA  1 
ATOM   4692  C C   . LEU B  1 230 ? 70.623  47.070  7.647   1.00   28.60  ? 230 LEU B C   1 
ATOM   4693  O O   . LEU B  1 230 ? 70.296  46.298  6.765   1.00   31.16  ? 230 LEU B O   1 
ATOM   4694  C CB  . LEU B  1 230 ? 69.129  46.565  9.565   1.00   25.49  ? 230 LEU B CB  1 
ATOM   4695  C CG  . LEU B  1 230 ? 70.132  45.886  10.463  1.00   24.10  ? 230 LEU B CG  1 
ATOM   4696  C CD1 . LEU B  1 230 ? 70.735  46.889  11.403  1.00   21.16  ? 230 LEU B CD1 1 
ATOM   4697  C CD2 . LEU B  1 230 ? 69.344  44.833  11.192  1.00   24.86  ? 230 LEU B CD2 1 
ATOM   4698  N N   . THR B  1 231 ? 71.875  47.485  7.814   1.00   29.50  ? 231 THR B N   1 
ATOM   4699  C CA  . THR B  1 231 ? 72.970  46.923  7.036   1.00   28.86  ? 231 THR B CA  1 
ATOM   4700  C C   . THR B  1 231 ? 73.975  46.341  7.987   1.00   27.30  ? 231 THR B C   1 
ATOM   4701  O O   . THR B  1 231 ? 74.093  46.779  9.126   1.00   26.57  ? 231 THR B O   1 
ATOM   4702  C CB  . THR B  1 231 ? 73.671  47.969  6.122   1.00   31.76  ? 231 THR B CB  1 
ATOM   4703  O OG1 . THR B  1 231 ? 73.884  49.184  6.843   1.00   30.06  ? 231 THR B OG1 1 
ATOM   4704  C CG2 . THR B  1 231 ? 72.827  48.280  4.915   1.00   31.07  ? 231 THR B CG2 1 
ATOM   4705  N N   . ILE B  1 232 ? 74.695  45.349  7.501   1.00   27.64  ? 232 ILE B N   1 
ATOM   4706  C CA  . ILE B  1 232 ? 75.587  44.572  8.332   1.00   26.06  ? 232 ILE B CA  1 
ATOM   4707  C C   . ILE B  1 232 ? 76.973  44.611  7.724   1.00   24.73  ? 232 ILE B C   1 
ATOM   4708  O O   . ILE B  1 232 ? 77.127  44.383  6.535   1.00   26.40  ? 232 ILE B O   1 
ATOM   4709  C CB  . ILE B  1 232 ? 75.104  43.121  8.436   1.00   25.15  ? 232 ILE B CB  1 
ATOM   4710  C CG1 . ILE B  1 232 ? 73.637  43.090  8.844   1.00   23.59  ? 232 ILE B CG1 1 
ATOM   4711  C CG2 . ILE B  1 232 ? 75.951  42.349  9.416   1.00   23.11  ? 232 ILE B CG2 1 
ATOM   4712  C CD1 . ILE B  1 232 ? 73.388  43.675  10.220  1.00   22.28  ? 232 ILE B CD1 1 
ATOM   4713  N N   . SER B  1 233 ? 77.978  44.923  8.526   1.00   24.78  ? 233 SER B N   1 
ATOM   4714  C CA  . SER B  1 233 ? 79.360  44.927  8.049   1.00   27.64  ? 233 SER B CA  1 
ATOM   4715  C C   . SER B  1 233 ? 79.944  43.514  7.913   1.00   29.31  ? 233 SER B C   1 
ATOM   4716  O O   . SER B  1 233 ? 79.357  42.549  8.401   1.00   30.28  ? 233 SER B O   1 
ATOM   4717  C CB  . SER B  1 233 ? 80.235  45.718  9.003   1.00   29.57  ? 233 SER B CB  1 
ATOM   4718  O OG  . SER B  1 233 ? 80.446  44.981  10.199  1.00   29.28  ? 233 SER B OG  1 
ATOM   4719  N N   . LYS B  1 234 ? 81.125  43.403  7.309   1.00   29.33  ? 234 LYS B N   1 
ATOM   4720  C CA  . LYS B  1 234 ? 81.788  42.113  7.138   1.00   29.95  ? 234 LYS B CA  1 
ATOM   4721  C C   . LYS B  1 234 ? 82.116  41.503  8.472   1.00   29.75  ? 234 LYS B C   1 
ATOM   4722  O O   . LYS B  1 234 ? 82.400  40.313  8.563   1.00   32.06  ? 234 LYS B O   1 
ATOM   4723  C CB  . LYS B  1 234 ? 83.086  42.256  6.367   1.00   34.39  ? 234 LYS B CB  1 
ATOM   4724  C CG  . LYS B  1 234 ? 82.915  42.756  4.988   1.00   41.74  ? 234 LYS B CG  1 
ATOM   4725  C CD  . LYS B  1 234 ? 84.268  42.991  4.362   1.00   51.79  ? 234 LYS B CD  1 
ATOM   4726  C CE  . LYS B  1 234 ? 84.127  43.761  3.057   1.00   60.12  ? 234 LYS B CE  1 
ATOM   4727  N NZ  . LYS B  1 234 ? 85.421  44.408  2.687   1.00   65.27  ? 234 LYS B NZ  1 
ATOM   4728  N N   . GLN B  1 235 ? 82.078  42.306  9.522   1.00   29.77  ? 235 GLN B N   1 
ATOM   4729  C CA  . GLN B  1 235 ? 82.402  41.775  10.828  1.00   31.33  ? 235 GLN B CA  1 
ATOM   4730  C C   . GLN B  1 235 ? 81.172  41.421  11.654  1.00   29.13  ? 235 GLN B C   1 
ATOM   4731  O O   . GLN B  1 235 ? 81.298  40.977  12.789  1.00   29.63  ? 235 GLN B O   1 
ATOM   4732  C CB  . GLN B  1 235 ? 83.261  42.782  11.589  1.00   39.30  ? 235 GLN B CB  1 
ATOM   4733  C CG  . GLN B  1 235 ? 84.666  42.919  11.048  1.00   46.84  ? 235 GLN B CG  1 
ATOM   4734  C CD  . GLN B  1 235 ? 85.439  41.604  11.094  1.00   57.36  ? 235 GLN B CD  1 
ATOM   4735  O OE1 . GLN B  1 235 ? 85.316  40.818  12.038  1.00   59.67  ? 235 GLN B OE1 1 
ATOM   4736  N NE2 . GLN B  1 235 ? 86.240  41.356  10.058  1.00   62.39  ? 235 GLN B NE2 1 
ATOM   4737  N N   . GLY B  1 236 ? 79.991  41.568  11.069  1.00   28.81  ? 236 GLY B N   1 
ATOM   4738  C CA  . GLY B  1 236 ? 78.754  41.196  11.741  1.00   31.05  ? 236 GLY B CA  1 
ATOM   4739  C C   . GLY B  1 236 ? 78.124  42.286  12.613  1.00   30.14  ? 236 GLY B C   1 
ATOM   4740  O O   . GLY B  1 236 ? 77.267  42.009  13.457  1.00   28.47  ? 236 GLY B O   1 
ATOM   4741  N N   . GLU B  1 237 ? 78.534  43.534  12.397  1.00   28.20  ? 237 GLU B N   1 
ATOM   4742  C CA  . GLU B  1 237 ? 78.035  44.669  13.173  1.00   23.05  ? 237 GLU B CA  1 
ATOM   4743  C C   . GLU B  1 237 ? 76.784  45.272  12.574  1.00   23.55  ? 237 GLU B C   1 
ATOM   4744  O O   . GLU B  1 237 ? 76.595  45.237  11.362  1.00   24.41  ? 237 GLU B O   1 
ATOM   4745  C CB  . GLU B  1 237 ? 79.102  45.760  13.276  1.00   22.52  ? 237 GLU B CB  1 
ATOM   4746  C CG  . GLU B  1 237 ? 80.421  45.330  13.858  1.00   24.56  ? 237 GLU B CG  1 
ATOM   4747  C CD  . GLU B  1 237 ? 81.579  46.192  13.370  1.00   29.30  ? 237 GLU B CD  1 
ATOM   4748  O OE1 . GLU B  1 237 ? 81.873  46.203  12.156  1.00   31.47  ? 237 GLU B OE1 1 
ATOM   4749  O OE2 . GLU B  1 237 ? 82.193  46.868  14.201  1.00   29.09  1 237 GLU B OE2 1 
ATOM   4750  N N   . TYR B  1 238 ? 75.959  45.871  13.432  1.00   25.59  ? 238 TYR B N   1 
ATOM   4751  C CA  . TYR B  1 238 ? 74.700  46.488  13.021  1.00   21.97  ? 238 TYR B CA  1 
ATOM   4752  C C   . TYR B  1 238 ? 74.873  47.966  12.659  1.00   22.20  ? 238 TYR B C   1 
ATOM   4753  O O   . TYR B  1 238 ? 75.390  48.738  13.452  1.00   23.70  ? 238 TYR B O   1 
ATOM   4754  C CB  . TYR B  1 238 ? 73.672  46.321  14.143  1.00   21.46  ? 238 TYR B CB  1 
ATOM   4755  C CG  . TYR B  1 238 ? 73.385  44.862  14.469  1.00   20.10  ? 238 TYR B CG  1 
ATOM   4756  C CD1 . TYR B  1 238 ? 72.622  44.095  13.628  1.00   22.25  ? 238 TYR B CD1 1 
ATOM   4757  C CD2 . TYR B  1 238 ? 73.857  44.269  15.633  1.00   20.62  ? 238 TYR B CD2 1 
ATOM   4758  C CE1 . TYR B  1 238 ? 72.354  42.753  13.910  1.00   23.55  ? 238 TYR B CE1 1 
ATOM   4759  C CE2 . TYR B  1 238 ? 73.589  42.928  15.928  1.00   21.59  ? 238 TYR B CE2 1 
ATOM   4760  C CZ  . TYR B  1 238 ? 72.835  42.173  15.061  1.00   21.86  ? 238 TYR B CZ  1 
ATOM   4761  O OH  . TYR B  1 238 ? 72.567  40.826  15.306  1.00   23.15  ? 238 TYR B OH  1 
ATOM   4762  N N   . PHE B  1 239 ? 74.446  48.343  11.455  1.00   22.33  ? 239 PHE B N   1 
ATOM   4763  C CA  . PHE B  1 239 ? 74.534  49.718  10.986  1.00   24.29  ? 239 PHE B CA  1 
ATOM   4764  C C   . PHE B  1 239 ? 73.206  50.239  10.482  1.00   25.46  ? 239 PHE B C   1 
ATOM   4765  O O   . PHE B  1 239 ? 72.458  49.503  9.879   1.00   26.20  ? 239 PHE B O   1 
ATOM   4766  C CB  . PHE B  1 239 ? 75.555  49.833  9.854   1.00   26.74  ? 239 PHE B CB  1 
ATOM   4767  C CG  . PHE B  1 239 ? 76.977  49.871  10.328  1.00   27.52  ? 239 PHE B CG  1 
ATOM   4768  C CD1 . PHE B  1 239 ? 77.664  48.705  10.589  1.00   28.32  ? 239 PHE B CD1 1 
ATOM   4769  C CD2 . PHE B  1 239 ? 77.628  51.080  10.501  1.00   28.91  ? 239 PHE B CD2 1 
ATOM   4770  C CE1 . PHE B  1 239 ? 78.970  48.738  11.049  1.00   28.13  ? 239 PHE B CE1 1 
ATOM   4771  C CE2 . PHE B  1 239 ? 78.936  51.124  10.940  1.00   30.38  ? 239 PHE B CE2 1 
ATOM   4772  C CZ  . PHE B  1 239 ? 79.609  49.948  11.211  1.00   30.02  ? 239 PHE B CZ  1 
ATOM   4773  N N   . ILE B  1 240 ? 72.931  51.525  10.700  1.00   26.65  ? 240 ILE B N   1 
ATOM   4774  C CA  . ILE B  1 240 ? 71.837  52.214  9.995   1.00   29.04  ? 240 ILE B CA  1 
ATOM   4775  C C   . ILE B  1 240 ? 72.385  53.455  9.321   1.00   28.85  ? 240 ILE B C   1 
ATOM   4776  O O   . ILE B  1 240 ? 73.511  53.848  9.574   1.00   31.64  ? 240 ILE B O   1 
ATOM   4777  C CB  . ILE B  1 240 ? 70.675  52.622  10.929  1.00   24.94  ? 240 ILE B CB  1 
ATOM   4778  C CG1 . ILE B  1 240 ? 71.183  53.453  12.088  1.00   25.16  ? 240 ILE B CG1 1 
ATOM   4779  C CG2 . ILE B  1 240 ? 69.977  51.403  11.458  1.00   26.18  ? 240 ILE B CG2 1 
ATOM   4780  C CD1 . ILE B  1 240 ? 70.075  54.033  12.941  1.00   27.29  ? 240 ILE B CD1 1 
ATOM   4781  N N   . GLN B  1 241 ? 71.591  54.072  8.462   1.00   29.26  ? 241 GLN B N   1 
ATOM   4782  C CA  . GLN B  1 241 ? 72.066  55.232  7.742   1.00   29.23  ? 241 GLN B CA  1 
ATOM   4783  C C   . GLN B  1 241 ? 71.488  56.525  8.349   1.00   28.95  ? 241 GLN B C   1 
ATOM   4784  O O   . GLN B  1 241 ? 70.281  56.716  8.454   1.00   29.95  ? 241 GLN B O   1 
ATOM   4785  C CB  . GLN B  1 241 ? 71.744  55.082  6.250   1.00   33.11  ? 241 GLN B CB  1 
ATOM   4786  C CG  . GLN B  1 241 ? 72.039  56.309  5.394   1.00   41.11  ? 241 GLN B CG  1 
ATOM   4787  C CD  . GLN B  1 241 ? 73.500  56.791  5.469   1.00   45.98  ? 241 GLN B CD  1 
ATOM   4788  O OE1 . GLN B  1 241 ? 74.420  56.029  5.792   1.00   45.15  ? 241 GLN B OE1 1 
ATOM   4789  N NE2 . GLN B  1 241 ? 73.708  58.071  5.156   1.00   47.98  ? 241 GLN B NE2 1 
ATOM   4790  N N   . VAL B  1 242 ? 72.384  57.384  8.812   1.00   27.78  ? 242 VAL B N   1 
ATOM   4791  C CA  . VAL B  1 242 ? 72.019  58.697  9.294   1.00   27.14  ? 242 VAL B CA  1 
ATOM   4792  C C   . VAL B  1 242 ? 72.488  59.711  8.248   1.00   32.14  ? 242 VAL B C   1 
ATOM   4793  O O   . VAL B  1 242 ? 73.690  59.864  8.034   1.00   34.64  ? 242 VAL B O   1 
ATOM   4794  C CB  . VAL B  1 242 ? 72.661  58.971  10.639  1.00   25.28  ? 242 VAL B CB  1 
ATOM   4795  C CG1 . VAL B  1 242 ? 72.324  60.352  11.123  1.00   25.17  ? 242 VAL B CG1 1 
ATOM   4796  C CG2 . VAL B  1 242 ? 72.189  57.924  11.641  1.00   27.49  ? 242 VAL B CG2 1 
ATOM   4797  N N   . ASN B  1 243 ? 71.552  60.372  7.573   1.00   30.59  ? 243 ASN B N   1 
ATOM   4798  C CA  . ASN B  1 243 ? 71.889  61.346  6.557   1.00   32.87  ? 243 ASN B CA  1 
ATOM   4799  C C   . ASN B  1 243 ? 72.371  62.658  7.153   1.00   34.58  ? 243 ASN B C   1 
ATOM   4800  O O   . ASN B  1 243 ? 73.178  63.357  6.550   1.00   36.79  ? 243 ASN B O   1 
ATOM   4801  C CB  . ASN B  1 243 ? 70.676  61.620  5.679   1.00   36.22  ? 243 ASN B CB  1 
ATOM   4802  C CG  . ASN B  1 243 ? 70.500  60.591  4.610   1.00   37.75  ? 243 ASN B CG  1 
ATOM   4803  O OD1 . ASN B  1 243 ? 71.267  59.649  4.518   1.00   38.91  ? 243 ASN B OD1 1 
ATOM   4804  N ND2 . ASN B  1 243 ? 69.484  60.759  3.791   1.00   40.03  ? 243 ASN B ND2 1 
ATOM   4805  N N   . ALA B  1 244 ? 71.865  63.000  8.334   1.00   32.24  ? 244 ALA B N   1 
ATOM   4806  C CA  . ALA B  1 244 ? 72.217  64.261  8.981   1.00   32.31  ? 244 ALA B CA  1 
ATOM   4807  C C   . ALA B  1 244 ? 71.838  64.225  10.436  1.00   31.88  ? 244 ALA B C   1 
ATOM   4808  O O   . ALA B  1 244 ? 70.999  63.433  10.827  1.00   32.54  ? 244 ALA B O   1 
ATOM   4809  C CB  . ALA B  1 244 ? 71.527  65.426  8.301   1.00   33.64  ? 244 ALA B CB  1 
ATOM   4810  N N   . ILE B  1 245 ? 72.479  65.066  11.232  1.00   36.80  ? 245 ILE B N   1 
ATOM   4811  C CA  . ILE B  1 245 ? 72.010  65.393  12.577  1.00   36.71  ? 245 ILE B CA  1 
ATOM   4812  C C   . ILE B  1 245 ? 71.405  66.801  12.587  1.00   36.74  ? 245 ILE B C   1 
ATOM   4813  O O   . ILE B  1 245 ? 72.053  67.771  12.187  1.00   37.20  ? 245 ILE B O   1 
ATOM   4814  C CB  . ILE B  1 245 ? 73.126  65.319  13.619  1.00   35.15  ? 245 ILE B CB  1 
ATOM   4815  C CG1 . ILE B  1 245 ? 73.839  63.982  13.513  1.00   35.08  ? 245 ILE B CG1 1 
ATOM   4816  C CG2 . ILE B  1 245 ? 72.563  65.538  15.011  1.00   33.62  ? 245 ILE B CG2 1 
ATOM   4817  C CD1 . ILE B  1 245 ? 75.115  63.965  14.265  1.00   38.57  ? 245 ILE B CD1 1 
ATOM   4818  N N   . ARG B  1 246 ? 70.143  66.894  12.995  1.00   35.51  ? 246 ARG B N   1 
ATOM   4819  C CA  . ARG B  1 246 ? 69.434  68.163  13.025  1.00   38.15  ? 246 ARG B CA  1 
ATOM   4820  C C   . ARG B  1 246 ? 69.403  68.758  14.416  1.00   39.34  ? 246 ARG B C   1 
ATOM   4821  O O   . ARG B  1 246 ? 68.961  68.108  15.357  1.00   38.37  ? 246 ARG B O   1 
ATOM   4822  C CB  . ARG B  1 246 ? 68.005  67.993  12.560  1.00   38.60  ? 246 ARG B CB  1 
ATOM   4823  C CG  . ARG B  1 246 ? 67.224  69.286  12.621  1.00   52.35  ? 246 ARG B CG  1 
ATOM   4824  C CD  . ARG B  1 246 ? 65.769  68.953  12.802  1.00   53.74  ? 246 ARG B CD  1 
ATOM   4825  N NE  . ARG B  1 246 ? 65.093  68.478  11.605  1.00   52.08  ? 246 ARG B NE  1 
ATOM   4826  C CZ  . ARG B  1 246 ? 64.121  67.569  11.620  1.00   49.25  ? 246 ARG B CZ  1 
ATOM   4827  N NH1 . ARG B  1 246 ? 63.764  66.994  12.767  1.00   46.67  ? 246 ARG B NH1 1 
ATOM   4828  N NH2 . ARG B  1 246 ? 63.539  67.198  10.484  1.00   49.69  ? 246 ARG B NH2 1 
ATOM   4829  N N   . VAL B  1 247 ? 69.828  70.009  14.538  1.00   41.70  ? 247 VAL B N   1 
ATOM   4830  C CA  . VAL B  1 247 ? 69.678  70.740  15.790  1.00   45.30  ? 247 VAL B CA  1 
ATOM   4831  C C   . VAL B  1 247 ? 68.901  72.024  15.533  1.00   48.17  ? 247 VAL B C   1 
ATOM   4832  O O   . VAL B  1 247 ? 69.429  72.991  14.985  1.00   48.47  ? 247 VAL B O   1 
ATOM   4833  C CB  . VAL B  1 247 ? 71.044  71.076  16.424  1.00   46.74  ? 247 VAL B CB  1 
ATOM   4834  C CG1 . VAL B  1 247 ? 70.846  71.788  17.750  1.00   51.27  ? 247 VAL B CG1 1 
ATOM   4835  C CG2 . VAL B  1 247 ? 71.872  69.833  16.604  1.00   41.22  ? 247 VAL B CG2 1 
ATOM   4836  N N   . ASN B  1 248 ? 67.656  72.038  15.977  1.00   40.89  ? 248 ASN B N   1 
ATOM   4837  C CA  . ASN B  1 248 ? 66.728  73.078  15.582  1.00   44.50  ? 248 ASN B CA  1 
ATOM   4838  C C   . ASN B  1 248 ? 66.677  73.175  14.048  1.00   42.13  ? 248 ASN B C   1 
ATOM   4839  O O   . ASN B  1 248 ? 66.196  72.248  13.424  1.00   45.76  ? 248 ASN B O   1 
ATOM   4840  C CB  . ASN B  1 248 ? 67.106  74.395  16.240  1.00   53.16  ? 248 ASN B CB  1 
ATOM   4841  C CG  . ASN B  1 248 ? 66.874  74.382  17.761  1.00   57.23  ? 248 ASN B CG  1 
ATOM   4842  O OD1 . ASN B  1 248 ? 66.117  73.567  18.285  1.00   56.02  ? 248 ASN B OD1 1 
ATOM   4843  N ND2 . ASN B  1 248 ? 67.516  75.304  18.463  1.00   61.01  ? 248 ASN B ND2 1 
ATOM   4844  N N   . LYS B  1 249 ? 67.146  74.249  13.414  1.00   43.82  ? 249 LYS B N   1 
ATOM   4845  C CA  . LYS B  1 249 ? 67.118  74.231  11.941  1.00   51.03  ? 249 LYS B CA  1 
ATOM   4846  C C   . LYS B  1 249 ? 68.493  74.160  11.282  1.00   46.24  ? 249 LYS B C   1 
ATOM   4847  O O   . LYS B  1 249 ? 68.650  74.433  10.086  1.00   43.55  ? 249 LYS B O   1 
ATOM   4848  C CB  . LYS B  1 249 ? 66.361  75.432  11.393  1.00   59.81  ? 249 LYS B CB  1 
ATOM   4849  C CG  . LYS B  1 249 ? 65.378  76.033  12.363  1.00   67.27  ? 249 LYS B CG  1 
ATOM   4850  C CD  . LYS B  1 249 ? 64.290  76.735  11.595  1.00   75.36  ? 249 LYS B CD  1 
ATOM   4851  C CE  . LYS B  1 249 ? 63.595  75.701  10.698  1.00   77.84  ? 249 LYS B CE  1 
ATOM   4852  N NZ  . LYS B  1 249 ? 62.482  76.259  9.877   1.00   83.84  ? 249 LYS B NZ  1 
ATOM   4853  N N   . HIS B  1 250 ? 69.461  73.704  12.057  1.00   43.77  ? 250 HIS B N   1 
ATOM   4854  C CA  . HIS B  1 250 ? 70.807  73.463  11.568  1.00   44.22  ? 250 HIS B CA  1 
ATOM   4855  C C   . HIS B  1 250 ? 70.955  71.966  11.297  1.00   41.30  ? 250 HIS B C   1 
ATOM   4856  O O   . HIS B  1 250 ? 70.379  71.133  11.999  1.00   33.81  ? 250 HIS B O   1 
ATOM   4857  C CB  . HIS B  1 250 ? 71.872  73.933  12.563  1.00   38.04  ? 250 HIS B CB  1 
ATOM   4858  C CG  . HIS B  1 250 ? 71.990  75.430  12.696  1.00   44.53  ? 250 HIS B CG  1 
ATOM   4859  N ND1 . HIS B  1 250 ? 72.775  76.196  11.858  1.00   47.94  ? 250 HIS B ND1 1 
ATOM   4860  C CD2 . HIS B  1 250 ? 71.476  76.289  13.605  1.00   44.44  ? 250 HIS B CD2 1 
ATOM   4861  C CE1 . HIS B  1 250 ? 72.712  77.463  12.225  1.00   49.85  ? 250 HIS B CE1 1 
ATOM   4862  N NE2 . HIS B  1 250 ? 71.932  77.548  13.285  1.00   48.92  ? 250 HIS B NE2 1 
ATOM   4863  N N   . LEU B  1 251 ? 71.630  71.658  10.195  1.00   39.46  ? 251 LEU B N   1 
ATOM   4864  C CA  . LEU B  1 251 ? 71.961  70.299  9.787   1.00   35.30  ? 251 LEU B CA  1 
ATOM   4865  C C   . LEU B  1 251 ? 73.465  70.047  9.839   1.00   34.63  ? 251 LEU B C   1 
ATOM   4866  O O   . LEU B  1 251 ? 74.227  70.794  9.244   1.00   35.88  ? 251 LEU B O   1 
ATOM   4867  C CB  . LEU B  1 251 ? 71.480  70.030  8.362   1.00   36.75  ? 251 LEU B CB  1 
ATOM   4868  C CG  . LEU B  1 251 ? 69.982  69.936  8.134   1.00   36.45  ? 251 LEU B CG  1 
ATOM   4869  C CD1 . LEU B  1 251 ? 69.725  69.635  6.685   1.00   36.73  ? 251 LEU B CD1 1 
ATOM   4870  C CD2 . LEU B  1 251 ? 69.435  68.840  8.994   1.00   33.85  ? 251 LEU B CD2 1 
ATOM   4871  N N   . VAL B  1 252 ? 73.889  69.035  10.584  1.00   32.29  ? 252 VAL B N   1 
ATOM   4872  C CA  . VAL B  1 252 ? 75.265  68.589  10.525  1.00   31.69  ? 252 VAL B CA  1 
ATOM   4873  C C   . VAL B  1 252 ? 75.213  67.388  9.571   1.00   31.64  ? 252 VAL B C   1 
ATOM   4874  O O   . VAL B  1 252 ? 74.631  66.348  9.896   1.00   31.97  ? 252 VAL B O   1 
ATOM   4875  C CB  . VAL B  1 252 ? 75.806  68.193  11.917  1.00   30.38  ? 252 VAL B CB  1 
ATOM   4876  C CG1 . VAL B  1 252 ? 77.296  67.819  11.846  1.00   29.53  ? 252 VAL B CG1 1 
ATOM   4877  C CG2 . VAL B  1 252 ? 75.616  69.330  12.896  1.00   30.16  ? 252 VAL B CG2 1 
ATOM   4878  N N   . ILE B  1 253 ? 75.781  67.536  8.381   1.00   32.23  ? 253 ILE B N   1 
ATOM   4879  C CA  . ILE B  1 253 ? 75.642  66.509  7.345   1.00   30.01  ? 253 ILE B CA  1 
ATOM   4880  C C   . ILE B  1 253 ? 76.931  65.740  6.985   1.00   29.19  ? 253 ILE B C   1 
ATOM   4881  O O   . ILE B  1 253 ? 77.808  66.250  6.297   1.00   33.51  ? 253 ILE B O   1 
ATOM   4882  C CB  . ILE B  1 253 ? 75.054  67.136  6.075   1.00   32.17  ? 253 ILE B CB  1 
ATOM   4883  C CG1 . ILE B  1 253 ? 73.770  67.898  6.417   1.00   31.30  ? 253 ILE B CG1 1 
ATOM   4884  C CG2 . ILE B  1 253 ? 74.782  66.074  5.025   1.00   30.70  ? 253 ILE B CG2 1 
ATOM   4885  C CD1 . ILE B  1 253 ? 73.416  68.970  5.391   1.00   34.51  ? 253 ILE B CD1 1 
ATOM   4886  N N   . PRO B  1 254 ? 77.033  64.486  7.429   1.00   31.94  ? 254 PRO B N   1 
ATOM   4887  C CA  . PRO B  1 254 ? 78.212  63.652  7.189   1.00   34.71  ? 254 PRO B CA  1 
ATOM   4888  C C   . PRO B  1 254 ? 78.416  63.243  5.708   1.00   38.86  ? 254 PRO B C   1 
ATOM   4889  O O   . PRO B  1 254 ? 77.418  63.064  5.005   1.00   41.06  ? 254 PRO B O   1 
ATOM   4890  C CB  . PRO B  1 254 ? 77.942  62.434  8.083   1.00   32.98  ? 254 PRO B CB  1 
ATOM   4891  C CG  . PRO B  1 254 ? 76.867  62.853  9.016   1.00   31.89  ? 254 PRO B CG  1 
ATOM   4892  C CD  . PRO B  1 254 ? 76.034  63.781  8.251   1.00   31.14  ? 254 PRO B CD  1 
ATOM   4893  N N   . THR B  1 255 ? 79.664  63.177  5.229   1.00   39.99  ? 255 THR B N   1 
ATOM   4894  C CA  . THR B  1 255 ? 79.959  62.600  3.905   1.00   42.72  ? 255 THR B CA  1 
ATOM   4895  C C   . THR B  1 255 ? 80.667  61.229  4.015   1.00   45.13  ? 255 THR B C   1 
ATOM   4896  O O   . THR B  1 255 ? 81.016  60.608  2.998   1.00   47.24  ? 255 THR B O   1 
ATOM   4897  C CB  . THR B  1 255 ? 80.836  63.511  3.032   1.00   43.07  ? 255 THR B CB  1 
ATOM   4898  O OG1 . THR B  1 255 ? 82.129  63.643  3.623   1.00   45.09  ? 255 THR B OG1 1 
ATOM   4899  C CG2 . THR B  1 255 ? 80.204  64.872  2.831   1.00   41.76  ? 255 THR B CG2 1 
ATOM   4900  N N   . GLY B  1 271 ? 74.309  51.636  -2.767  1.00   75.23  ? 271 GLY B N   1 
ATOM   4901  C CA  . GLY B  1 271 ? 74.465  50.312  -2.194  1.00   73.93  ? 271 GLY B CA  1 
ATOM   4902  C C   . GLY B  1 271 ? 75.648  50.177  -1.259  1.00   71.00  ? 271 GLY B C   1 
ATOM   4903  O O   . GLY B  1 271 ? 76.626  49.488  -1.578  1.00   70.65  ? 271 GLY B O   1 
ATOM   4904  N N   . GLU B  1 272 ? 75.547  50.819  -0.094  1.00   68.96  ? 272 GLU B N   1 
ATOM   4905  C CA  . GLU B  1 272 ? 76.637  50.825  0.880   1.00   67.77  ? 272 GLU B CA  1 
ATOM   4906  C C   . GLU B  1 272 ? 76.140  50.613  2.323   1.00   57.51  ? 272 GLU B C   1 
ATOM   4907  O O   . GLU B  1 272 ? 74.951  50.743  2.596   1.00   53.89  ? 272 GLU B O   1 
ATOM   4908  C CB  . GLU B  1 272 ? 77.400  52.153  0.746   1.00   74.63  ? 272 GLU B CB  1 
ATOM   4909  C CG  . GLU B  1 272 ? 78.713  52.254  1.514   1.00   78.99  ? 272 GLU B CG  1 
ATOM   4910  C CD  . GLU B  1 272 ? 79.870  52.662  0.600   1.00   84.96  ? 272 GLU B CD  1 
ATOM   4911  O OE1 . GLU B  1 272 ? 79.605  53.110  -0.539  1.00   87.92  ? 272 GLU B OE1 1 
ATOM   4912  O OE2 . GLU B  1 272 ? 81.042  52.517  1.009   1.00   86.42  ? 272 GLU B OE2 1 
ATOM   4913  N N   . ILE B  1 273 ? 77.049  50.255  3.231   1.00   54.11  ? 273 ILE B N   1 
ATOM   4914  C CA  . ILE B  1 273 ? 76.699  50.036  4.629   1.00   52.67  ? 273 ILE B CA  1 
ATOM   4915  C C   . ILE B  1 273 ? 76.377  51.413  5.212   1.00   50.71  ? 273 ILE B C   1 
ATOM   4916  O O   . ILE B  1 273 ? 76.970  52.414  4.821   1.00   54.40  ? 273 ILE B O   1 
ATOM   4917  C CB  . ILE B  1 273 ? 77.854  49.354  5.454   1.00   47.71  ? 273 ILE B CB  1 
ATOM   4918  C CG1 . ILE B  1 273 ? 78.476  48.179  4.716   1.00   52.50  ? 273 ILE B CG1 1 
ATOM   4919  C CG2 . ILE B  1 273 ? 77.382  48.916  6.845   1.00   41.36  ? 273 ILE B CG2 1 
ATOM   4920  C CD1 . ILE B  1 273 ? 79.494  47.480  5.542   1.00   54.26  ? 273 ILE B CD1 1 
ATOM   4921  N N   . GLY B  1 274 ? 75.429  51.463  6.133   1.00   45.75  ? 274 GLY B N   1 
ATOM   4922  C CA  . GLY B  1 274 ? 75.085  52.700  6.806   1.00   42.21  ? 274 GLY B CA  1 
ATOM   4923  C C   . GLY B  1 274 ? 76.253  53.336  7.535   1.00   40.79  ? 274 GLY B C   1 
ATOM   4924  O O   . GLY B  1 274 ? 77.298  52.732  7.725   1.00   41.47  ? 274 GLY B O   1 
ATOM   4925  N N   . GLY B  1 275 ? 76.098  54.589  7.913   1.00   36.72  ? 275 GLY B N   1 
ATOM   4926  C CA  . GLY B  1 275 ? 77.197  55.262  8.522   1.00   35.49  ? 275 GLY B CA  1 
ATOM   4927  C C   . GLY B  1 275 ? 77.141  55.250  10.020  1.00   32.90  ? 275 GLY B C   1 
ATOM   4928  O O   . GLY B  1 275 ? 78.107  55.644  10.651  1.00   35.19  ? 275 GLY B O   1 
ATOM   4929  N N   . ALA B  1 276 ? 76.031  54.816  10.599  1.00   29.10  ? 276 ALA B N   1 
ATOM   4930  C CA  . ALA B  1 276 ? 75.915  54.829  12.056  1.00   26.30  ? 276 ALA B CA  1 
ATOM   4931  C C   . ALA B  1 276 ? 75.920  53.430  12.661  1.00   25.35  ? 276 ALA B C   1 
ATOM   4932  O O   . ALA B  1 276 ? 75.057  52.629  12.375  1.00   25.35  ? 276 ALA B O   1 
ATOM   4933  C CB  . ALA B  1 276 ? 74.670  55.560  12.472  1.00   25.73  ? 276 ALA B CB  1 
ATOM   4934  N N   . LEU B  1 277 ? 76.917  53.142  13.481  1.00   24.99  ? 277 LEU B N   1 
ATOM   4935  C CA  . LEU B  1 277 ? 76.995  51.878  14.201  1.00   25.79  ? 277 LEU B CA  1 
ATOM   4936  C C   . LEU B  1 277 ? 76.076  51.858  15.397  1.00   26.33  ? 277 LEU B C   1 
ATOM   4937  O O   . LEU B  1 277 ? 75.931  52.877  16.082  1.00   27.83  ? 277 LEU B O   1 
ATOM   4938  C CB  . LEU B  1 277 ? 78.417  51.621  14.692  1.00   26.65  ? 277 LEU B CB  1 
ATOM   4939  C CG  . LEU B  1 277 ? 78.664  50.393  15.578  1.00   27.10  ? 277 LEU B CG  1 
ATOM   4940  C CD1 . LEU B  1 277 ? 78.601  49.073  14.779  1.00   25.88  ? 277 LEU B CD1 1 
ATOM   4941  C CD2 . LEU B  1 277 ? 80.014  50.540  16.239  1.00   30.90  ? 277 LEU B CD2 1 
ATOM   4942  N N   . ILE B  1 278 ? 75.485  50.702  15.677  1.00   25.63  ? 278 ILE B N   1 
ATOM   4943  C CA  . ILE B  1 278 ? 74.774  50.522  16.941  1.00   25.50  ? 278 ILE B CA  1 
ATOM   4944  C C   . ILE B  1 278 ? 75.536  49.554  17.819  1.00   26.33  ? 278 ILE B C   1 
ATOM   4945  O O   . ILE B  1 278 ? 75.916  48.476  17.359  1.00   27.88  ? 278 ILE B O   1 
ATOM   4946  C CB  . ILE B  1 278 ? 73.354  50.009  16.731  1.00   23.30  ? 278 ILE B CB  1 
ATOM   4947  C CG1 . ILE B  1 278 ? 72.643  50.889  15.695  1.00   23.59  ? 278 ILE B CG1 1 
ATOM   4948  C CG2 . ILE B  1 278 ? 72.616  49.972  18.084  1.00   20.59  ? 278 ILE B CG2 1 
ATOM   4949  C CD1 . ILE B  1 278 ? 71.351  50.343  15.217  1.00   24.78  ? 278 ILE B CD1 1 
ATOM   4950  N N   . THR B  1 279 ? 75.777  49.932  19.070  1.00   24.68  ? 279 THR B N   1 
ATOM   4951  C CA  . THR B  1 279 ? 76.600  49.104  19.944  1.00   24.88  ? 279 THR B CA  1 
ATOM   4952  C C   . THR B  1 279 ? 76.147  49.217  21.393  1.00   27.39  ? 279 THR B C   1 
ATOM   4953  O O   . THR B  1 279 ? 75.514  50.202  21.790  1.00   26.82  ? 279 THR B O   1 
ATOM   4954  C CB  . THR B  1 279 ? 78.104  49.495  19.866  1.00   22.98  ? 279 THR B CB  1 
ATOM   4955  O OG1 . THR B  1 279 ? 78.855  48.643  20.727  1.00   28.80  ? 279 THR B OG1 1 
ATOM   4956  C CG2 . THR B  1 279 ? 78.345  50.926  20.313  1.00   23.51  ? 279 THR B CG2 1 
ATOM   4957  N N   . THR B  1 280 ? 76.484  48.220  22.198  1.00   27.50  ? 280 THR B N   1 
ATOM   4958  C CA  . THR B  1 280 ? 76.175  48.303  23.612  1.00   26.76  ? 280 THR B CA  1 
ATOM   4959  C C   . THR B  1 280 ? 77.417  48.426  24.443  1.00   27.37  ? 280 THR B C   1 
ATOM   4960  O O   . THR B  1 280 ? 77.320  48.440  25.671  1.00   28.86  ? 280 THR B O   1 
ATOM   4961  C CB  . THR B  1 280 ? 75.417  47.069  24.108  1.00   27.93  ? 280 THR B CB  1 
ATOM   4962  O OG1 . THR B  1 280 ? 76.134  45.881  23.746  1.00   27.29  ? 280 THR B OG1 1 
ATOM   4963  C CG2 . THR B  1 280 ? 74.061  47.020  23.488  1.00   28.55  ? 280 THR B CG2 1 
ATOM   4964  N N   . THR B  1 281 ? 78.584  48.542  23.798  1.00   26.85  ? 281 THR B N   1 
ATOM   4965  C CA  . THR B  1 281 ? 79.836  48.372  24.552  1.00   29.36  ? 281 THR B CA  1 
ATOM   4966  C C   . THR B  1 281 ? 80.569  49.663  24.927  1.00   27.07  ? 281 THR B C   1 
ATOM   4967  O O   . THR B  1 281 ? 81.649  49.626  25.486  1.00   27.95  ? 281 THR B O   1 
ATOM   4968  C CB  . THR B  1 281 ? 80.809  47.399  23.812  1.00   30.48  ? 281 THR B CB  1 
ATOM   4969  O OG1 . THR B  1 281 ? 81.016  47.806  22.459  1.00   28.76  ? 281 THR B OG1 1 
ATOM   4970  C CG2 . THR B  1 281 ? 80.227  45.985  23.821  1.00   32.20  ? 281 THR B CG2 1 
ATOM   4971  N N   . HIS B  1 282 ? 79.922  50.795  24.699  1.00   27.80  ? 282 HIS B N   1 
ATOM   4972  C CA  . HIS B  1 282 ? 80.316  52.024  25.373  1.00   31.55  ? 282 HIS B CA  1 
ATOM   4973  C C   . HIS B  1 282 ? 79.053  52.804  25.718  1.00   30.84  ? 282 HIS B C   1 
ATOM   4974  O O   . HIS B  1 282 ? 78.068  52.715  24.994  1.00   29.71  ? 282 HIS B O   1 
ATOM   4975  C CB  . HIS B  1 282 ? 81.306  52.850  24.519  1.00   31.99  ? 282 HIS B CB  1 
ATOM   4976  C CG  . HIS B  1 282 ? 80.859  53.126  23.112  1.00   27.45  ? 282 HIS B CG  1 
ATOM   4977  N ND1 . HIS B  1 282 ? 79.786  53.939  22.809  1.00   28.49  ? 282 HIS B ND1 1 
ATOM   4978  C CD2 . HIS B  1 282 ? 81.384  52.743  21.920  1.00   24.83  ? 282 HIS B CD2 1 
ATOM   4979  C CE1 . HIS B  1 282 ? 79.656  54.024  21.496  1.00   27.68  ? 282 HIS B CE1 1 
ATOM   4980  N NE2 . HIS B  1 282 ? 80.618  53.311  20.933  1.00   25.83  ? 282 HIS B NE2 1 
ATOM   4981  N N   . PRO B  1 283 ? 79.062  53.539  26.848  1.00   29.81  ? 283 PRO B N   1 
ATOM   4982  C CA  . PRO B  1 283 ? 77.821  54.194  27.271  1.00   28.97  ? 283 PRO B CA  1 
ATOM   4983  C C   . PRO B  1 283 ? 77.401  55.334  26.372  1.00   30.43  ? 283 PRO B C   1 
ATOM   4984  O O   . PRO B  1 283 ? 76.247  55.370  25.973  1.00   32.27  ? 283 PRO B O   1 
ATOM   4985  C CB  . PRO B  1 283 ? 78.149  54.712  28.677  1.00   30.69  ? 283 PRO B CB  1 
ATOM   4986  C CG  . PRO B  1 283 ? 79.629  54.779  28.732  1.00   32.14  ? 283 PRO B CG  1 
ATOM   4987  C CD  . PRO B  1 283 ? 80.126  53.670  27.857  1.00   30.91  ? 283 PRO B CD  1 
ATOM   4988  N N   . TYR B  1 284 ? 78.304  56.243  26.045  1.00   30.47  ? 284 TYR B N   1 
ATOM   4989  C CA  . TYR B  1 284 ? 77.898  57.440  25.327  1.00   30.22  ? 284 TYR B CA  1 
ATOM   4990  C C   . TYR B  1 284 ? 78.065  57.309  23.831  1.00   30.28  ? 284 TYR B C   1 
ATOM   4991  O O   . TYR B  1 284 ? 78.809  56.460  23.363  1.00   32.88  ? 284 TYR B O   1 
ATOM   4992  C CB  . TYR B  1 284 ? 78.663  58.654  25.872  1.00   32.17  ? 284 TYR B CB  1 
ATOM   4993  C CG  . TYR B  1 284 ? 78.489  58.718  27.360  1.00   31.50  ? 284 TYR B CG  1 
ATOM   4994  C CD1 . TYR B  1 284 ? 77.227  58.787  27.897  1.00   34.06  ? 284 TYR B CD1 1 
ATOM   4995  C CD2 . TYR B  1 284 ? 79.563  58.647  28.218  1.00   33.30  ? 284 TYR B CD2 1 
ATOM   4996  C CE1 . TYR B  1 284 ? 77.021  58.792  29.241  1.00   36.63  ? 284 TYR B CE1 1 
ATOM   4997  C CE2 . TYR B  1 284 ? 79.372  58.663  29.582  1.00   37.18  ? 284 TYR B CE2 1 
ATOM   4998  C CZ  . TYR B  1 284 ? 78.087  58.731  30.082  1.00   39.65  ? 284 TYR B CZ  1 
ATOM   4999  O OH  . TYR B  1 284 ? 77.840  58.751  31.438  1.00   45.17  ? 284 TYR B OH  1 
ATOM   5000  N N   . THR B  1 285 ? 77.355  58.158  23.093  1.00   31.31  ? 285 THR B N   1 
ATOM   5001  C CA  . THR B  1 285 ? 77.428  58.180  21.641  1.00   28.00  ? 285 THR B CA  1 
ATOM   5002  C C   . THR B  1 285 ? 78.733  58.830  21.246  1.00   27.84  ? 285 THR B C   1 
ATOM   5003  O O   . THR B  1 285 ? 79.118  59.867  21.772  1.00   31.16  ? 285 THR B O   1 
ATOM   5004  C CB  . THR B  1 285 ? 76.216  58.908  21.047  1.00   24.09  ? 285 THR B CB  1 
ATOM   5005  O OG1 . THR B  1 285 ? 75.064  58.153  21.367  1.00   26.58  ? 285 THR B OG1 1 
ATOM   5006  C CG2 . THR B  1 285 ? 76.286  59.003  19.545  1.00   22.10  ? 285 THR B CG2 1 
ATOM   5007  N N   . VAL B  1 286 ? 79.442  58.166  20.350  1.00   26.39  ? 286 VAL B N   1 
ATOM   5008  C CA  . VAL B  1 286 ? 80.776  58.561  19.963  1.00   26.62  ? 286 VAL B CA  1 
ATOM   5009  C C   . VAL B  1 286 ? 80.749  59.116  18.559  1.00   27.08  ? 286 VAL B C   1 
ATOM   5010  O O   . VAL B  1 286 ? 80.178  58.502  17.682  1.00   27.35  ? 286 VAL B O   1 
ATOM   5011  C CB  . VAL B  1 286 ? 81.733  57.364  20.050  1.00   27.36  ? 286 VAL B CB  1 
ATOM   5012  C CG1 . VAL B  1 286 ? 83.061  57.685  19.440  1.00   26.93  ? 286 VAL B CG1 1 
ATOM   5013  C CG2 . VAL B  1 286 ? 81.873  56.891  21.480  1.00   27.03  ? 286 VAL B CG2 1 
ATOM   5014  N N   . LEU B  1 287 ? 81.334  60.288  18.357  1.00   26.87  ? 287 LEU B N   1 
ATOM   5015  C CA  . LEU B  1 287 ? 81.387  60.908  17.034  1.00   27.72  ? 287 LEU B CA  1 
ATOM   5016  C C   . LEU B  1 287 ? 82.832  61.019  16.542  1.00   29.27  ? 287 LEU B C   1 
ATOM   5017  O O   . LEU B  1 287 ? 83.736  61.317  17.329  1.00   29.48  ? 287 LEU B O   1 
ATOM   5018  C CB  . LEU B  1 287 ? 80.758  62.296  17.080  1.00   26.83  ? 287 LEU B CB  1 
ATOM   5019  C CG  . LEU B  1 287 ? 79.373  62.423  17.668  1.00   27.34  ? 287 LEU B CG  1 
ATOM   5020  C CD1 . LEU B  1 287 ? 79.013  63.860  17.869  1.00   30.91  ? 287 LEU B CD1 1 
ATOM   5021  C CD2 . LEU B  1 287 ? 78.410  61.816  16.707  1.00   25.44  ? 287 LEU B CD2 1 
ATOM   5022  N N   . SER B  1 288 ? 83.066  60.793  15.253  1.00   31.46  ? 288 SER B N   1 
ATOM   5023  C CA  . SER B  1 288 ? 84.406  61.000  14.731  1.00   35.39  ? 288 SER B CA  1 
ATOM   5024  C C   . SER B  1 288 ? 84.696  62.472  14.876  1.00   39.64  ? 288 SER B C   1 
ATOM   5025  O O   . SER B  1 288 ? 83.777  63.275  14.946  1.00   41.56  ? 288 SER B O   1 
ATOM   5026  C CB  . SER B  1 288 ? 84.545  60.534  13.286  1.00   36.85  ? 288 SER B CB  1 
ATOM   5027  O OG  . SER B  1 288 ? 83.686  61.275  12.457  1.00   37.82  ? 288 SER B OG  1 
ATOM   5028  N N   . HIS B  1 289 ? 85.972  62.822  14.924  1.00   39.58  ? 289 HIS B N   1 
ATOM   5029  C CA  . HIS B  1 289 ? 86.407  64.151  15.336  1.00   37.15  ? 289 HIS B CA  1 
ATOM   5030  C C   . HIS B  1 289 ? 85.810  65.364  14.614  1.00   36.22  ? 289 HIS B C   1 
ATOM   5031  O O   . HIS B  1 289 ? 85.388  66.318  15.255  1.00   32.11  ? 289 HIS B O   1 
ATOM   5032  C CB  . HIS B  1 289 ? 87.927  64.192  15.223  1.00   41.00  ? 289 HIS B CB  1 
ATOM   5033  C CG  . HIS B  1 289 ? 88.517  65.508  15.590  1.00   46.94  ? 289 HIS B CG  1 
ATOM   5034  N ND1 . HIS B  1 289 ? 88.465  66.013  16.871  1.00   48.84  ? 289 HIS B ND1 1 
ATOM   5035  C CD2 . HIS B  1 289 ? 89.198  66.416  14.852  1.00   50.14  ? 289 HIS B CD2 1 
ATOM   5036  C CE1 . HIS B  1 289 ? 89.069  67.188  16.902  1.00   52.06  ? 289 HIS B CE1 1 
ATOM   5037  N NE2 . HIS B  1 289 ? 89.521  67.457  15.690  1.00   53.00  ? 289 HIS B NE2 1 
ATOM   5038  N N   . SER B  1 290 ? 85.765  65.334  13.289  1.00   40.98  ? 290 SER B N   1 
ATOM   5039  C CA  . SER B  1 290 ? 85.247  66.471  12.534  1.00   44.48  ? 290 SER B CA  1 
ATOM   5040  C C   . SER B  1 290 ? 83.777  66.684  12.805  1.00   39.14  ? 290 SER B C   1 
ATOM   5041  O O   . SER B  1 290 ? 83.299  67.813  12.892  1.00   40.07  ? 290 SER B O   1 
ATOM   5042  C CB  . SER B  1 290 ? 85.481  66.282  11.048  1.00   52.36  ? 290 SER B CB  1 
ATOM   5043  O OG  . SER B  1 290 ? 85.500  67.533  10.400  1.00   59.37  ? 290 SER B OG  1 
ATOM   5044  N N   . ILE B  1 291 ? 83.047  65.589  12.931  1.00   35.29  ? 291 ILE B N   1 
ATOM   5045  C CA  . ILE B  1 291 ? 81.633  65.685  13.260  1.00   31.00  ? 291 ILE B CA  1 
ATOM   5046  C C   . ILE B  1 291 ? 81.435  66.206  14.671  1.00   29.03  ? 291 ILE B C   1 
ATOM   5047  O O   . ILE B  1 291 ? 80.644  67.109  14.903  1.00   30.80  ? 291 ILE B O   1 
ATOM   5048  C CB  . ILE B  1 291 ? 80.969  64.331  13.147  1.00   32.54  ? 291 ILE B CB  1 
ATOM   5049  C CG1 . ILE B  1 291 ? 81.029  63.857  11.706  1.00   36.48  ? 291 ILE B CG1 1 
ATOM   5050  C CG2 . ILE B  1 291 ? 79.521  64.380  13.621  1.00   32.34  ? 291 ILE B CG2 1 
ATOM   5051  C CD1 . ILE B  1 291 ? 80.382  62.510  11.508  1.00   36.91  ? 291 ILE B CD1 1 
ATOM   5052  N N   . PHE B  1 292 ? 82.205  65.659  15.602  1.00   28.93  ? 292 PHE B N   1 
ATOM   5053  C CA  . PHE B  1 292 ? 82.156  66.061  16.998  1.00   29.25  ? 292 PHE B CA  1 
ATOM   5054  C C   . PHE B  1 292 ? 82.412  67.529  17.128  1.00   34.94  ? 292 PHE B C   1 
ATOM   5055  O O   . PHE B  1 292 ? 81.732  68.202  17.873  1.00   36.44  ? 292 PHE B O   1 
ATOM   5056  C CB  . PHE B  1 292 ? 83.173  65.295  17.815  1.00   31.00  ? 292 PHE B CB  1 
ATOM   5057  C CG  . PHE B  1 292 ? 83.280  65.758  19.231  1.00   33.73  ? 292 PHE B CG  1 
ATOM   5058  C CD1 . PHE B  1 292 ? 82.368  65.335  20.176  1.00   33.92  ? 292 PHE B CD1 1 
ATOM   5059  C CD2 . PHE B  1 292 ? 84.306  66.586  19.625  1.00   38.35  ? 292 PHE B CD2 1 
ATOM   5060  C CE1 . PHE B  1 292 ? 82.470  65.735  21.486  1.00   37.55  ? 292 PHE B CE1 1 
ATOM   5061  C CE2 . PHE B  1 292 ? 84.419  66.985  20.941  1.00   42.22  ? 292 PHE B CE2 1 
ATOM   5062  C CZ  . PHE B  1 292 ? 83.496  66.554  21.875  1.00   40.34  ? 292 PHE B CZ  1 
ATOM   5063  N N   . GLU B  1 293 ? 83.420  68.011  16.415  1.00   37.60  ? 293 GLU B N   1 
ATOM   5064  C CA  . GLU B  1 293 ? 83.782  69.416  16.470  1.00   44.11  ? 293 GLU B CA  1 
ATOM   5065  C C   . GLU B  1 293 ? 82.681  70.308  15.953  1.00   41.66  ? 293 GLU B C   1 
ATOM   5066  O O   . GLU B  1 293 ? 82.322  71.291  16.588  1.00   40.10  ? 293 GLU B O   1 
ATOM   5067  C CB  . GLU B  1 293 ? 85.023  69.672  15.620  1.00   49.33  ? 293 GLU B CB  1 
ATOM   5068  C CG  . GLU B  1 293 ? 86.330  69.327  16.233  1.00   51.96  ? 293 GLU B CG  1 
ATOM   5069  C CD  . GLU B  1 293 ? 86.813  70.394  17.163  1.00   54.66  ? 293 GLU B CD  1 
ATOM   5070  O OE1 . GLU B  1 293 ? 87.910  70.908  16.887  1.00   58.05  ? 293 GLU B OE1 1 
ATOM   5071  O OE2 . GLU B  1 293 ? 86.117  70.729  18.140  1.00   53.37  1 293 GLU B OE2 1 
ATOM   5072  N N   . VAL B  1 294 ? 82.129  69.952  14.803  1.00   39.52  ? 294 VAL B N   1 
ATOM   5073  C CA  . VAL B  1 294 ? 81.129  70.796  14.205  1.00   39.44  ? 294 VAL B CA  1 
ATOM   5074  C C   . VAL B  1 294 ? 79.816  70.688  14.981  1.00   39.00  ? 294 VAL B C   1 
ATOM   5075  O O   . VAL B  1 294 ? 79.204  71.693  15.303  1.00   40.94  ? 294 VAL B O   1 
ATOM   5076  C CB  . VAL B  1 294 ? 80.949  70.474  12.725  1.00   35.95  ? 294 VAL B CB  1 
ATOM   5077  C CG1 . VAL B  1 294 ? 79.811  71.279  12.170  1.00   36.20  ? 294 VAL B CG1 1 
ATOM   5078  C CG2 . VAL B  1 294 ? 82.217  70.807  11.985  1.00   34.09  ? 294 VAL B CG2 1 
ATOM   5079  N N   . PHE B  1 295 ? 79.412  69.478  15.327  1.00   34.98  ? 295 PHE B N   1 
ATOM   5080  C CA  . PHE B  1 295 ? 78.165  69.279  16.045  1.00   30.61  ? 295 PHE B CA  1 
ATOM   5081  C C   . PHE B  1 295 ? 78.121  69.976  17.399  1.00   32.75  ? 295 PHE B C   1 
ATOM   5082  O O   . PHE B  1 295 ? 77.147  70.633  17.737  1.00   35.08  ? 295 PHE B O   1 
ATOM   5083  C CB  . PHE B  1 295 ? 77.926  67.792  16.262  1.00   28.58  ? 295 PHE B CB  1 
ATOM   5084  C CG  . PHE B  1 295 ? 76.809  67.503  17.206  1.00   29.80  ? 295 PHE B CG  1 
ATOM   5085  C CD1 . PHE B  1 295 ? 75.488  67.616  16.784  1.00   29.73  ? 295 PHE B CD1 1 
ATOM   5086  C CD2 . PHE B  1 295 ? 77.070  67.144  18.518  1.00   29.18  ? 295 PHE B CD2 1 
ATOM   5087  C CE1 . PHE B  1 295 ? 74.461  67.368  17.642  1.00   30.57  ? 295 PHE B CE1 1 
ATOM   5088  C CE2 . PHE B  1 295 ? 76.059  66.896  19.382  1.00   30.12  ? 295 PHE B CE2 1 
ATOM   5089  C CZ  . PHE B  1 295 ? 74.738  67.004  18.947  1.00   31.66  ? 295 PHE B CZ  1 
ATOM   5090  N N   . THR B  1 296 ? 79.186  69.854  18.172  1.00   34.41  ? 296 THR B N   1 
ATOM   5091  C CA  . THR B  1 296 ? 79.193  70.406  19.516  1.00   36.24  ? 296 THR B CA  1 
ATOM   5092  C C   . THR B  1 296 ? 79.085  71.914  19.503  1.00   39.83  ? 296 THR B C   1 
ATOM   5093  O O   . THR B  1 296 ? 78.418  72.495  20.348  1.00   41.38  ? 296 THR B O   1 
ATOM   5094  C CB  . THR B  1 296 ? 80.460  70.008  20.281  1.00   38.01  ? 296 THR B CB  1 
ATOM   5095  O OG1 . THR B  1 296 ? 80.450  68.593  20.514  1.00   39.87  ? 296 THR B OG1 1 
ATOM   5096  C CG2 . THR B  1 296 ? 80.487  70.676  21.624  1.00   41.93  ? 296 THR B CG2 1 
ATOM   5097  N N   . GLN B  1 297 ? 79.693  72.546  18.510  1.00   41.48  ? 297 GLN B N   1 
ATOM   5098  C CA  . GLN B  1 297 ? 79.646  73.996  18.415  1.00   44.68  ? 297 GLN B CA  1 
ATOM   5099  C C   . GLN B  1 297 ? 78.265  74.440  18.016  1.00   44.42  ? 297 GLN B C   1 
ATOM   5100  O O   . GLN B  1 297 ? 77.725  75.375  18.597  1.00   49.10  ? 297 GLN B O   1 
ATOM   5101  C CB  . GLN B  1 297 ? 80.681  74.516  17.414  1.00   48.25  ? 297 GLN B CB  1 
ATOM   5102  C CG  . GLN B  1 297 ? 80.808  76.019  17.404  1.00   55.45  ? 297 GLN B CG  1 
ATOM   5103  C CD  . GLN B  1 297 ? 81.175  76.555  18.771  1.00   61.19  ? 297 GLN B CD  1 
ATOM   5104  O OE1 . GLN B  1 297 ? 82.193  76.167  19.344  1.00   65.50  ? 297 GLN B OE1 1 
ATOM   5105  N NE2 . GLN B  1 297 ? 80.349  77.450  19.304  1.00   60.41  ? 297 GLN B NE2 1 
ATOM   5106  N N   . VAL B  1 298 ? 77.701  73.764  17.022  1.00   41.51  ? 298 VAL B N   1 
ATOM   5107  C CA  . VAL B  1 298 ? 76.332  74.032  16.602  1.00   39.51  ? 298 VAL B CA  1 
ATOM   5108  C C   . VAL B  1 298 ? 75.430  73.891  17.817  1.00   39.21  ? 298 VAL B C   1 
ATOM   5109  O O   . VAL B  1 298 ? 74.517  74.676  18.017  1.00   40.07  ? 298 VAL B O   1 
ATOM   5110  C CB  . VAL B  1 298 ? 75.857  73.087  15.450  1.00   34.47  ? 298 VAL B CB  1 
ATOM   5111  C CG1 . VAL B  1 298 ? 74.355  73.089  15.325  1.00   36.57  ? 298 VAL B CG1 1 
ATOM   5112  C CG2 . VAL B  1 298 ? 76.474  73.494  14.144  1.00   35.30  ? 298 VAL B CG2 1 
ATOM   5113  N N   . PHE B  1 299 ? 75.692  72.899  18.650  1.00   39.64  ? 299 PHE B N   1 
ATOM   5114  C CA  . PHE B  1 299 ? 74.879  72.757  19.841  1.00   39.17  ? 299 PHE B CA  1 
ATOM   5115  C C   . PHE B  1 299 ? 75.087  73.937  20.758  1.00   43.28  ? 299 PHE B C   1 
ATOM   5116  O O   . PHE B  1 299 ? 74.121  74.522  21.253  1.00   47.43  ? 299 PHE B O   1 
ATOM   5117  C CB  . PHE B  1 299 ? 75.188  71.476  20.612  1.00   36.24  ? 299 PHE B CB  1 
ATOM   5118  C CG  . PHE B  1 299 ? 74.192  71.200  21.706  1.00   39.26  ? 299 PHE B CG  1 
ATOM   5119  C CD1 . PHE B  1 299 ? 74.361  71.746  22.980  1.00   40.81  ? 299 PHE B CD1 1 
ATOM   5120  C CD2 . PHE B  1 299 ? 73.071  70.404  21.461  1.00   37.56  ? 299 PHE B CD2 1 
ATOM   5121  C CE1 . PHE B  1 299 ? 73.425  71.499  23.990  1.00   42.05  ? 299 PHE B CE1 1 
ATOM   5122  C CE2 . PHE B  1 299 ? 72.131  70.152  22.467  1.00   39.24  ? 299 PHE B CE2 1 
ATOM   5123  C CZ  . PHE B  1 299 ? 72.308  70.706  23.733  1.00   40.96  ? 299 PHE B CZ  1 
ATOM   5124  N N   . ALA B  1 300 ? 76.345  74.292  20.993  1.00   43.68  ? 300 ALA B N   1 
ATOM   5125  C CA  . ALA B  1 300 ? 76.647  75.382  21.902  1.00   43.43  ? 300 ALA B CA  1 
ATOM   5126  C C   . ALA B  1 300 ? 76.008  76.676  21.429  1.00   49.92  ? 300 ALA B C   1 
ATOM   5127  O O   . ALA B  1 300 ? 75.591  77.501  22.247  1.00   53.05  ? 300 ALA B O   1 
ATOM   5128  C CB  . ALA B  1 300 ? 78.132  75.541  22.059  1.00   46.21  ? 300 ALA B CB  1 
ATOM   5129  N N   . ASN B  1 301 ? 75.902  76.840  20.110  1.00   48.83  ? 301 ASN B N   1 
ATOM   5130  C CA  . ASN B  1 301 ? 75.272  78.019  19.509  1.00   50.79  ? 301 ASN B CA  1 
ATOM   5131  C C   . ASN B  1 301 ? 73.758  78.093  19.684  1.00   53.19  ? 301 ASN B C   1 
ATOM   5132  O O   . ASN B  1 301 ? 73.164  79.158  19.555  1.00   56.99  ? 301 ASN B O   1 
ATOM   5133  C CB  . ASN B  1 301 ? 75.590  78.068  18.020  1.00   50.55  ? 301 ASN B CB  1 
ATOM   5134  C CG  . ASN B  1 301 ? 77.037  78.360  17.750  1.00   52.67  ? 301 ASN B CG  1 
ATOM   5135  O OD1 . ASN B  1 301 ? 77.766  78.816  18.630  1.00   51.08  ? 301 ASN B OD1 1 
ATOM   5136  N ND2 . ASN B  1 301 ? 77.478  78.069  16.532  1.00   54.54  ? 301 ASN B ND2 1 
ATOM   5137  N N   . ASN B  1 302 ? 73.130  76.965  19.978  1.00   53.38  ? 302 ASN B N   1 
ATOM   5138  C CA  . ASN B  1 302 ? 71.687  76.945  20.187  1.00   57.77  ? 302 ASN B CA  1 
ATOM   5139  C C   . ASN B  1 302 ? 71.366  76.888  21.679  1.00   61.66  ? 302 ASN B C   1 
ATOM   5140  O O   . ASN B  1 302 ? 70.309  76.410  22.084  1.00   62.90  ? 302 ASN B O   1 
ATOM   5141  C CB  . ASN B  1 302 ? 71.051  75.753  19.463  1.00   55.13  ? 302 ASN B CB  1 
ATOM   5142  C CG  . ASN B  1 302 ? 70.939  75.961  17.960  1.00   54.88  ? 302 ASN B CG  1 
ATOM   5143  O OD1 . ASN B  1 302 ? 69.919  76.429  17.472  1.00   59.00  ? 302 ASN B OD1 1 
ATOM   5144  N ND2 . ASN B  1 302 ? 71.968  75.578  17.221  1.00   51.91  ? 302 ASN B ND2 1 
ATOM   5145  N N   . MET B  1 303 ? 72.304  77.373  22.487  1.00   61.49  ? 303 MET B N   1 
ATOM   5146  C CA  . MET B  1 303 ? 72.195  77.357  23.942  1.00   60.60  ? 303 MET B CA  1 
ATOM   5147  C C   . MET B  1 303 ? 72.699  78.685  24.513  1.00   62.87  ? 303 MET B C   1 
ATOM   5148  O O   . MET B  1 303 ? 73.447  79.399  23.841  1.00   64.69  ? 303 MET B O   1 
ATOM   5149  C CB  . MET B  1 303 ? 73.008  76.177  24.497  1.00   56.39  ? 303 MET B CB  1 
ATOM   5150  C CG  . MET B  1 303 ? 72.428  74.824  24.126  1.00   52.36  ? 303 MET B CG  1 
ATOM   5151  S SD  . MET B  1 303 ? 70.917  74.452  25.019  1.00   67.85  ? 303 MET B SD  1 
ATOM   5152  C CE  . MET B  1 303 ? 71.631  73.930  26.556  1.00   46.19  ? 303 MET B CE  1 
ATOM   5153  N N   . PRO B  1 304 ? 72.291  79.026  25.751  1.00   62.50  ? 304 PRO B N   1 
ATOM   5154  C CA  . PRO B  1 304 ? 72.812  80.193  26.478  1.00   63.84  ? 304 PRO B CA  1 
ATOM   5155  C C   . PRO B  1 304 ? 74.262  80.031  26.869  1.00   64.79  ? 304 PRO B C   1 
ATOM   5156  O O   . PRO B  1 304 ? 74.572  79.220  27.745  1.00   65.48  ? 304 PRO B O   1 
ATOM   5157  C CB  . PRO B  1 304 ? 71.946  80.248  27.726  1.00   65.34  ? 304 PRO B CB  1 
ATOM   5158  C CG  . PRO B  1 304 ? 71.419  78.878  27.873  1.00   63.46  ? 304 PRO B CG  1 
ATOM   5159  C CD  . PRO B  1 304 ? 71.213  78.363  26.495  1.00   60.91  ? 304 PRO B CD  1 
ATOM   5160  N N   . LYS B  1 305 ? 75.128  80.835  26.263  1.00   65.32  ? 305 LYS B N   1 
ATOM   5161  C CA  . LYS B  1 305 ? 76.574  80.706  26.411  1.00   62.44  ? 305 LYS B CA  1 
ATOM   5162  C C   . LYS B  1 305 ? 76.990  81.000  27.851  1.00   63.49  ? 305 LYS B C   1 
ATOM   5163  O O   . LYS B  1 305 ? 77.997  80.495  28.340  1.00   62.82  ? 305 LYS B O   1 
ATOM   5164  C CB  . LYS B  1 305 ? 77.249  81.636  25.411  0.0000 62.31  ? 305 LYS B CB  1 
ATOM   5165  C CG  . LYS B  1 305 ? 78.748  81.570  25.343  0.0000 60.73  ? 305 LYS B CG  1 
ATOM   5166  C CD  . LYS B  1 305 ? 79.150  82.234  24.043  0.0000 60.33  ? 305 LYS B CD  1 
ATOM   5167  C CE  . LYS B  1 305 ? 80.434  81.681  23.475  0.0000 58.54  ? 305 LYS B CE  1 
ATOM   5168  N NZ  . LYS B  1 305 ? 80.472  81.902  22.001  0.0000 58.14  ? 305 LYS B NZ  1 
ATOM   5169  N N   . GLN B  1 306 ? 76.126  81.729  28.549  1.00   64.41  ? 306 GLN B N   1 
ATOM   5170  C CA  . GLN B  1 306 ? 76.347  82.157  29.918  1.00   64.44  ? 306 GLN B CA  1 
ATOM   5171  C C   . GLN B  1 306 ? 75.928  81.075  30.899  1.00   62.12  ? 306 GLN B C   1 
ATOM   5172  O O   . GLN B  1 306 ? 76.020  81.251  32.106  1.00   62.04  ? 306 GLN B O   1 
ATOM   5173  C CB  . GLN B  1 306 ? 75.534  83.444  30.192  0.0000 68.17  ? 306 GLN B CB  1 
ATOM   5174  C CG  . GLN B  1 306 ? 74.081  83.471  29.618  0.0000 64.70  ? 306 GLN B CG  1 
ATOM   5175  C CD  . GLN B  1 306 ? 74.039  83.571  28.086  0.0000 63.26  ? 306 GLN B CD  1 
ATOM   5176  O OE1 . GLN B  1 306 ? 75.067  83.810  27.448  0.0000 62.51  ? 306 GLN B OE1 1 
ATOM   5177  N NE2 . GLN B  1 306 ? 72.859  83.377  27.497  0.0000 63.32  ? 306 GLN B NE2 1 
ATOM   5178  N N   . ALA B  1 307 ? 75.573  79.908  30.379  1.00   59.08  ? 307 ALA B N   1 
ATOM   5179  C CA  . ALA B  1 307 ? 75.190  78.809  31.247  1.00   58.67  ? 307 ALA B CA  1 
ATOM   5180  C C   . ALA B  1 307 ? 76.247  77.734  31.332  1.00   57.37  ? 307 ALA B C   1 
ATOM   5181  O O   . ALA B  1 307 ? 76.103  76.785  32.098  1.00   53.92  ? 307 ALA B O   1 
ATOM   5182  C CB  . ALA B  1 307 ? 73.901  78.215  30.777  1.00   55.62  ? 307 ALA B CB  1 
ATOM   5183  N N   . GLN B  1 308 ? 77.310  77.874  30.552  1.00   58.22  ? 308 GLN B N   1 
ATOM   5184  C CA  . GLN B  1 308 ? 78.330  76.840  30.546  1.00   58.86  ? 308 GLN B CA  1 
ATOM   5185  C C   . GLN B  1 308 ? 79.143  76.863  31.836  1.00   62.89  ? 308 GLN B C   1 
ATOM   5186  O O   . GLN B  1 308 ? 79.241  77.880  32.538  1.00   66.52  ? 308 GLN B O   1 
ATOM   5187  C CB  . GLN B  1 308 ? 79.237  76.970  29.332  1.00   59.50  ? 308 GLN B CB  1 
ATOM   5188  C CG  . GLN B  1 308 ? 78.466  77.094  28.035  1.00   61.58  ? 308 GLN B CG  1 
ATOM   5189  C CD  . GLN B  1 308 ? 79.370  77.056  26.819  1.00   64.01  ? 308 GLN B CD  1 
ATOM   5190  O OE1 . GLN B  1 308 ? 80.565  76.760  26.926  1.00   65.52  ? 308 GLN B OE1 1 
ATOM   5191  N NE2 . GLN B  1 308 ? 78.817  77.404  25.663  1.00   63.46  ? 308 GLN B NE2 1 
ATOM   5192  N N   . VAL B  1 309 ? 79.652  75.690  32.173  1.00   62.72  ? 309 VAL B N   1 
ATOM   5193  C CA  . VAL B  1 309 ? 80.499  75.483  33.335  1.00   64.56  ? 309 VAL B CA  1 
ATOM   5194  C C   . VAL B  1 309 ? 81.730  74.688  32.928  1.00   63.75  ? 309 VAL B C   1 
ATOM   5195  O O   . VAL B  1 309 ? 81.812  74.236  31.789  1.00   59.47  ? 309 VAL B O   1 
ATOM   5196  C CB  . VAL B  1 309 ? 79.746  74.776  34.472  1.00   63.97  ? 309 VAL B CB  1 
ATOM   5197  C CG1 . VAL B  1 309 ? 78.621  75.646  34.992  1.00   65.99  ? 309 VAL B CG1 1 
ATOM   5198  C CG2 . VAL B  1 309 ? 79.250  73.405  34.023  1.00   59.72  ? 309 VAL B CG2 1 
ATOM   5199  N N   . LYS B  1 310 ? 82.700  74.574  33.836  1.00   67.72  ? 310 LYS B N   1 
ATOM   5200  C CA  . LYS B  1 310 ? 83.899  73.763  33.615  1.00   67.83  ? 310 LYS B CA  1 
ATOM   5201  C C   . LYS B  1 310 ? 83.527  72.373  33.113  1.00   65.64  ? 310 LYS B C   1 
ATOM   5202  O O   . LYS B  1 310 ? 82.727  71.681  33.737  1.00   66.86  ? 310 LYS B O   1 
ATOM   5203  C CB  . LYS B  1 310 ? 84.689  73.626  34.908  1.00   71.76  ? 310 LYS B CB  1 
ATOM   5204  C CG  . LYS B  1 310 ? 85.450  74.835  35.336  1.00   76.57  ? 310 LYS B CG  1 
ATOM   5205  C CD  . LYS B  1 310 ? 85.099  75.150  36.778  1.00   80.30  ? 310 LYS B CD  1 
ATOM   5206  C CE  . LYS B  1 310 ? 85.772  76.400  37.262  1.00   84.92  ? 310 LYS B CE  1 
ATOM   5207  N NZ  . LYS B  1 310 ? 87.197  76.325  36.872  1.00   86.02  ? 310 LYS B NZ  1 
ATOM   5208  N N   . ALA B  1 311 ? 84.078  71.990  31.967  1.00   61.00  ? 311 ALA B N   1 
ATOM   5209  C CA  . ALA B  1 311 ? 83.794  70.689  31.367  1.00   56.66  ? 311 ALA B CA  1 
ATOM   5210  C C   . ALA B  1 311 ? 84.135  69.568  32.319  1.00   57.25  ? 311 ALA B C   1 
ATOM   5211  O O   . ALA B  1 311 ? 85.093  69.656  33.071  1.00   61.72  ? 311 ALA B O   1 
ATOM   5212  C CB  . ALA B  1 311 ? 84.551  70.518  30.068  1.00   54.81  ? 311 ALA B CB  1 
ATOM   5213  N N   . VAL B  1 312 ? 83.340  68.512  32.300  1.00   54.79  ? 312 VAL B N   1 
ATOM   5214  C CA  . VAL B  1 312 ? 83.529  67.456  33.271  1.00   56.09  ? 312 VAL B CA  1 
ATOM   5215  C C   . VAL B  1 312 ? 83.504  66.100  32.609  1.00   55.66  ? 312 VAL B C   1 
ATOM   5216  O O   . VAL B  1 312 ? 82.749  65.873  31.658  1.00   53.67  ? 312 VAL B O   1 
ATOM   5217  C CB  . VAL B  1 312 ? 82.426  67.525  34.365  1.00   68.38  ? 312 VAL B CB  1 
ATOM   5218  C CG1 . VAL B  1 312 ? 82.296  66.216  35.135  1.00   67.20  ? 312 VAL B CG1 1 
ATOM   5219  C CG2 . VAL B  1 312 ? 82.681  68.696  35.306  1.00   73.62  ? 312 VAL B CG2 1 
ATOM   5220  N N   . GLY B  1 313 ? 84.358  65.209  33.104  1.00   56.94  ? 313 GLY B N   1 
ATOM   5221  C CA  . GLY B  1 313 ? 84.370  63.836  32.647  1.00   55.32  ? 313 GLY B CA  1 
ATOM   5222  C C   . GLY B  1 313 ? 84.881  63.788  31.231  1.00   51.67  ? 313 GLY B C   1 
ATOM   5223  O O   . GLY B  1 313 ? 85.705  64.610  30.836  1.00   52.88  ? 313 GLY B O   1 
ATOM   5224  N N   . PRO B  1 314 ? 84.305  62.888  30.434  1.00   47.88  ? 314 PRO B N   1 
ATOM   5225  C CA  . PRO B  1 314 ? 84.602  62.671  29.020  1.00   47.23  ? 314 PRO B CA  1 
ATOM   5226  C C   . PRO B  1 314 ? 83.931  63.688  28.110  1.00   48.29  ? 314 PRO B C   1 
ATOM   5227  O O   . PRO B  1 314 ? 84.134  63.639  26.891  1.00   47.28  ? 314 PRO B O   1 
ATOM   5228  C CB  . PRO B  1 314 ? 84.046  61.271  28.768  1.00   43.92  ? 314 PRO B CB  1 
ATOM   5229  C CG  . PRO B  1 314 ? 82.922  61.159  29.690  1.00   44.40  ? 314 PRO B CG  1 
ATOM   5230  C CD  . PRO B  1 314 ? 83.313  61.922  30.930  1.00   47.07  ? 314 PRO B CD  1 
ATOM   5231  N N   . PHE B  1 315 ? 83.152  64.593  28.697  1.00   49.64  ? 315 PHE B N   1 
ATOM   5232  C CA  . PHE B  1 315 ? 82.334  65.511  27.924  1.00   48.59  ? 315 PHE B CA  1 
ATOM   5233  C C   . PHE B  1 315 ? 83.011  66.813  27.551  1.00   54.89  ? 315 PHE B C   1 
ATOM   5234  O O   . PHE B  1 315 ? 83.869  67.310  28.276  1.00   59.89  ? 315 PHE B O   1 
ATOM   5235  C CB  . PHE B  1 315 ? 81.068  65.817  28.692  1.00   45.91  ? 315 PHE B CB  1 
ATOM   5236  C CG  . PHE B  1 315 ? 80.258  64.603  29.001  1.00   43.96  ? 315 PHE B CG  1 
ATOM   5237  C CD1 . PHE B  1 315 ? 79.711  63.855  27.971  1.00   39.99  ? 315 PHE B CD1 1 
ATOM   5238  C CD2 . PHE B  1 315 ? 80.005  64.233  30.304  1.00   46.71  ? 315 PHE B CD2 1 
ATOM   5239  C CE1 . PHE B  1 315 ? 78.950  62.757  28.234  1.00   40.55  ? 315 PHE B CE1 1 
ATOM   5240  C CE2 . PHE B  1 315 ? 79.236  63.129  30.575  1.00   47.06  ? 315 PHE B CE2 1 
ATOM   5241  C CZ  . PHE B  1 315 ? 78.701  62.393  29.539  1.00   44.93  ? 315 PHE B CZ  1 
ATOM   5242  N N   . GLY B  1 316 ? 82.564  67.398  26.444  1.00   54.77  ? 316 GLY B N   1 
ATOM   5243  C CA  . GLY B  1 316 ? 83.183  68.605  25.940  1.00   54.86  ? 316 GLY B CA  1 
ATOM   5244  C C   . GLY B  1 316 ? 82.364  69.855  26.174  1.00   56.14  ? 316 GLY B C   1 
ATOM   5245  O O   . GLY B  1 316 ? 82.896  70.954  26.145  1.00   60.65  ? 316 GLY B O   1 
ATOM   5246  N N   . LEU B  1 317 ? 81.069  69.694  26.410  1.00   53.06  ? 317 LEU B N   1 
ATOM   5247  C CA  . LEU B  1 317 ? 80.182  70.840  26.571  1.00   48.18  ? 317 LEU B CA  1 
ATOM   5248  C C   . LEU B  1 317 ? 79.205  70.595  27.742  1.00   46.76  ? 317 LEU B C   1 
ATOM   5249  O O   . LEU B  1 317 ? 78.284  69.758  27.658  1.00   43.39  ? 317 LEU B O   1 
ATOM   5250  C CB  . LEU B  1 317 ? 79.437  71.095  25.260  1.00   43.80  ? 317 LEU B CB  1 
ATOM   5251  C CG  . LEU B  1 317 ? 78.523  72.297  25.115  1.00   43.11  ? 317 LEU B CG  1 
ATOM   5252  C CD1 . LEU B  1 317 ? 79.296  73.589  25.289  1.00   40.08  ? 317 LEU B CD1 1 
ATOM   5253  C CD2 . LEU B  1 317 ? 77.823  72.218  23.782  1.00   43.53  ? 317 LEU B CD2 1 
ATOM   5254  N N   . CYS B  1 318 ? 79.434  71.315  28.838  1.00   47.59  ? 318 CYS B N   1 
ATOM   5255  C CA  . CYS B  1 318 ? 78.631  71.177  30.050  1.00   46.85  ? 318 CYS B CA  1 
ATOM   5256  C C   . CYS B  1 318 ? 77.961  72.475  30.500  1.00   47.75  ? 318 CYS B C   1 
ATOM   5257  O O   . CYS B  1 318 ? 78.433  73.576  30.219  1.00   47.28  ? 318 CYS B O   1 
ATOM   5258  C CB  . CYS B  1 318 ? 79.486  70.642  31.199  1.00   47.58  ? 318 CYS B CB  1 
ATOM   5259  S SG  . CYS B  1 318 ? 80.069  68.969  30.988  1.00   50.79  ? 318 CYS B SG  1 
ATOM   5260  N N   . TYR B  1 319 ? 76.841  72.330  31.198  1.00   49.16  ? 319 TYR B N   1 
ATOM   5261  C CA  . TYR B  1 319 ? 76.096  73.479  31.662  1.00   49.66  ? 319 TYR B CA  1 
ATOM   5262  C C   . TYR B  1 319 ? 75.783  73.394  33.141  1.00   51.82  ? 319 TYR B C   1 
ATOM   5263  O O   . TYR B  1 319 ? 75.803  72.323  33.743  1.00   52.35  ? 319 TYR B O   1 
ATOM   5264  C CB  . TYR B  1 319 ? 74.801  73.587  30.880  1.00   51.66  ? 319 TYR B CB  1 
ATOM   5265  C CG  . TYR B  1 319 ? 75.030  73.850  29.416  1.00   52.06  ? 319 TYR B CG  1 
ATOM   5266  C CD1 . TYR B  1 319 ? 75.215  72.799  28.521  1.00   50.30  ? 319 TYR B CD1 1 
ATOM   5267  C CD2 . TYR B  1 319 ? 75.079  75.145  28.925  1.00   54.23  ? 319 TYR B CD2 1 
ATOM   5268  C CE1 . TYR B  1 319 ? 75.435  73.040  27.181  1.00   49.92  ? 319 TYR B CE1 1 
ATOM   5269  C CE2 . TYR B  1 319 ? 75.294  75.396  27.593  1.00   53.60  ? 319 TYR B CE2 1 
ATOM   5270  C CZ  . TYR B  1 319 ? 75.476  74.345  26.728  1.00   52.90  ? 319 TYR B CZ  1 
ATOM   5271  O OH  . TYR B  1 319 ? 75.689  74.615  25.404  1.00   54.14  ? 319 TYR B OH  1 
ATOM   5272  N N   . ASP B  1 320 ? 75.475  74.539  33.729  1.00   56.49  ? 320 ASP B N   1 
ATOM   5273  C CA  . ASP B  1 320 ? 74.939  74.560  35.072  1.00   62.35  ? 320 ASP B CA  1 
ATOM   5274  C C   . ASP B  1 320 ? 73.500  74.087  34.908  1.00   62.18  ? 320 ASP B C   1 
ATOM   5275  O O   . ASP B  1 320 ? 72.724  74.691  34.174  1.00   62.78  ? 320 ASP B O   1 
ATOM   5276  C CB  . ASP B  1 320 ? 75.069  75.972  35.657  1.00   68.51  ? 320 ASP B CB  1 
ATOM   5277  C CG  . ASP B  1 320 ? 74.334  76.163  36.968  1.00   76.84  ? 320 ASP B CG  1 
ATOM   5278  O OD1 . ASP B  1 320 ? 73.742  75.207  37.507  1.00   79.04  ? 320 ASP B OD1 1 
ATOM   5279  O OD2 . ASP B  1 320 ? 74.384  77.304  37.481  1.00   81.32  1 320 ASP B OD2 1 
ATOM   5280  N N   . SER B  1 321 ? 73.112  73.088  35.683  1.00   61.98  ? 321 SER B N   1 
ATOM   5281  C CA  . SER B  1 321 ? 71.828  72.431  35.498  1.00   62.06  ? 321 SER B CA  1 
ATOM   5282  C C   . SER B  1 321 ? 70.649  73.346  35.761  1.00   67.73  ? 321 SER B C   1 
ATOM   5283  O O   . SER B  1 321 ? 69.587  73.151  35.173  1.00   68.53  ? 321 SER B O   1 
ATOM   5284  C CB  . SER B  1 321 ? 71.717  71.211  36.409  1.00   64.07  ? 321 SER B CB  1 
ATOM   5285  O OG  . SER B  1 321 ? 72.869  70.402  36.334  1.00   64.76  ? 321 SER B OG  1 
ATOM   5286  N N   . ARG B  1 322 ? 70.840  74.335  36.643  1.00   71.40  ? 322 ARG B N   1 
ATOM   5287  C CA  . ARG B  1 322 ? 69.756  75.239  37.038  1.00   75.57  ? 322 ARG B CA  1 
ATOM   5288  C C   . ARG B  1 322 ? 69.347  76.176  35.898  1.00   76.05  ? 322 ARG B C   1 
ATOM   5289  O O   . ARG B  1 322 ? 68.158  76.467  35.737  1.00   78.83  ? 322 ARG B O   1 
ATOM   5290  C CB  . ARG B  1 322 ? 70.138  76.043  38.283  0.0000 78.09  ? 322 ARG B CB  1 
ATOM   5291  C CG  . ARG B  1 322 ? 70.500  75.181  39.471  0.0000 78.39  ? 322 ARG B CG  1 
ATOM   5292  C CD  . ARG B  1 322 ? 70.652  75.986  40.754  0.0000 81.38  ? 322 ARG B CD  1 
ATOM   5293  N NE  . ARG B  1 322 ? 69.982  75.321  41.871  0.0000 83.50  ? 322 ARG B NE  1 
ATOM   5294  C CZ  . ARG B  1 322 ? 69.386  75.946  42.881  0.0000 87.59  ? 322 ARG B CZ  1 
ATOM   5295  N NH1 . ARG B  1 322 ? 69.359  77.271  42.928  0.0000 89.45  ? 322 ARG B NH1 1 
ATOM   5296  N NH2 . ARG B  1 322 ? 68.810  75.240  43.847  0.0000 90.37  ? 322 ARG B NH2 1 
ATOM   5297  N N   . LYS B  1 323 ? 70.287  76.622  35.073  1.00   73.15  ? 323 LYS B N   1 
ATOM   5298  C CA  . LYS B  1 323 ? 69.864  77.384  33.914  1.00   74.33  ? 323 LYS B CA  1 
ATOM   5299  C C   . LYS B  1 323 ? 69.427  76.240  32.972  1.00   78.53  ? 323 LYS B C   1 
ATOM   5300  O O   . LYS B  1 323 ? 69.095  75.158  33.450  1.00   80.38  ? 323 LYS B O   1 
ATOM   5301  C CB  . LYS B  1 323 ? 70.984  78.279  33.366  0.0000 71.09  ? 323 LYS B CB  1 
ATOM   5302  C CG  . LYS B  1 323 ? 70.644  79.018  32.076  0.0000 69.34  ? 323 LYS B CG  1 
ATOM   5303  C CD  . LYS B  1 323 ? 70.406  80.490  32.306  0.0000 72.19  ? 323 LYS B CD  1 
ATOM   5304  C CE  . LYS B  1 323 ? 69.720  81.102  31.109  0.0000 72.22  ? 323 LYS B CE  1 
ATOM   5305  N NZ  . LYS B  1 323 ? 68.501  80.327  30.733  0.0000 72.04  ? 323 LYS B NZ  1 
ATOM   5306  N N   . ILE B  1 324 ? 69.348  76.447  31.668  1.00   81.17  ? 324 ILE B N   1 
ATOM   5307  C CA  . ILE B  1 324 ? 69.079  75.350  30.730  1.00   81.28  ? 324 ILE B CA  1 
ATOM   5308  C C   . ILE B  1 324 ? 67.740  74.636  30.924  1.00   84.81  ? 324 ILE B C   1 
ATOM   5309  O O   . ILE B  1 324 ? 67.124  74.199  29.948  1.00   85.72  ? 324 ILE B O   1 
ATOM   5310  C CB  . ILE B  1 324 ? 70.201  74.264  30.816  1.00   72.10  ? 324 ILE B CB  1 
ATOM   5311  C CG1 . ILE B  1 324 ? 71.574  74.898  30.604  1.00   71.86  ? 324 ILE B CG1 1 
ATOM   5312  C CG2 . ILE B  1 324 ? 69.938  73.063  29.891  1.00   69.48  ? 324 ILE B CG2 1 
ATOM   5313  C CD1 . ILE B  1 324 ? 71.616  75.818  29.441  1.00   72.18  ? 324 ILE B CD1 1 
ATOM   5314  N N   . SER B  1 325 ? 67.294  74.522  32.170  1.00   86.83  ? 325 SER B N   1 
ATOM   5315  C CA  . SER B  1 325 ? 66.041  73.834  32.464  1.00   89.77  ? 325 SER B CA  1 
ATOM   5316  C C   . SER B  1 325 ? 64.961  74.194  31.453  1.00   92.23  ? 325 SER B C   1 
ATOM   5317  O O   . SER B  1 325 ? 64.453  75.314  31.444  1.00   93.24  ? 325 SER B O   1 
ATOM   5318  C CB  . SER B  1 325 ? 65.560  74.151  33.878  1.00   95.03  ? 325 SER B CB  1 
ATOM   5319  O OG  . SER B  1 325 ? 64.455  73.336  34.225  1.00   100.52 ? 325 SER B OG  1 
ATOM   5320  N N   . GLY B  1 326 ? 64.618  73.233  30.602  1.00   93.20  ? 326 GLY B N   1 
ATOM   5321  C CA  . GLY B  1 326 ? 63.628  73.444  29.564  1.00   97.17  ? 326 GLY B CA  1 
ATOM   5322  C C   . GLY B  1 326 ? 64.157  74.331  28.458  1.00   95.16  ? 326 GLY B C   1 
ATOM   5323  O O   . GLY B  1 326 ? 63.399  75.059  27.822  1.00   99.79  ? 326 GLY B O   1 
ATOM   5324  N N   . GLY B  1 327 ? 65.465  74.270  28.230  1.00   88.69  ? 327 GLY B N   1 
ATOM   5325  C CA  . GLY B  1 327 ? 66.103  75.116  27.238  1.00   85.62  ? 327 GLY B CA  1 
ATOM   5326  C C   . GLY B  1 327 ? 66.991  74.382  26.249  1.00   79.87  ? 327 GLY B C   1 
ATOM   5327  O O   . GLY B  1 327 ? 67.768  75.007  25.528  1.00   81.21  ? 327 GLY B O   1 
ATOM   5328  N N   . ALA B  1 328 ? 66.877  73.059  26.210  1.00   72.81  ? 328 ALA B N   1 
ATOM   5329  C CA  . ALA B  1 328 ? 67.644  72.255  25.264  1.00   63.26  ? 328 ALA B CA  1 
ATOM   5330  C C   . ALA B  1 328 ? 66.922  72.194  23.925  1.00   56.18  ? 328 ALA B C   1 
ATOM   5331  O O   . ALA B  1 328 ? 65.695  72.150  23.882  1.00   58.85  ? 328 ALA B O   1 
ATOM   5332  C CB  . ALA B  1 328 ? 67.863  70.856  25.813  1.00   62.63  ? 328 ALA B CB  1 
ATOM   5333  N N   . PRO B  1 329 ? 67.674  72.198  22.830  1.00   49.26  ? 329 PRO B N   1 
ATOM   5334  C CA  . PRO B  1 329 ? 67.048  72.203  21.501  1.00   48.87  ? 329 PRO B CA  1 
ATOM   5335  C C   . PRO B  1 329 ? 66.637  70.820  20.989  1.00   48.96  ? 329 PRO B C   1 
ATOM   5336  O O   . PRO B  1 329 ? 67.058  69.808  21.540  1.00   48.64  ? 329 PRO B O   1 
ATOM   5337  C CB  . PRO B  1 329 ? 68.143  72.786  20.603  1.00   46.88  ? 329 PRO B CB  1 
ATOM   5338  C CG  . PRO B  1 329 ? 69.416  72.494  21.317  1.00   44.57  ? 329 PRO B CG  1 
ATOM   5339  C CD  . PRO B  1 329 ? 69.092  72.587  22.777  1.00   45.95  ? 329 PRO B CD  1 
ATOM   5340  N N   . SER B  1 330 ? 65.815  70.799  19.943  1.00   50.70  ? 330 SER B N   1 
ATOM   5341  C CA  . SER B  1 330 ? 65.497  69.576  19.205  1.00   51.39  ? 330 SER B CA  1 
ATOM   5342  C C   . SER B  1 330 ? 66.762  68.969  18.626  1.00   48.22  ? 330 SER B C   1 
ATOM   5343  O O   . SER B  1 330 ? 67.465  69.633  17.866  1.00   49.40  ? 330 SER B O   1 
ATOM   5344  C CB  . SER B  1 330 ? 64.517  69.857  18.071  1.00   54.03  ? 330 SER B CB  1 
ATOM   5345  O OG  . SER B  1 330 ? 65.217  70.049  16.851  1.00   54.00  ? 330 SER B OG  1 
ATOM   5346  N N   . VAL B  1 331 ? 67.057  67.727  18.997  1.00   40.88  ? 331 VAL B N   1 
ATOM   5347  C CA  . VAL B  1 331 ? 68.137  66.961  18.375  1.00   40.75  ? 331 VAL B CA  1 
ATOM   5348  C C   . VAL B  1 331 ? 67.603  65.698  17.719  1.00   38.52  ? 331 VAL B C   1 
ATOM   5349  O O   . VAL B  1 331 ? 67.149  64.808  18.420  1.00   39.97  ? 331 VAL B O   1 
ATOM   5350  C CB  . VAL B  1 331 ? 69.229  66.576  19.404  1.00   42.63  ? 331 VAL B CB  1 
ATOM   5351  C CG1 . VAL B  1 331 ? 70.288  65.687  18.780  1.00   38.50  ? 331 VAL B CG1 1 
ATOM   5352  C CG2 . VAL B  1 331 ? 69.866  67.834  20.004  1.00   44.53  ? 331 VAL B CG2 1 
ATOM   5353  N N   . ASP B  1 332 ? 67.661  65.633  16.384  1.00   34.27  ? 332 ASP B N   1 
ATOM   5354  C CA  . ASP B  1 332 ? 67.071  64.533  15.607  1.00   33.68  ? 332 ASP B CA  1 
ATOM   5355  C C   . ASP B  1 332 ? 68.073  63.882  14.641  1.00   30.79  ? 332 ASP B C   1 
ATOM   5356  O O   . ASP B  1 332 ? 68.853  64.577  14.003  1.00   32.47  ? 332 ASP B O   1 
ATOM   5357  C CB  . ASP B  1 332 ? 65.889  65.040  14.776  1.00   39.93  ? 332 ASP B CB  1 
ATOM   5358  C CG  . ASP B  1 332 ? 64.862  65.769  15.593  1.00   44.71  ? 332 ASP B CG  1 
ATOM   5359  O OD1 . ASP B  1 332 ? 64.723  65.466  16.787  1.00   46.79  ? 332 ASP B OD1 1 
ATOM   5360  O OD2 . ASP B  1 332 ? 64.225  66.684  15.042  1.00   46.98  ? 332 ASP B OD2 1 
ATOM   5361  N N   . LEU B  1 333 ? 68.035  62.562  14.510  1.00   28.69  ? 333 LEU B N   1 
ATOM   5362  C CA  . LEU B  1 333 ? 68.767  61.866  13.458  1.00   28.55  ? 333 LEU B CA  1 
ATOM   5363  C C   . LEU B  1 333 ? 67.917  61.747  12.217  1.00   31.28  ? 333 LEU B C   1 
ATOM   5364  O O   . LEU B  1 333 ? 66.862  61.136  12.244  1.00   33.43  ? 333 LEU B O   1 
ATOM   5365  C CB  . LEU B  1 333 ? 69.177  60.469  13.904  1.00   26.42  ? 333 LEU B CB  1 
ATOM   5366  C CG  . LEU B  1 333 ? 69.912  60.390  15.233  1.00   24.74  ? 333 LEU B CG  1 
ATOM   5367  C CD1 . LEU B  1 333 ? 70.265  58.958  15.581  1.00   22.73  ? 333 LEU B CD1 1 
ATOM   5368  C CD2 . LEU B  1 333 ? 71.150  61.251  15.116  1.00   28.12  ? 333 LEU B CD2 1 
ATOM   5369  N N   . ILE B  1 334 ? 68.380  62.313  11.123  1.00   29.30  ? 334 ILE B N   1 
ATOM   5370  C CA  . ILE B  1 334 ? 67.671  62.173  9.877   1.00   31.46  ? 334 ILE B CA  1 
ATOM   5371  C C   . ILE B  1 334 ? 68.160  60.921  9.238   1.00   33.02  ? 334 ILE B C   1 
ATOM   5372  O O   . ILE B  1 334 ? 69.334  60.827  8.896   1.00   33.16  ? 334 ILE B O   1 
ATOM   5373  C CB  . ILE B  1 334 ? 67.915  63.341  8.936   1.00   34.20  ? 334 ILE B CB  1 
ATOM   5374  C CG1 . ILE B  1 334 ? 67.749  64.656  9.685   1.00   42.16  ? 334 ILE B CG1 1 
ATOM   5375  C CG2 . ILE B  1 334 ? 66.961  63.290  7.755   1.00   37.37  ? 334 ILE B CG2 1 
ATOM   5376  C CD1 . ILE B  1 334 ? 66.380  64.827  10.295  1.00   42.72  ? 334 ILE B CD1 1 
ATOM   5377  N N   . LEU B  1 335 ? 67.252  59.979  9.013   1.00   32.70  ? 335 LEU B N   1 
ATOM   5378  C CA  . LEU B  1 335 ? 67.669  58.633  8.641   1.00   33.14  ? 335 LEU B CA  1 
ATOM   5379  C C   . LEU B  1 335 ? 67.624  58.387  7.148   1.00   36.81  ? 335 LEU B C   1 
ATOM   5380  O O   . LEU B  1 335 ? 67.285  59.262  6.382   1.00   40.94  ? 335 LEU B O   1 
ATOM   5381  C CB  . LEU B  1 335 ? 66.845  57.582  9.386   1.00   28.58  ? 335 LEU B CB  1 
ATOM   5382  C CG  . LEU B  1 335 ? 66.878  57.703  10.916  1.00   27.04  ? 335 LEU B CG  1 
ATOM   5383  C CD1 . LEU B  1 335 ? 66.051  56.600  11.554  1.00   27.01  ? 335 LEU B CD1 1 
ATOM   5384  C CD2 . LEU B  1 335 ? 68.290  57.734  11.469  1.00   25.05  ? 335 LEU B CD2 1 
ATOM   5385  N N   . ASP B  1 336 ? 67.987  57.172  6.769   1.00   42.66  ? 336 ASP B N   1 
ATOM   5386  C CA  . ASP B  1 336 ? 68.212  56.783  5.390   1.00   48.46  ? 336 ASP B CA  1 
ATOM   5387  C C   . ASP B  1 336 ? 67.151  57.375  4.504   1.00   51.92  ? 336 ASP B C   1 
ATOM   5388  O O   . ASP B  1 336 ? 65.964  57.260  4.767   1.00   52.68  ? 336 ASP B O   1 
ATOM   5389  C CB  . ASP B  1 336 ? 68.241  55.242  5.287   1.00   51.48  ? 336 ASP B CB  1 
ATOM   5390  C CG  . ASP B  1 336 ? 68.673  54.729  3.910   1.00   57.44  ? 336 ASP B CG  1 
ATOM   5391  O OD1 . ASP B  1 336 ? 69.890  54.762  3.600   1.00   58.49  ? 336 ASP B OD1 1 
ATOM   5392  O OD2 . ASP B  1 336 ? 67.799  54.254  3.153   1.00   60.11  ? 336 ASP B OD2 1 
ATOM   5393  N N   . LYS B  1 337 ? 67.622  58.096  3.500   1.00   56.48  ? 337 LYS B N   1 
ATOM   5394  C CA  . LYS B  1 337 ? 66.781  58.628  2.452   1.00   64.27  ? 337 LYS B CA  1 
ATOM   5395  C C   . LYS B  1 337 ? 65.745  59.655  2.949   1.00   69.44  ? 337 LYS B C   1 
ATOM   5396  O O   . LYS B  1 337 ? 64.773  59.942  2.246   1.00   74.82  ? 337 LYS B O   1 
ATOM   5397  C CB  . LYS B  1 337 ? 66.103  57.465  1.738   1.00   64.60  ? 337 LYS B CB  1 
ATOM   5398  C CG  . LYS B  1 337 ? 66.974  56.847  0.668   1.00   66.23  ? 337 LYS B CG  1 
ATOM   5399  C CD  . LYS B  1 337 ? 66.245  55.757  -0.079  1.00   66.69  ? 337 LYS B CD  1 
ATOM   5400  C CE  . LYS B  1 337 ? 67.208  55.004  -0.973  1.00   68.19  ? 337 LYS B CE  1 
ATOM   5401  N NZ  . LYS B  1 337 ? 68.302  55.896  -1.449  1.00   70.20  ? 337 LYS B NZ  1 
ATOM   5402  N N   . ASN B  1 338 ? 65.973  60.216  4.142   1.00   68.66  ? 338 ASN B N   1 
ATOM   5403  C CA  . ASN B  1 338 ? 65.042  61.149  4.816   1.00   70.80  ? 338 ASN B CA  1 
ATOM   5404  C C   . ASN B  1 338 ? 63.615  60.643  4.958   1.00   72.43  ? 338 ASN B C   1 
ATOM   5405  O O   . ASN B  1 338 ? 62.665  61.436  5.036   1.00   74.31  ? 338 ASN B O   1 
ATOM   5406  C CB  . ASN B  1 338 ? 64.979  62.485  4.068   1.00   77.13  ? 338 ASN B CB  1 
ATOM   5407  C CG  . ASN B  1 338 ? 66.341  63.089  3.828   1.00   80.44  ? 338 ASN B CG  1 
ATOM   5408  O OD1 . ASN B  1 338 ? 67.337  62.662  4.407   1.00   79.67  ? 338 ASN B OD1 1 
ATOM   5409  N ND2 . ASN B  1 338 ? 66.393  64.090  2.968   1.00   85.16  ? 338 ASN B ND2 1 
ATOM   5410  N N   . ASP B  1 339 ? 63.464  59.325  4.987   1.00   70.75  ? 339 ASP B N   1 
ATOM   5411  C CA  . ASP B  1 339 ? 62.152  58.724  5.127   1.00   72.23  ? 339 ASP B CA  1 
ATOM   5412  C C   . ASP B  1 339 ? 61.709  58.721  6.574   1.00   70.26  ? 339 ASP B C   1 
ATOM   5413  O O   . ASP B  1 339 ? 60.524  58.559  6.874   1.00   76.22  ? 339 ASP B O   1 
ATOM   5414  C CB  . ASP B  1 339 ? 62.162  57.306  4.590   1.00   72.82  ? 339 ASP B CB  1 
ATOM   5415  C CG  . ASP B  1 339 ? 62.340  57.266  3.101   1.00   78.31  ? 339 ASP B CG  1 
ATOM   5416  O OD1 . ASP B  1 339 ? 61.510  57.855  2.385   1.00   82.56  ? 339 ASP B OD1 1 
ATOM   5417  O OD2 . ASP B  1 339 ? 63.328  56.663  2.642   1.00   79.87  ? 339 ASP B OD2 1 
ATOM   5418  N N   . ALA B  1 340 ? 62.679  58.837  7.470   1.00   60.43  ? 340 ALA B N   1 
ATOM   5419  C CA  . ALA B  1 340 ? 62.403  58.672  8.876   1.00   52.78  ? 340 ALA B CA  1 
ATOM   5420  C C   . ALA B  1 340 ? 63.269  59.598  9.697   1.00   45.08  ? 340 ALA B C   1 
ATOM   5421  O O   . ALA B  1 340 ? 64.217  60.172  9.189   1.00   45.56  ? 340 ALA B O   1 
ATOM   5422  C CB  . ALA B  1 340 ? 62.609  57.216  9.289   1.00   49.13  ? 340 ALA B CB  1 
ATOM   5423  N N   . VAL B  1 341 ? 62.902  59.759  10.962  1.00   41.56  ? 341 VAL B N   1 
ATOM   5424  C CA  . VAL B  1 341 ? 63.594  60.635  11.904  1.00   38.84  ? 341 VAL B CA  1 
ATOM   5425  C C   . VAL B  1 341 ? 63.716  59.919  13.239  1.00   36.05  ? 341 VAL B C   1 
ATOM   5426  O O   . VAL B  1 341 ? 62.750  59.362  13.714  1.00   38.17  ? 341 VAL B O   1 
ATOM   5427  C CB  . VAL B  1 341 ? 62.836  61.952  12.115  1.00   39.91  ? 341 VAL B CB  1 
ATOM   5428  C CG1 . VAL B  1 341 ? 63.311  62.645  13.362  1.00   35.22  ? 341 VAL B CG1 1 
ATOM   5429  C CG2 . VAL B  1 341 ? 62.986  62.834  10.902  1.00   43.39  ? 341 VAL B CG2 1 
ATOM   5430  N N   . TRP B  1 342 ? 64.881  59.912  13.853  1.00   32.16  ? 342 TRP B N   1 
ATOM   5431  C CA  . TRP B  1 342 ? 64.941  59.427  15.215  1.00   29.16  ? 342 TRP B CA  1 
ATOM   5432  C C   . TRP B  1 342 ? 65.105  60.634  16.124  1.00   33.50  ? 342 TRP B C   1 
ATOM   5433  O O   . TRP B  1 342 ? 66.211  61.128  16.277  1.00   34.05  ? 342 TRP B O   1 
ATOM   5434  C CB  . TRP B  1 342 ? 66.093  58.420  15.398  1.00   31.53  ? 342 TRP B CB  1 
ATOM   5435  C CG  . TRP B  1 342 ? 65.913  57.520  16.579  1.00   31.34  ? 342 TRP B CG  1 
ATOM   5436  C CD1 . TRP B  1 342 ? 65.061  57.705  17.642  1.00   33.86  ? 342 TRP B CD1 1 
ATOM   5437  C CD2 . TRP B  1 342 ? 66.543  56.262  16.792  1.00   32.47  ? 342 TRP B CD2 1 
ATOM   5438  N NE1 . TRP B  1 342 ? 65.138  56.643  18.512  1.00   33.62  ? 342 TRP B NE1 1 
ATOM   5439  C CE2 . TRP B  1 342 ? 66.042  55.740  18.013  1.00   34.61  ? 342 TRP B CE2 1 
ATOM   5440  C CE3 . TRP B  1 342 ? 67.485  55.520  16.078  1.00   32.12  ? 342 TRP B CE3 1 
ATOM   5441  C CZ2 . TRP B  1 342 ? 66.463  54.509  18.531  1.00   34.52  ? 342 TRP B CZ2 1 
ATOM   5442  C CZ3 . TRP B  1 342 ? 67.899  54.285  16.597  1.00   30.75  ? 342 TRP B CZ3 1 
ATOM   5443  C CH2 . TRP B  1 342 ? 67.385  53.799  17.809  1.00   32.52  ? 342 TRP B CH2 1 
ATOM   5444  N N   . ARG B  1 343 ? 64.012  61.122  16.701  1.00   36.94  ? 343 ARG B N   1 
ATOM   5445  C CA  . ARG B  1 343 ? 64.070  62.288  17.559  1.00   39.19  ? 343 ARG B CA  1 
ATOM   5446  C C   . ARG B  1 343 ? 64.714  61.853  18.853  1.00   41.61  ? 343 ARG B C   1 
ATOM   5447  O O   . ARG B  1 343 ? 64.348  60.831  19.385  1.00   46.01  ? 343 ARG B O   1 
ATOM   5448  C CB  . ARG B  1 343 ? 62.681  62.878  17.817  1.00   44.17  ? 343 ARG B CB  1 
ATOM   5449  C CG  . ARG B  1 343 ? 62.023  63.520  16.588  1.00   48.96  ? 343 ARG B CG  1 
ATOM   5450  C CD  . ARG B  1 343 ? 60.577  64.048  16.801  1.00   76.10  ? 343 ARG B CD  1 
ATOM   5451  N NE  . ARG B  1 343 ? 59.541  63.049  17.117  1.00   79.03  ? 343 ARG B NE  1 
ATOM   5452  C CZ  . ARG B  1 343 ? 59.012  62.865  18.330  1.00   81.79  ? 343 ARG B CZ  1 
ATOM   5453  N NH1 . ARG B  1 343 ? 59.420  63.605  19.351  1.00   86.59  ? 343 ARG B NH1 1 
ATOM   5454  N NH2 . ARG B  1 343 ? 58.069  61.950  18.532  1.00   80.15  ? 343 ARG B NH2 1 
ATOM   5455  N N   . ILE B  1 344 ? 65.675  62.612  19.360  1.00   39.43  ? 344 ILE B N   1 
ATOM   5456  C CA  . ILE B  1 344 ? 66.338  62.256  20.609  1.00   36.32  ? 344 ILE B CA  1 
ATOM   5457  C C   . ILE B  1 344 ? 65.997  63.196  21.720  1.00   40.43  ? 344 ILE B C   1 
ATOM   5458  O O   . ILE B  1 344 ? 66.223  64.391  21.610  1.00   44.82  ? 344 ILE B O   1 
ATOM   5459  C CB  . ILE B  1 344 ? 67.837  62.256  20.451  1.00   34.14  ? 344 ILE B CB  1 
ATOM   5460  C CG1 . ILE B  1 344 ? 68.204  61.355  19.278  1.00   32.16  ? 344 ILE B CG1 1 
ATOM   5461  C CG2 . ILE B  1 344 ? 68.509  61.790  21.737  1.00   32.99  ? 344 ILE B CG2 1 
ATOM   5462  C CD1 . ILE B  1 344 ? 69.644  61.378  18.934  1.00   29.33  ? 344 ILE B CD1 1 
ATOM   5463  N N   . SER B  1 345 ? 65.474  62.646  22.804  1.00   40.24  ? 345 SER B N   1 
ATOM   5464  C CA  . SER B  1 345 ? 65.047  63.441  23.944  1.00   43.83  ? 345 SER B CA  1 
ATOM   5465  C C   . SER B  1 345 ? 66.183  64.101  24.705  1.00   42.24  ? 345 SER B C   1 
ATOM   5466  O O   . SER B  1 345 ? 67.252  63.511  24.871  1.00   40.14  ? 345 SER B O   1 
ATOM   5467  C CB  . SER B  1 345 ? 64.268  62.563  24.912  1.00   49.89  ? 345 SER B CB  1 
ATOM   5468  O OG  . SER B  1 345 ? 64.291  63.124  26.212  1.00   56.82  ? 345 SER B OG  1 
ATOM   5469  N N   . SER B  1 346 ? 65.934  65.315  25.194  1.00   45.80  ? 346 SER B N   1 
ATOM   5470  C CA  . SER B  1 346 ? 66.937  66.040  25.964  1.00   48.35  ? 346 SER B CA  1 
ATOM   5471  C C   . SER B  1 346 ? 67.158  65.386  27.327  1.00   53.03  ? 346 SER B C   1 
ATOM   5472  O O   . SER B  1 346 ? 68.079  65.745  28.047  1.00   54.68  ? 346 SER B O   1 
ATOM   5473  C CB  . SER B  1 346 ? 66.541  67.496  26.153  1.00   43.43  ? 346 SER B CB  1 
ATOM   5474  O OG  . SER B  1 346 ? 65.545  67.589  27.133  1.00   47.31  ? 346 SER B OG  1 
ATOM   5475  N N   . GLU B  1 347 ? 66.320  64.420  27.685  1.00   54.23  ? 347 GLU B N   1 
ATOM   5476  C CA  . GLU B  1 347 ? 66.510  63.714  28.940  1.00   55.76  ? 347 GLU B CA  1 
ATOM   5477  C C   . GLU B  1 347 ? 67.422  62.553  28.710  1.00   51.18  ? 347 GLU B C   1 
ATOM   5478  O O   . GLU B  1 347 ? 67.895  61.913  29.646  1.00   54.12  ? 347 GLU B O   1 
ATOM   5479  C CB  . GLU B  1 347 ? 65.192  63.191  29.464  1.00   62.17  ? 347 GLU B CB  1 
ATOM   5480  C CG  . GLU B  1 347 ? 64.143  64.216  29.582  1.00   70.77  ? 347 GLU B CG  1 
ATOM   5481  C CD  . GLU B  1 347 ? 62.921  63.631  30.202  1.00   83.47  ? 347 GLU B CD  1 
ATOM   5482  O OE1 . GLU B  1 347 ? 63.052  62.537  30.801  1.00   89.38  ? 347 GLU B OE1 1 
ATOM   5483  O OE2 . GLU B  1 347 ? 61.842  64.257  30.103  1.00   87.40  ? 347 GLU B OE2 1 
ATOM   5484  N N   . ASN B  1 348 ? 67.591  62.245  27.437  1.00   46.54  ? 348 ASN B N   1 
ATOM   5485  C CA  . ASN B  1 348 ? 68.543  61.255  27.003  1.00   45.47  ? 348 ASN B CA  1 
ATOM   5486  C C   . ASN B  1 348 ? 69.884  61.883  26.624  1.00   45.91  ? 348 ASN B C   1 
ATOM   5487  O O   . ASN B  1 348 ? 70.920  61.385  27.031  1.00   47.73  ? 348 ASN B O   1 
ATOM   5488  C CB  . ASN B  1 348 ? 67.947  60.432  25.865  1.00   46.97  ? 348 ASN B CB  1 
ATOM   5489  C CG  . ASN B  1 348 ? 68.857  59.326  25.409  1.00   49.14  ? 348 ASN B CG  1 
ATOM   5490  O OD1 . ASN B  1 348 ? 69.990  59.580  25.021  1.00   49.55  ? 348 ASN B OD1 1 
ATOM   5491  N ND2 . ASN B  1 348 ? 68.385  58.079  25.499  1.00   51.46  ? 348 ASN B ND2 1 
ATOM   5492  N N   . PHE B  1 349 ? 69.885  62.977  25.863  1.00   44.44  ? 349 PHE B N   1 
ATOM   5493  C CA  . PHE B  1 349 ? 71.164  63.476  25.382  1.00   44.45  ? 349 PHE B CA  1 
ATOM   5494  C C   . PHE B  1 349 ? 71.846  64.455  26.343  1.00   51.31  ? 349 PHE B C   1 
ATOM   5495  O O   . PHE B  1 349 ? 73.008  64.791  26.143  1.00   53.28  ? 349 PHE B O   1 
ATOM   5496  C CB  . PHE B  1 349 ? 71.046  64.089  23.954  1.00   36.27  ? 349 PHE B CB  1 
ATOM   5497  C CG  . PHE B  1 349 ? 70.134  65.301  23.809  1.00   36.57  ? 349 PHE B CG  1 
ATOM   5498  C CD1 . PHE B  1 349 ? 70.480  66.549  24.312  1.00   37.02  ? 349 PHE B CD1 1 
ATOM   5499  C CD2 . PHE B  1 349 ? 68.987  65.217  23.030  1.00   36.82  ? 349 PHE B CD2 1 
ATOM   5500  C CE1 . PHE B  1 349 ? 69.635  67.660  24.120  1.00   38.66  ? 349 PHE B CE1 1 
ATOM   5501  C CE2 . PHE B  1 349 ? 68.156  66.336  22.832  1.00   38.73  ? 349 PHE B CE2 1 
ATOM   5502  C CZ  . PHE B  1 349 ? 68.485  67.550  23.374  1.00   38.45  ? 349 PHE B CZ  1 
ATOM   5503  N N   . MET B  1 350 ? 71.154  64.883  27.396  1.00   44.86  ? 350 MET B N   1 
ATOM   5504  C CA  . MET B  1 350 ? 71.800  65.641  28.465  1.00   46.67  ? 350 MET B CA  1 
ATOM   5505  C C   . MET B  1 350 ? 72.158  64.696  29.597  1.00   46.44  ? 350 MET B C   1 
ATOM   5506  O O   . MET B  1 350 ? 71.323  63.929  30.059  1.00   48.53  ? 350 MET B O   1 
ATOM   5507  C CB  . MET B  1 350 ? 70.918  66.787  28.949  1.00   50.82  ? 350 MET B CB  1 
ATOM   5508  C CG  . MET B  1 350 ? 70.716  67.897  27.917  1.00   52.29  ? 350 MET B CG  1 
ATOM   5509  S SD  . MET B  1 350 ? 72.224  68.671  27.273  1.00   50.79  ? 350 MET B SD  1 
ATOM   5510  C CE  . MET B  1 350 ? 72.941  69.398  28.739  1.00   39.02  ? 350 MET B CE  1 
ATOM   5511  N N   . VAL B  1 351 ? 73.419  64.728  30.005  1.00   45.42  ? 351 VAL B N   1 
ATOM   5512  C CA  . VAL B  1 351 ? 73.927  63.850  31.050  1.00   43.97  ? 351 VAL B CA  1 
ATOM   5513  C C   . VAL B  1 351 ? 74.212  64.653  32.306  1.00   47.76  ? 351 VAL B C   1 
ATOM   5514  O O   . VAL B  1 351 ? 74.646  65.790  32.219  1.00   51.20  ? 351 VAL B O   1 
ATOM   5515  C CB  . VAL B  1 351 ? 75.221  63.124  30.601  1.00   45.76  ? 351 VAL B CB  1 
ATOM   5516  C CG1 . VAL B  1 351 ? 75.749  62.204  31.699  1.00   47.44  ? 351 VAL B CG1 1 
ATOM   5517  C CG2 . VAL B  1 351 ? 74.998  62.373  29.301  1.00   40.10  ? 351 VAL B CG2 1 
ATOM   5518  N N   . GLN B  1 352 ? 73.956  64.077  33.474  1.00   49.46  ? 352 GLN B N   1 
ATOM   5519  C CA  . GLN B  1 352 ? 74.190  64.784  34.726  1.00   53.31  ? 352 GLN B CA  1 
ATOM   5520  C C   . GLN B  1 352 ? 75.527  64.413  35.313  1.00   59.08  ? 352 GLN B C   1 
ATOM   5521  O O   . GLN B  1 352 ? 75.591  63.759  36.343  1.00   63.44  ? 352 GLN B O   1 
ATOM   5522  C CB  . GLN B  1 352 ? 73.096  64.526  35.751  1.00   52.32  ? 352 GLN B CB  1 
ATOM   5523  C CG  . GLN B  1 352 ? 72.834  65.737  36.636  1.00   56.76  ? 352 GLN B CG  1 
ATOM   5524  C CD  . GLN B  1 352 ? 72.184  66.884  35.873  1.00   62.35  ? 352 GLN B CD  1 
ATOM   5525  O OE1 . GLN B  1 352 ? 72.382  68.051  36.201  1.00   64.58  ? 352 GLN B OE1 1 
ATOM   5526  N NE2 . GLN B  1 352 ? 71.405  66.548  34.834  1.00   65.41  ? 352 GLN B NE2 1 
ATOM   5527  N N   . ALA B  1 353 ? 76.583  64.792  34.610  1.00   61.60  ? 353 ALA B N   1 
ATOM   5528  C CA  . ALA B  1 353 ? 77.952  64.604  35.062  1.00   65.80  ? 353 ALA B CA  1 
ATOM   5529  C C   . ALA B  1 353 ? 78.160  64.791  36.565  1.00   71.68  ? 353 ALA B C   1 
ATOM   5530  O O   . ALA B  1 353 ? 78.715  63.928  37.223  1.00   75.25  ? 353 ALA B O   1 
ATOM   5531  C CB  . ALA B  1 353 ? 78.865  65.547  34.310  1.00   65.60  ? 353 ALA B CB  1 
ATOM   5532  N N   . GLN B  1 354 ? 77.689  65.894  37.124  1.00   71.72  ? 354 GLN B N   1 
ATOM   5533  C CA  . GLN B  1 354 ? 77.937  66.147  38.537  1.00   72.71  ? 354 GLN B CA  1 
ATOM   5534  C C   . GLN B  1 354 ? 76.729  66.743  39.194  1.00   70.01  ? 354 GLN B C   1 
ATOM   5535  O O   . GLN B  1 354 ? 75.745  67.058  38.526  1.00   69.96  ? 354 GLN B O   1 
ATOM   5536  C CB  . GLN B  1 354 ? 79.124  67.087  38.760  1.00   78.16  ? 354 GLN B CB  1 
ATOM   5537  C CG  . GLN B  1 354 ? 80.488  66.507  38.476  1.00   81.71  ? 354 GLN B CG  1 
ATOM   5538  C CD  . GLN B  1 354 ? 81.578  67.559  38.556  1.00   89.13  ? 354 GLN B CD  1 
ATOM   5539  O OE1 . GLN B  1 354 ? 81.312  68.752  38.426  1.00   92.41  ? 354 GLN B OE1 1 
ATOM   5540  N NE2 . GLN B  1 354 ? 82.815  67.122  38.768  1.00   91.74  ? 354 GLN B NE2 1 
ATOM   5541  N N   . ASP B  1 355 ? 76.789  66.817  40.517  1.00   67.58  ? 355 ASP B N   1 
ATOM   5542  C CA  . ASP B  1 355 ? 75.864  67.625  41.287  1.00   67.92  ? 355 ASP B CA  1 
ATOM   5543  C C   . ASP B  1 355 ? 75.666  68.995  40.644  1.00   67.63  ? 355 ASP B C   1 
ATOM   5544  O O   . ASP B  1 355 ? 76.539  69.851  40.693  1.00   71.43  ? 355 ASP B O   1 
ATOM   5545  C CB  . ASP B  1 355 ? 76.363  67.780  42.720  1.00   73.42  ? 355 ASP B CB  1 
ATOM   5546  C CG  . ASP B  1 355 ? 75.267  68.227  43.686  1.00   79.36  ? 355 ASP B CG  1 
ATOM   5547  O OD1 . ASP B  1 355 ? 74.339  68.950  43.255  1.00   79.43  ? 355 ASP B OD1 1 
ATOM   5548  O OD2 . ASP B  1 355 ? 75.338  67.862  44.884  1.00   83.60  ? 355 ASP B OD2 1 
ATOM   5549  N N   . GLY B  1 356 ? 74.521  69.170  40.002  1.00   64.86  ? 356 GLY B N   1 
ATOM   5550  C CA  . GLY B  1 356 ? 74.174  70.404  39.327  1.00   64.59  ? 356 GLY B CA  1 
ATOM   5551  C C   . GLY B  1 356 ? 74.965  70.733  38.076  1.00   62.59  ? 356 GLY B C   1 
ATOM   5552  O O   . GLY B  1 356 ? 75.020  71.887  37.676  1.00   64.92  ? 356 GLY B O   1 
ATOM   5553  N N   . VAL B  1 357 ? 75.543  69.731  37.423  1.00   59.60  ? 357 VAL B N   1 
ATOM   5554  C CA  . VAL B  1 357 ? 76.212  69.966  36.146  1.00   57.48  ? 357 VAL B CA  1 
ATOM   5555  C C   . VAL B  1 357 ? 75.638  69.063  35.065  1.00   54.46  ? 357 VAL B C   1 
ATOM   5556  O O   . VAL B  1 357 ? 75.669  67.834  35.173  1.00   53.32  ? 357 VAL B O   1 
ATOM   5557  C CB  . VAL B  1 357 ? 77.728  69.762  36.246  1.00   57.43  ? 357 VAL B CB  1 
ATOM   5558  C CG1 . VAL B  1 357 ? 78.388  69.945  34.871  1.00   53.84  ? 357 VAL B CG1 1 
ATOM   5559  C CG2 . VAL B  1 357 ? 78.303  70.727  37.254  1.00   57.29  ? 357 VAL B CG2 1 
ATOM   5560  N N   . SER B  1 358 ? 75.153  69.674  33.995  1.00   52.47  ? 358 SER B N   1 
ATOM   5561  C CA  . SER B  1 358 ? 74.501  68.921  32.937  1.00   47.84  ? 358 SER B CA  1 
ATOM   5562  C C   . SER B  1 358 ? 75.238  69.012  31.600  1.00   46.45  ? 358 SER B C   1 
ATOM   5563  O O   . SER B  1 358 ? 75.339  70.086  31.015  1.00   48.71  ? 358 SER B O   1 
ATOM   5564  C CB  . SER B  1 358 ? 73.080  69.443  32.798  1.00   48.64  ? 358 SER B CB  1 
ATOM   5565  O OG  . SER B  1 358 ? 72.412  68.772  31.769  1.00   48.86  ? 358 SER B OG  1 
ATOM   5566  N N   . CYS B  1 359 ? 75.678  67.868  31.088  1.00   44.82  ? 359 CYS B N   1 
ATOM   5567  C CA  . CYS B  1 359 ? 76.586  67.817  29.947  1.00   40.20  ? 359 CYS B CA  1 
ATOM   5568  C C   . CYS B  1 359 ? 75.977  67.256  28.690  1.00   36.53  ? 359 CYS B C   1 
ATOM   5569  O O   . CYS B  1 359 ? 75.155  66.353  28.742  1.00   35.25  ? 359 CYS B O   1 
ATOM   5570  C CB  . CYS B  1 359 ? 77.777  66.954  30.309  1.00   37.60  ? 359 CYS B CB  1 
ATOM   5571  S SG  . CYS B  1 359 ? 78.727  67.608  31.654  1.00   54.09  ? 359 CYS B SG  1 
ATOM   5572  N N   . LEU B  1 360 ? 76.430  67.754  27.549  1.00   38.80  ? 360 LEU B N   1 
ATOM   5573  C CA  . LEU B  1 360 ? 76.025  67.179  26.271  1.00   36.45  ? 360 LEU B CA  1 
ATOM   5574  C C   . LEU B  1 360 ? 76.671  65.818  26.049  1.00   36.51  ? 360 LEU B C   1 
ATOM   5575  O O   . LEU B  1 360 ? 77.876  65.734  25.827  1.00   40.76  ? 360 LEU B O   1 
ATOM   5576  C CB  . LEU B  1 360 ? 76.383  68.136  25.138  1.00   36.37  ? 360 LEU B CB  1 
ATOM   5577  C CG  . LEU B  1 360 ? 76.106  67.672  23.717  1.00   32.53  ? 360 LEU B CG  1 
ATOM   5578  C CD1 . LEU B  1 360 ? 74.652  67.405  23.559  1.00   31.44  ? 360 LEU B CD1 1 
ATOM   5579  C CD2 . LEU B  1 360 ? 76.545  68.769  22.783  1.00   33.40  ? 360 LEU B CD2 1 
ATOM   5580  N N   . GLY B  1 361 ? 75.853  64.767  26.032  1.00   32.19  ? 361 GLY B N   1 
ATOM   5581  C CA  . GLY B  1 361 ? 76.324  63.391  26.076  1.00   31.15  ? 361 GLY B CA  1 
ATOM   5582  C C   . GLY B  1 361 ? 76.831  62.799  24.772  1.00   29.73  ? 361 GLY B C   1 
ATOM   5583  O O   . GLY B  1 361 ? 76.428  61.720  24.370  1.00   30.46  ? 361 GLY B O   1 
ATOM   5584  N N   . PHE B  1 362 ? 77.706  63.524  24.088  1.00   33.61  ? 362 PHE B N   1 
ATOM   5585  C CA  . PHE B  1 362 ? 78.395  62.999  22.909  1.00   33.26  ? 362 PHE B CA  1 
ATOM   5586  C C   . PHE B  1 362 ? 79.890  63.133  23.103  1.00   33.48  ? 362 PHE B C   1 
ATOM   5587  O O   . PHE B  1 362 ? 80.353  64.155  23.600  1.00   37.82  ? 362 PHE B O   1 
ATOM   5588  C CB  . PHE B  1 362 ? 77.971  63.743  21.662  1.00   32.61  ? 362 PHE B CB  1 
ATOM   5589  C CG  . PHE B  1 362 ? 76.524  63.598  21.349  1.00   33.77  ? 362 PHE B CG  1 
ATOM   5590  C CD1 . PHE B  1 362 ? 75.572  64.268  22.093  1.00   33.73  ? 362 PHE B CD1 1 
ATOM   5591  C CD2 . PHE B  1 362 ? 76.106  62.808  20.295  1.00   32.95  ? 362 PHE B CD2 1 
ATOM   5592  C CE1 . PHE B  1 362 ? 74.235  64.155  21.807  1.00   32.94  ? 362 PHE B CE1 1 
ATOM   5593  C CE2 . PHE B  1 362 ? 74.757  62.687  19.999  1.00   33.30  ? 362 PHE B CE2 1 
ATOM   5594  C CZ  . PHE B  1 362 ? 73.824  63.365  20.757  1.00   33.80  ? 362 PHE B CZ  1 
ATOM   5595  N N   . VAL B  1 363 ? 80.646  62.114  22.718  1.00   29.70  ? 363 VAL B N   1 
ATOM   5596  C CA  . VAL B  1 363 ? 82.076  62.144  22.964  1.00   31.36  ? 363 VAL B CA  1 
ATOM   5597  C C   . VAL B  1 363 ? 82.863  61.982  21.671  1.00   30.21  ? 363 VAL B C   1 
ATOM   5598  O O   . VAL B  1 363 ? 82.390  61.346  20.736  1.00   28.62  ? 363 VAL B O   1 
ATOM   5599  C CB  . VAL B  1 363 ? 82.464  61.070  23.975  1.00   32.59  ? 363 VAL B CB  1 
ATOM   5600  C CG1 . VAL B  1 363 ? 81.572  61.212  25.218  1.00   31.38  ? 363 VAL B CG1 1 
ATOM   5601  C CG2 . VAL B  1 363 ? 82.225  59.734  23.405  1.00   33.41  ? 363 VAL B CG2 1 
ATOM   5602  N N   . ASP B  1 364 ? 84.060  62.572  21.637  1.00   34.02  ? 364 ASP B N   1 
ATOM   5603  C CA  . ASP B  1 364 ? 84.949  62.591  20.462  1.00   38.35  ? 364 ASP B CA  1 
ATOM   5604  C C   . ASP B  1 364 ? 85.635  61.250  20.269  1.00   38.55  ? 364 ASP B C   1 
ATOM   5605  O O   . ASP B  1 364 ? 86.372  60.799  21.137  1.00   39.74  ? 364 ASP B O   1 
ATOM   5606  C CB  . ASP B  1 364 ? 86.020  63.684  20.626  1.00   42.83  ? 364 ASP B CB  1 
ATOM   5607  C CG  . ASP B  1 364 ? 86.796  63.994  19.327  1.00   44.04  ? 364 ASP B CG  1 
ATOM   5608  O OD1 . ASP B  1 364 ? 86.713  63.243  18.339  1.00   43.35  ? 364 ASP B OD1 1 
ATOM   5609  O OD2 . ASP B  1 364 ? 87.550  64.988  19.325  1.00   47.50  1 364 ASP B OD2 1 
ATOM   5610  N N   . GLY B  1 365 ? 85.391  60.612  19.135  1.00   35.72  ? 365 GLY B N   1 
ATOM   5611  C CA  . GLY B  1 365 ? 86.037  59.347  18.851  1.00   33.18  ? 365 GLY B CA  1 
ATOM   5612  C C   . GLY B  1 365 ? 87.416  59.487  18.248  1.00   36.62  ? 365 GLY B C   1 
ATOM   5613  O O   . GLY B  1 365 ? 88.105  58.501  18.031  1.00   39.27  ? 365 GLY B O   1 
ATOM   5614  N N   . GLY B  1 366 ? 87.839  60.716  18.022  1.00   38.70  ? 366 GLY B N   1 
ATOM   5615  C CA  . GLY B  1 366 ? 89.135  60.957  17.433  1.00   43.86  ? 366 GLY B CA  1 
ATOM   5616  C C   . GLY B  1 366 ? 89.032  60.859  15.934  1.00   47.18  ? 366 GLY B C   1 
ATOM   5617  O O   . GLY B  1 366 ? 87.933  60.796  15.383  1.00   46.23  ? 366 GLY B O   1 
ATOM   5618  N N   . VAL B  1 367 ? 90.182  60.835  15.278  1.00   52.26  ? 367 VAL B N   1 
ATOM   5619  C CA  . VAL B  1 367 ? 90.259  60.920  13.827  1.00   55.40  ? 367 VAL B CA  1 
ATOM   5620  C C   . VAL B  1 367 ? 90.290  59.577  13.127  1.00   58.52  ? 367 VAL B C   1 
ATOM   5621  O O   . VAL B  1 367 ? 90.168  59.507  11.911  1.00   62.49  ? 367 VAL B O   1 
ATOM   5622  C CB  . VAL B  1 367 ? 91.500  61.685  13.408  1.00   58.31  ? 367 VAL B CB  1 
ATOM   5623  C CG1 . VAL B  1 367 ? 91.433  63.113  13.939  1.00   57.18  ? 367 VAL B CG1 1 
ATOM   5624  C CG2 . VAL B  1 367 ? 92.727  60.989  13.949  1.00   60.52  ? 367 VAL B CG2 1 
ATOM   5625  N N   . HIS B  1 368 ? 90.507  58.516  13.889  1.00   58.15  ? 368 HIS B N   1 
ATOM   5626  C CA  . HIS B  1 368 ? 90.507  57.154  13.354  1.00   61.27  ? 368 HIS B CA  1 
ATOM   5627  C C   . HIS B  1 368 ? 89.410  56.295  13.969  1.00   60.14  ? 368 HIS B C   1 
ATOM   5628  O O   . HIS B  1 368 ? 89.594  55.098  14.223  1.00   60.53  ? 368 HIS B O   1 
ATOM   5629  C CB  . HIS B  1 368 ? 91.875  56.531  13.599  1.00   66.56  ? 368 HIS B CB  1 
ATOM   5630  C CG  . HIS B  1 368 ? 92.952  57.088  12.721  1.00   70.84  ? 368 HIS B CG  1 
ATOM   5631  N ND1 . HIS B  1 368 ? 94.179  57.487  13.213  1.00   73.00  ? 368 HIS B ND1 1 
ATOM   5632  C CD2 . HIS B  1 368 ? 93.028  57.213  11.376  1.00   73.56  ? 368 HIS B CD2 1 
ATOM   5633  C CE1 . HIS B  1 368 ? 94.930  57.913  12.215  1.00   77.09  ? 368 HIS B CE1 1 
ATOM   5634  N NE2 . HIS B  1 368 ? 94.263  57.742  11.086  1.00   77.48  ? 368 HIS B NE2 1 
ATOM   5635  N N   . ALA B  1 369 ? 88.250  56.916  14.163  1.00   55.77  ? 369 ALA B N   1 
ATOM   5636  C CA  . ALA B  1 369 ? 87.094  56.259  14.744  1.00   46.97  ? 369 ALA B CA  1 
ATOM   5637  C C   . ALA B  1 369 ? 86.572  55.154  13.848  1.00   47.41  ? 369 ALA B C   1 
ATOM   5638  O O   . ALA B  1 369 ? 86.771  55.173  12.636  1.00   49.35  ? 369 ALA B O   1 
ATOM   5639  C CB  . ALA B  1 369 ? 86.010  57.268  15.027  1.00   40.39  ? 369 ALA B CB  1 
ATOM   5640  N N   . ARG B  1 370 ? 85.924  54.171  14.465  1.00   48.14  ? 370 ARG B N   1 
ATOM   5641  C CA  . ARG B  1 370 ? 85.413  53.012  13.746  1.00   49.52  ? 370 ARG B CA  1 
ATOM   5642  C C   . ARG B  1 370 ? 84.330  53.482  12.755  1.00   44.65  ? 370 ARG B C   1 
ATOM   5643  O O   . ARG B  1 370 ? 84.322  53.095  11.583  1.00   45.72  ? 370 ARG B O   1 
ATOM   5644  C CB  . ARG B  1 370 ? 84.851  51.971  14.743  1.00   53.16  ? 370 ARG B CB  1 
ATOM   5645  C CG  . ARG B  1 370 ? 83.959  50.895  14.129  1.00   56.38  ? 370 ARG B CG  1 
ATOM   5646  C CD  . ARG B  1 370 ? 84.795  50.051  13.209  1.00   63.45  ? 370 ARG B CD  1 
ATOM   5647  N NE  . ARG B  1 370 ? 84.044  49.097  12.399  1.00   66.27  ? 370 ARG B NE  1 
ATOM   5648  C CZ  . ARG B  1 370 ? 83.642  49.339  11.149  1.00   68.08  ? 370 ARG B CZ  1 
ATOM   5649  N NH1 . ARG B  1 370 ? 83.907  50.510  10.578  1.00   70.74  ? 370 ARG B NH1 1 
ATOM   5650  N NH2 . ARG B  1 370 ? 82.977  48.417  10.463  1.00   66.10  ? 370 ARG B NH2 1 
ATOM   5651  N N   . ALA B  1 371 ? 83.462  54.375  13.218  1.00   39.07  ? 371 ALA B N   1 
ATOM   5652  C CA  . ALA B  1 371 ? 82.417  54.952  12.376  1.00   35.58  ? 371 ALA B CA  1 
ATOM   5653  C C   . ALA B  1 371 ? 82.270  56.453  12.636  1.00   32.08  ? 371 ALA B C   1 
ATOM   5654  O O   . ALA B  1 371 ? 82.753  56.965  13.641  1.00   32.15  ? 371 ALA B O   1 
ATOM   5655  C CB  . ALA B  1 371 ? 81.093  54.228  12.626  1.00   31.88  ? 371 ALA B CB  1 
ATOM   5656  N N   . GLY B  1 372 ? 81.605  57.164  11.741  1.00   30.29  ? 372 GLY B N   1 
ATOM   5657  C CA  . GLY B  1 372 ? 81.392  58.576  11.976  1.00   30.09  ? 372 GLY B CA  1 
ATOM   5658  C C   . GLY B  1 372 ? 80.527  58.784  13.212  1.00   28.02  ? 372 GLY B C   1 
ATOM   5659  O O   . GLY B  1 372 ? 80.749  59.709  14.002  1.00   32.31  ? 372 GLY B O   1 
ATOM   5660  N N   . ILE B  1 373 ? 79.534  57.918  13.365  1.00   27.68  ? 373 ILE B N   1 
ATOM   5661  C CA  . ILE B  1 373 ? 78.620  57.903  14.513  1.00   27.18  ? 373 ILE B CA  1 
ATOM   5662  C C   . ILE B  1 373 ? 78.482  56.533  15.102  1.00   24.08  ? 373 ILE B C   1 
ATOM   5663  O O   . ILE B  1 373 ? 78.154  55.617  14.386  1.00   27.61  ? 373 ILE B O   1 
ATOM   5664  C CB  . ILE B  1 373 ? 77.212  58.349  14.114  1.00   28.35  ? 373 ILE B CB  1 
ATOM   5665  C CG1 . ILE B  1 373 ? 77.272  59.730  13.463  1.00   31.43  ? 373 ILE B CG1 1 
ATOM   5666  C CG2 . ILE B  1 373 ? 76.280  58.323  15.323  1.00   27.49  ? 373 ILE B CG2 1 
ATOM   5667  C CD1 . ILE B  1 373 ? 75.968  60.193  12.807  1.00   31.15  ? 373 ILE B CD1 1 
ATOM   5668  N N   . ALA B  1 374 ? 78.674  56.393  16.411  1.00   24.64  ? 374 ALA B N   1 
ATOM   5669  C CA  . ALA B  1 374 ? 78.407  55.126  17.085  1.00   24.10  ? 374 ALA B CA  1 
ATOM   5670  C C   . ALA B  1 374 ? 77.424  55.331  18.230  1.00   24.65  ? 374 ALA B C   1 
ATOM   5671  O O   . ALA B  1 374 ? 77.784  55.888  19.259  1.00   28.42  ? 374 ALA B O   1 
ATOM   5672  C CB  . ALA B  1 374 ? 79.704  54.492  17.596  1.00   23.78  ? 374 ALA B CB  1 
ATOM   5673  N N   . LEU B  1 375 ? 76.183  54.907  18.026  1.00   24.01  ? 375 LEU B N   1 
ATOM   5674  C CA  . LEU B  1 375 ? 75.125  55.028  19.026  1.00   24.79  ? 375 LEU B CA  1 
ATOM   5675  C C   . LEU B  1 375 ? 75.312  53.965  20.078  1.00   25.26  ? 375 LEU B C   1 
ATOM   5676  O O   . LEU B  1 375 ? 75.402  52.806  19.740  1.00   27.86  ? 375 LEU B O   1 
ATOM   5677  C CB  . LEU B  1 375 ? 73.764  54.895  18.369  1.00   24.53  ? 375 LEU B CB  1 
ATOM   5678  C CG  . LEU B  1 375 ? 73.528  55.831  17.190  1.00   25.77  ? 375 LEU B CG  1 
ATOM   5679  C CD1 . LEU B  1 375 ? 72.301  55.431  16.390  1.00   24.48  ? 375 LEU B CD1 1 
ATOM   5680  C CD2 . LEU B  1 375 ? 73.353  57.270  17.702  1.00   27.59  ? 375 LEU B CD2 1 
ATOM   5681  N N   . GLY B  1 376 ? 75.395  54.363  21.345  1.00   23.99  ? 376 GLY B N   1 
ATOM   5682  C CA  . GLY B  1 376 ? 75.804  53.452  22.399  1.00   23.37  ? 376 GLY B CA  1 
ATOM   5683  C C   . GLY B  1 376 ? 74.697  53.093  23.349  1.00   24.74  ? 376 GLY B C   1 
ATOM   5684  O O   . GLY B  1 376 ? 73.546  53.324  23.033  1.00   26.10  ? 376 GLY B O   1 
ATOM   5685  N N   . ALA B  1 377 ? 75.046  52.571  24.522  1.00   24.71  ? 377 ALA B N   1 
ATOM   5686  C CA  . ALA B  1 377 ? 74.039  52.065  25.445  1.00   24.89  ? 377 ALA B CA  1 
ATOM   5687  C C   . ALA B  1 377 ? 73.096  53.181  25.924  1.00   28.66  ? 377 ALA B C   1 
ATOM   5688  O O   . ALA B  1 377 ? 71.894  52.967  26.100  1.00   30.33  ? 377 ALA B O   1 
ATOM   5689  C CB  . ALA B  1 377 ? 74.703  51.364  26.621  1.00   23.11  ? 377 ALA B CB  1 
ATOM   5690  N N   . HIS B  1 378 ? 73.634  54.376  26.142  1.00   27.85  ? 378 HIS B N   1 
ATOM   5691  C CA  . HIS B  1 378 ? 72.830  55.466  26.664  1.00   27.13  ? 378 HIS B CA  1 
ATOM   5692  C C   . HIS B  1 378 ? 71.745  55.876  25.670  1.00   25.61  ? 378 HIS B C   1 
ATOM   5693  O O   . HIS B  1 378 ? 70.624  56.198  26.031  1.00   27.89  ? 378 HIS B O   1 
ATOM   5694  C CB  . HIS B  1 378 ? 73.740  56.634  27.006  1.00   29.18  ? 378 HIS B CB  1 
ATOM   5695  C CG  . HIS B  1 378 ? 73.143  57.579  27.980  1.00   37.00  ? 378 HIS B CG  1 
ATOM   5696  N ND1 . HIS B  1 378 ? 73.197  57.362  29.339  1.00   43.34  ? 378 HIS B ND1 1 
ATOM   5697  C CD2 . HIS B  1 378 ? 72.478  58.745  27.808  1.00   41.47  ? 378 HIS B CD2 1 
ATOM   5698  C CE1 . HIS B  1 378 ? 72.578  58.349  29.964  1.00   46.15  ? 378 HIS B CE1 1 
ATOM   5699  N NE2 . HIS B  1 378 ? 72.135  59.204  29.058  1.00   44.57  ? 378 HIS B NE2 1 
ATOM   5700  N N   . HIS B  1 379 ? 72.078  55.842  24.397  1.00   24.60  ? 379 HIS B N   1 
ATOM   5701  C CA  . HIS B  1 379 ? 71.110  56.136  23.350  1.00   23.31  ? 379 HIS B CA  1 
ATOM   5702  C C   . HIS B  1 379 ? 69.930  55.157  23.338  1.00   26.59  ? 379 HIS B C   1 
ATOM   5703  O O   . HIS B  1 379 ? 68.785  55.565  23.179  1.00   29.87  ? 379 HIS B O   1 
ATOM   5704  C CB  . HIS B  1 379 ? 71.804  56.106  21.994  1.00   22.74  ? 379 HIS B CB  1 
ATOM   5705  C CG  . HIS B  1 379 ? 70.876  56.318  20.842  1.00   25.91  ? 379 HIS B CG  1 
ATOM   5706  N ND1 . HIS B  1 379 ? 70.567  57.566  20.354  1.00   27.07  ? 379 HIS B ND1 1 
ATOM   5707  C CD2 . HIS B  1 379 ? 70.168  55.438  20.095  1.00   27.99  ? 379 HIS B CD2 1 
ATOM   5708  C CE1 . HIS B  1 379 ? 69.721  57.449  19.347  1.00   27.30  ? 379 HIS B CE1 1 
ATOM   5709  N NE2 . HIS B  1 379 ? 69.463  56.167  19.170  1.00   27.71  ? 379 HIS B NE2 1 
ATOM   5710  N N   . LEU B  1 380 ? 70.238  53.867  23.517  1.00   27.19  ? 380 LEU B N   1 
ATOM   5711  C CA  . LEU B  1 380 ? 69.282  52.753  23.472  1.00   22.79  ? 380 LEU B CA  1 
ATOM   5712  C C   . LEU B  1 380 ? 68.396  52.653  24.689  1.00   23.90  ? 380 LEU B C   1 
ATOM   5713  O O   . LEU B  1 380 ? 67.313  52.115  24.615  1.00   26.49  ? 380 LEU B O   1 
ATOM   5714  C CB  . LEU B  1 380 ? 70.036  51.434  23.347  1.00   21.33  ? 380 LEU B CB  1 
ATOM   5715  C CG  . LEU B  1 380 ? 70.897  51.258  22.111  1.00   22.59  ? 380 LEU B CG  1 
ATOM   5716  C CD1 . LEU B  1 380 ? 71.781  50.035  22.263  1.00   21.11  ? 380 LEU B CD1 1 
ATOM   5717  C CD2 . LEU B  1 380 ? 69.982  51.107  20.917  1.00   23.19  ? 380 LEU B CD2 1 
ATOM   5718  N N   . GLU B  1 381 ? 68.900  53.116  25.824  1.00   23.59  ? 381 GLU B N   1 
ATOM   5719  C CA  . GLU B  1 381 ? 68.202  53.001  27.084  1.00   23.81  ? 381 GLU B CA  1 
ATOM   5720  C C   . GLU B  1 381 ? 66.857  53.704  27.054  1.00   30.14  ? 381 GLU B C   1 
ATOM   5721  O O   . GLU B  1 381 ? 66.760  54.845  26.591  1.00   33.26  ? 381 GLU B O   1 
ATOM   5722  C CB  . GLU B  1 381 ? 69.059  53.564  28.205  1.00   24.46  ? 381 GLU B CB  1 
ATOM   5723  C CG  . GLU B  1 381 ? 70.182  52.663  28.643  1.00   26.24  ? 381 GLU B CG  1 
ATOM   5724  C CD  . GLU B  1 381 ? 71.192  53.373  29.497  1.00   28.14  ? 381 GLU B CD  1 
ATOM   5725  O OE1 . GLU B  1 381 ? 71.028  54.573  29.746  1.00   29.62  ? 381 GLU B OE1 1 
ATOM   5726  O OE2 . GLU B  1 381 ? 72.122  52.714  29.976  1.00   30.03  1 381 GLU B OE2 1 
ATOM   5727  N N   . GLU B  1 382 ? 65.844  53.009  27.597  1.00   31.16  ? 382 GLU B N   1 
ATOM   5728  C CA  . GLU B  1 382 ? 64.441  53.429  27.655  1.00   28.28  ? 382 GLU B CA  1 
ATOM   5729  C C   . GLU B  1 382 ? 63.785  53.589  26.298  1.00   27.12  ? 382 GLU B C   1 
ATOM   5730  O O   . GLU B  1 382 ? 62.822  54.336  26.139  1.00   28.43  ? 382 GLU B O   1 
ATOM   5731  C CB  . GLU B  1 382 ? 64.300  54.728  28.437  1.00   31.68  ? 382 GLU B CB  1 
ATOM   5732  C CG  . GLU B  1 382 ? 64.731  54.614  29.884  1.00   34.80  ? 382 GLU B CG  1 
ATOM   5733  C CD  . GLU B  1 382 ? 64.066  53.450  30.589  1.00   37.29  ? 382 GLU B CD  1 
ATOM   5734  O OE1 . GLU B  1 382 ? 62.877  53.179  30.342  1.00   41.19  ? 382 GLU B OE1 1 
ATOM   5735  O OE2 . GLU B  1 382 ? 64.729  52.805  31.412  1.00   37.95  1 382 GLU B OE2 1 
ATOM   5736  N N   . ASN B  1 383 ? 64.314  52.876  25.322  1.00   25.59  ? 383 ASN B N   1 
ATOM   5737  C CA  . ASN B  1 383 ? 63.693  52.762  24.019  1.00   27.62  ? 383 ASN B CA  1 
ATOM   5738  C C   . ASN B  1 383 ? 63.514  51.308  23.694  1.00   26.41  ? 383 ASN B C   1 
ATOM   5739  O O   . ASN B  1 383 ? 64.334  50.480  24.065  1.00   28.28  ? 383 ASN B O   1 
ATOM   5740  C CB  . ASN B  1 383 ? 64.547  53.424  22.937  1.00   27.82  ? 383 ASN B CB  1 
ATOM   5741  C CG  . ASN B  1 383 ? 64.632  54.916  23.098  1.00   31.43  ? 383 ASN B CG  1 
ATOM   5742  O OD1 . ASN B  1 383 ? 63.647  55.637  22.909  1.00   32.93  ? 383 ASN B OD1 1 
ATOM   5743  N ND2 . ASN B  1 383 ? 65.816  55.398  23.455  1.00   31.60  ? 383 ASN B ND2 1 
ATOM   5744  N N   . LEU B  1 384 ? 62.453  50.988  22.985  1.00   27.21  ? 384 LEU B N   1 
ATOM   5745  C CA  . LEU B  1 384 ? 62.320  49.643  22.478  1.00   27.68  ? 384 LEU B CA  1 
ATOM   5746  C C   . LEU B  1 384 ? 62.857  49.575  21.069  1.00   28.03  ? 384 LEU B C   1 
ATOM   5747  O O   . LEU B  1 384 ? 62.311  50.231  20.193  1.00   29.24  ? 384 LEU B O   1 
ATOM   5748  C CB  . LEU B  1 384 ? 60.870  49.221  22.482  1.00   28.61  ? 384 LEU B CB  1 
ATOM   5749  C CG  . LEU B  1 384 ? 60.697  47.847  21.880  1.00   28.64  ? 384 LEU B CG  1 
ATOM   5750  C CD1 . LEU B  1 384 ? 61.187  46.755  22.802  1.00   30.80  ? 384 LEU B CD1 1 
ATOM   5751  C CD2 . LEU B  1 384 ? 59.256  47.666  21.519  1.00   32.14  ? 384 LEU B CD2 1 
ATOM   5752  N N   . VAL B  1 385 ? 63.912  48.782  20.855  1.00   29.20  ? 385 VAL B N   1 
ATOM   5753  C CA  . VAL B  1 385 ? 64.578  48.700  19.558  1.00   28.54  ? 385 VAL B CA  1 
ATOM   5754  C C   . VAL B  1 385 ? 64.525  47.266  18.980  1.00   26.28  ? 385 VAL B C   1 
ATOM   5755  O O   . VAL B  1 385 ? 65.134  46.340  19.513  1.00   23.96  ? 385 VAL B O   1 
ATOM   5756  C CB  . VAL B  1 385 ? 66.047  49.167  19.674  1.00   27.35  ? 385 VAL B CB  1 
ATOM   5757  C CG1 . VAL B  1 385 ? 66.704  49.229  18.291  1.00   24.52  ? 385 VAL B CG1 1 
ATOM   5758  C CG2 . VAL B  1 385 ? 66.107  50.533  20.341  1.00   25.10  ? 385 VAL B CG2 1 
ATOM   5759  N N   . VAL B  1 386 ? 63.815  47.117  17.862  1.00   25.75  ? 386 VAL B N   1 
ATOM   5760  C CA  . VAL B  1 386 ? 63.548  45.813  17.260  1.00   27.82  ? 386 VAL B CA  1 
ATOM   5761  C C   . VAL B  1 386 ? 64.452  45.533  16.095  1.00   27.19  ? 386 VAL B C   1 
ATOM   5762  O O   . VAL B  1 386 ? 64.442  46.254  15.105  1.00   26.99  ? 386 VAL B O   1 
ATOM   5763  C CB  . VAL B  1 386 ? 62.088  45.702  16.740  1.00   32.07  ? 386 VAL B CB  1 
ATOM   5764  C CG1 . VAL B  1 386 ? 61.840  44.344  16.095  1.00   31.05  ? 386 VAL B CG1 1 
ATOM   5765  C CG2 . VAL B  1 386 ? 61.115  45.951  17.853  1.00   31.60  ? 386 VAL B CG2 1 
ATOM   5766  N N   . PHE B  1 387 ? 65.209  44.457  16.214  1.00   28.02  ? 387 PHE B N   1 
ATOM   5767  C CA  . PHE B  1 387 ? 66.082  43.993  15.158  1.00   26.89  ? 387 PHE B CA  1 
ATOM   5768  C C   . PHE B  1 387 ? 65.395  42.923  14.335  1.00   26.40  ? 387 PHE B C   1 
ATOM   5769  O O   . PHE B  1 387 ? 65.389  41.754  14.676  1.00   29.97  ? 387 PHE B O   1 
ATOM   5770  C CB  . PHE B  1 387 ? 67.383  43.472  15.753  1.00   25.45  ? 387 PHE B CB  1 
ATOM   5771  C CG  . PHE B  1 387 ? 68.212  44.542  16.383  1.00   24.80  ? 387 PHE B CG  1 
ATOM   5772  C CD1 . PHE B  1 387 ? 67.930  44.993  17.652  1.00   24.99  ? 387 PHE B CD1 1 
ATOM   5773  C CD2 . PHE B  1 387 ? 69.254  45.119  15.691  1.00   28.39  ? 387 PHE B CD2 1 
ATOM   5774  C CE1 . PHE B  1 387 ? 68.685  45.988  18.234  1.00   27.98  ? 387 PHE B CE1 1 
ATOM   5775  C CE2 . PHE B  1 387 ? 70.018  46.126  16.265  1.00   29.57  ? 387 PHE B CE2 1 
ATOM   5776  C CZ  . PHE B  1 387 ? 69.732  46.558  17.544  1.00   27.69  ? 387 PHE B CZ  1 
ATOM   5777  N N   . ASP B  1 388 ? 64.814  43.366  13.238  1.00   25.68  ? 388 ASP B N   1 
ATOM   5778  C CA  . ASP B  1 388 ? 64.035  42.526  12.350  1.00   28.68  ? 388 ASP B CA  1 
ATOM   5779  C C   . ASP B  1 388 ? 64.942  41.969  11.257  1.00   30.14  ? 388 ASP B C   1 
ATOM   5780  O O   . ASP B  1 388 ? 65.121  42.576  10.212  1.00   33.89  ? 388 ASP B O   1 
ATOM   5781  C CB  . ASP B  1 388 ? 62.870  43.355  11.775  1.00   28.56  ? 388 ASP B CB  1 
ATOM   5782  C CG  . ASP B  1 388 ? 61.876  42.530  10.974  1.00   38.42  ? 388 ASP B CG  1 
ATOM   5783  O OD1 . ASP B  1 388 ? 62.140  41.345  10.682  1.00   39.95  ? 388 ASP B OD1 1 
ATOM   5784  O OD2 . ASP B  1 388 ? 60.822  43.097  10.610  1.00   43.59  1 388 ASP B OD2 1 
ATOM   5785  N N   . LEU B  1 389 ? 65.522  40.804  11.497  1.00   27.53  ? 389 LEU B N   1 
ATOM   5786  C CA  . LEU B  1 389 ? 66.490  40.263  10.560  1.00   28.28  ? 389 LEU B CA  1 
ATOM   5787  C C   . LEU B  1 389 ? 65.866  39.673  9.293   1.00   29.34  ? 389 LEU B C   1 
ATOM   5788  O O   . LEU B  1 389 ? 66.509  39.622  8.258   1.00   32.15  ? 389 LEU B O   1 
ATOM   5789  C CB  . LEU B  1 389 ? 67.355  39.242  11.283  1.00   30.62  ? 389 LEU B CB  1 
ATOM   5790  C CG  . LEU B  1 389 ? 67.867  39.847  12.601  1.00   31.50  ? 389 LEU B CG  1 
ATOM   5791  C CD1 . LEU B  1 389 ? 68.420  38.802  13.503  1.00   32.48  ? 389 LEU B CD1 1 
ATOM   5792  C CD2 . LEU B  1 389 ? 68.925  40.918  12.353  1.00   31.33  ? 389 LEU B CD2 1 
ATOM   5793  N N   . GLU B  1 390 ? 64.606  39.260  9.356   1.00   30.28  ? 390 GLU B N   1 
ATOM   5794  C CA  . GLU B  1 390 ? 63.957  38.673  8.187   1.00   30.07  ? 390 GLU B CA  1 
ATOM   5795  C C   . GLU B  1 390 ? 63.703  39.697  7.101   1.00   31.51  ? 390 GLU B C   1 
ATOM   5796  O O   . GLU B  1 390 ? 63.694  39.356  5.926   1.00   35.56  ? 390 GLU B O   1 
ATOM   5797  C CB  . GLU B  1 390 ? 62.652  38.009  8.591   1.00   32.53  ? 390 GLU B CB  1 
ATOM   5798  C CG  . GLU B  1 390 ? 62.931  36.880  9.521   1.00   38.12  ? 390 GLU B CG  1 
ATOM   5799  C CD  . GLU B  1 390 ? 61.800  35.919  9.691   1.00   46.49  ? 390 GLU B CD  1 
ATOM   5800  O OE1 . GLU B  1 390 ? 60.642  36.302  9.379   1.00   52.76  ? 390 GLU B OE1 1 
ATOM   5801  O OE2 . GLU B  1 390 ? 62.092  34.778  10.135  1.00   44.70  ? 390 GLU B OE2 1 
ATOM   5802  N N   . ARG B  1 391 ? 63.497  40.949  7.498   1.00   31.52  ? 391 ARG B N   1 
ATOM   5803  C CA  . ARG B  1 391 ? 63.241  42.035  6.553   1.00   34.60  ? 391 ARG B CA  1 
ATOM   5804  C C   . ARG B  1 391 ? 64.419  43.029  6.503   1.00   35.13  ? 391 ARG B C   1 
ATOM   5805  O O   . ARG B  1 391 ? 64.383  44.015  5.786   1.00   40.70  ? 391 ARG B O   1 
ATOM   5806  C CB  A ARG B  1 391 ? 61.938  42.765  6.921   0.50   35.26  ? 391 ARG B CB  1 
ATOM   5807  C CB  B ARG B  1 391 ? 61.934  42.751  6.924   0.50   35.24  ? 391 ARG B CB  1 
ATOM   5808  C CG  A ARG B  1 391 ? 60.730  42.326  6.105   0.50   38.94  ? 391 ARG B CG  1 
ATOM   5809  C CG  B ARG B  1 391 ? 60.745  41.805  7.018   0.50   37.41  ? 391 ARG B CG  1 
ATOM   5810  C CD  A ARG B  1 391 ? 59.418  42.746  6.738   0.50   41.45  ? 391 ARG B CD  1 
ATOM   5811  C CD  B ARG B  1 391 ? 59.439  42.539  7.223   0.50   40.67  ? 391 ARG B CD  1 
ATOM   5812  N NE  A ARG B  1 391 ? 59.253  42.146  8.055   0.50   41.48  ? 391 ARG B NE  1 
ATOM   5813  N NE  B ARG B  1 391 ? 59.268  43.629  6.273   0.50   42.21  ? 391 ARG B NE  1 
ATOM   5814  C CZ  A ARG B  1 391 ? 58.084  41.971  8.661   0.50   43.41  ? 391 ARG B CZ  1 
ATOM   5815  C CZ  B ARG B  1 391 ? 58.091  44.146  5.943   0.50   43.97  ? 391 ARG B CZ  1 
ATOM   5816  N NH1 A ARG B  1 391 ? 56.963  42.339  8.061   0.50   43.81  ? 391 ARG B NH1 1 
ATOM   5817  N NH1 B ARG B  1 391 ? 56.981  43.647  6.466   0.50   38.34  ? 391 ARG B NH1 1 
ATOM   5818  N NH2 A ARG B  1 391 ? 58.037  41.414  9.865   0.50   43.63  ? 391 ARG B NH2 1 
ATOM   5819  N NH2 B ARG B  1 391 ? 58.025  45.148  5.079   0.50   44.19  ? 391 ARG B NH2 1 
ATOM   5820  N N   . SER B  1 392 ? 65.466  42.736  7.261   1.00   29.84  ? 392 SER B N   1 
ATOM   5821  C CA  . SER B  1 392 ? 66.669  43.559  7.319   1.00   26.78  ? 392 SER B CA  1 
ATOM   5822  C C   . SER B  1 392 ? 66.367  45.018  7.647   1.00   26.03  ? 392 SER B C   1 
ATOM   5823  O O   . SER B  1 392 ? 66.688  45.926  6.884   1.00   25.99  ? 392 SER B O   1 
ATOM   5824  C CB  . SER B  1 392 ? 67.437  43.444  5.999   1.00   27.76  ? 392 SER B CB  1 
ATOM   5825  O OG  . SER B  1 392 ? 68.780  43.860  6.161   1.00   27.09  ? 392 SER B OG  1 
ATOM   5826  N N   . ARG B  1 393 ? 65.740  45.240  8.795   1.00   24.44  ? 393 ARG B N   1 
ATOM   5827  C CA  . ARG B  1 393 ? 65.370  46.575  9.197   1.00   24.06  ? 393 ARG B CA  1 
ATOM   5828  C C   . ARG B  1 393 ? 65.385  46.673  10.706  1.00   27.48  ? 393 ARG B C   1 
ATOM   5829  O O   . ARG B  1 393 ? 65.298  45.666  11.394  1.00   27.60  ? 393 ARG B O   1 
ATOM   5830  C CB  . ARG B  1 393 ? 63.984  46.936  8.637   1.00   24.76  ? 393 ARG B CB  1 
ATOM   5831  C CG  . ARG B  1 393 ? 62.888  46.092  9.215   1.00   25.21  ? 393 ARG B CG  1 
ATOM   5832  C CD  . ARG B  1 393 ? 61.564  46.291  8.537   1.00   31.72  ? 393 ARG B CD  1 
ATOM   5833  N NE  . ARG B  1 393 ? 60.572  45.553  9.303   1.00   33.61  ? 393 ARG B NE  1 
ATOM   5834  C CZ  . ARG B  1 393 ? 59.264  45.763  9.262   1.00   37.30  ? 393 ARG B CZ  1 
ATOM   5835  N NH1 . ARG B  1 393 ? 58.756  46.715  8.493   1.00   36.19  ? 393 ARG B NH1 1 
ATOM   5836  N NH2 . ARG B  1 393 ? 58.466  45.019  10.018  1.00   41.06  ? 393 ARG B NH2 1 
ATOM   5837  N N   . VAL B  1 394 ? 65.526  47.890  11.213  1.00   28.36  ? 394 VAL B N   1 
ATOM   5838  C CA  . VAL B  1 394 ? 65.436  48.173  12.642  1.00   28.75  ? 394 VAL B CA  1 
ATOM   5839  C C   . VAL B  1 394 ? 64.217  49.074  12.922  1.00   31.32  ? 394 VAL B C   1 
ATOM   5840  O O   . VAL B  1 394 ? 64.026  50.059  12.218  1.00   31.58  ? 394 VAL B O   1 
ATOM   5841  C CB  . VAL B  1 394 ? 66.709  48.878  13.142  1.00   30.64  ? 394 VAL B CB  1 
ATOM   5842  C CG1 . VAL B  1 394 ? 66.565  49.325  14.579  1.00   31.57  ? 394 VAL B CG1 1 
ATOM   5843  C CG2 . VAL B  1 394 ? 67.888  47.991  13.004  1.00   30.09  ? 394 VAL B CG2 1 
ATOM   5844  N N   . GLY B  1 395 ? 63.425  48.755  13.952  1.00   29.81  ? 395 GLY B N   1 
ATOM   5845  C CA  . GLY B  1 395 ? 62.291  49.570  14.390  1.00   27.16  ? 395 GLY B CA  1 
ATOM   5846  C C   . GLY B  1 395 ? 62.493  50.159  15.780  1.00   27.79  ? 395 GLY B C   1 
ATOM   5847  O O   . GLY B  1 395 ? 63.197  49.569  16.582  1.00   28.39  ? 395 GLY B O   1 
ATOM   5848  N N   . PHE B  1 396 ? 61.908  51.328  16.068  1.00   29.63  ? 396 PHE B N   1 
ATOM   5849  C CA  . PHE B  1 396 ? 62.056  51.960  17.390  1.00   29.09  ? 396 PHE B CA  1 
ATOM   5850  C C   . PHE B  1 396 ? 60.796  52.744  17.762  1.00   29.60  ? 396 PHE B C   1 
ATOM   5851  O O   . PHE B  1 396 ? 59.984  53.057  16.900  1.00   33.44  ? 396 PHE B O   1 
ATOM   5852  C CB  . PHE B  1 396 ? 63.292  52.868  17.415  1.00   28.83  ? 396 PHE B CB  1 
ATOM   5853  C CG  . PHE B  1 396 ? 63.325  53.853  16.280  1.00   31.61  ? 396 PHE B CG  1 
ATOM   5854  C CD1 . PHE B  1 396 ? 62.670  55.068  16.377  1.00   34.48  ? 396 PHE B CD1 1 
ATOM   5855  C CD2 . PHE B  1 396 ? 63.970  53.541  15.092  1.00   32.39  ? 396 PHE B CD2 1 
ATOM   5856  C CE1 . PHE B  1 396 ? 62.672  55.974  15.311  1.00   36.28  ? 396 PHE B CE1 1 
ATOM   5857  C CE2 . PHE B  1 396 ? 63.978  54.436  14.024  1.00   32.95  ? 396 PHE B CE2 1 
ATOM   5858  C CZ  . PHE B  1 396 ? 63.330  55.654  14.136  1.00   34.55  ? 396 PHE B CZ  1 
ATOM   5859  N N   . ASN B  1 397 ? 60.604  53.037  19.046  1.00   29.70  ? 397 ASN B N   1 
ATOM   5860  C CA  . ASN B  1 397 ? 59.424  53.792  19.452  1.00   31.54  ? 397 ASN B CA  1 
ATOM   5861  C C   . ASN B  1 397 ? 59.499  55.216  18.910  1.00   33.35  ? 397 ASN B C   1 
ATOM   5862  O O   . ASN B  1 397 ? 60.543  55.851  18.981  1.00   33.75  ? 397 ASN B O   1 
ATOM   5863  C CB  . ASN B  1 397 ? 59.243  53.788  20.978  1.00   29.30  ? 397 ASN B CB  1 
ATOM   5864  C CG  . ASN B  1 397 ? 60.502  54.118  21.724  1.00   25.93  ? 397 ASN B CG  1 
ATOM   5865  O OD1 . ASN B  1 397 ? 61.473  53.398  21.647  1.00   28.23  ? 397 ASN B OD1 1 
ATOM   5866  N ND2 . ASN B  1 397 ? 60.471  55.170  22.503  1.00   28.30  ? 397 ASN B ND2 1 
ATOM   5867  N N   . SER B  1 398 ? 58.404  55.689  18.315  1.00   35.90  ? 398 SER B N   1 
ATOM   5868  C CA  . SER B  1 398 ? 58.360  57.014  17.723  1.00   37.69  ? 398 SER B CA  1 
ATOM   5869  C C   . SER B  1 398 ? 57.967  58.067  18.735  1.00   38.96  ? 398 SER B C   1 
ATOM   5870  O O   . SER B  1 398 ? 58.092  59.259  18.487  1.00   41.96  ? 398 SER B O   1 
ATOM   5871  C CB  . SER B  1 398 ? 57.372  57.045  16.567  1.00   40.35  ? 398 SER B CB  1 
ATOM   5872  O OG  . SER B  1 398 ? 56.090  56.652  17.019  1.00   43.68  ? 398 SER B OG  1 
ATOM   5873  N N   . ASN B  1 399 ? 57.468  57.636  19.876  1.00   37.48  ? 399 ASN B N   1 
ATOM   5874  C CA  . ASN B  1 399 ? 57.288  58.566  20.967  1.00   38.90  ? 399 ASN B CA  1 
ATOM   5875  C C   . ASN B  1 399 ? 57.999  57.957  22.153  1.00   34.72  ? 399 ASN B C   1 
ATOM   5876  O O   . ASN B  1 399 ? 58.217  56.752  22.187  1.00   35.13  ? 399 ASN B O   1 
ATOM   5877  C CB  . ASN B  1 399 ? 55.808  58.822  21.270  1.00   44.84  ? 399 ASN B CB  1 
ATOM   5878  C CG  . ASN B  1 399 ? 55.057  59.347  20.075  1.00   49.46  ? 399 ASN B CG  1 
ATOM   5879  O OD1 . ASN B  1 399 ? 55.244  60.487  19.678  1.00   52.53  ? 399 ASN B OD1 1 
ATOM   5880  N ND2 . ASN B  1 399 ? 54.170  58.535  19.523  1.00   51.08  ? 399 ASN B ND2 1 
ATOM   5881  N N   . SER B  1 400 ? 58.347  58.772  23.134  1.00   34.55  ? 400 SER B N   1 
ATOM   5882  C CA  . SER B  1 400 ? 59.069  58.266  24.284  1.00   35.59  ? 400 SER B CA  1 
ATOM   5883  C C   . SER B  1 400 ? 58.215  57.231  24.994  1.00   41.19  ? 400 SER B C   1 
ATOM   5884  O O   . SER B  1 400 ? 56.995  57.326  24.972  1.00   44.90  ? 400 SER B O   1 
ATOM   5885  C CB  . SER B  1 400 ? 59.417  59.394  25.243  1.00   34.88  ? 400 SER B CB  1 
ATOM   5886  O OG  . SER B  1 400 ? 58.247  59.825  25.913  1.00   39.42  ? 400 SER B OG  1 
ATOM   5887  N N   . LEU B  1 401 ? 58.853  56.242  25.614  1.00   42.10  ? 401 LEU B N   1 
ATOM   5888  C CA  . LEU B  1 401 ? 58.116  55.256  26.387  1.00   43.89  ? 401 LEU B CA  1 
ATOM   5889  C C   . LEU B  1 401 ? 57.340  55.962  27.478  1.00   46.94  ? 401 LEU B C   1 
ATOM   5890  O O   . LEU B  1 401 ? 56.205  55.600  27.759  1.00   49.81  ? 401 LEU B O   1 
ATOM   5891  C CB  . LEU B  1 401 ? 59.044  54.212  27.005  1.00   41.55  ? 401 LEU B CB  1 
ATOM   5892  C CG  . LEU B  1 401 ? 59.782  53.308  26.025  1.00   38.68  ? 401 LEU B CG  1 
ATOM   5893  C CD1 . LEU B  1 401 ? 60.399  52.151  26.760  1.00   33.37  ? 401 LEU B CD1 1 
ATOM   5894  C CD2 . LEU B  1 401 ? 58.855  52.849  24.921  1.00   41.02  ? 401 LEU B CD2 1 
ATOM   5895  N N   . LYS B  1 402 ? 57.926  56.999  28.069  1.00   45.86  ? 402 LYS B N   1 
ATOM   5896  C CA  . LYS B  1 402 ? 57.267  57.655  29.193  1.00   46.30  ? 402 LYS B CA  1 
ATOM   5897  C C   . LYS B  1 402 ? 55.947  58.287  28.797  1.00   47.83  ? 402 LYS B C   1 
ATOM   5898  O O   . LYS B  1 402 ? 55.011  58.335  29.597  1.00   50.25  ? 402 LYS B O   1 
ATOM   5899  C CB  . LYS B  1 402 ? 58.183  58.692  29.820  1.00   47.99  ? 402 LYS B CB  1 
ATOM   5900  C CG  . LYS B  1 402 ? 57.500  59.563  30.838  1.00   57.27  ? 402 LYS B CG  1 
ATOM   5901  C CD  . LYS B  1 402 ? 58.477  60.479  31.561  1.00   63.48  ? 402 LYS B CD  1 
ATOM   5902  C CE  . LYS B  1 402 ? 58.792  61.749  30.796  1.00   67.63  ? 402 LYS B CE  1 
ATOM   5903  N NZ  . LYS B  1 402 ? 59.605  62.685  31.641  1.00   69.71  ? 402 LYS B NZ  1 
ATOM   5904  N N   . SER B  1 403 ? 55.836  58.697  27.540  1.00   48.08  ? 403 SER B N   1 
ATOM   5905  C CA  . SER B  1 403 ? 54.579  59.270  27.053  1.00   51.87  ? 403 SER B CA  1 
ATOM   5906  C C   . SER B  1 403 ? 53.464  58.226  26.969  1.00   50.07  ? 403 SER B C   1 
ATOM   5907  O O   . SER B  1 403 ? 52.298  58.580  26.841  1.00   53.15  ? 403 SER B O   1 
ATOM   5908  C CB  . SER B  1 403 ? 54.782  59.950  25.691  1.00   53.34  ? 403 SER B CB  1 
ATOM   5909  O OG  . SER B  1 403 ? 54.691  59.037  24.611  1.00   52.40  ? 403 SER B OG  1 
ATOM   5910  N N   . TYR B  1 404 ? 53.827  56.948  27.040  1.00   45.17  ? 404 TYR B N   1 
ATOM   5911  C CA  . TYR B  1 404 ? 52.849  55.868  27.112  1.00   44.00  ? 404 TYR B CA  1 
ATOM   5912  C C   . TYR B  1 404 ? 52.618  55.481  28.559  1.00   45.91  ? 404 TYR B C   1 
ATOM   5913  O O   . TYR B  1 404 ? 51.786  54.624  28.851  1.00   47.71  ? 404 TYR B O   1 
ATOM   5914  C CB  . TYR B  1 404 ? 53.309  54.638  26.320  1.00   40.57  ? 404 TYR B CB  1 
ATOM   5915  C CG  . TYR B  1 404 ? 53.469  54.867  24.839  1.00   40.71  ? 404 TYR B CG  1 
ATOM   5916  C CD1 . TYR B  1 404 ? 52.395  54.752  23.990  1.00   44.54  ? 404 TYR B CD1 1 
ATOM   5917  C CD2 . TYR B  1 404 ? 54.694  55.205  24.296  1.00   40.52  ? 404 TYR B CD2 1 
ATOM   5918  C CE1 . TYR B  1 404 ? 52.528  54.965  22.645  1.00   46.13  ? 404 TYR B CE1 1 
ATOM   5919  C CE2 . TYR B  1 404 ? 54.839  55.417  22.947  1.00   41.19  ? 404 TYR B CE2 1 
ATOM   5920  C CZ  . TYR B  1 404 ? 53.749  55.299  22.125  1.00   45.21  ? 404 TYR B CZ  1 
ATOM   5921  O OH  . TYR B  1 404 ? 53.874  55.512  20.769  1.00   47.77  ? 404 TYR B OH  1 
ATOM   5922  N N   . GLY B  1 405 ? 53.353  56.123  29.461  1.00   46.77  ? 405 GLY B N   1 
ATOM   5923  C CA  . GLY B  1 405 ? 53.329  55.769  30.872  1.00   49.14  ? 405 GLY B CA  1 
ATOM   5924  C C   . GLY B  1 405 ? 54.136  54.513  31.181  1.00   47.22  ? 405 GLY B C   1 
ATOM   5925  O O   . GLY B  1 405 ? 53.919  53.862  32.207  1.00   48.32  ? 405 GLY B O   1 
ATOM   5926  N N   . LYS B  1 406 ? 55.065  54.178  30.287  1.00   44.38  ? 406 LYS B N   1 
ATOM   5927  C CA  . LYS B  1 406 ? 55.832  52.935  30.358  1.00   39.81  ? 406 LYS B CA  1 
ATOM   5928  C C   . LYS B  1 406 ? 57.320  53.183  30.546  1.00   39.13  ? 406 LYS B C   1 
ATOM   5929  O O   . LYS B  1 406 ? 57.827  54.275  30.315  1.00   39.24  ? 406 LYS B O   1 
ATOM   5930  C CB  . LYS B  1 406 ? 55.629  52.097  29.093  1.00   38.53  ? 406 LYS B CB  1 
ATOM   5931  C CG  . LYS B  1 406 ? 54.186  51.887  28.695  1.00   43.82  ? 406 LYS B CG  1 
ATOM   5932  C CD  . LYS B  1 406 ? 53.459  50.931  29.620  1.00   50.19  ? 406 LYS B CD  1 
ATOM   5933  C CE  . LYS B  1 406 ? 51.971  50.990  29.354  1.00   56.61  ? 406 LYS B CE  1 
ATOM   5934  N NZ  . LYS B  1 406 ? 51.761  51.027  27.880  1.00   58.38  ? 406 LYS B NZ  1 
ATOM   5935  N N   . THR B  1 407 ? 58.018  52.140  30.970  1.00   38.22  ? 407 THR B N   1 
ATOM   5936  C CA  . THR B  1 407 ? 59.464  52.137  31.042  1.00   34.69  ? 407 THR B CA  1 
ATOM   5937  C C   . THR B  1 407 ? 59.986  50.821  30.455  1.00   33.99  ? 407 THR B C   1 
ATOM   5938  O O   . THR B  1 407 ? 59.208  49.890  30.254  1.00   34.97  ? 407 THR B O   1 
ATOM   5939  C CB  . THR B  1 407 ? 59.940  52.272  32.492  1.00   34.85  ? 407 THR B CB  1 
ATOM   5940  O OG1 . THR B  1 407 ? 59.642  51.063  33.184  1.00   34.59  ? 407 THR B OG1 1 
ATOM   5941  C CG2 . THR B  1 407 ? 59.242  53.413  33.196  1.00   36.21  ? 407 THR B CG2 1 
ATOM   5942  N N   . CYS B  1 408 ? 61.294  50.707  30.219  1.00   31.15  ? 408 CYS B N   1 
ATOM   5943  C CA  . CYS B  1 408 ? 61.824  49.442  29.730  1.00   29.18  ? 408 CYS B CA  1 
ATOM   5944  C C   . CYS B  1 408 ? 61.749  48.332  30.788  1.00   31.20  ? 408 CYS B C   1 
ATOM   5945  O O   . CYS B  1 408 ? 61.740  47.139  30.467  1.00   32.88  ? 408 CYS B O   1 
ATOM   5946  C CB  . CYS B  1 408 ? 63.271  49.609  29.249  1.00   26.08  ? 408 CYS B CB  1 
ATOM   5947  S SG  . CYS B  1 408 ? 63.425  50.023  27.485  1.00   36.51  ? 408 CYS B SG  1 
ATOM   5948  N N   . SER B  1 409 ? 61.646  48.716  32.049  1.00   30.92  ? 409 SER B N   1 
ATOM   5949  C CA  . SER B  1 409 ? 61.528  47.730  33.106  1.00   34.21  ? 409 SER B CA  1 
ATOM   5950  C C   . SER B  1 409 ? 60.099  47.188  33.259  1.00   36.18  ? 409 SER B C   1 
ATOM   5951  O O   . SER B  1 409 ? 59.940  46.045  33.675  1.00   38.62  ? 409 SER B O   1 
ATOM   5952  C CB  . SER B  1 409 ? 62.017  48.317  34.423  1.00   40.61  ? 409 SER B CB  1 
ATOM   5953  O OG  . SER B  1 409 ? 63.370  48.710  34.299  1.00   43.31  ? 409 SER B OG  1 
ATOM   5954  N N   . ASN B  1 410 ? 59.065  47.979  32.933  1.00   35.81  ? 410 ASN B N   1 
ATOM   5955  C CA  . ASN B  1 410 ? 57.676  47.502  33.103  1.00   39.38  ? 410 ASN B CA  1 
ATOM   5956  C C   . ASN B  1 410 ? 56.879  47.311  31.797  1.00   39.12  ? 410 ASN B C   1 
ATOM   5957  O O   . ASN B  1 410 ? 55.692  47.005  31.829  1.00   42.16  ? 410 ASN B O   1 
ATOM   5958  C CB  . ASN B  1 410 ? 56.872  48.413  34.087  1.00   45.21  ? 410 ASN B CB  1 
ATOM   5959  C CG  . ASN B  1 410 ? 56.652  49.860  33.587  1.00   45.02  ? 410 ASN B CG  1 
ATOM   5960  O OD1 . ASN B  1 410 ? 56.488  50.124  32.395  1.00   42.51  ? 410 ASN B OD1 1 
ATOM   5961  N ND2 . ASN B  1 410 ? 56.623  50.796  34.530  1.00   41.55  ? 410 ASN B ND2 1 
ATOM   5962  N N   . LEU B  1 411 ? 57.535  47.450  30.655  1.00   37.86  ? 411 LEU B N   1 
ATOM   5963  C CA  . LEU B  1 411 ? 56.880  47.183  29.379  1.00   36.13  ? 411 LEU B CA  1 
ATOM   5964  C C   . LEU B  1 411 ? 56.444  45.737  29.309  1.00   38.54  ? 411 LEU B C   1 
ATOM   5965  O O   . LEU B  1 411 ? 55.348  45.429  28.827  1.00   38.67  ? 411 LEU B O   1 
ATOM   5966  C CB  A LEU B  1 411 ? 57.820  47.488  28.214  0.50   30.81  ? 411 LEU B CB  1 
ATOM   5967  C CB  B LEU B  1 411 ? 57.815  47.521  28.223  0.50   30.82  ? 411 LEU B CB  1 
ATOM   5968  C CG  A LEU B  1 411 ? 57.567  48.724  27.364  0.50   30.55  ? 411 LEU B CG  1 
ATOM   5969  C CG  B LEU B  1 411 ? 57.143  47.731  26.876  0.50   29.87  ? 411 LEU B CG  1 
ATOM   5970  C CD1 A LEU B  1 411 ? 58.509  48.717  26.143  0.50   27.69  ? 411 LEU B CD1 1 
ATOM   5971  C CD1 B LEU B  1 411 ? 56.003  48.725  27.027  0.50   31.88  ? 411 LEU B CD1 1 
ATOM   5972  C CD2 A LEU B  1 411 ? 56.101  48.788  26.957  0.50   31.65  ? 411 LEU B CD2 1 
ATOM   5973  C CD2 B LEU B  1 411 ? 58.190  48.222  25.869  0.50   28.06  ? 411 LEU B CD2 1 
ATOM   5974  N N   . PHE B  1 412 ? 57.308  44.865  29.838  1.00   38.71  ? 412 PHE B N   1 
ATOM   5975  C CA  . PHE B  1 412 ? 57.055  43.433  29.923  1.00   35.72  ? 412 PHE B CA  1 
ATOM   5976  C C   . PHE B  1 412 ? 57.179  43.003  31.355  1.00   37.41  ? 412 PHE B C   1 
ATOM   5977  O O   . PHE B  1 412 ? 57.835  43.664  32.155  1.00   38.34  ? 412 PHE B O   1 
ATOM   5978  C CB  . PHE B  1 412 ? 58.030  42.652  29.038  1.00   32.53  ? 412 PHE B CB  1 
ATOM   5979  C CG  . PHE B  1 412 ? 58.082  43.171  27.650  1.00   31.83  ? 412 PHE B CG  1 
ATOM   5980  C CD1 . PHE B  1 412 ? 57.051  42.887  26.763  1.00   33.70  ? 412 PHE B CD1 1 
ATOM   5981  C CD2 . PHE B  1 412 ? 59.110  43.994  27.245  1.00   32.12  ? 412 PHE B CD2 1 
ATOM   5982  C CE1 . PHE B  1 412 ? 57.052  43.406  25.487  1.00   31.94  ? 412 PHE B CE1 1 
ATOM   5983  C CE2 . PHE B  1 412 ? 59.131  44.513  25.961  1.00   33.34  ? 412 PHE B CE2 1 
ATOM   5984  C CZ  . PHE B  1 412 ? 58.092  44.223  25.077  1.00   27.07  ? 412 PHE B CZ  1 
ATOM   5985  N N   . ASP B  1 413 ? 56.504  41.914  31.689  1.00   39.79  ? 413 ASP B N   1 
ATOM   5986  C CA  . ASP B  1 413 ? 56.604  41.355  33.018  1.00   45.99  ? 413 ASP B CA  1 
ATOM   5987  C C   . ASP B  1 413 ? 57.922  40.603  33.120  1.00   48.38  ? 413 ASP B C   1 
ATOM   5988  O O   . ASP B  1 413 ? 58.121  39.589  32.443  1.00   46.61  ? 413 ASP B O   1 
ATOM   5989  C CB  . ASP B  1 413 ? 55.429  40.436  33.317  1.00   47.19  ? 413 ASP B CB  1 
ATOM   5990  C CG  . ASP B  1 413 ? 55.338  40.053  34.775  1.00   50.78  ? 413 ASP B CG  1 
ATOM   5991  O OD1 . ASP B  1 413 ? 56.366  39.916  35.451  1.00   47.43  ? 413 ASP B OD1 1 
ATOM   5992  O OD2 . ASP B  1 413 ? 54.211  39.893  35.259  1.00   59.66  1 413 ASP B OD2 1 
ATOM   5993  N N   . LEU B  1 414 ? 58.826  41.125  33.945  1.00   47.00  ? 414 LEU B N   1 
ATOM   5994  C CA  . LEU B  1 414 ? 60.116  40.492  34.144  1.00   45.72  ? 414 LEU B CA  1 
ATOM   5995  C C   . LEU B  1 414 ? 60.261  39.866  35.551  1.00   53.70  ? 414 LEU B C   1 
ATOM   5996  O O   . LEU B  1 414 ? 61.368  39.555  35.958  1.00   53.89  ? 414 LEU B O   1 
ATOM   5997  C CB  . LEU B  1 414 ? 61.242  41.507  33.870  1.00   38.94  ? 414 LEU B CB  1 
ATOM   5998  C CG  . LEU B  1 414 ? 61.273  42.157  32.479  1.00   32.59  ? 414 LEU B CG  1 
ATOM   5999  C CD1 . LEU B  1 414 ? 62.339  43.246  32.376  1.00   30.78  ? 414 LEU B CD1 1 
ATOM   6000  C CD2 . LEU B  1 414 ? 61.496  41.141  31.383  1.00   33.03  ? 414 LEU B CD2 1 
ATOM   6001  N N   . ASN B  1 415 ? 59.164  39.660  36.288  1.00   61.11  ? 415 ASN B N   1 
ATOM   6002  C CA  . ASN B  1 415 ? 59.264  38.956  37.577  1.00   66.89  ? 415 ASN B CA  1 
ATOM   6003  C C   . ASN B  1 415 ? 59.272  37.467  37.318  1.00   66.77  ? 415 ASN B C   1 
ATOM   6004  O O   . ASN B  1 415 ? 58.384  36.933  36.647  1.00   63.61  ? 415 ASN B O   1 
ATOM   6005  C CB  . ASN B  1 415 ? 58.113  39.307  38.530  1.00   73.57  ? 415 ASN B CB  1 
ATOM   6006  C CG  . ASN B  1 415 ? 58.058  40.782  38.878  1.00   74.17  ? 415 ASN B CG  1 
ATOM   6007  O OD1 . ASN B  1 415 ? 57.017  41.426  38.738  1.00   74.61  ? 415 ASN B OD1 1 
ATOM   6008  N ND2 . ASN B  1 415 ? 59.171  41.316  39.367  1.00   73.57  ? 415 ASN B ND2 1 
ATOM   6009  N N   . ASN B  1 416 ? 60.284  36.819  37.876  1.00   71.99  ? 416 ASN B N   1 
ATOM   6010  C CA  . ASN B  1 416 ? 60.520  35.386  37.720  1.00   77.48  ? 416 ASN B CA  1 
ATOM   6011  C C   . ASN B  1 416 ? 59.351  34.489  38.133  1.00   79.85  ? 416 ASN B C   1 
ATOM   6012  O O   . ASN B  1 416 ? 59.229  33.358  37.657  1.00   79.18  ? 416 ASN B O   1 
ATOM   6013  C CB  . ASN B  1 416 ? 61.795  35.019  38.479  1.00   82.10  ? 416 ASN B CB  1 
ATOM   6014  C CG  . ASN B  1 416 ? 63.048  35.719  37.908  1.00   81.65  ? 416 ASN B CG  1 
ATOM   6015  O OD1 . ASN B  1 416 ? 63.627  35.290  36.903  1.00   81.79  ? 416 ASN B OD1 1 
ATOM   6016  N ND2 . ASN B  1 416 ? 63.436  36.823  38.534  1.00   80.36  ? 416 ASN B ND2 1 
ATOM   6017  N N   . LYS C  1 11  ? 54.600  22.292  14.280  1.00   79.15  ? 11  LYS C N   1 
ATOM   6018  C CA  . LYS C  1 11  ? 55.950  22.046  13.749  1.00   78.07  ? 11  LYS C CA  1 
ATOM   6019  C C   . LYS C  1 11  ? 56.338  20.563  13.696  1.00   74.00  ? 11  LYS C C   1 
ATOM   6020  O O   . LYS C  1 11  ? 56.344  19.890  14.730  1.00   75.97  ? 11  LYS C O   1 
ATOM   6021  C CB  . LYS C  1 11  ? 57.012  22.814  14.550  1.00   80.71  ? 11  LYS C CB  1 
ATOM   6022  C CG  . LYS C  1 11  ? 57.365  24.192  13.981  1.00   79.77  ? 11  LYS C CG  1 
ATOM   6023  C CD  . LYS C  1 11  ? 58.288  24.976  14.914  1.00   77.95  ? 11  LYS C CD  1 
ATOM   6024  C CE  . LYS C  1 11  ? 58.487  26.406  14.431  1.00   74.64  ? 11  LYS C CE  1 
ATOM   6025  N NZ  . LYS C  1 11  ? 58.441  26.507  12.946  1.00   70.27  ? 11  LYS C NZ  1 
ATOM   6026  N N   . PRO C  1 12  ? 56.568  20.041  12.475  1.00   67.69  ? 12  PRO C N   1 
ATOM   6027  C CA  . PRO C  1 12  ? 56.920  18.641  12.247  1.00   65.29  ? 12  PRO C CA  1 
ATOM   6028  C C   . PRO C  1 12  ? 58.335  18.380  12.744  1.00   60.78  ? 12  PRO C C   1 
ATOM   6029  O O   . PRO C  1 12  ? 59.144  19.305  12.711  1.00   60.27  ? 12  PRO C O   1 
ATOM   6030  C CB  . PRO C  1 12  ? 56.814  18.490  10.724  1.00   64.04  ? 12  PRO C CB  1 
ATOM   6031  C CG  . PRO C  1 12  ? 57.091  19.842  10.199  1.00   61.75  ? 12  PRO C CG  1 
ATOM   6032  C CD  . PRO C  1 12  ? 56.523  20.800  11.212  1.00   64.20  ? 12  PRO C CD  1 
ATOM   6033  N N   . ASN C  1 13  ? 58.637  17.152  13.160  1.00   55.45  ? 13  ASN C N   1 
ATOM   6034  C CA  . ASN C  1 13  ? 59.961  16.842  13.672  1.00   48.30  ? 13  ASN C CA  1 
ATOM   6035  C C   . ASN C  1 13  ? 60.748  16.110  12.642  1.00   43.82  ? 13  ASN C C   1 
ATOM   6036  O O   . ASN C  1 13  ? 61.930  15.819  12.838  1.00   43.22  ? 13  ASN C O   1 
ATOM   6037  C CB  . ASN C  1 13  ? 59.904  15.966  14.917  1.00   54.25  ? 13  ASN C CB  1 
ATOM   6038  C CG  . ASN C  1 13  ? 59.397  16.706  16.124  1.00   67.10  ? 13  ASN C CG  1 
ATOM   6039  O OD1 . ASN C  1 13  ? 58.245  16.552  16.524  1.00   74.57  ? 13  ASN C OD1 1 
ATOM   6040  N ND2 . ASN C  1 13  ? 60.210  17.625  16.627  1.00   70.66  ? 13  ASN C ND2 1 
ATOM   6041  N N   . LEU C  1 14  ? 60.109  15.845  11.515  1.00   39.17  ? 14  LEU C N   1 
ATOM   6042  C CA  . LEU C  1 14  ? 60.783  15.083  10.492  1.00   36.73  ? 14  LEU C CA  1 
ATOM   6043  C C   . LEU C  1 14  ? 60.241  15.444  9.147   1.00   34.67  ? 14  LEU C C   1 
ATOM   6044  O O   . LEU C  1 14  ? 59.039  15.514  8.956   1.00   34.18  ? 14  LEU C O   1 
ATOM   6045  C CB  . LEU C  1 14  ? 60.627  13.586  10.753  1.00   36.70  ? 14  LEU C CB  1 
ATOM   6046  C CG  . LEU C  1 14  ? 61.496  12.591  9.982   1.00   35.31  ? 14  LEU C CG  1 
ATOM   6047  C CD1 . LEU C  1 14  ? 62.917  12.630  10.452  1.00   33.55  ? 14  LEU C CD1 1 
ATOM   6048  C CD2 . LEU C  1 14  ? 60.937  11.194  10.178  1.00   35.88  ? 14  LEU C CD2 1 
ATOM   6049  N N   . LEU C  1 15  ? 61.173  15.683  8.235   1.00   33.29  ? 15  LEU C N   1 
ATOM   6050  C CA  . LEU C  1 15  ? 60.891  16.066  6.862   1.00   32.28  ? 15  LEU C CA  1 
ATOM   6051  C C   . LEU C  1 15  ? 61.535  15.064  5.916   1.00   31.48  ? 15  LEU C C   1 
ATOM   6052  O O   . LEU C  1 15  ? 62.569  14.473  6.215   1.00   32.33  ? 15  LEU C O   1 
ATOM   6053  C CB  . LEU C  1 15  ? 61.422  17.464  6.573   1.00   29.96  ? 15  LEU C CB  1 
ATOM   6054  C CG  . LEU C  1 15  ? 61.063  18.501  7.626   1.00   31.58  ? 15  LEU C CG  1 
ATOM   6055  C CD1 . LEU C  1 15  ? 61.844  19.761  7.338   1.00   30.46  ? 15  LEU C CD1 1 
ATOM   6056  C CD2 . LEU C  1 15  ? 59.554  18.769  7.704   1.00   31.27  ? 15  LEU C CD2 1 
ATOM   6057  N N   . VAL C  1 16  ? 60.917  14.877  4.766   1.00   32.47  ? 16  VAL C N   1 
ATOM   6058  C CA  . VAL C  1 16  ? 61.351  13.837  3.857   1.00   35.43  ? 16  VAL C CA  1 
ATOM   6059  C C   . VAL C  1 16  ? 61.415  14.382  2.445   1.00   36.46  ? 16  VAL C C   1 
ATOM   6060  O O   . VAL C  1 16  ? 60.500  15.076  1.993   1.00   34.80  ? 16  VAL C O   1 
ATOM   6061  C CB  . VAL C  1 16  ? 60.415  12.606  3.881   1.00   36.33  ? 16  VAL C CB  1 
ATOM   6062  C CG1 . VAL C  1 16  ? 60.964  11.525  2.963   1.00   37.45  ? 16  VAL C CG1 1 
ATOM   6063  C CG2 . VAL C  1 16  ? 60.247  12.048  5.293   1.00   33.30  ? 16  VAL C CG2 1 
ATOM   6064  N N   . LEU C  1 17  ? 62.529  14.106  1.780   1.00   35.65  ? 17  LEU C N   1 
ATOM   6065  C CA  . LEU C  1 17  ? 62.729  14.483  0.392   1.00   32.01  ? 17  LEU C CA  1 
ATOM   6066  C C   . LEU C  1 17  ? 63.031  13.264  -0.460  1.00   33.22  ? 17  LEU C C   1 
ATOM   6067  O O   . LEU C  1 17  ? 64.074  12.648  -0.306  1.00   32.96  ? 17  LEU C O   1 
ATOM   6068  C CB  . LEU C  1 17  ? 63.870  15.483  0.277   1.00   28.33  ? 17  LEU C CB  1 
ATOM   6069  C CG  . LEU C  1 17  ? 64.163  15.909  -1.153  1.00   28.51  ? 17  LEU C CG  1 
ATOM   6070  C CD1 . LEU C  1 17  ? 63.047  16.771  -1.670  1.00   32.23  ? 17  LEU C CD1 1 
ATOM   6071  C CD2 . LEU C  1 17  ? 65.451  16.647  -1.215  1.00   27.30  ? 17  LEU C CD2 1 
ATOM   6072  N N   . PRO C  1 18  ? 62.101  12.869  -1.327  1.00   34.05  ? 18  PRO C N   1 
ATOM   6073  C CA  . PRO C  1 18  ? 62.400  11.762  -2.237  1.00   34.71  ? 18  PRO C CA  1 
ATOM   6074  C C   . PRO C  1 18  ? 63.412  12.160  -3.309  1.00   34.72  ? 18  PRO C C   1 
ATOM   6075  O O   . PRO C  1 18  ? 63.376  13.274  -3.804  1.00   30.16  ? 18  PRO C O   1 
ATOM   6076  C CB  . PRO C  1 18  ? 61.037  11.441  -2.846  1.00   38.18  ? 18  PRO C CB  1 
ATOM   6077  C CG  . PRO C  1 18  ? 60.053  12.014  -1.889  1.00   37.59  ? 18  PRO C CG  1 
ATOM   6078  C CD  . PRO C  1 18  ? 60.684  13.247  -1.377  1.00   35.30  ? 18  PRO C CD  1 
ATOM   6079  N N   . VAL C  1 19  ? 64.332  11.265  -3.634  1.00   35.84  ? 19  VAL C N   1 
ATOM   6080  C CA  . VAL C  1 19  ? 65.354  11.549  -4.627  1.00   33.93  ? 19  VAL C CA  1 
ATOM   6081  C C   . VAL C  1 19  ? 65.341  10.391  -5.613  1.00   37.28  ? 19  VAL C C   1 
ATOM   6082  O O   . VAL C  1 19  ? 64.849  9.304   -5.285  1.00   39.40  ? 19  VAL C O   1 
ATOM   6083  C CB  . VAL C  1 19  ? 66.768  11.712  -4.017  1.00   30.68  ? 19  VAL C CB  1 
ATOM   6084  C CG1 . VAL C  1 19  ? 66.747  12.710  -2.917  1.00   30.56  ? 19  VAL C CG1 1 
ATOM   6085  C CG2 . VAL C  1 19  ? 67.265  10.424  -3.450  1.00   34.90  ? 19  VAL C CG2 1 
ATOM   6086  N N   . GLN C  1 20  ? 65.814  10.626  -6.836  1.00   37.06  ? 20  GLN C N   1 
ATOM   6087  C CA  . GLN C  1 20  ? 65.816  9.579   -7.859  1.00   37.53  ? 20  GLN C CA  1 
ATOM   6088  C C   . GLN C  1 20  ? 67.167  9.422   -8.575  1.00   36.53  ? 20  GLN C C   1 
ATOM   6089  O O   . GLN C  1 20  ? 67.867  10.390  -8.810  1.00   36.29  ? 20  GLN C O   1 
ATOM   6090  C CB  . GLN C  1 20  ? 64.726  9.859   -8.879  1.00   40.64  ? 20  GLN C CB  1 
ATOM   6091  C CG  . GLN C  1 20  ? 64.510  8.730   -9.836  1.00   46.40  ? 20  GLN C CG  1 
ATOM   6092  C CD  . GLN C  1 20  ? 63.333  8.973   -10.723 1.00   49.93  ? 20  GLN C CD  1 
ATOM   6093  O OE1 . GLN C  1 20  ? 63.453  8.942   -11.945 1.00   51.86  ? 20  GLN C OE1 1 
ATOM   6094  N NE2 . GLN C  1 20  ? 62.182  9.232   -10.120 1.00   51.63  ? 20  GLN C NE2 1 
ATOM   6095  N N   . GLU C  1 21  ? 67.533  8.194   -8.906  1.00   38.38  ? 21  GLU C N   1 
ATOM   6096  C CA  . GLU C  1 21  ? 68.731  7.926   -9.697  1.00   40.90  ? 21  GLU C CA  1 
ATOM   6097  C C   . GLU C  1 21  ? 68.512  8.136   -11.201 1.00   43.51  ? 21  GLU C C   1 
ATOM   6098  O O   . GLU C  1 21  ? 67.481  7.743   -11.746 1.00   44.31  ? 21  GLU C O   1 
ATOM   6099  C CB  . GLU C  1 21  ? 69.215  6.486   -9.457  1.00   43.38  ? 21  GLU C CB  1 
ATOM   6100  C CG  . GLU C  1 21  ? 70.677  6.227   -9.853  1.00   46.48  ? 21  GLU C CG  1 
ATOM   6101  C CD  . GLU C  1 21  ? 70.832  5.513   -11.185 1.00   53.28  ? 21  GLU C CD  1 
ATOM   6102  O OE1 . GLU C  1 21  ? 69.797  5.228   -11.813 1.00   58.26  ? 21  GLU C OE1 1 
ATOM   6103  O OE2 . GLU C  1 21  ? 71.981  5.229   -11.607 1.00   52.82  ? 21  GLU C OE2 1 
ATOM   6104  N N   . ASP C  1 22  ? 69.480  8.762   -11.861 1.00   42.33  ? 22  ASP C N   1 
ATOM   6105  C CA  . ASP C  1 22  ? 69.469  8.903   -13.315 1.00   45.19  ? 22  ASP C CA  1 
ATOM   6106  C C   . ASP C  1 22  ? 70.313  7.811   -13.946 1.00   46.83  ? 22  ASP C C   1 
ATOM   6107  O O   . ASP C  1 22  ? 71.515  7.735   -13.712 1.00   47.42  ? 22  ASP C O   1 
ATOM   6108  C CB  . ASP C  1 22  ? 69.974  10.298  -13.721 1.00   46.12  ? 22  ASP C CB  1 
ATOM   6109  C CG  . ASP C  1 22  ? 70.145  10.459  -15.231 1.00   50.70  ? 22  ASP C CG  1 
ATOM   6110  O OD1 . ASP C  1 22  ? 69.157  10.298  -15.978 1.00   56.87  ? 22  ASP C OD1 1 
ATOM   6111  O OD2 . ASP C  1 22  ? 71.261  10.812  -15.667 1.00   47.52  1 22  ASP C OD2 1 
ATOM   6112  N N   . ALA C  1 23  ? 69.676  6.952   -14.732 1.00   50.30  ? 23  ALA C N   1 
ATOM   6113  C CA  . ALA C  1 23  ? 70.336  5.760   -15.246 1.00   52.36  ? 23  ALA C CA  1 
ATOM   6114  C C   . ALA C  1 23  ? 71.503  6.175   -16.116 1.00   53.58  ? 23  ALA C C   1 
ATOM   6115  O O   . ALA C  1 23  ? 72.599  5.618   -16.054 1.00   52.87  ? 23  ALA C O   1 
ATOM   6116  C CB  . ALA C  1 23  ? 69.357  4.902   -16.020 1.00   53.75  ? 23  ALA C CB  1 
ATOM   6117  N N   . SER C  1 24  ? 71.243  7.190   -16.915 1.00   54.36  ? 24  SER C N   1 
ATOM   6118  C CA  . SER C  1 24  ? 72.202  7.693   -17.856 1.00   55.94  ? 24  SER C CA  1 
ATOM   6119  C C   . SER C  1 24  ? 73.480  8.183   -17.191 1.00   49.33  ? 24  SER C C   1 
ATOM   6120  O O   . SER C  1 24  ? 74.571  7.818   -17.601 1.00   50.01  ? 24  SER C O   1 
ATOM   6121  C CB  . SER C  1 24  ? 71.560  8.810   -18.656 1.00   59.83  ? 24  SER C CB  1 
ATOM   6122  O OG  . SER C  1 24  ? 72.514  9.419   -19.482 1.00   62.37  ? 24  SER C OG  1 
ATOM   6123  N N   . THR C  1 25  ? 73.340  9.014   -16.163 1.00   46.88  ? 25  THR C N   1 
ATOM   6124  C CA  . THR C  1 25  ? 74.484  9.678   -15.531 1.00   44.51  ? 25  THR C CA  1 
ATOM   6125  C C   . THR C  1 25  ? 74.974  8.990   -14.252 1.00   43.33  ? 25  THR C C   1 
ATOM   6126  O O   . THR C  1 25  ? 76.088  9.231   -13.795 1.00   40.92  ? 25  THR C O   1 
ATOM   6127  C CB  . THR C  1 25  ? 74.170  11.161  -15.197 1.00   41.31  ? 25  THR C CB  1 
ATOM   6128  O OG1 . THR C  1 25  ? 73.092  11.226  -14.266 1.00   42.69  ? 25  THR C OG1 1 
ATOM   6129  C CG2 . THR C  1 25  ? 73.768  11.919  -16.432 1.00   44.30  ? 25  THR C CG2 1 
ATOM   6130  N N   . GLY C  1 26  ? 74.132  8.164   -13.649 1.00   42.73  ? 26  GLY C N   1 
ATOM   6131  C CA  . GLY C  1 26  ? 74.512  7.515   -12.416 1.00   37.77  ? 26  GLY C CA  1 
ATOM   6132  C C   . GLY C  1 26  ? 74.382  8.468   -11.255 1.00   37.23  ? 26  GLY C C   1 
ATOM   6133  O O   . GLY C  1 26  ? 74.767  8.141   -10.133 1.00   36.95  ? 26  GLY C O   1 
ATOM   6134  N N   . LEU C  1 27  ? 73.833  9.652   -11.536 1.00   35.76  ? 27  LEU C N   1 
ATOM   6135  C CA  . LEU C  1 27  ? 73.618  10.687  -10.542 1.00   32.05  ? 27  LEU C CA  1 
ATOM   6136  C C   . LEU C  1 27  ? 72.202  10.691  -10.037 1.00   35.96  ? 27  LEU C C   1 
ATOM   6137  O O   . LEU C  1 27  ? 71.309  10.109  -10.636 1.00   40.36  ? 27  LEU C O   1 
ATOM   6138  C CB  . LEU C  1 27  ? 73.919  12.064  -11.116 1.00   38.84  ? 27  LEU C CB  1 
ATOM   6139  C CG  . LEU C  1 27  ? 75.317  12.253  -11.678 1.00   36.92  ? 27  LEU C CG  1 
ATOM   6140  C CD1 . LEU C  1 27  ? 75.427  13.624  -12.279 1.00   34.96  ? 27  LEU C CD1 1 
ATOM   6141  C CD2 . LEU C  1 27  ? 76.338  12.027  -10.589 1.00   33.77  ? 27  LEU C CD2 1 
ATOM   6142  N N   . HIS C  1 28  ? 72.006  11.410  -8.950  1.00   32.62  ? 28  HIS C N   1 
ATOM   6143  C CA  . HIS C  1 28  ? 70.723  11.504  -8.285  1.00   33.39  ? 28  HIS C CA  1 
ATOM   6144  C C   . HIS C  1 28  ? 70.183  12.921  -8.283  1.00   34.45  ? 28  HIS C C   1 
ATOM   6145  O O   . HIS C  1 28  ? 70.935  13.898  -8.200  1.00   33.30  ? 28  HIS C O   1 
ATOM   6146  C CB  . HIS C  1 28  ? 70.844  10.988  -6.856  1.00   30.15  ? 28  HIS C CB  1 
ATOM   6147  C CG  . HIS C  1 28  ? 71.113  9.523   -6.786  1.00   28.96  ? 28  HIS C CG  1 
ATOM   6148  N ND1 . HIS C  1 28  ? 70.180  8.616   -6.332  1.00   32.51  ? 28  HIS C ND1 1 
ATOM   6149  C CD2 . HIS C  1 28  ? 72.191  8.800   -7.167  1.00   29.32  ? 28  HIS C CD2 1 
ATOM   6150  C CE1 . HIS C  1 28  ? 70.684  7.395   -6.414  1.00   32.02  ? 28  HIS C CE1 1 
ATOM   6151  N NE2 . HIS C  1 28  ? 71.903  7.480   -6.922  1.00   31.47  ? 28  HIS C NE2 1 
ATOM   6152  N N   . TRP C  1 29  ? 68.862  13.016  -8.340  1.00   37.59  ? 29  TRP C N   1 
ATOM   6153  C CA  . TRP C  1 29  ? 68.181  14.304  -8.411  1.00   37.94  ? 29  TRP C CA  1 
ATOM   6154  C C   . TRP C  1 29  ? 66.868  14.277  -7.617  1.00   36.52  ? 29  TRP C C   1 
ATOM   6155  O O   . TRP C  1 29  ? 66.352  13.200  -7.294  1.00   37.91  ? 29  TRP C O   1 
ATOM   6156  C CB  . TRP C  1 29  ? 67.899  14.680  -9.873  1.00   39.96  ? 29  TRP C CB  1 
ATOM   6157  C CG  . TRP C  1 29  ? 66.945  13.728  -10.563 1.00   40.33  ? 29  TRP C CG  1 
ATOM   6158  C CD1 . TRP C  1 29  ? 67.254  12.542  -11.144 1.00   41.55  ? 29  TRP C CD1 1 
ATOM   6159  C CD2 . TRP C  1 29  ? 65.525  13.892  -10.714 1.00   41.52  ? 29  TRP C CD2 1 
ATOM   6160  N NE1 . TRP C  1 29  ? 66.118  11.952  -11.659 1.00   43.27  ? 29  TRP C NE1 1 
ATOM   6161  C CE2 . TRP C  1 29  ? 65.044  12.765  -11.402 1.00   44.73  ? 29  TRP C CE2 1 
ATOM   6162  C CE3 . TRP C  1 29  ? 64.614  14.894  -10.338 1.00   42.76  ? 29  TRP C CE3 1 
ATOM   6163  C CZ2 . TRP C  1 29  ? 63.692  12.605  -11.723 1.00   47.67  ? 29  TRP C CZ2 1 
ATOM   6164  C CZ3 . TRP C  1 29  ? 63.266  14.734  -10.659 1.00   45.31  ? 29  TRP C CZ3 1 
ATOM   6165  C CH2 . TRP C  1 29  ? 62.822  13.602  -11.343 1.00   46.94  ? 29  TRP C CH2 1 
ATOM   6166  N N   . ALA C  1 30  ? 66.338  15.461  -7.318  1.00   36.42  ? 30  ALA C N   1 
ATOM   6167  C CA  . ALA C  1 30  ? 65.050  15.609  -6.630  1.00   39.95  ? 30  ALA C CA  1 
ATOM   6168  C C   . ALA C  1 30  ? 64.218  16.744  -7.228  1.00   41.36  ? 30  ALA C C   1 
ATOM   6169  O O   . ALA C  1 30  ? 64.774  17.728  -7.698  1.00   40.29  ? 30  ALA C O   1 
ATOM   6170  C CB  . ALA C  1 30  ? 65.261  15.858  -5.151  1.00   38.53  ? 30  ALA C CB  1 
ATOM   6171  N N   . ASN C  1 31  ? 62.894  16.587  -7.221  1.00   43.10  ? 31  ASN C N   1 
ATOM   6172  C CA  . ASN C  1 31  ? 61.971  17.699  -7.474  1.00   46.11  ? 31  ASN C CA  1 
ATOM   6173  C C   . ASN C  1 31  ? 61.771  18.529  -6.207  1.00   45.40  ? 31  ASN C C   1 
ATOM   6174  O O   . ASN C  1 31  ? 61.294  18.019  -5.197  1.00   46.57  ? 31  ASN C O   1 
ATOM   6175  C CB  . ASN C  1 31  ? 60.627  17.179  -7.981  1.00   46.56  ? 31  ASN C CB  1 
ATOM   6176  C CG  . ASN C  1 31  ? 60.610  16.959  -9.485  1.00   49.51  ? 31  ASN C CG  1 
ATOM   6177  O OD1 . ASN C  1 31  ? 61.030  17.814  -10.271 1.00   49.88  ? 31  ASN C OD1 1 
ATOM   6178  N ND2 . ASN C  1 31  ? 60.180  15.776  -9.888  1.00   52.43  ? 31  ASN C ND2 1 
ATOM   6179  N N   . ILE C  1 32  ? 62.175  19.793  -6.249  1.00   44.08  ? 32  ILE C N   1 
ATOM   6180  C CA  . ILE C  1 32  ? 61.997  20.688  -5.116  1.00   43.34  ? 32  ILE C CA  1 
ATOM   6181  C C   . ILE C  1 32  ? 60.823  21.598  -5.387  1.00   45.03  ? 32  ILE C C   1 
ATOM   6182  O O   . ILE C  1 32  ? 60.692  22.124  -6.489  1.00   46.83  ? 32  ILE C O   1 
ATOM   6183  C CB  . ILE C  1 32  ? 63.240  21.553  -4.861  1.00   40.44  ? 32  ILE C CB  1 
ATOM   6184  C CG1 . ILE C  1 32  ? 64.488  20.687  -4.808  1.00   38.50  ? 32  ILE C CG1 1 
ATOM   6185  C CG2 . ILE C  1 32  ? 63.073  22.329  -3.591  1.00   36.31  ? 32  ILE C CG2 1 
ATOM   6186  C CD1 . ILE C  1 32  ? 64.542  19.844  -3.621  1.00   37.07  ? 32  ILE C CD1 1 
ATOM   6187  N N   . HIS C  1 33  ? 59.962  21.772  -4.392  1.00   45.13  ? 33  HIS C N   1 
ATOM   6188  C CA  . HIS C  1 33  ? 58.813  22.667  -4.533  1.00   43.25  ? 33  HIS C CA  1 
ATOM   6189  C C   . HIS C  1 33  ? 59.175  24.060  -4.081  1.00   38.95  ? 33  HIS C C   1 
ATOM   6190  O O   . HIS C  1 33  ? 59.599  24.263  -2.948  1.00   35.49  ? 33  HIS C O   1 
ATOM   6191  C CB  . HIS C  1 33  ? 57.623  22.163  -3.743  1.00   41.58  ? 33  HIS C CB  1 
ATOM   6192  C CG  . HIS C  1 33  ? 57.117  20.844  -4.223  1.00   40.34  ? 33  HIS C CG  1 
ATOM   6193  N ND1 . HIS C  1 33  ? 57.810  19.675  -4.018  1.00   41.99  ? 33  HIS C ND1 1 
ATOM   6194  C CD2 . HIS C  1 33  ? 56.012  20.513  -4.924  1.00   41.18  ? 33  HIS C CD2 1 
ATOM   6195  C CE1 . HIS C  1 33  ? 57.143  18.671  -4.558  1.00   42.23  ? 33  HIS C CE1 1 
ATOM   6196  N NE2 . HIS C  1 33  ? 56.053  19.154  -5.119  1.00   41.94  ? 33  HIS C NE2 1 
ATOM   6197  N N   . LYS C  1 34  ? 58.992  25.015  -4.982  1.00   40.39  ? 34  LYS C N   1 
ATOM   6198  C CA  . LYS C  1 34  ? 59.376  26.399  -4.746  1.00   42.52  ? 34  LYS C CA  1 
ATOM   6199  C C   . LYS C  1 34  ? 58.341  27.383  -5.284  1.00   45.68  ? 34  LYS C C   1 
ATOM   6200  O O   . LYS C  1 34  ? 57.500  26.984  -6.061  1.00   50.12  ? 34  LYS C O   1 
ATOM   6201  C CB  . LYS C  1 34  ? 60.715  26.671  -5.409  1.00   42.05  ? 34  LYS C CB  1 
ATOM   6202  C CG  . LYS C  1 34  ? 61.758  25.627  -5.058  1.00   41.66  ? 34  LYS C CG  1 
ATOM   6203  C CD  . LYS C  1 34  ? 63.116  26.166  -5.224  1.00   38.08  ? 34  LYS C CD  1 
ATOM   6204  C CE  . LYS C  1 34  ? 63.295  27.323  -4.299  1.00   34.97  ? 34  LYS C CE  1 
ATOM   6205  N NZ  . LYS C  1 34  ? 64.339  28.102  -4.908  1.00   33.74  ? 34  LYS C NZ  1 
ATOM   6206  N N   . ARG C  1 35  ? 58.406  28.643  -4.841  1.00   45.40  ? 35  ARG C N   1 
ATOM   6207  C CA  . ARG C  1 35  ? 57.663  29.784  -5.410  1.00   45.55  ? 35  ARG C CA  1 
ATOM   6208  C C   . ARG C  1 35  ? 56.200  29.845  -5.023  1.00   42.19  ? 35  ARG C C   1 
ATOM   6209  O O   . ARG C  1 35  ? 55.668  28.943  -4.384  1.00   41.84  ? 35  ARG C O   1 
ATOM   6210  C CB  . ARG C  1 35  ? 57.777  29.792  -6.927  1.00   42.82  ? 35  ARG C CB  1 
ATOM   6211  C CG  . ARG C  1 35  ? 59.208  29.797  -7.333  1.00   41.74  ? 35  ARG C CG  1 
ATOM   6212  C CD  . ARG C  1 35  ? 59.432  29.464  -8.774  1.00   51.55  ? 35  ARG C CD  1 
ATOM   6213  N NE  . ARG C  1 35  ? 60.803  28.975  -8.924  1.00   50.33  ? 35  ARG C NE  1 
ATOM   6214  C CZ  . ARG C  1 35  ? 61.370  28.668  -10.086 1.00   50.99  ? 35  ARG C CZ  1 
ATOM   6215  N NH1 . ARG C  1 35  ? 60.679  28.809  -11.206 1.00   57.85  ? 35  ARG C NH1 1 
ATOM   6216  N NH2 . ARG C  1 35  ? 62.623  28.231  -10.134 1.00   43.88  ? 35  ARG C NH2 1 
ATOM   6217  N N   . THR C  1 36  ? 55.574  30.957  -5.374  1.00   44.52  ? 36  THR C N   1 
ATOM   6218  C CA  . THR C  1 36  ? 54.137  31.106  -5.229  1.00   46.47  ? 36  THR C CA  1 
ATOM   6219  C C   . THR C  1 36  ? 53.536  31.549  -6.554  1.00   49.72  ? 36  THR C C   1 
ATOM   6220  O O   . THR C  1 36  ? 53.858  32.616  -7.046  1.00   51.17  ? 36  THR C O   1 
ATOM   6221  C CB  . THR C  1 36  ? 53.774  32.107  -4.134  1.00   46.84  ? 36  THR C CB  1 
ATOM   6222  O OG1 . THR C  1 36  ? 54.378  31.716  -2.898  1.00   45.01  ? 36  THR C OG1 1 
ATOM   6223  C CG2 . THR C  1 36  ? 52.309  32.103  -3.932  1.00   51.01  ? 36  THR C CG2 1 
ATOM   6224  N N   . PRO C  1 37  ? 52.693  30.708  -7.164  1.00   51.19  ? 37  PRO C N   1 
ATOM   6225  C CA  . PRO C  1 37  ? 52.245  29.393  -6.704  1.00   50.06  ? 37  PRO C CA  1 
ATOM   6226  C C   . PRO C  1 37  ? 53.354  28.341  -6.728  1.00   51.99  ? 37  PRO C C   1 
ATOM   6227  O O   . PRO C  1 37  ? 54.324  28.441  -7.489  1.00   49.27  ? 37  PRO C O   1 
ATOM   6228  C CB  . PRO C  1 37  ? 51.142  29.033  -7.696  1.00   53.29  ? 37  PRO C CB  1 
ATOM   6229  C CG  . PRO C  1 37  ? 51.486  29.779  -8.920  1.00   55.52  ? 37  PRO C CG  1 
ATOM   6230  C CD  . PRO C  1 37  ? 52.090  31.066  -8.459  1.00   54.76  ? 37  PRO C CD  1 
ATOM   6231  N N   . LEU C  1 38  ? 53.189  27.335  -5.881  1.00   50.24  ? 38  LEU C N   1 
ATOM   6232  C CA  . LEU C  1 38  ? 54.186  26.314  -5.683  1.00   48.10  ? 38  LEU C CA  1 
ATOM   6233  C C   . LEU C  1 38  ? 54.370  25.558  -6.967  1.00   47.16  ? 38  LEU C C   1 
ATOM   6234  O O   . LEU C  1 38  ? 53.403  25.314  -7.664  1.00   47.43  ? 38  LEU C O   1 
ATOM   6235  C CB  . LEU C  1 38  ? 53.742  25.379  -4.584  1.00   48.83  ? 38  LEU C CB  1 
ATOM   6236  C CG  . LEU C  1 38  ? 54.767  24.687  -3.720  1.00   46.20  ? 38  LEU C CG  1 
ATOM   6237  C CD1 . LEU C  1 38  ? 55.579  25.690  -2.919  1.00   43.63  ? 38  LEU C CD1 1 
ATOM   6238  C CD2 . LEU C  1 38  ? 54.022  23.710  -2.824  1.00   48.58  ? 38  LEU C CD2 1 
ATOM   6239  N N   . MET C  1 39  ? 55.607  25.224  -7.305  1.00   43.36  ? 39  MET C N   1 
ATOM   6240  C CA  . MET C  1 39  ? 55.852  24.404  -8.483  1.00   45.66  ? 39  MET C CA  1 
ATOM   6241  C C   . MET C  1 39  ? 57.093  23.531  -8.261  1.00   44.14  ? 39  MET C C   1 
ATOM   6242  O O   . MET C  1 39  ? 57.744  23.647  -7.237  1.00   43.24  ? 39  MET C O   1 
ATOM   6243  C CB  . MET C  1 39  ? 56.023  25.264  -9.735  1.00   47.48  ? 39  MET C CB  1 
ATOM   6244  C CG  . MET C  1 39  ? 57.093  26.323  -9.639  1.00   47.69  ? 39  MET C CG  1 
ATOM   6245  S SD  . MET C  1 39  ? 58.763  25.646  -9.906  1.00   77.73  ? 39  MET C SD  1 
ATOM   6246  C CE  . MET C  1 39  ? 58.708  25.277  -11.664 1.00   62.85  ? 39  MET C CE  1 
ATOM   6247  N N   . GLN C  1 40  ? 57.401  22.636  -9.199  1.00   47.09  ? 40  GLN C N   1 
ATOM   6248  C CA  . GLN C  1 40  ? 58.534  21.720  -9.031  1.00   46.71  ? 40  GLN C CA  1 
ATOM   6249  C C   . GLN C  1 40  ? 59.757  22.082  -9.875  1.00   44.67  ? 40  GLN C C   1 
ATOM   6250  O O   . GLN C  1 40  ? 59.663  22.361  -11.079 1.00   45.80  ? 40  GLN C O   1 
ATOM   6251  C CB  . GLN C  1 40  ? 58.098  20.284  -9.321  1.00   49.74  ? 40  GLN C CB  1 
ATOM   6252  C CG  . GLN C  1 40  ? 57.125  19.812  -8.290  1.00   52.42  ? 40  GLN C CG  1 
ATOM   6253  C CD  . GLN C  1 40  ? 56.659  18.417  -8.503  1.00   56.24  ? 40  GLN C CD  1 
ATOM   6254  O OE1 . GLN C  1 40  ? 57.415  17.479  -8.366  1.00   56.34  ? 40  GLN C OE1 1 
ATOM   6255  N NE2 . GLN C  1 40  ? 55.401  18.267  -8.855  1.00   63.61  ? 40  GLN C NE2 1 
ATOM   6256  N N   . VAL C  1 41  ? 60.905  22.074  -9.212  1.00   41.46  ? 41  VAL C N   1 
ATOM   6257  C CA  . VAL C  1 41  ? 62.177  22.321  -9.857  1.00   42.76  ? 41  VAL C CA  1 
ATOM   6258  C C   . VAL C  1 41  ? 63.053  21.105  -9.719  1.00   40.04  ? 41  VAL C C   1 
ATOM   6259  O O   . VAL C  1 41  ? 63.425  20.752  -8.614  1.00   36.08  ? 41  VAL C O   1 
ATOM   6260  C CB  . VAL C  1 41  ? 62.920  23.496  -9.229  1.00   43.85  ? 41  VAL C CB  1 
ATOM   6261  C CG1 . VAL C  1 41  ? 64.086  23.886  -10.112 1.00   44.92  ? 41  VAL C CG1 1 
ATOM   6262  C CG2 . VAL C  1 41  ? 61.979  24.654  -9.022  1.00   45.45  ? 41  VAL C CG2 1 
ATOM   6263  N N   . PRO C  1 42  ? 63.406  20.467  -10.842 1.00   43.60  ? 42  PRO C N   1 
ATOM   6264  C CA  . PRO C  1 42  ? 64.327  19.322  -10.773 1.00   44.11  ? 42  PRO C CA  1 
ATOM   6265  C C   . PRO C  1 42  ? 65.795  19.747  -10.550 1.00   39.74  ? 42  PRO C C   1 
ATOM   6266  O O   . PRO C  1 42  ? 66.347  20.442  -11.394 1.00   39.93  ? 42  PRO C O   1 
ATOM   6267  C CB  . PRO C  1 42  ? 64.124  18.641  -12.136 1.00   46.47  ? 42  PRO C CB  1 
ATOM   6268  C CG  . PRO C  1 42  ? 63.621  19.738  -13.050 1.00   48.55  ? 42  PRO C CG  1 
ATOM   6269  C CD  . PRO C  1 42  ? 62.836  20.666  -12.190 1.00   47.51  ? 42  PRO C CD  1 
ATOM   6270  N N   . LEU C  1 43  ? 66.414  19.290  -9.460  1.00   32.75  ? 43  LEU C N   1 
ATOM   6271  C CA  . LEU C  1 43  ? 67.753  19.738  -9.065  1.00   36.20  ? 43  LEU C CA  1 
ATOM   6272  C C   . LEU C  1 43  ? 68.673  18.574  -8.719  1.00   36.31  ? 43  LEU C C   1 
ATOM   6273  O O   . LEU C  1 43  ? 68.229  17.600  -8.133  1.00   37.48  ? 43  LEU C O   1 
ATOM   6274  C CB  . LEU C  1 43  ? 67.679  20.683  -7.844  1.00   30.85  ? 43  LEU C CB  1 
ATOM   6275  C CG  . LEU C  1 43  ? 66.880  21.972  -7.972  1.00   30.33  ? 43  LEU C CG  1 
ATOM   6276  C CD1 . LEU C  1 43  ? 66.757  22.689  -6.658  1.00   28.76  ? 43  LEU C CD1 1 
ATOM   6277  C CD2 . LEU C  1 43  ? 67.582  22.853  -8.949  1.00   34.26  ? 43  LEU C CD2 1 
ATOM   6278  N N   . LEU C  1 44  ? 69.958  18.697  -9.040  1.00   34.33  ? 44  LEU C N   1 
ATOM   6279  C CA  . LEU C  1 44  ? 70.941  17.674  -8.704  1.00   32.89  ? 44  LEU C CA  1 
ATOM   6280  C C   . LEU C  1 44  ? 71.214  17.567  -7.220  1.00   30.41  ? 44  LEU C C   1 
ATOM   6281  O O   . LEU C  1 44  ? 71.301  18.556  -6.528  1.00   28.60  ? 44  LEU C O   1 
ATOM   6282  C CB  . LEU C  1 44  ? 72.253  17.944  -9.426  1.00   34.96  ? 44  LEU C CB  1 
ATOM   6283  C CG  . LEU C  1 44  ? 73.364  16.944  -9.110  1.00   34.85  ? 44  LEU C CG  1 
ATOM   6284  C CD1 . LEU C  1 44  ? 73.168  15.659  -9.881  1.00   35.92  ? 44  LEU C CD1 1 
ATOM   6285  C CD2 . LEU C  1 44  ? 74.715  17.541  -9.418  1.00   34.00  ? 44  LEU C CD2 1 
ATOM   6286  N N   . LEU C  1 45  ? 71.321  16.341  -6.729  1.00   33.88  ? 45  LEU C N   1 
ATOM   6287  C CA  . LEU C  1 45  ? 71.726  16.111  -5.351  1.00   30.89  ? 45  LEU C CA  1 
ATOM   6288  C C   . LEU C  1 45  ? 73.242  16.238  -5.211  1.00   31.28  ? 45  LEU C C   1 
ATOM   6289  O O   . LEU C  1 45  ? 73.998  15.452  -5.769  1.00   29.73  ? 45  LEU C O   1 
ATOM   6290  C CB  . LEU C  1 45  ? 71.279  14.742  -4.878  1.00   28.29  ? 45  LEU C CB  1 
ATOM   6291  C CG  . LEU C  1 45  ? 71.798  14.399  -3.485  1.00   29.21  ? 45  LEU C CG  1 
ATOM   6292  C CD1 . LEU C  1 45  ? 71.197  15.301  -2.392  1.00   27.80  ? 45  LEU C CD1 1 
ATOM   6293  C CD2 . LEU C  1 45  ? 71.531  12.942  -3.221  1.00   30.85  ? 45  LEU C CD2 1 
ATOM   6294  N N   . ASP C  1 46  ? 73.676  17.261  -4.487  1.00   34.19  ? 46  ASP C N   1 
ATOM   6295  C CA  . ASP C  1 46  ? 75.086  17.543  -4.279  1.00   33.18  ? 46  ASP C CA  1 
ATOM   6296  C C   . ASP C  1 46  ? 75.362  17.568  -2.786  1.00   31.54  ? 46  ASP C C   1 
ATOM   6297  O O   . ASP C  1 46  ? 75.190  18.598  -2.143  1.00   33.86  ? 46  ASP C O   1 
ATOM   6298  C CB  . ASP C  1 46  ? 75.440  18.878  -4.926  1.00   34.16  ? 46  ASP C CB  1 
ATOM   6299  C CG  . ASP C  1 46  ? 76.915  19.229  -4.823  1.00   33.70  ? 46  ASP C CG  1 
ATOM   6300  O OD1 . ASP C  1 46  ? 77.732  18.406  -4.367  1.00   34.99  ? 46  ASP C OD1 1 
ATOM   6301  O OD2 . ASP C  1 46  ? 77.256  20.352  -5.229  1.00   34.73  1 46  ASP C OD2 1 
ATOM   6302  N N   . LEU C  1 47  ? 75.794  16.444  -2.236  1.00   29.18  ? 47  LEU C N   1 
ATOM   6303  C CA  . LEU C  1 47  ? 75.983  16.327  -0.793  1.00   27.53  ? 47  LEU C CA  1 
ATOM   6304  C C   . LEU C  1 47  ? 76.883  17.423  -0.213  1.00   26.74  ? 47  LEU C C   1 
ATOM   6305  O O   . LEU C  1 47  ? 76.601  17.959  0.852   1.00   27.64  ? 47  LEU C O   1 
ATOM   6306  C CB  . LEU C  1 47  ? 76.551  14.955  -0.452  1.00   26.84  ? 47  LEU C CB  1 
ATOM   6307  C CG  . LEU C  1 47  ? 76.912  14.711  1.015   1.00   26.52  ? 47  LEU C CG  1 
ATOM   6308  C CD1 . LEU C  1 47  ? 75.684  14.746  1.891   1.00   27.44  ? 47  LEU C CD1 1 
ATOM   6309  C CD2 . LEU C  1 47  ? 77.620  13.382  1.155   1.00   25.18  ? 47  LEU C CD2 1 
ATOM   6310  N N   . ASN C  1 48  ? 77.958  17.770  -0.911  1.00   29.21  ? 48  ASN C N   1 
ATOM   6311  C CA  . ASN C  1 48  ? 78.922  18.743  -0.386  1.00   25.67  ? 48  ASN C CA  1 
ATOM   6312  C C   . ASN C  1 48  ? 78.677  20.167  -0.838  1.00   27.28  ? 48  ASN C C   1 
ATOM   6313  O O   . ASN C  1 48  ? 79.435  21.052  -0.485  1.00   31.91  ? 48  ASN C O   1 
ATOM   6314  C CB  . ASN C  1 48  ? 80.338  18.344  -0.779  1.00   22.58  ? 48  ASN C CB  1 
ATOM   6315  C CG  . ASN C  1 48  ? 80.768  17.034  -0.129  1.00   24.39  ? 48  ASN C CG  1 
ATOM   6316  O OD1 . ASN C  1 48  ? 80.645  16.855  1.076   1.00   27.13  ? 48  ASN C OD1 1 
ATOM   6317  N ND2 . ASN C  1 48  ? 81.260  16.115  -0.932  1.00   23.96  ? 48  ASN C ND2 1 
ATOM   6318  N N   . GLY C  1 49  ? 77.616  20.404  -1.597  1.00   26.87  ? 49  GLY C N   1 
ATOM   6319  C CA  . GLY C  1 49  ? 77.343  21.743  -2.101  1.00   25.91  ? 49  GLY C CA  1 
ATOM   6320  C C   . GLY C  1 49  ? 77.030  22.777  -1.030  1.00   24.67  ? 49  GLY C C   1 
ATOM   6321  O O   . GLY C  1 49  ? 76.343  22.485  -0.071  1.00   28.08  ? 49  GLY C O   1 
ATOM   6322  N N   . LYS C  1 50  ? 77.523  23.994  -1.189  1.00   24.85  ? 50  LYS C N   1 
ATOM   6323  C CA  . LYS C  1 50  ? 77.358  25.005  -0.149  1.00   26.52  ? 50  LYS C CA  1 
ATOM   6324  C C   . LYS C  1 50  ? 75.982  25.650  -0.086  1.00   29.31  ? 50  LYS C C   1 
ATOM   6325  O O   . LYS C  1 50  ? 75.614  26.198  0.943   1.00   31.09  ? 50  LYS C O   1 
ATOM   6326  C CB  . LYS C  1 50  ? 78.386  26.106  -0.315  1.00   27.01  ? 50  LYS C CB  1 
ATOM   6327  C CG  . LYS C  1 50  ? 79.776  25.682  0.003   1.00   24.61  ? 50  LYS C CG  1 
ATOM   6328  C CD  . LYS C  1 50  ? 80.682  26.849  -0.062  1.00   30.07  ? 50  LYS C CD  1 
ATOM   6329  C CE  . LYS C  1 50  ? 82.093  26.381  0.051   1.00   32.73  ? 50  LYS C CE  1 
ATOM   6330  N NZ  . LYS C  1 50  ? 82.982  27.529  -0.125  1.00   38.35  ? 50  LYS C NZ  1 
ATOM   6331  N N   . HIS C  1 51  ? 75.241  25.587  -1.188  1.00   28.43  ? 51  HIS C N   1 
ATOM   6332  C CA  . HIS C  1 51  ? 73.900  26.141  -1.269  1.00   28.15  ? 51  HIS C CA  1 
ATOM   6333  C C   . HIS C  1 51  ? 73.093  25.521  -2.396  1.00   26.95  ? 51  HIS C C   1 
ATOM   6334  O O   . HIS C  1 51  ? 73.618  24.773  -3.214  1.00   26.69  ? 51  HIS C O   1 
ATOM   6335  C CB  . HIS C  1 51  ? 73.968  27.674  -1.432  1.00   30.72  ? 51  HIS C CB  1 
ATOM   6336  C CG  . HIS C  1 51  ? 74.701  28.137  -2.656  1.00   27.84  ? 51  HIS C CG  1 
ATOM   6337  N ND1 . HIS C  1 51  ? 75.983  28.630  -2.607  1.00   27.77  ? 51  HIS C ND1 1 
ATOM   6338  C CD2 . HIS C  1 51  ? 74.326  28.199  -3.955  1.00   28.10  ? 51  HIS C CD2 1 
ATOM   6339  C CE1 . HIS C  1 51  ? 76.368  28.973  -3.822  1.00   30.32  ? 51  HIS C CE1 1 
ATOM   6340  N NE2 . HIS C  1 51  ? 75.379  28.718  -4.659  1.00   27.34  ? 51  HIS C NE2 1 
ATOM   6341  N N   . LEU C  1 52  ? 71.806  25.833  -2.413  1.00   27.26  ? 52  LEU C N   1 
ATOM   6342  C CA  . LEU C  1 52  ? 70.942  25.464  -3.518  1.00   26.56  ? 52  LEU C CA  1 
ATOM   6343  C C   . LEU C  1 52  ? 71.075  26.520  -4.562  1.00   28.74  ? 52  LEU C C   1 
ATOM   6344  O O   . LEU C  1 52  ? 71.011  27.713  -4.261  1.00   30.14  ? 52  LEU C O   1 
ATOM   6345  C CB  . LEU C  1 52  ? 69.475  25.335  -3.071  1.00   26.20  ? 52  LEU C CB  1 
ATOM   6346  C CG  . LEU C  1 52  ? 68.383  24.864  -4.034  1.00   28.01  ? 52  LEU C CG  1 
ATOM   6347  C CD1 . LEU C  1 52  ? 67.291  24.178  -3.253  1.00   29.72  ? 52  LEU C CD1 1 
ATOM   6348  C CD2 . LEU C  1 52  ? 67.764  26.010  -4.760  1.00   29.54  ? 52  LEU C CD2 1 
ATOM   6349  N N   . TRP C  1 53  ? 71.270  26.106  -5.802  1.00   28.85  ? 53  TRP C N   1 
ATOM   6350  C CA  . TRP C  1 53  ? 71.258  27.089  -6.854  1.00   30.94  ? 53  TRP C CA  1 
ATOM   6351  C C   . TRP C  1 53  ? 70.403  26.615  -8.005  1.00   34.69  ? 53  TRP C C   1 
ATOM   6352  O O   . TRP C  1 53  ? 70.255  25.413  -8.262  1.00   37.07  ? 53  TRP C O   1 
ATOM   6353  C CB  . TRP C  1 53  ? 72.675  27.428  -7.329  1.00   29.63  ? 53  TRP C CB  1 
ATOM   6354  C CG  . TRP C  1 53  ? 73.480  26.317  -7.902  1.00   29.18  ? 53  TRP C CG  1 
ATOM   6355  C CD1 . TRP C  1 53  ? 74.312  25.514  -7.232  1.00   30.15  ? 53  TRP C CD1 1 
ATOM   6356  C CD2 . TRP C  1 53  ? 73.602  25.955  -9.290  1.00   32.69  ? 53  TRP C CD2 1 
ATOM   6357  N NE1 . TRP C  1 53  ? 74.932  24.638  -8.091  1.00   30.43  ? 53  TRP C NE1 1 
ATOM   6358  C CE2 . TRP C  1 53  ? 74.512  24.892  -9.363  1.00   32.36  ? 53  TRP C CE2 1 
ATOM   6359  C CE3 . TRP C  1 53  ? 73.015  26.417  -10.473 1.00   35.98  ? 53  TRP C CE3 1 
ATOM   6360  C CZ2 . TRP C  1 53  ? 74.852  24.273  -10.570 1.00   33.77  ? 53  TRP C CZ2 1 
ATOM   6361  C CZ3 . TRP C  1 53  ? 73.356  25.806  -11.675 1.00   35.35  ? 53  TRP C CZ3 1 
ATOM   6362  C CH2 . TRP C  1 53  ? 74.264  24.749  -11.710 1.00   34.29  ? 53  TRP C CH2 1 
ATOM   6363  N N   . VAL C  1 54  ? 69.796  27.585  -8.664  1.00   35.35  ? 54  VAL C N   1 
ATOM   6364  C CA  . VAL C  1 54  ? 68.949  27.303  -9.788  1.00   37.56  ? 54  VAL C CA  1 
ATOM   6365  C C   . VAL C  1 54  ? 69.156  28.415  -10.833 1.00   42.02  ? 54  VAL C C   1 
ATOM   6366  O O   . VAL C  1 54  ? 69.478  29.549  -10.499 1.00   42.08  ? 54  VAL C O   1 
ATOM   6367  C CB  . VAL C  1 54  ? 67.491  27.167  -9.334  1.00   37.58  ? 54  VAL C CB  1 
ATOM   6368  C CG1 . VAL C  1 54  ? 66.953  28.503  -8.850  1.00   37.97  ? 54  VAL C CG1 1 
ATOM   6369  C CG2 . VAL C  1 54  ? 66.628  26.590  -10.467 1.00   44.47  ? 54  VAL C CG2 1 
ATOM   6370  N N   . THR C  1 55  ? 68.986  28.077  -12.104 1.00   47.44  ? 55  THR C N   1 
ATOM   6371  C CA  . THR C  1 55  ? 69.034  29.054  -13.183 1.00   53.03  ? 55  THR C CA  1 
ATOM   6372  C C   . THR C  1 55  ? 67.764  29.913  -13.227 1.00   54.78  ? 55  THR C C   1 
ATOM   6373  O O   . THR C  1 55  ? 66.651  29.405  -13.143 1.00   53.56  ? 55  THR C O   1 
ATOM   6374  C CB  . THR C  1 55  ? 69.267  28.346  -14.528 1.00   57.78  ? 55  THR C CB  1 
ATOM   6375  O OG1 . THR C  1 55  ? 68.335  27.270  -14.650 1.00   57.79  ? 55  THR C OG1 1 
ATOM   6376  C CG2 . THR C  1 55  ? 70.666  27.741  -14.572 1.00   55.97  ? 55  THR C CG2 1 
ATOM   6377  N N   . CYS C  1 56  ? 67.944  31.227  -13.280 1.00   56.71  ? 56  CYS C N   1 
ATOM   6378  C CA  . CYS C  1 56  ? 66.824  32.166  -13.273 1.00   58.81  ? 56  CYS C CA  1 
ATOM   6379  C C   . CYS C  1 56  ? 66.645  32.931  -14.609 1.00   67.66  ? 56  CYS C C   1 
ATOM   6380  O O   . CYS C  1 56  ? 67.532  33.677  -15.032 1.00   71.85  ? 56  CYS C O   1 
ATOM   6381  C CB  . CYS C  1 56  ? 66.980  33.148  -12.099 1.00   55.42  ? 56  CYS C CB  1 
ATOM   6382  S SG  . CYS C  1 56  ? 66.821  32.396  -10.422 1.00   55.86  ? 56  CYS C SG  1 
ATOM   6383  N N   . SER C  1 57  ? 65.537  32.711  -15.308 1.00   70.75  ? 57  SER C N   1 
ATOM   6384  C CA  . SER C  1 57  ? 65.367  33.409  -16.573 1.00   78.38  ? 57  SER C CA  1 
ATOM   6385  C C   . SER C  1 57  ? 64.302  34.466  -16.349 1.00   83.76  ? 57  SER C C   1 
ATOM   6386  O O   . SER C  1 57  ? 63.826  34.646  -15.224 1.00   82.15  ? 57  SER C O   1 
ATOM   6387  C CB  . SER C  1 57  ? 64.957  32.467  -17.710 1.00   80.53  ? 57  SER C CB  1 
ATOM   6388  O OG  . SER C  1 57  ? 63.607  32.050  -17.585 1.00   80.83  ? 57  SER C OG  1 
ATOM   6389  N N   . GLN C  1 58  ? 63.911  35.150  -17.419 1.00   89.11  ? 58  GLN C N   1 
ATOM   6390  C CA  . GLN C  1 58  ? 62.801  36.100  -17.391 1.00   89.05  ? 58  GLN C CA  1 
ATOM   6391  C C   . GLN C  1 58  ? 61.481  35.439  -17.003 1.00   88.59  ? 58  GLN C C   1 
ATOM   6392  O O   . GLN C  1 58  ? 60.591  36.090  -16.458 1.00   87.26  ? 58  GLN C O   1 
ATOM   6393  C CB  . GLN C  1 58  ? 62.661  36.741  -18.761 0.0000 91.77  ? 58  GLN C CB  1 
ATOM   6394  C CG  . GLN C  1 58  ? 62.477  35.663  -19.802 0.0000 91.35  ? 58  GLN C CG  1 
ATOM   6395  C CD  . GLN C  1 58  ? 62.669  36.132  -21.209 0.0000 95.56  ? 58  GLN C CD  1 
ATOM   6396  O OE1 . GLN C  1 58  ? 63.027  37.284  -21.459 0.0000 97.78  ? 58  GLN C OE1 1 
ATOM   6397  N NE2 . GLN C  1 58  ? 62.471  35.225  -22.147 0.0000 97.33  ? 58  GLN C NE2 1 
ATOM   6398  N N   . HIS C  1 59  ? 61.374  34.135  -17.254 1.00   88.91  ? 59  HIS C N   1 
ATOM   6399  C CA  . HIS C  1 59  ? 60.125  33.427  -17.008 1.00   88.74  ? 59  HIS C CA  1 
ATOM   6400  C C   . HIS C  1 59  ? 60.056  32.747  -15.657 1.00   83.16  ? 59  HIS C C   1 
ATOM   6401  O O   . HIS C  1 59  ? 59.330  31.777  -15.466 1.00   84.30  ? 59  HIS C O   1 
ATOM   6402  C CB  . HIS C  1 59  ? 59.894  32.415  -18.121 1.00   91.45  ? 59  HIS C CB  1 
ATOM   6403  C CG  . HIS C  1 59  ? 59.833  33.038  -19.479 1.00   96.92  ? 59  HIS C CG  1 
ATOM   6404  N ND1 . HIS C  1 59  ? 60.033  32.320  -20.636 1.00   100.45 ? 59  HIS C ND1 1 
ATOM   6405  C CD2 . HIS C  1 59  ? 59.528  34.300  -19.866 1.00   100.23 ? 59  HIS C CD2 1 
ATOM   6406  C CE1 . HIS C  1 59  ? 59.897  33.122  -21.675 1.00   105.40 ? 59  HIS C CE1 1 
ATOM   6407  N NE2 . HIS C  1 59  ? 59.588  34.329  -21.238 1.00   105.23 ? 59  HIS C NE2 1 
ATOM   6408  N N   . TYR C  1 60  ? 60.823  33.283  -14.722 1.00   76.03  ? 60  TYR C N   1 
ATOM   6409  C CA  . TYR C  1 60  ? 60.677  32.974  -13.316 1.00   66.44  ? 60  TYR C CA  1 
ATOM   6410  C C   . TYR C  1 60  ? 59.401  33.688  -12.878 1.00   63.16  ? 60  TYR C C   1 
ATOM   6411  O O   . TYR C  1 60  ? 59.267  34.905  -13.064 1.00   63.13  ? 60  TYR C O   1 
ATOM   6412  C CB  . TYR C  1 60  ? 61.901  33.422  -12.505 1.00   62.47  ? 60  TYR C CB  1 
ATOM   6413  C CG  . TYR C  1 60  ? 61.930  33.045  -11.020 1.00   55.64  ? 60  TYR C CG  1 
ATOM   6414  C CD1 . TYR C  1 60  ? 60.972  33.533  -10.126 1.00   55.12  ? 60  TYR C CD1 1 
ATOM   6415  C CD2 . TYR C  1 60  ? 62.962  32.278  -10.504 1.00   51.81  ? 60  TYR C CD2 1 
ATOM   6416  C CE1 . TYR C  1 60  ? 61.018  33.216  -8.775  1.00   51.07  ? 60  TYR C CE1 1 
ATOM   6417  C CE2 . TYR C  1 60  ? 63.016  31.956  -9.154  1.00   49.10  ? 60  TYR C CE2 1 
ATOM   6418  C CZ  . TYR C  1 60  ? 62.044  32.433  -8.295  1.00   48.78  ? 60  TYR C CZ  1 
ATOM   6419  O OH  . TYR C  1 60  ? 62.105  32.113  -6.952  1.00   46.39  ? 60  TYR C OH  1 
ATOM   6420  N N   . SER C  1 61  ? 58.424  32.925  -12.413 1.00   59.34  ? 61  SER C N   1 
ATOM   6421  C CA  . SER C  1 61  ? 57.183  33.516  -11.929 1.00   62.42  ? 61  SER C CA  1 
ATOM   6422  C C   . SER C  1 61  ? 56.945  33.212  -10.459 1.00   62.76  ? 61  SER C C   1 
ATOM   6423  O O   . SER C  1 61  ? 56.886  32.045  -10.066 1.00   65.76  ? 61  SER C O   1 
ATOM   6424  C CB  . SER C  1 61  ? 55.993  33.025  -12.735 1.00   66.52  ? 61  SER C CB  1 
ATOM   6425  O OG  . SER C  1 61  ? 54.800  33.557  -12.188 1.00   67.15  ? 61  SER C OG  1 
ATOM   6426  N N   . SER C  1 62  ? 56.849  34.255  -9.644  1.00   59.19  ? 62  SER C N   1 
ATOM   6427  C CA  . SER C  1 62  ? 56.575  34.066  -8.229  1.00   55.66  ? 62  SER C CA  1 
ATOM   6428  C C   . SER C  1 62  ? 56.178  35.355  -7.546  1.00   54.37  ? 62  SER C C   1 
ATOM   6429  O O   . SER C  1 62  ? 56.847  36.381  -7.686  1.00   53.32  ? 62  SER C O   1 
ATOM   6430  C CB  . SER C  1 62  ? 57.778  33.479  -7.506  1.00   43.70  ? 62  SER C CB  1 
ATOM   6431  O OG  . SER C  1 62  ? 57.467  33.346  -6.134  1.00   44.91  ? 62  SER C OG  1 
ATOM   6432  N N   . SER C  1 63  ? 55.124  35.280  -6.751  1.00   53.95  ? 63  SER C N   1 
ATOM   6433  C CA  . SER C  1 63  ? 54.671  36.436  -6.010  1.00   53.31  ? 63  SER C CA  1 
ATOM   6434  C C   . SER C  1 63  ? 55.413  36.578  -4.688  1.00   53.56  ? 63  SER C C   1 
ATOM   6435  O O   . SER C  1 63  ? 55.147  37.508  -3.930  1.00   54.27  ? 63  SER C O   1 
ATOM   6436  C CB  . SER C  1 63  ? 53.168  36.350  -5.753  1.00   53.16  ? 63  SER C CB  1 
ATOM   6437  O OG  . SER C  1 63  ? 52.857  35.299  -4.863  1.00   50.30  ? 63  SER C OG  1 
ATOM   6438  N N   . THR C  1 64  ? 56.335  35.664  -4.396  1.00   50.68  ? 64  THR C N   1 
ATOM   6439  C CA  . THR C  1 64  ? 57.075  35.750  -3.142  1.00   46.03  ? 64  THR C CA  1 
ATOM   6440  C C   . THR C  1 64  ? 58.587  35.921  -3.356  1.00   44.02  ? 64  THR C C   1 
ATOM   6441  O O   . THR C  1 64  ? 59.388  35.893  -2.412  1.00   42.20  ? 64  THR C O   1 
ATOM   6442  C CB  . THR C  1 64  ? 56.818  34.516  -2.270  1.00   42.32  ? 64  THR C CB  1 
ATOM   6443  O OG1 . THR C  1 64  ? 56.846  33.341  -3.086  1.00   43.20  ? 64  THR C OG1 1 
ATOM   6444  C CG2 . THR C  1 64  ? 55.464  34.631  -1.611  1.00   41.00  ? 64  THR C CG2 1 
ATOM   6445  N N   . TYR C  1 65  ? 58.981  36.144  -4.593  1.00   40.75  ? 65  TYR C N   1 
ATOM   6446  C CA  . TYR C  1 65  ? 60.382  36.279  -4.867  1.00   38.68  ? 65  TYR C CA  1 
ATOM   6447  C C   . TYR C  1 65  ? 60.901  37.653  -4.453  1.00   40.03  ? 65  TYR C C   1 
ATOM   6448  O O   . TYR C  1 65  ? 60.246  38.645  -4.708  1.00   41.56  ? 65  TYR C O   1 
ATOM   6449  C CB  . TYR C  1 65  ? 60.619  36.044  -6.348  1.00   41.19  ? 65  TYR C CB  1 
ATOM   6450  C CG  . TYR C  1 65  ? 61.993  36.453  -6.799  1.00   39.96  ? 65  TYR C CG  1 
ATOM   6451  C CD1 . TYR C  1 65  ? 63.078  35.595  -6.659  1.00   37.11  ? 65  TYR C CD1 1 
ATOM   6452  C CD2 . TYR C  1 65  ? 62.212  37.704  -7.354  1.00   40.86  ? 65  TYR C CD2 1 
ATOM   6453  C CE1 . TYR C  1 65  ? 64.343  35.978  -7.068  1.00   36.91  ? 65  TYR C CE1 1 
ATOM   6454  C CE2 . TYR C  1 65  ? 63.467  38.089  -7.762  1.00   40.34  ? 65  TYR C CE2 1 
ATOM   6455  C CZ  . TYR C  1 65  ? 64.525  37.226  -7.615  1.00   37.69  ? 65  TYR C CZ  1 
ATOM   6456  O OH  . TYR C  1 65  ? 65.765  37.624  -8.037  1.00   38.97  ? 65  TYR C OH  1 
ATOM   6457  N N   . GLN C  1 66  ? 62.093  37.692  -3.853  1.00   38.54  ? 66  GLN C N   1 
ATOM   6458  C CA  . GLN C  1 66  ? 62.840  38.910  -3.535  1.00   40.78  ? 66  GLN C CA  1 
ATOM   6459  C C   . GLN C  1 66  ? 64.320  38.715  -3.756  1.00   39.32  ? 66  GLN C C   1 
ATOM   6460  O O   . GLN C  1 66  ? 64.814  37.623  -3.568  1.00   41.75  ? 66  GLN C O   1 
ATOM   6461  C CB  . GLN C  1 66  ? 62.713  39.338  -2.083  1.00   47.56  ? 66  GLN C CB  1 
ATOM   6462  C CG  . GLN C  1 66  ? 61.458  39.972  -1.618  1.00   57.83  ? 66  GLN C CG  1 
ATOM   6463  C CD  . GLN C  1 66  ? 61.543  40.230  -0.124  1.00   63.33  ? 66  GLN C CD  1 
ATOM   6464  O OE1 . GLN C  1 66  ? 62.571  40.705  0.375   1.00   64.58  ? 66  GLN C OE1 1 
ATOM   6465  N NE2 . GLN C  1 66  ? 60.467  39.936  0.596   1.00   66.51  ? 66  GLN C NE2 1 
ATOM   6466  N N   . ALA C  1 67  ? 65.033  39.774  -4.134  1.00   35.91  ? 67  ALA C N   1 
ATOM   6467  C CA  . ALA C  1 67  ? 66.507  39.756  -4.143  1.00   32.85  ? 67  ALA C CA  1 
ATOM   6468  C C   . ALA C  1 67  ? 67.083  40.633  -3.015  1.00   31.15  ? 67  ALA C C   1 
ATOM   6469  O O   . ALA C  1 67  ? 66.936  41.852  -3.072  1.00   32.31  ? 67  ALA C O   1 
ATOM   6470  C CB  . ALA C  1 67  ? 67.028  40.219  -5.483  1.00   32.70  ? 67  ALA C CB  1 
ATOM   6471  N N   . PRO C  1 68  ? 67.684  40.029  -1.958  1.00   30.03  ? 68  PRO C N   1 
ATOM   6472  C CA  . PRO C  1 68  ? 68.186  40.895  -0.875  1.00   31.00  ? 68  PRO C CA  1 
ATOM   6473  C C   . PRO C  1 68  ? 69.185  41.984  -1.341  1.00   32.81  ? 68  PRO C C   1 
ATOM   6474  O O   . PRO C  1 68  ? 69.980  41.775  -2.265  1.00   33.85  ? 68  PRO C O   1 
ATOM   6475  C CB  . PRO C  1 68  ? 68.848  39.898  0.080   1.00   22.72  ? 68  PRO C CB  1 
ATOM   6476  C CG  . PRO C  1 68  ? 68.080  38.641  -0.115  1.00   25.03  ? 68  PRO C CG  1 
ATOM   6477  C CD  . PRO C  1 68  ? 67.731  38.602  -1.584  1.00   27.42  ? 68  PRO C CD  1 
ATOM   6478  N N   . PHE C  1 69  ? 69.147  43.144  -0.698  1.00   33.02  ? 69  PHE C N   1 
ATOM   6479  C CA  . PHE C  1 69  ? 70.036  44.231  -1.098  1.00   32.50  ? 69  PHE C CA  1 
ATOM   6480  C C   . PHE C  1 69  ? 71.410  43.987  -0.494  1.00   31.07  ? 69  PHE C C   1 
ATOM   6481  O O   . PHE C  1 69  ? 71.548  43.269  0.495   1.00   29.63  ? 69  PHE C O   1 
ATOM   6482  C CB  . PHE C  1 69  ? 69.484  45.624  -0.698  1.00   36.92  ? 69  PHE C CB  1 
ATOM   6483  C CG  . PHE C  1 69  ? 69.237  45.807  0.785   1.00   36.76  ? 69  PHE C CG  1 
ATOM   6484  C CD1 . PHE C  1 69  ? 70.278  46.146  1.647   1.00   37.65  ? 69  PHE C CD1 1 
ATOM   6485  C CD2 . PHE C  1 69  ? 67.965  45.694  1.305   1.00   33.40  ? 69  PHE C CD2 1 
ATOM   6486  C CE1 . PHE C  1 69  ? 70.060  46.330  3.000   1.00   33.69  ? 69  PHE C CE1 1 
ATOM   6487  C CE2 . PHE C  1 69  ? 67.748  45.870  2.650   1.00   33.08  ? 69  PHE C CE2 1 
ATOM   6488  C CZ  . PHE C  1 69  ? 68.800  46.188  3.498   1.00   32.93  ? 69  PHE C CZ  1 
ATOM   6489  N N   . CYS C  1 70  ? 72.425  44.582  -1.101  1.00   32.86  ? 70  CYS C N   1 
ATOM   6490  C CA  . CYS C  1 70  ? 73.774  44.400  -0.637  1.00   32.63  ? 70  CYS C CA  1 
ATOM   6491  C C   . CYS C  1 70  ? 73.883  44.901  0.787   1.00   33.41  ? 70  CYS C C   1 
ATOM   6492  O O   . CYS C  1 70  ? 73.270  45.899  1.135   1.00   27.11  ? 70  CYS C O   1 
ATOM   6493  C CB  . CYS C  1 70  ? 74.759  45.127  -1.537  1.00   34.88  ? 70  CYS C CB  1 
ATOM   6494  S SG  . CYS C  1 70  ? 76.395  44.424  -1.418  1.00   41.77  ? 70  CYS C SG  1 
ATOM   6495  N N   . HIS C  1 71  ? 74.629  44.155  1.603   1.00   30.98  ? 71  HIS C N   1 
ATOM   6496  C CA  . HIS C  1 71  ? 74.878  44.448  3.025   1.00   28.44  ? 71  HIS C CA  1 
ATOM   6497  C C   . HIS C  1 71  ? 73.696  44.218  3.908   1.00   28.41  ? 71  HIS C C   1 
ATOM   6498  O O   . HIS C  1 71  ? 73.722  44.643  5.056   1.00   30.87  ? 71  HIS C O   1 
ATOM   6499  C CB  . HIS C  1 71  ? 75.349  45.889  3.241   1.00   29.78  ? 71  HIS C CB  1 
ATOM   6500  C CG  . HIS C  1 71  ? 76.429  46.290  2.303   1.00   30.79  ? 71  HIS C CG  1 
ATOM   6501  N ND1 . HIS C  1 71  ? 77.653  45.664  2.277   1.00   31.11  ? 71  HIS C ND1 1 
ATOM   6502  C CD2 . HIS C  1 71  ? 76.457  47.221  1.328   1.00   33.75  ? 71  HIS C CD2 1 
ATOM   6503  C CE1 . HIS C  1 71  ? 78.393  46.198  1.326   1.00   32.42  ? 71  HIS C CE1 1 
ATOM   6504  N NE2 . HIS C  1 71  ? 77.692  47.149  0.739   1.00   34.86  ? 71  HIS C NE2 1 
ATOM   6505  N N   . SER C  1 72  ? 72.675  43.547  3.383   1.00   26.26  ? 72  SER C N   1 
ATOM   6506  C CA  . SER C  1 72  ? 71.511  43.184  4.180   1.00   26.52  ? 72  SER C CA  1 
ATOM   6507  C C   . SER C  1 72  ? 71.832  42.032  5.125   1.00   27.79  ? 72  SER C C   1 
ATOM   6508  O O   . SER C  1 72  ? 72.879  41.395  5.018   1.00   27.70  ? 72  SER C O   1 
ATOM   6509  C CB  . SER C  1 72  ? 70.336  42.809  3.281   1.00   25.90  ? 72  SER C CB  1 
ATOM   6510  O OG  . SER C  1 72  ? 70.674  41.688  2.498   1.00   27.93  ? 72  SER C OG  1 
ATOM   6511  N N   . THR C  1 73  ? 70.927  41.784  6.059   1.00   29.30  ? 73  THR C N   1 
ATOM   6512  C CA  . THR C  1 73  ? 71.046  40.662  6.966   1.00   27.41  ? 73  THR C CA  1 
ATOM   6513  C C   . THR C  1 73  ? 70.997  39.352  6.215   1.00   28.18  ? 73  THR C C   1 
ATOM   6514  O O   . THR C  1 73  ? 71.609  38.380  6.645   1.00   27.12  ? 73  THR C O   1 
ATOM   6515  C CB  . THR C  1 73  ? 69.946  40.681  8.040   1.00   27.27  ? 73  THR C CB  1 
ATOM   6516  O OG1 . THR C  1 73  ? 68.665  40.766  7.407   1.00   29.09  ? 73  THR C OG1 1 
ATOM   6517  C CG2 . THR C  1 73  ? 70.135  41.862  8.995   1.00   26.72  ? 73  THR C CG2 1 
ATOM   6518  N N   . GLN C  1 74  ? 70.258  39.302  5.107   1.00   29.63  ? 74  GLN C N   1 
ATOM   6519  C CA  . GLN C  1 74  ? 70.265  38.089  4.274   1.00   27.57  ? 74  GLN C CA  1 
ATOM   6520  C C   . GLN C  1 74  ? 71.631  37.818  3.646   1.00   25.24  ? 74  GLN C C   1 
ATOM   6521  O O   . GLN C  1 74  ? 72.064  36.682  3.580   1.00   24.11  ? 74  GLN C O   1 
ATOM   6522  C CB  . GLN C  1 74  ? 69.204  38.164  3.177   1.00   25.92  ? 74  GLN C CB  1 
ATOM   6523  C CG  . GLN C  1 74  ? 67.806  38.150  3.713   1.00   25.54  ? 74  GLN C CG  1 
ATOM   6524  C CD  . GLN C  1 74  ? 67.241  39.523  3.824   1.00   29.81  ? 74  GLN C CD  1 
ATOM   6525  O OE1 . GLN C  1 74  ? 67.970  40.482  4.013   1.00   32.85  ? 74  GLN C OE1 1 
ATOM   6526  N NE2 . GLN C  1 74  ? 65.935  39.636  3.695   1.00   32.70  ? 74  GLN C NE2 1 
ATOM   6527  N N   . CYS C  1 75  ? 72.303  38.860  3.169   1.00   26.44  ? 75  CYS C N   1 
ATOM   6528  C CA  . CYS C  1 75  ? 73.637  38.696  2.588   1.00   24.93  ? 75  CYS C CA  1 
ATOM   6529  C C   . CYS C  1 75  ? 74.665  38.285  3.641   1.00   26.14  ? 75  CYS C C   1 
ATOM   6530  O O   . CYS C  1 75  ? 75.564  37.486  3.382   1.00   26.22  ? 75  CYS C O   1 
ATOM   6531  C CB  . CYS C  1 75  ? 74.067  39.984  1.888   1.00   23.58  ? 75  CYS C CB  1 
ATOM   6532  S SG  . CYS C  1 75  ? 73.016  40.342  0.502   1.00   36.53  ? 75  CYS C SG  1 
ATOM   6533  N N   . SER C  1 76  ? 74.511  38.825  4.840   1.00   27.33  ? 76  SER C N   1 
ATOM   6534  C CA  . SER C  1 76  ? 75.362  38.462  5.960   1.00   25.51  ? 76  SER C CA  1 
ATOM   6535  C C   . SER C  1 76  ? 75.238  36.976  6.261   1.00   25.11  ? 76  SER C C   1 
ATOM   6536  O O   . SER C  1 76  ? 76.241  36.265  6.347   1.00   28.60  ? 76  SER C O   1 
ATOM   6537  C CB  . SER C  1 76  ? 74.987  39.289  7.193   1.00   27.23  ? 76  SER C CB  1 
ATOM   6538  O OG  . SER C  1 76  ? 75.832  39.000  8.279   1.00   29.56  ? 76  SER C OG  1 
ATOM   6539  N N   . ARG C  1 77  ? 74.009  36.493  6.372   1.00   24.79  ? 77  ARG C N   1 
ATOM   6540  C CA  . ARG C  1 77  ? 73.770  35.094  6.683   1.00   25.18  ? 77  ARG C CA  1 
ATOM   6541  C C   . ARG C  1 77  ? 74.340  34.132  5.621   1.00   27.22  ? 77  ARG C C   1 
ATOM   6542  O O   . ARG C  1 77  ? 74.874  33.077  5.950   1.00   24.83  ? 77  ARG C O   1 
ATOM   6543  C CB  . ARG C  1 77  ? 72.271  34.851  6.866   1.00   27.25  ? 77  ARG C CB  1 
ATOM   6544  C CG  . ARG C  1 77  ? 71.995  33.472  7.401   1.00   30.15  ? 77  ARG C CG  1 
ATOM   6545  C CD  . ARG C  1 77  ? 70.538  33.153  7.608   1.00   35.06  ? 77  ARG C CD  1 
ATOM   6546  N NE  . ARG C  1 77  ? 70.443  31.775  8.109   1.00   41.31  ? 77  ARG C NE  1 
ATOM   6547  C CZ  . ARG C  1 77  ? 69.335  31.037  8.134   1.00   43.43  ? 77  ARG C CZ  1 
ATOM   6548  N NH1 . ARG C  1 77  ? 68.186  31.535  7.687   1.00   43.17  ? 77  ARG C NH1 1 
ATOM   6549  N NH2 . ARG C  1 77  ? 69.385  29.802  8.622   1.00   44.49  ? 77  ARG C NH2 1 
ATOM   6550  N N   . ALA C  1 78  ? 74.239  34.518  4.357   1.00   28.80  ? 78  ALA C N   1 
ATOM   6551  C CA  . ALA C  1 78  ? 74.766  33.742  3.237   1.00   27.12  ? 78  ALA C CA  1 
ATOM   6552  C C   . ALA C  1 78  ? 76.266  33.837  3.110   1.00   27.88  ? 78  ALA C C   1 
ATOM   6553  O O   . ALA C  1 78  ? 76.855  33.105  2.327   1.00   31.67  ? 78  ALA C O   1 
ATOM   6554  C CB  . ALA C  1 78  ? 74.133  34.218  1.940   1.00   25.28  ? 78  ALA C CB  1 
ATOM   6555  N N   . ASN C  1 79  ? 76.866  34.736  3.889   1.00   28.87  ? 79  ASN C N   1 
ATOM   6556  C CA  . ASN C  1 79  ? 78.311  34.983  3.905   1.00   32.68  ? 79  ASN C CA  1 
ATOM   6557  C C   . ASN C  1 79  ? 78.846  35.571  2.591   1.00   34.16  ? 79  ASN C C   1 
ATOM   6558  O O   . ASN C  1 79  ? 79.886  35.154  2.082   1.00   35.59  ? 79  ASN C O   1 
ATOM   6559  C CB  . ASN C  1 79  ? 79.051  33.686  4.256   1.00   39.80  ? 79  ASN C CB  1 
ATOM   6560  C CG  . ASN C  1 79  ? 80.495  33.910  4.644   1.00   47.52  ? 79  ASN C CG  1 
ATOM   6561  O OD1 . ASN C  1 79  ? 80.869  34.974  5.131   1.00   52.02  ? 79  ASN C OD1 1 
ATOM   6562  N ND2 . ASN C  1 79  ? 81.325  32.902  4.407   1.00   51.13  ? 79  ASN C ND2 1 
ATOM   6563  N N   . THR C  1 80  ? 78.104  36.521  2.026   1.00   37.20  ? 80  THR C N   1 
ATOM   6564  C CA  . THR C  1 80  ? 78.572  37.288  0.879   1.00   40.69  ? 80  THR C CA  1 
ATOM   6565  C C   . THR C  1 80  ? 78.421  38.771  1.086   1.00   40.07  ? 80  THR C C   1 
ATOM   6566  O O   . THR C  1 80  ? 77.318  39.258  1.323   1.00   37.89  ? 80  THR C O   1 
ATOM   6567  C CB  . THR C  1 80  ? 77.843  36.934  -0.421  1.00   45.12  ? 80  THR C CB  1 
ATOM   6568  O OG1 . THR C  1 80  ? 78.145  37.943  -1.394  1.00   51.52  ? 80  THR C OG1 1 
ATOM   6569  C CG2 . THR C  1 80  ? 76.327  36.869  -0.245  1.00   42.09  ? 80  THR C CG2 1 
ATOM   6570  N N   . HIS C  1 81  ? 79.529  39.489  0.948   1.00   42.81  ? 81  HIS C N   1 
ATOM   6571  C CA  . HIS C  1 81  ? 79.527  40.953  1.064   1.00   44.80  ? 81  HIS C CA  1 
ATOM   6572  C C   . HIS C  1 81  ? 80.016  41.584  -0.212  1.00   42.60  ? 81  HIS C C   1 
ATOM   6573  O O   . HIS C  1 81  ? 80.421  42.742  -0.222  1.00   44.87  ? 81  HIS C O   1 
ATOM   6574  C CB  . HIS C  1 81  ? 80.364  41.439  2.260   1.00   48.07  ? 81  HIS C CB  1 
ATOM   6575  C CG  . HIS C  1 81  ? 79.750  41.102  3.586   1.00   52.55  ? 81  HIS C CG  1 
ATOM   6576  N ND1 . HIS C  1 81  ? 79.935  39.884  4.206   1.00   54.07  ? 81  HIS C ND1 1 
ATOM   6577  C CD2 . HIS C  1 81  ? 78.886  41.793  4.369   1.00   54.00  ? 81  HIS C CD2 1 
ATOM   6578  C CE1 . HIS C  1 81  ? 79.251  39.859  5.336   1.00   54.06  ? 81  HIS C CE1 1 
ATOM   6579  N NE2 . HIS C  1 81  ? 78.602  41.004  5.456   1.00   54.59  ? 81  HIS C NE2 1 
ATOM   6580  N N   . GLN C  1 82  ? 79.972  40.800  -1.287  1.00   42.03  ? 82  GLN C N   1 
ATOM   6581  C CA  . GLN C  1 82  ? 80.289  41.293  -2.614  1.00   43.17  ? 82  GLN C CA  1 
ATOM   6582  C C   . GLN C  1 82  ? 79.001  41.682  -3.291  1.00   37.78  ? 82  GLN C C   1 
ATOM   6583  O O   . GLN C  1 82  ? 78.078  40.899  -3.349  1.00   35.03  ? 82  GLN C O   1 
ATOM   6584  C CB  . GLN C  1 82  ? 81.017  40.253  -3.450  1.00   50.94  ? 82  GLN C CB  1 
ATOM   6585  C CG  . GLN C  1 82  ? 80.810  40.465  -4.935  1.00   60.81  ? 82  GLN C CG  1 
ATOM   6586  C CD  . GLN C  1 82  ? 81.543  39.457  -5.811  1.00   68.87  ? 82  GLN C CD  1 
ATOM   6587  O OE1 . GLN C  1 82  ? 82.165  38.502  -5.325  1.00   72.04  ? 82  GLN C OE1 1 
ATOM   6588  N NE2 . GLN C  1 82  ? 81.502  39.692  -7.121  1.00   71.35  ? 82  GLN C NE2 1 
ATOM   6589  N N   . CYS C  1 83  ? 78.917  42.925  -3.734  1.00   36.05  ? 83  CYS C N   1 
ATOM   6590  C CA  . CYS C  1 83  ? 77.700  43.410  -4.351  1.00   37.25  ? 83  CYS C CA  1 
ATOM   6591  C C   . CYS C  1 83  ? 77.612  42.887  -5.775  1.00   40.35  ? 83  CYS C C   1 
ATOM   6592  O O   . CYS C  1 83  ? 78.625  42.609  -6.414  1.00   44.75  ? 83  CYS C O   1 
ATOM   6593  C CB  . CYS C  1 83  ? 77.646  44.937  -4.330  1.00   38.53  ? 83  CYS C CB  1 
ATOM   6594  S SG  . CYS C  1 83  ? 77.504  45.599  -2.634  1.00   54.34  ? 83  CYS C SG  1 
ATOM   6595  N N   . PHE C  1 84  ? 76.386  42.740  -6.256  1.00   37.99  ? 84  PHE C N   1 
ATOM   6596  C CA  . PHE C  1 84  ? 76.118  42.181  -7.563  1.00   38.30  ? 84  PHE C CA  1 
ATOM   6597  C C   . PHE C  1 84  ? 75.683  43.303  -8.484  1.00   41.57  ? 84  PHE C C   1 
ATOM   6598  O O   . PHE C  1 84  ? 75.034  44.241  -8.047  1.00   41.69  ? 84  PHE C O   1 
ATOM   6599  C CB  . PHE C  1 84  ? 75.054  41.089  -7.482  1.00   38.16  ? 84  PHE C CB  1 
ATOM   6600  C CG  . PHE C  1 84  ? 74.754  40.416  -8.801  1.00   42.25  ? 84  PHE C CG  1 
ATOM   6601  C CD1 . PHE C  1 84  ? 75.481  39.312  -9.222  1.00   41.49  ? 84  PHE C CD1 1 
ATOM   6602  C CD2 . PHE C  1 84  ? 73.708  40.865  -9.602  1.00   45.82  ? 84  PHE C CD2 1 
ATOM   6603  C CE1 . PHE C  1 84  ? 75.187  38.689  -10.426 1.00   44.95  ? 84  PHE C CE1 1 
ATOM   6604  C CE2 . PHE C  1 84  ? 73.411  40.246  -10.807 1.00   48.30  ? 84  PHE C CE2 1 
ATOM   6605  C CZ  . PHE C  1 84  ? 74.146  39.159  -11.221 1.00   48.51  ? 84  PHE C CZ  1 
ATOM   6606  N N   . THR C  1 85  ? 76.147  43.251  -9.728  1.00   45.00  ? 85  THR C N   1 
ATOM   6607  C CA  . THR C  1 85  ? 75.715  44.164  -10.775 1.00   52.98  ? 85  THR C CA  1 
ATOM   6608  C C   . THR C  1 85  ? 75.272  43.395  -12.016 1.00   57.03  ? 85  THR C C   1 
ATOM   6609  O O   . THR C  1 85  ? 76.066  42.650  -12.573 1.00   57.61  ? 85  THR C O   1 
ATOM   6610  C CB  . THR C  1 85  ? 76.843  45.157  -11.153 1.00   65.66  ? 85  THR C CB  1 
ATOM   6611  O OG1 . THR C  1 85  ? 77.206  45.941  -10.001 1.00   66.29  ? 85  THR C OG1 1 
ATOM   6612  C CG2 . THR C  1 85  ? 76.384  46.079  -12.273 1.00   66.08  ? 85  THR C CG2 1 
ATOM   6613  N N   . CYS C  1 86  ? 74.048  43.593  -12.494 1.00   59.48  ? 86  CYS C N   1 
ATOM   6614  C CA  . CYS C  1 86  ? 73.639  42.794  -13.641 1.00   64.49  ? 86  CYS C CA  1 
ATOM   6615  C C   . CYS C  1 86  ? 74.167  43.423  -14.894 1.00   70.46  ? 86  CYS C C   1 
ATOM   6616  O O   . CYS C  1 86  ? 73.804  44.545  -15.260 1.00   70.74  ? 86  CYS C O   1 
ATOM   6617  C CB  . CYS C  1 86  ? 72.142  42.631  -13.771 1.00   66.51  ? 86  CYS C CB  1 
ATOM   6618  S SG  . CYS C  1 86  ? 71.719  41.322  -14.963 1.00   64.96  ? 86  CYS C SG  1 
ATOM   6619  N N   . THR C  1 87  ? 74.962  42.637  -15.600 1.00   74.50  ? 87  THR C N   1 
ATOM   6620  C CA  . THR C  1 87  ? 75.665  43.096  -16.779 1.00   79.64  ? 87  THR C CA  1 
ATOM   6621  C C   . THR C  1 87  ? 75.047  42.479  -17.997 1.00   80.55  ? 87  THR C C   1 
ATOM   6622  O O   . THR C  1 87  ? 75.568  42.588  -19.096 1.00   85.59  ? 87  THR C O   1 
ATOM   6623  C CB  . THR C  1 87  ? 77.108  42.632  -16.714 1.00   81.90  ? 87  THR C CB  1 
ATOM   6624  O OG1 . THR C  1 87  ? 77.130  41.197  -16.720 1.00   82.37  ? 87  THR C OG1 1 
ATOM   6625  C CG2 . THR C  1 87  ? 77.774  43.147  -15.445 1.00   78.29  ? 87  THR C CG2 1 
ATOM   6626  N N   . ASP C  1 88  ? 73.917  41.830  -17.797 1.00   76.95  ? 88  ASP C N   1 
ATOM   6627  C CA  . ASP C  1 88  ? 73.220  41.273  -18.919 1.00   79.82  ? 88  ASP C CA  1 
ATOM   6628  C C   . ASP C  1 88  ? 72.025  42.078  -19.312 1.00   83.63  ? 88  ASP C C   1 
ATOM   6629  O O   . ASP C  1 88  ? 72.167  43.090  -20.009 1.00   90.18  ? 88  ASP C O   1 
ATOM   6630  C CB  . ASP C  1 88  ? 72.851  39.844  -18.615 1.00   77.61  ? 88  ASP C CB  1 
ATOM   6631  C CG  . ASP C  1 88  ? 74.075  38.999  -18.424 1.00   78.58  ? 88  ASP C CG  1 
ATOM   6632  O OD1 . ASP C  1 88  ? 74.907  38.922  -19.350 1.00   79.87  ? 88  ASP C OD1 1 
ATOM   6633  O OD2 . ASP C  1 88  ? 74.238  38.444  -17.325 1.00   77.94  ? 88  ASP C OD2 1 
ATOM   6634  N N   . SER C  1 89  ? 70.853  41.617  -18.897 1.00   79.70  ? 89  SER C N   1 
ATOM   6635  C CA  . SER C  1 89  ? 69.618  42.288  -19.236 1.00   80.01  ? 89  SER C CA  1 
ATOM   6636  C C   . SER C  1 89  ? 69.776  43.777  -19.011 1.00   80.95  ? 89  SER C C   1 
ATOM   6637  O O   . SER C  1 89  ? 70.383  44.215  -18.035 1.00   76.24  ? 89  SER C O   1 
ATOM   6638  C CB  . SER C  1 89  ? 68.460  41.746  -18.399 0.0000 75.21  ? 89  SER C CB  1 
ATOM   6639  O OG  . SER C  1 89  ? 68.120  40.429  -18.794 0.0000 75.64  ? 89  SER C OG  1 
ATOM   6640  N N   . THR C  1 90  ? 69.233  44.548  -19.940 1.00   86.85  ? 90  THR C N   1 
ATOM   6641  C CA  . THR C  1 90  ? 69.201  45.999  -19.834 1.00   89.33  ? 90  THR C CA  1 
ATOM   6642  C C   . THR C  1 90  ? 68.201  46.428  -18.767 1.00   86.37  ? 90  THR C C   1 
ATOM   6643  O O   . THR C  1 90  ? 68.306  47.512  -18.180 1.00   85.85  ? 90  THR C O   1 
ATOM   6644  C CB  . THR C  1 90  ? 68.853  46.649  -21.201 1.00   105.84 ? 90  THR C CB  1 
ATOM   6645  O OG1 . THR C  1 90  ? 69.089  48.061  -21.131 1.00   108.20 ? 90  THR C OG1 1 
ATOM   6646  C CG2 . THR C  1 90  ? 67.380  46.436  -21.568 1.00   107.17 ? 90  THR C CG2 1 
ATOM   6647  N N   . THR C  1 91  ? 67.256  45.537  -18.491 1.00   83.45  ? 91  THR C N   1 
ATOM   6648  C CA  . THR C  1 91  ? 66.280  45.741  -17.439 1.00   79.68  ? 91  THR C CA  1 
ATOM   6649  C C   . THR C  1 91  ? 66.350  44.629  -16.405 1.00   75.01  ? 91  THR C C   1 
ATOM   6650  O O   . THR C  1 91  ? 66.888  43.541  -16.658 1.00   75.30  ? 91  THR C O   1 
ATOM   6651  C CB  . THR C  1 91  ? 64.860  45.782  -17.998 1.00   80.61  ? 91  THR C CB  1 
ATOM   6652  O OG1 . THR C  1 91  ? 64.705  44.716  -18.942 1.00   81.87  ? 91  THR C OG1 1 
ATOM   6653  C CG2 . THR C  1 91  ? 64.638  47.083  -18.744 1.00   85.88  ? 91  THR C CG2 1 
ATOM   6654  N N   . THR C  1 92  ? 65.746  44.887  -15.255 1.00   69.93  ? 92  THR C N   1 
ATOM   6655  C CA  . THR C  1 92  ? 65.819  43.945  -14.167 1.00   67.65  ? 92  THR C CA  1 
ATOM   6656  C C   . THR C  1 92  ? 64.882  42.783  -14.392 1.00   66.15  ? 92  THR C C   1 
ATOM   6657  O O   . THR C  1 92  ? 63.882  42.879  -15.106 1.00   67.31  ? 92  THR C O   1 
ATOM   6658  C CB  . THR C  1 92  ? 65.442  44.571  -12.824 1.00   68.19  ? 92  THR C CB  1 
ATOM   6659  O OG1 . THR C  1 92  ? 64.025  44.803  -12.788 1.00   71.67  ? 92  THR C OG1 1 
ATOM   6660  C CG2 . THR C  1 92  ? 66.217  45.862  -12.597 1.00   68.84  ? 92  THR C CG2 1 
ATOM   6661  N N   . ARG C  1 93  ? 65.251  41.674  -13.775 1.00   63.04  ? 93  ARG C N   1 
ATOM   6662  C CA  . ARG C  1 93  ? 64.504  40.439  -13.825 1.00   63.34  ? 93  ARG C CA  1 
ATOM   6663  C C   . ARG C  1 93  ? 65.065  39.583  -12.707 1.00   56.66  ? 93  ARG C C   1 
ATOM   6664  O O   . ARG C  1 93  ? 66.087  39.944  -12.132 1.00   52.78  ? 93  ARG C O   1 
ATOM   6665  C CB  . ARG C  1 93  ? 64.646  39.777  -15.185 1.00   69.71  ? 93  ARG C CB  1 
ATOM   6666  C CG  . ARG C  1 93  ? 66.067  39.435  -15.530 1.00   73.17  ? 93  ARG C CG  1 
ATOM   6667  C CD  . ARG C  1 93  ? 66.090  38.727  -16.850 1.00   82.93  ? 93  ARG C CD  1 
ATOM   6668  N NE  . ARG C  1 93  ? 67.440  38.349  -17.258 1.00   90.16  ? 93  ARG C NE  1 
ATOM   6669  C CZ  . ARG C  1 93  ? 68.010  37.189  -16.947 1.00   95.02  ? 93  ARG C CZ  1 
ATOM   6670  N NH1 . ARG C  1 93  ? 67.356  36.302  -16.206 1.00   96.10  ? 93  ARG C NH1 1 
ATOM   6671  N NH2 . ARG C  1 93  ? 69.236  36.917  -17.368 1.00   97.10  ? 93  ARG C NH2 1 
ATOM   6672  N N   . PRO C  1 94  ? 64.385  38.481  -12.358 1.00   54.34  ? 94  PRO C N   1 
ATOM   6673  C CA  . PRO C  1 94  ? 64.990  37.598  -11.356 1.00   49.14  ? 94  PRO C CA  1 
ATOM   6674  C C   . PRO C  1 94  ? 66.395  37.153  -11.771 1.00   47.16  ? 94  PRO C C   1 
ATOM   6675  O O   . PRO C  1 94  ? 66.615  36.674  -12.882 1.00   50.50  ? 94  PRO C O   1 
ATOM   6676  C CB  . PRO C  1 94  ? 64.018  36.424  -11.299 1.00   49.85  ? 94  PRO C CB  1 
ATOM   6677  C CG  . PRO C  1 94  ? 62.702  36.998  -11.739 1.00   51.83  ? 94  PRO C CG  1 
ATOM   6678  C CD  . PRO C  1 94  ? 63.059  37.998  -12.797 1.00   54.73  ? 94  PRO C CD  1 
ATOM   6679  N N   . GLY C  1 95  ? 67.351  37.341  -10.878 1.00   43.23  ? 95  GLY C N   1 
ATOM   6680  C CA  . GLY C  1 95  ? 68.725  37.001  -11.179 1.00   44.61  ? 95  GLY C CA  1 
ATOM   6681  C C   . GLY C  1 95  ? 69.512  38.178  -11.723 1.00   48.77  ? 95  GLY C C   1 
ATOM   6682  O O   . GLY C  1 95  ? 70.723  38.116  -11.792 1.00   50.36  ? 95  GLY C O   1 
ATOM   6683  N N   . CYS C  1 96  ? 68.814  39.264  -12.065 1.00   51.58  ? 96  CYS C N   1 
ATOM   6684  C CA  . CYS C  1 96  ? 69.437  40.464  -12.641 1.00   53.88  ? 96  CYS C CA  1 
ATOM   6685  C C   . CYS C  1 96  ? 68.964  41.757  -12.001 1.00   52.18  ? 96  CYS C C   1 
ATOM   6686  O O   . CYS C  1 96  ? 67.926  42.281  -12.357 1.00   53.92  ? 96  CYS C O   1 
ATOM   6687  C CB  . CYS C  1 96  ? 69.196  40.522  -14.161 1.00   59.16  ? 96  CYS C CB  1 
ATOM   6688  S SG  . CYS C  1 96  ? 69.884  42.009  -14.979 1.00   105.38 ? 96  CYS C SG  1 
ATOM   6689  N N   . HIS C  1 97  ? 69.753  42.219  -11.031 1.00   50.13  ? 97  HIS C N   1 
ATOM   6690  C CA  . HIS C  1 97  ? 69.595  43.525  -10.408 1.00   48.59  ? 97  HIS C CA  1 
ATOM   6691  C C   . HIS C  1 97  ? 70.923  44.209  -10.161 1.00   48.34  ? 97  HIS C C   1 
ATOM   6692  O O   . HIS C  1 97  ? 71.972  43.622  -10.355 1.00   42.14  ? 97  HIS C O   1 
ATOM   6693  C CB  . HIS C  1 97  ? 68.840  43.429  -9.078  1.00   44.33  ? 97  HIS C CB  1 
ATOM   6694  C CG  . HIS C  1 97  ? 67.531  42.719  -9.163  1.00   43.96  ? 97  HIS C CG  1 
ATOM   6695  N ND1 . HIS C  1 97  ? 67.415  41.348  -9.100  1.00   43.75  ? 97  HIS C ND1 1 
ATOM   6696  C CD2 . HIS C  1 97  ? 66.270  43.198  -9.257  1.00   41.31  ? 97  HIS C CD2 1 
ATOM   6697  C CE1 . HIS C  1 97  ? 66.139  41.013  -9.184  1.00   44.17  ? 97  HIS C CE1 1 
ATOM   6698  N NE2 . HIS C  1 97  ? 65.424  42.118  -9.277  1.00   46.46  ? 97  HIS C NE2 1 
ATOM   6699  N N   . ASN C  1 98  ? 70.859  45.473  -9.755  1.00   51.82  ? 98  ASN C N   1 
ATOM   6700  C CA  . ASN C  1 98  ? 72.024  46.186  -9.254  1.00   58.75  ? 98  ASN C CA  1 
ATOM   6701  C C   . ASN C  1 98  ? 71.865  46.395  -7.742  1.00   50.59  ? 98  ASN C C   1 
ATOM   6702  O O   . ASN C  1 98  ? 70.763  46.343  -7.226  1.00   45.55  ? 98  ASN C O   1 
ATOM   6703  C CB  . ASN C  1 98  ? 72.184  47.488  -10.018 1.00   77.24  ? 98  ASN C CB  1 
ATOM   6704  C CG  . ASN C  1 98  ? 72.674  47.261  -11.449 1.00   92.68  ? 98  ASN C CG  1 
ATOM   6705  O OD1 . ASN C  1 98  ? 73.321  46.256  -11.741 1.00   89.82  ? 98  ASN C OD1 1 
ATOM   6706  N ND2 . ASN C  1 98  ? 72.352  48.189  -12.346 1.00   109.67 ? 98  ASN C ND2 1 
ATOM   6707  N N   . ASN C  1 99  ? 72.963  46.592  -7.031  1.00   51.40  ? 99  ASN C N   1 
ATOM   6708  C CA  . ASN C  1 99  ? 72.928  46.645  -5.568  1.00   53.01  ? 99  ASN C CA  1 
ATOM   6709  C C   . ASN C  1 99  ? 72.385  45.396  -4.885  1.00   43.71  ? 99  ASN C C   1 
ATOM   6710  O O   . ASN C  1 99  ? 71.768  45.468  -3.830  1.00   41.46  ? 99  ASN C O   1 
ATOM   6711  C CB  . ASN C  1 99  ? 72.121  47.843  -5.064  1.00   64.68  ? 99  ASN C CB  1 
ATOM   6712  C CG  . ASN C  1 99  ? 72.354  48.111  -3.576  1.00   72.19  ? 99  ASN C CG  1 
ATOM   6713  O OD1 . ASN C  1 99  ? 73.412  47.784  -3.038  1.00   74.26  ? 99  ASN C OD1 1 
ATOM   6714  N ND2 . ASN C  1 99  ? 71.343  48.654  -2.899  1.00   74.38  ? 99  ASN C ND2 1 
ATOM   6715  N N   . THR C  1 100 ? 72.630  44.240  -5.462  1.00   39.37  ? 100 THR C N   1 
ATOM   6716  C CA  . THR C  1 100 ? 72.296  43.006  -4.787  1.00   36.20  ? 100 THR C CA  1 
ATOM   6717  C C   . THR C  1 100 ? 73.593  42.354  -4.329  1.00   33.71  ? 100 THR C C   1 
ATOM   6718  O O   . THR C  1 100 ? 74.626  43.005  -4.348  1.00   35.14  ? 100 THR C O   1 
ATOM   6719  C CB  . THR C  1 100 ? 71.479  42.083  -5.709  1.00   37.16  ? 100 THR C CB  1 
ATOM   6720  O OG1 . THR C  1 100 ? 72.026  42.109  -7.027  1.00   37.56  ? 100 THR C OG1 1 
ATOM   6721  C CG2 . THR C  1 100 ? 70.058  42.571  -5.811  1.00   38.73  ? 100 THR C CG2 1 
ATOM   6722  N N   . CYS C  1 101 ? 73.570  41.091  -3.912  1.00   34.11  ? 101 CYS C N   1 
ATOM   6723  C CA  . CYS C  1 101 ? 74.855  40.444  -3.618  1.00   35.12  ? 101 CYS C CA  1 
ATOM   6724  C C   . CYS C  1 101 ? 75.101  39.208  -4.459  1.00   31.53  ? 101 CYS C C   1 
ATOM   6725  O O   . CYS C  1 101 ? 74.193  38.463  -4.822  1.00   32.17  ? 101 CYS C O   1 
ATOM   6726  C CB  A CYS C  1 101 ? 75.019  40.113  -2.122  0.50   35.53  ? 101 CYS C CB  1 
ATOM   6727  C CB  B CYS C  1 101 ? 74.927  40.038  -2.154  0.50   35.50  ? 101 CYS C CB  1 
ATOM   6728  S SG  A CYS C  1 101 ? 73.629  39.450  -1.214  0.50   33.42  ? 101 CYS C SG  1 
ATOM   6729  S SG  B CYS C  1 101 ? 73.917  41.058  -1.135  0.50   34.59  ? 101 CYS C SG  1 
ATOM   6730  N N   . GLY C  1 102 ? 76.378  39.032  -4.755  1.00   29.70  ? 102 GLY C N   1 
ATOM   6731  C CA  . GLY C  1 102 ? 76.858  38.021  -5.645  1.00   28.20  ? 102 GLY C CA  1 
ATOM   6732  C C   . GLY C  1 102 ? 77.289  36.839  -4.823  1.00   37.94  ? 102 GLY C C   1 
ATOM   6733  O O   . GLY C  1 102 ? 77.838  36.959  -3.716  1.00   34.54  ? 102 GLY C O   1 
ATOM   6734  N N   . LEU C  1 103 ? 77.022  35.677  -5.389  1.00   38.23  ? 103 LEU C N   1 
ATOM   6735  C CA  . LEU C  1 103 ? 77.247  34.406  -4.742  1.00   37.68  ? 103 LEU C CA  1 
ATOM   6736  C C   . LEU C  1 103 ? 77.872  33.478  -5.785  1.00   38.27  ? 103 LEU C C   1 
ATOM   6737  O O   . LEU C  1 103 ? 77.325  33.342  -6.876  1.00   40.07  ? 103 LEU C O   1 
ATOM   6738  C CB  . LEU C  1 103 ? 75.912  33.885  -4.226  1.00   38.95  ? 103 LEU C CB  1 
ATOM   6739  C CG  . LEU C  1 103 ? 75.912  32.789  -3.193  1.00   43.33  ? 103 LEU C CG  1 
ATOM   6740  C CD1 . LEU C  1 103 ? 76.828  33.190  -2.065  1.00   45.59  ? 103 LEU C CD1 1 
ATOM   6741  C CD2 . LEU C  1 103 ? 74.488  32.614  -2.724  1.00   42.23  ? 103 LEU C CD2 1 
ATOM   6742  N N   . LEU C  1 104 ? 79.015  32.865  -5.485  1.00   35.06  ? 104 LEU C N   1 
ATOM   6743  C CA  . LEU C  1 104 ? 79.635  31.962  -6.442  1.00   38.62  ? 104 LEU C CA  1 
ATOM   6744  C C   . LEU C  1 104 ? 79.029  30.540  -6.357  1.00   37.28  ? 104 LEU C C   1 
ATOM   6745  O O   . LEU C  1 104 ? 79.004  29.953  -5.282  1.00   35.01  ? 104 LEU C O   1 
ATOM   6746  C CB  . LEU C  1 104 ? 81.143  31.951  -6.222  1.00   39.17  ? 104 LEU C CB  1 
ATOM   6747  C CG  . LEU C  1 104 ? 81.954  31.508  -7.427  1.00   44.65  ? 104 LEU C CG  1 
ATOM   6748  C CD1 . LEU C  1 104 ? 81.823  32.485  -8.577  1.00   45.58  ? 104 LEU C CD1 1 
ATOM   6749  C CD2 . LEU C  1 104 ? 83.395  31.420  -6.975  1.00   47.98  ? 104 LEU C CD2 1 
ATOM   6750  N N   . SER C  1 105 ? 78.480  30.047  -7.469  1.00   33.61  ? 105 SER C N   1 
ATOM   6751  C CA  . SER C  1 105 ? 77.869  28.711  -7.561  1.00   34.80  ? 105 SER C CA  1 
ATOM   6752  C C   . SER C  1 105 ? 78.683  27.759  -8.416  1.00   37.80  ? 105 SER C C   1 
ATOM   6753  O O   . SER C  1 105 ? 79.280  28.181  -9.383  1.00   41.55  ? 105 SER C O   1 
ATOM   6754  C CB  . SER C  1 105 ? 76.457  28.799  -8.142  1.00   35.48  ? 105 SER C CB  1 
ATOM   6755  O OG  . SER C  1 105 ? 75.582  29.614  -7.366  1.00   36.28  ? 105 SER C OG  1 
ATOM   6756  N N   . SER C  1 106 ? 78.692  26.470  -8.077  1.00   49.07  ? 106 SER C N   1 
ATOM   6757  C CA  . SER C  1 106 ? 79.474  25.476  -8.826  1.00   51.47  ? 106 SER C CA  1 
ATOM   6758  C C   . SER C  1 106 ? 78.720  24.325  -9.401  1.00   44.74  ? 106 SER C C   1 
ATOM   6759  O O   . SER C  1 106 ? 77.888  23.733  -8.740  1.00   44.12  ? 106 SER C O   1 
ATOM   6760  C CB  . SER C  1 106 ? 80.558  24.856  -7.963  1.00   52.59  ? 106 SER C CB  1 
ATOM   6761  O OG  . SER C  1 106 ? 81.649  25.730  -7.862  1.00   54.39  ? 106 SER C OG  1 
ATOM   6762  N N   . ASN C  1 107 ? 79.054  24.007  -10.640 1.00   34.48  ? 107 ASN C N   1 
ATOM   6763  C CA  . ASN C  1 107 ? 78.667  22.756  -11.253 1.00   38.34  ? 107 ASN C CA  1 
ATOM   6764  C C   . ASN C  1 107 ? 79.697  21.716  -10.820 1.00   38.21  ? 107 ASN C C   1 
ATOM   6765  O O   . ASN C  1 107 ? 80.823  21.741  -11.292 1.00   40.10  ? 107 ASN C O   1 
ATOM   6766  C CB  . ASN C  1 107 ? 78.605  22.908  -12.788 1.00   40.39  ? 107 ASN C CB  1 
ATOM   6767  C CG  . ASN C  1 107 ? 78.209  21.625  -13.500 1.00   41.47  ? 107 ASN C CG  1 
ATOM   6768  O OD1 . ASN C  1 107 ? 78.566  20.540  -13.065 1.00   39.21  ? 107 ASN C OD1 1 
ATOM   6769  N ND2 . ASN C  1 107 ? 77.498  21.751  -14.628 1.00   37.07  ? 107 ASN C ND2 1 
ATOM   6770  N N   . PRO C  1 108 ? 79.312  20.790  -9.925  1.00   37.61  ? 108 PRO C N   1 
ATOM   6771  C CA  . PRO C  1 108 ? 80.270  19.860  -9.324  1.00   36.73  ? 108 PRO C CA  1 
ATOM   6772  C C   . PRO C  1 108 ? 80.700  18.787  -10.306 1.00   41.51  ? 108 PRO C C   1 
ATOM   6773  O O   . PRO C  1 108 ? 81.678  18.095  -10.077 1.00   44.80  ? 108 PRO C O   1 
ATOM   6774  C CB  . PRO C  1 108 ? 79.495  19.260  -8.162  1.00   33.17  ? 108 PRO C CB  1 
ATOM   6775  C CG  . PRO C  1 108 ? 78.109  19.303  -8.599  1.00   33.16  ? 108 PRO C CG  1 
ATOM   6776  C CD  . PRO C  1 108 ? 77.955  20.563  -9.408  1.00   36.05  ? 108 PRO C CD  1 
ATOM   6777  N N   . VAL C  1 109 ? 79.965  18.652  -11.399 1.00   41.19  ? 109 VAL C N   1 
ATOM   6778  C CA  . VAL C  1 109 ? 80.310  17.683  -12.413 1.00   40.39  ? 109 VAL C CA  1 
ATOM   6779  C C   . VAL C  1 109 ? 81.394  18.227  -13.328 1.00   40.95  ? 109 VAL C C   1 
ATOM   6780  O O   . VAL C  1 109 ? 82.415  17.579  -13.561 1.00   40.96  ? 109 VAL C O   1 
ATOM   6781  C CB  . VAL C  1 109 ? 79.077  17.311  -13.291 1.00   36.93  ? 109 VAL C CB  1 
ATOM   6782  C CG1 . VAL C  1 109 ? 79.503  16.485  -14.495 1.00   39.56  ? 109 VAL C CG1 1 
ATOM   6783  C CG2 . VAL C  1 109 ? 78.014  16.590  -12.473 1.00   37.55  ? 109 VAL C CG2 1 
ATOM   6784  N N   . THR C  1 110 ? 81.151  19.419  -13.860 1.00   40.62  ? 110 THR C N   1 
ATOM   6785  C CA  . THR C  1 110 ? 82.047  20.016  -14.832 1.00   42.79  ? 110 THR C CA  1 
ATOM   6786  C C   . THR C  1 110 ? 83.088  20.868  -14.164 1.00   43.32  ? 110 THR C C   1 
ATOM   6787  O O   . THR C  1 110 ? 84.073  21.237  -14.789 1.00   45.49  ? 110 THR C O   1 
ATOM   6788  C CB  . THR C  1 110 ? 81.291  20.873  -15.835 1.00   45.38  ? 110 THR C CB  1 
ATOM   6789  O OG1 . THR C  1 110 ? 80.702  21.975  -15.141 1.00   42.90  ? 110 THR C OG1 1 
ATOM   6790  C CG2 . THR C  1 110 ? 80.195  20.065  -16.494 1.00   48.35  ? 110 THR C CG2 1 
ATOM   6791  N N   . GLN C  1 111 ? 82.849  21.172  -12.892 1.00   42.29  ? 111 GLN C N   1 
ATOM   6792  C CA  . GLN C  1 111 ? 83.709  22.036  -12.098 1.00   46.05  ? 111 GLN C CA  1 
ATOM   6793  C C   . GLN C  1 111 ? 83.687  23.506  -12.565 1.00   47.67  ? 111 GLN C C   1 
ATOM   6794  O O   . GLN C  1 111 ? 84.498  24.315  -12.126 1.00   47.14  ? 111 GLN C O   1 
ATOM   6795  C CB  . GLN C  1 111 ? 85.140  21.503  -12.118 1.00   53.67  ? 111 GLN C CB  1 
ATOM   6796  C CG  . GLN C  1 111 ? 85.336  20.150  -11.432 1.00   61.44  ? 111 GLN C CG  1 
ATOM   6797  C CD  . GLN C  1 111 ? 85.082  20.166  -9.939  1.00   67.47  ? 111 GLN C CD  1 
ATOM   6798  O OE1 . GLN C  1 111 ? 84.027  19.713  -9.467  1.00   70.35  ? 111 GLN C OE1 1 
ATOM   6799  N NE2 . GLN C  1 111 ? 86.038  20.706  -9.181  1.00   68.68  ? 111 GLN C NE2 1 
ATOM   6800  N N   . GLU C  1 112 ? 82.770  23.853  -13.462 1.00   48.62  ? 112 GLU C N   1 
ATOM   6801  C CA  . GLU C  1 112 ? 82.528  25.253  -13.792 1.00   48.08  ? 112 GLU C CA  1 
ATOM   6802  C C   . GLU C  1 112 ? 81.929  25.993  -12.584 1.00   45.05  ? 112 GLU C C   1 
ATOM   6803  O O   . GLU C  1 112 ? 81.149  25.428  -11.825 1.00   42.97  ? 112 GLU C O   1 
ATOM   6804  C CB  . GLU C  1 112 ? 81.556  25.354  -14.970 1.00   52.49  ? 112 GLU C CB  1 
ATOM   6805  C CG  . GLU C  1 112 ? 82.091  25.016  -16.359 1.00   58.84  ? 112 GLU C CG  1 
ATOM   6806  C CD  . GLU C  1 112 ? 80.959  24.763  -17.362 1.00   64.27  ? 112 GLU C CD  1 
ATOM   6807  O OE1 . GLU C  1 112 ? 79.922  24.174  -16.976 1.00   64.34  ? 112 GLU C OE1 1 
ATOM   6808  O OE2 . GLU C  1 112 ? 81.082  25.171  -18.533 1.00   69.03  1 112 GLU C OE2 1 
ATOM   6809  N N   . SER C  1 113 ? 82.263  27.267  -12.418 1.00   44.58  ? 113 SER C N   1 
ATOM   6810  C CA  . SER C  1 113 ? 81.538  28.087  -11.470 1.00   39.90  ? 113 SER C CA  1 
ATOM   6811  C C   . SER C  1 113 ? 81.207  29.424  -12.120 1.00   37.72  ? 113 SER C C   1 
ATOM   6812  O O   . SER C  1 113 ? 81.841  29.844  -13.091 1.00   37.14  ? 113 SER C O   1 
ATOM   6813  C CB  . SER C  1 113 ? 82.321  28.300  -10.189 1.00   41.92  ? 113 SER C CB  1 
ATOM   6814  O OG  . SER C  1 113 ? 83.463  29.074  -10.453 1.00   48.18  ? 113 SER C OG  1 
ATOM   6815  N N   . GLY C  1 114 ? 80.206  30.097  -11.572 1.00   35.63  ? 114 GLY C N   1 
ATOM   6816  C CA  . GLY C  1 114 ? 79.744  31.353  -12.129 1.00   38.25  ? 114 GLY C CA  1 
ATOM   6817  C C   . GLY C  1 114 ? 79.127  32.189  -11.035 1.00   37.22  ? 114 GLY C C   1 
ATOM   6818  O O   . GLY C  1 114 ? 78.643  31.655  -10.044 1.00   34.97  ? 114 GLY C O   1 
ATOM   6819  N N   . LEU C  1 115 ? 79.136  33.502  -11.216 1.00   37.61  ? 115 LEU C N   1 
ATOM   6820  C CA  . LEU C  1 115 ? 78.638  34.395  -10.189 1.00   36.14  ? 115 LEU C CA  1 
ATOM   6821  C C   . LEU C  1 115 ? 77.129  34.549  -10.314 1.00   37.14  ? 115 LEU C C   1 
ATOM   6822  O O   . LEU C  1 115 ? 76.638  35.051  -11.325 1.00   39.66  ? 115 LEU C O   1 
ATOM   6823  C CB  . LEU C  1 115 ? 79.298  35.768  -10.283 1.00   36.83  ? 115 LEU C CB  1 
ATOM   6824  C CG  . LEU C  1 115 ? 79.048  36.542  -8.980  1.00   40.47  ? 115 LEU C CG  1 
ATOM   6825  C CD1 . LEU C  1 115 ? 80.075  36.173  -7.889  1.00   41.09  ? 115 LEU C CD1 1 
ATOM   6826  C CD2 . LEU C  1 115 ? 78.866  38.050  -9.162  1.00   45.27  ? 115 LEU C CD2 1 
ATOM   6827  N N   . GLY C  1 116 ? 76.405  34.110  -9.285  1.00   34.94  ? 116 GLY C N   1 
ATOM   6828  C CA  . GLY C  1 116 ? 74.961  34.237  -9.240  1.00   34.12  ? 116 GLY C CA  1 
ATOM   6829  C C   . GLY C  1 116 ? 74.512  35.345  -8.318  1.00   32.57  ? 116 GLY C C   1 
ATOM   6830  O O   . GLY C  1 116 ? 75.321  36.022  -7.711  1.00   31.90  ? 116 GLY C O   1 
ATOM   6831  N N   . GLU C  1 117 ? 73.212  35.541  -8.227  1.00   33.86  ? 117 GLU C N   1 
ATOM   6832  C CA  . GLU C  1 117 ? 72.670  36.563  -7.365  1.00   32.56  ? 117 GLU C CA  1 
ATOM   6833  C C   . GLU C  1 117 ? 71.910  35.919  -6.232  1.00   28.86  ? 117 GLU C C   1 
ATOM   6834  O O   . GLU C  1 117 ? 71.091  35.049  -6.463  1.00   28.08  ? 117 GLU C O   1 
ATOM   6835  C CB  . GLU C  1 117 ? 71.766  37.477  -8.162  1.00   36.41  ? 117 GLU C CB  1 
ATOM   6836  C CG  . GLU C  1 117 ? 71.313  38.702  -7.428  1.00   39.11  ? 117 GLU C CG  1 
ATOM   6837  C CD  . GLU C  1 117 ? 70.308  39.485  -8.235  1.00   45.40  ? 117 GLU C CD  1 
ATOM   6838  O OE1 . GLU C  1 117 ? 69.329  38.877  -8.689  1.00   46.68  ? 117 GLU C OE1 1 
ATOM   6839  O OE2 . GLU C  1 117 ? 70.480  40.707  -8.411  1.00   48.99  1 117 GLU C OE2 1 
ATOM   6840  N N   . LEU C  1 118 ? 72.150  36.363  -5.009  1.00   26.80  ? 118 LEU C N   1 
ATOM   6841  C CA  . LEU C  1 118 ? 71.401  35.838  -3.883  1.00   26.44  ? 118 LEU C CA  1 
ATOM   6842  C C   . LEU C  1 118 ? 69.908  36.112  -4.086  1.00   29.41  ? 118 LEU C C   1 
ATOM   6843  O O   . LEU C  1 118 ? 69.511  37.176  -4.545  1.00   31.04  ? 118 LEU C O   1 
ATOM   6844  C CB  . LEU C  1 118 ? 71.891  36.453  -2.571  1.00   24.72  ? 118 LEU C CB  1 
ATOM   6845  C CG  . LEU C  1 118 ? 71.294  35.872  -1.299  1.00   23.81  ? 118 LEU C CG  1 
ATOM   6846  C CD1 . LEU C  1 118 ? 71.695  34.432  -1.125  1.00   24.05  ? 118 LEU C CD1 1 
ATOM   6847  C CD2 . LEU C  1 118 ? 71.692  36.674  -0.098  1.00   23.98  ? 118 LEU C CD2 1 
ATOM   6848  N N   . ALA C  1 119 ? 69.094  35.116  -3.763  1.00   32.65  ? 119 ALA C N   1 
ATOM   6849  C CA  . ALA C  1 119 ? 67.653  35.170  -3.965  1.00   34.37  ? 119 ALA C CA  1 
ATOM   6850  C C   . ALA C  1 119 ? 66.867  34.713  -2.731  1.00   34.76  ? 119 ALA C C   1 
ATOM   6851  O O   . ALA C  1 119 ? 67.405  34.000  -1.888  1.00   35.43  ? 119 ALA C O   1 
ATOM   6852  C CB  . ALA C  1 119 ? 67.285  34.305  -5.165  1.00   36.27  ? 119 ALA C CB  1 
ATOM   6853  N N   . GLN C  1 120 ? 65.589  35.089  -2.644  1.00   35.41  ? 120 GLN C N   1 
ATOM   6854  C CA  . GLN C  1 120 ? 64.727  34.674  -1.531  1.00   36.28  ? 120 GLN C CA  1 
ATOM   6855  C C   . GLN C  1 120 ? 63.321  34.319  -2.065  1.00   39.35  ? 120 GLN C C   1 
ATOM   6856  O O   . GLN C  1 120 ? 62.741  35.089  -2.811  1.00   40.08  ? 120 GLN C O   1 
ATOM   6857  C CB  . GLN C  1 120 ? 64.666  35.786  -0.490  1.00   38.52  ? 120 GLN C CB  1 
ATOM   6858  C CG  . GLN C  1 120 ? 63.825  35.516  0.735   1.00   41.06  ? 120 GLN C CG  1 
ATOM   6859  C CD  . GLN C  1 120 ? 63.709  36.759  1.619   1.00   45.17  ? 120 GLN C CD  1 
ATOM   6860  O OE1 . GLN C  1 120 ? 64.684  37.170  2.262   1.00   44.80  ? 120 GLN C OE1 1 
ATOM   6861  N NE2 . GLN C  1 120 ? 62.515  37.352  1.668   1.00   45.14  ? 120 GLN C NE2 1 
ATOM   6862  N N   . ASP C  1 121 ? 62.794  33.147  -1.702  1.00   38.11  ? 121 ASP C N   1 
ATOM   6863  C CA  . ASP C  1 121 ? 61.461  32.725  -2.144  1.00   36.48  ? 121 ASP C CA  1 
ATOM   6864  C C   . ASP C  1 121 ? 60.960  31.559  -1.263  1.00   32.62  ? 121 ASP C C   1 
ATOM   6865  O O   . ASP C  1 121 ? 61.679  31.111  -0.402  1.00   31.32  ? 121 ASP C O   1 
ATOM   6866  C CB  . ASP C  1 121 ? 61.503  32.323  -3.630  1.00   35.52  ? 121 ASP C CB  1 
ATOM   6867  C CG  . ASP C  1 121 ? 60.174  32.531  -4.351  1.00   35.68  ? 121 ASP C CG  1 
ATOM   6868  O OD1 . ASP C  1 121 ? 59.087  32.488  -3.727  1.00   34.94  ? 121 ASP C OD1 1 
ATOM   6869  O OD2 . ASP C  1 121 ? 60.226  32.738  -5.573  1.00   38.16  1 121 ASP C OD2 1 
ATOM   6870  N N   . VAL C  1 122 ? 59.745  31.069  -1.502  1.00   35.40  ? 122 VAL C N   1 
ATOM   6871  C CA  . VAL C  1 122 ? 59.192  29.910  -0.788  1.00   33.42  ? 122 VAL C CA  1 
ATOM   6872  C C   . VAL C  1 122 ? 59.811  28.608  -1.220  1.00   35.36  ? 122 VAL C C   1 
ATOM   6873  O O   . VAL C  1 122 ? 59.909  28.359  -2.413  1.00   39.84  ? 122 VAL C O   1 
ATOM   6874  C CB  . VAL C  1 122 ? 57.679  29.763  -1.024  1.00   32.07  ? 122 VAL C CB  1 
ATOM   6875  C CG1 . VAL C  1 122 ? 57.181  28.440  -0.466  1.00   32.08  ? 122 VAL C CG1 1 
ATOM   6876  C CG2 . VAL C  1 122 ? 56.937  30.924  -0.427  1.00   33.49  ? 122 VAL C CG2 1 
ATOM   6877  N N   . LEU C  1 123 ? 60.214  27.776  -0.261  1.00   32.26  ? 123 LEU C N   1 
ATOM   6878  C CA  . LEU C  1 123 ? 60.510  26.376  -0.524  1.00   31.63  ? 123 LEU C CA  1 
ATOM   6879  C C   . LEU C  1 123 ? 59.580  25.529  0.321   1.00   33.03  ? 123 LEU C C   1 
ATOM   6880  O O   . LEU C  1 123 ? 59.345  25.867  1.482   1.00   31.22  ? 123 LEU C O   1 
ATOM   6881  C CB  . LEU C  1 123 ? 61.988  26.036  -0.219  1.00   25.68  ? 123 LEU C CB  1 
ATOM   6882  C CG  . LEU C  1 123 ? 62.476  24.571  -0.371  1.00   32.84  ? 123 LEU C CG  1 
ATOM   6883  C CD1 . LEU C  1 123 ? 63.885  24.487  -0.909  1.00   30.46  ? 123 LEU C CD1 1 
ATOM   6884  C CD2 . LEU C  1 123 ? 62.396  23.754  0.944   1.00   27.11  ? 123 LEU C CD2 1 
ATOM   6885  N N   . ALA C  1 124 ? 59.066  24.434  -0.254  1.00   32.77  ? 124 ALA C N   1 
ATOM   6886  C CA  . ALA C  1 124 ? 58.228  23.488  0.479   1.00   32.99  ? 124 ALA C CA  1 
ATOM   6887  C C   . ALA C  1 124 ? 58.777  22.057  0.466   1.00   34.85  ? 124 ALA C C   1 
ATOM   6888  O O   . ALA C  1 124 ? 59.533  21.654  -0.425  1.00   33.75  ? 124 ALA C O   1 
ATOM   6889  C CB  . ALA C  1 124 ? 56.812  23.508  -0.066  1.00   32.22  ? 124 ALA C CB  1 
ATOM   6890  N N   . ILE C  1 125 ? 58.408  21.304  1.496   1.00   37.49  ? 125 ILE C N   1 
ATOM   6891  C CA  . ILE C  1 125 ? 58.882  19.946  1.670   1.00   38.07  ? 125 ILE C CA  1 
ATOM   6892  C C   . ILE C  1 125 ? 57.870  19.125  2.471   1.00   38.11  ? 125 ILE C C   1 
ATOM   6893  O O   . ILE C  1 125 ? 57.172  19.659  3.318   1.00   37.72  ? 125 ILE C O   1 
ATOM   6894  C CB  . ILE C  1 125 ? 60.265  19.952  2.373   1.00   31.34  ? 125 ILE C CB  1 
ATOM   6895  C CG1 . ILE C  1 125 ? 60.909  18.565  2.379   1.00   28.86  ? 125 ILE C CG1 1 
ATOM   6896  C CG2 . ILE C  1 125 ? 60.152  20.540  3.768   1.00   32.98  ? 125 ILE C CG2 1 
ATOM   6897  C CD1 . ILE C  1 125 ? 62.266  18.540  2.993   1.00   28.90  ? 125 ILE C CD1 1 
ATOM   6898  N N   . HIS C  1 126 ? 57.800  17.827  2.215   1.00   38.06  ? 126 HIS C N   1 
ATOM   6899  C CA  . HIS C  1 126 ? 56.847  16.979  2.919   1.00   39.39  ? 126 HIS C CA  1 
ATOM   6900  C C   . HIS C  1 126 ? 57.163  16.837  4.391   1.00   36.91  ? 126 HIS C C   1 
ATOM   6901  O O   . HIS C  1 126 ? 58.315  16.679  4.772   1.00   33.60  ? 126 HIS C O   1 
ATOM   6902  C CB  . HIS C  1 126 ? 56.794  15.586  2.295   1.00   37.45  ? 126 HIS C CB  1 
ATOM   6903  C CG  . HIS C  1 126 ? 55.972  15.519  1.052   1.00   38.44  ? 126 HIS C CG  1 
ATOM   6904  N ND1 . HIS C  1 126 ? 54.594  15.552  1.070   1.00   42.43  ? 126 HIS C ND1 1 
ATOM   6905  C CD2 . HIS C  1 126 ? 56.332  15.427  -0.248  1.00   37.51  ? 126 HIS C CD2 1 
ATOM   6906  C CE1 . HIS C  1 126 ? 54.141  15.493  -0.169  1.00   44.01  ? 126 HIS C CE1 1 
ATOM   6907  N NE2 . HIS C  1 126 ? 55.174  15.412  -0.987  1.00   41.28  ? 126 HIS C NE2 1 
ATOM   6908  N N   . SER C  1 127 ? 56.126  16.890  5.213   1.00   38.09  ? 127 SER C N   1 
ATOM   6909  C CA  . SER C  1 127 ? 56.250  16.432  6.580   1.00   37.68  ? 127 SER C CA  1 
ATOM   6910  C C   . SER C  1 127 ? 55.855  14.968  6.570   1.00   38.31  ? 127 SER C C   1 
ATOM   6911  O O   . SER C  1 127 ? 55.833  14.344  5.516   1.00   38.20  ? 127 SER C O   1 
ATOM   6912  C CB  . SER C  1 127 ? 55.376  17.246  7.543   1.00   37.83  ? 127 SER C CB  1 
ATOM   6913  O OG  . SER C  1 127 ? 54.028  17.270  7.140   1.00   39.76  ? 127 SER C OG  1 
ATOM   6914  N N   . THR C  1 128 ? 55.605  14.394  7.736   1.00   40.41  ? 128 THR C N   1 
ATOM   6915  C CA  . THR C  1 128 ? 55.062  13.045  7.785   1.00   43.70  ? 128 THR C CA  1 
ATOM   6916  C C   . THR C  1 128 ? 53.760  13.059  8.564   1.00   47.43  ? 128 THR C C   1 
ATOM   6917  O O   . THR C  1 128 ? 53.541  13.938  9.398   1.00   49.79  ? 128 THR C O   1 
ATOM   6918  C CB  . THR C  1 128 ? 56.002  12.047  8.451   1.00   41.44  ? 128 THR C CB  1 
ATOM   6919  O OG1 . THR C  1 128 ? 56.072  12.322  9.856   1.00   42.89  ? 128 THR C OG1 1 
ATOM   6920  C CG2 . THR C  1 128 ? 57.373  12.097  7.824   1.00   35.98  ? 128 THR C CG2 1 
ATOM   6921  N N   . HIS C  1 129 ? 52.900  12.087  8.296   1.00   48.70  ? 129 HIS C N   1 
ATOM   6922  C CA  . HIS C  1 129 ? 51.653  11.944  9.036   1.00   50.80  ? 129 HIS C CA  1 
ATOM   6923  C C   . HIS C  1 129 ? 51.495  10.469  9.350   1.00   51.24  ? 129 HIS C C   1 
ATOM   6924  O O   . HIS C  1 129 ? 51.210  9.674   8.464   1.00   50.15  ? 129 HIS C O   1 
ATOM   6925  C CB  . HIS C  1 129 ? 50.453  12.488  8.250   1.00   55.87  ? 129 HIS C CB  1 
ATOM   6926  C CG  . HIS C  1 129 ? 49.156  12.460  9.012   1.00   62.63  ? 129 HIS C CG  1 
ATOM   6927  N ND1 . HIS C  1 129 ? 48.995  13.064  10.243  1.00   64.91  ? 129 HIS C ND1 1 
ATOM   6928  C CD2 . HIS C  1 129 ? 47.951  11.922  8.702   1.00   67.13  ? 129 HIS C CD2 1 
ATOM   6929  C CE1 . HIS C  1 129 ? 47.755  12.884  10.663  1.00   69.18  ? 129 HIS C CE1 1 
ATOM   6930  N NE2 . HIS C  1 129 ? 47.099  12.198  9.745   1.00   70.35  ? 129 HIS C NE2 1 
ATOM   6931  N N   . GLY C  1 130 ? 51.743  10.099  10.603  1.00   53.73  ? 130 GLY C N   1 
ATOM   6932  C CA  . GLY C  1 130 ? 51.791  8.695   10.966  1.00   56.10  ? 130 GLY C CA  1 
ATOM   6933  C C   . GLY C  1 130 ? 52.928  7.997   10.230  1.00   53.54  ? 130 GLY C C   1 
ATOM   6934  O O   . GLY C  1 130 ? 54.083  8.437   10.282  1.00   48.47  ? 130 GLY C O   1 
ATOM   6935  N N   . SER C  1 131 ? 52.588  6.919   9.523   1.00   54.12  ? 131 SER C N   1 
ATOM   6936  C CA  . SER C  1 131 ? 53.567  6.149   8.767   1.00   52.31  ? 131 SER C CA  1 
ATOM   6937  C C   . SER C  1 131 ? 53.701  6.562   7.290   1.00   54.59  ? 131 SER C C   1 
ATOM   6938  O O   . SER C  1 131 ? 54.463  5.958   6.539   1.00   57.16  ? 131 SER C O   1 
ATOM   6939  C CB  . SER C  1 131 ? 53.236  4.654   8.869   1.00   53.20  ? 131 SER C CB  1 
ATOM   6940  O OG  . SER C  1 131 ? 52.141  4.286   8.049   1.00   51.98  ? 131 SER C OG  1 
ATOM   6941  N N   . LYS C  1 132 ? 52.957  7.572   6.864   1.00   53.89  ? 132 LYS C N   1 
ATOM   6942  C CA  . LYS C  1 132 ? 52.995  7.997   5.473   1.00   51.28  ? 132 LYS C CA  1 
ATOM   6943  C C   . LYS C  1 132 ? 53.617  9.381   5.373   1.00   51.31  ? 132 LYS C C   1 
ATOM   6944  O O   . LYS C  1 132 ? 53.880  10.019  6.387   1.00   53.99  ? 132 LYS C O   1 
ATOM   6945  C CB  . LYS C  1 132 ? 51.588  8.002   4.888   1.00   51.04  ? 132 LYS C CB  1 
ATOM   6946  C CG  . LYS C  1 132 ? 50.908  6.664   4.998   1.00   57.95  ? 132 LYS C CG  1 
ATOM   6947  C CD  . LYS C  1 132 ? 50.614  6.073   3.645   1.00   65.94  ? 132 LYS C CD  1 
ATOM   6948  C CE  . LYS C  1 132 ? 50.694  7.117   2.546   1.00   70.64  ? 132 LYS C CE  1 
ATOM   6949  N NZ  . LYS C  1 132 ? 50.507  6.472   1.216   1.00   75.69  ? 132 LYS C NZ  1 
ATOM   6950  N N   . LEU C  1 133 ? 53.861  9.855   4.160   1.00   47.53  ? 133 LEU C N   1 
ATOM   6951  C CA  . LEU C  1 133 ? 54.181  11.272  3.971   1.00   45.99  ? 133 LEU C CA  1 
ATOM   6952  C C   . LEU C  1 133 ? 52.991  12.195  4.315   1.00   44.53  ? 133 LEU C C   1 
ATOM   6953  O O   . LEU C  1 133 ? 51.859  11.904  3.974   1.00   47.95  ? 133 LEU C O   1 
ATOM   6954  C CB  . LEU C  1 133 ? 54.620  11.531  2.528   1.00   46.17  ? 133 LEU C CB  1 
ATOM   6955  C CG  . LEU C  1 133 ? 55.964  10.996  2.034   1.00   44.60  ? 133 LEU C CG  1 
ATOM   6956  C CD1 . LEU C  1 133 ? 56.166  11.354  0.564   1.00   46.73  ? 133 LEU C CD1 1 
ATOM   6957  C CD2 . LEU C  1 133 ? 57.090  11.531  2.872   1.00   37.95  ? 133 LEU C CD2 1 
ATOM   6958  N N   . GLY C  1 134 ? 53.263  13.318  4.961   1.00   41.82  ? 134 GLY C N   1 
ATOM   6959  C CA  . GLY C  1 134 ? 52.223  14.263  5.315   1.00   43.07  ? 134 GLY C CA  1 
ATOM   6960  C C   . GLY C  1 134 ? 52.239  15.511  4.448   1.00   44.13  ? 134 GLY C C   1 
ATOM   6961  O O   . GLY C  1 134 ? 52.936  15.562  3.428   1.00   41.35  ? 134 GLY C O   1 
ATOM   6962  N N   . PRO C  1 135 ? 51.495  16.546  4.868   1.00   47.08  ? 135 PRO C N   1 
ATOM   6963  C CA  . PRO C  1 135 ? 51.378  17.769  4.062   1.00   51.37  ? 135 PRO C CA  1 
ATOM   6964  C C   . PRO C  1 135 ? 52.708  18.530  3.861   1.00   53.29  ? 135 PRO C C   1 
ATOM   6965  O O   . PRO C  1 135 ? 53.632  18.473  4.690   1.00   51.64  ? 135 PRO C O   1 
ATOM   6966  C CB  . PRO C  1 135 ? 50.387  18.620  4.869   1.00   49.29  ? 135 PRO C CB  1 
ATOM   6967  C CG  . PRO C  1 135 ? 50.459  18.089  6.255   1.00   48.12  ? 135 PRO C CG  1 
ATOM   6968  C CD  . PRO C  1 135 ? 50.747  16.633  6.133   1.00   47.24  ? 135 PRO C CD  1 
ATOM   6969  N N   . MET C  1 136 ? 52.800  19.245  2.748   1.00   38.13  ? 136 MET C N   1 
ATOM   6970  C CA  . MET C  1 136 ? 53.947  20.095  2.516   1.00   39.84  ? 136 MET C CA  1 
ATOM   6971  C C   . MET C  1 136 ? 53.982  21.170  3.573   1.00   41.90  ? 136 MET C C   1 
ATOM   6972  O O   . MET C  1 136 ? 52.934  21.672  3.977   1.00   42.63  ? 136 MET C O   1 
ATOM   6973  C CB  . MET C  1 136 ? 53.899  20.738  1.133   1.00   40.43  ? 136 MET C CB  1 
ATOM   6974  C CG  . MET C  1 136 ? 53.671  19.775  0.004   1.00   42.58  ? 136 MET C CG  1 
ATOM   6975  S SD  . MET C  1 136 ? 55.206  18.968  -0.431  1.00   58.48  ? 136 MET C SD  1 
ATOM   6976  C CE  . MET C  1 136 ? 56.070  20.287  -1.196  1.00   51.77  ? 136 MET C CE  1 
ATOM   6977  N N   . VAL C  1 137 ? 55.190  21.496  4.031   1.00   42.35  ? 137 VAL C N   1 
ATOM   6978  C CA  . VAL C  1 137 ? 55.436  22.641  4.898   1.00   40.20  ? 137 VAL C CA  1 
ATOM   6979  C C   . VAL C  1 137 ? 56.404  23.590  4.199   1.00   36.05  ? 137 VAL C C   1 
ATOM   6980  O O   . VAL C  1 137 ? 57.205  23.147  3.387   1.00   33.70  ? 137 VAL C O   1 
ATOM   6981  C CB  . VAL C  1 137 ? 56.003  22.213  6.264   1.00   40.07  ? 137 VAL C CB  1 
ATOM   6982  C CG1 . VAL C  1 137 ? 54.920  21.518  7.048   1.00   40.32  ? 137 VAL C CG1 1 
ATOM   6983  C CG2 . VAL C  1 137 ? 57.210  21.302  6.108   1.00   29.10  ? 137 VAL C CG2 1 
ATOM   6984  N N   . LYS C  1 138 ? 56.314  24.887  4.499   1.00   36.99  ? 138 LYS C N   1 
ATOM   6985  C CA  . LYS C  1 138 ? 57.086  25.908  3.781   1.00   35.48  ? 138 LYS C CA  1 
ATOM   6986  C C   . LYS C  1 138 ? 58.165  26.607  4.611   1.00   34.15  ? 138 LYS C C   1 
ATOM   6987  O O   . LYS C  1 138 ? 58.016  26.830  5.811   1.00   34.01  ? 138 LYS C O   1 
ATOM   6988  C CB  . LYS C  1 138 ? 56.168  26.987  3.200   1.00   37.42  ? 138 LYS C CB  1 
ATOM   6989  C CG  . LYS C  1 138 ? 55.151  26.509  2.184   1.00   41.19  ? 138 LYS C CG  1 
ATOM   6990  C CD  . LYS C  1 138 ? 54.280  27.659  1.668   1.00   43.45  ? 138 LYS C CD  1 
ATOM   6991  C CE  . LYS C  1 138 ? 53.226  27.149  0.679   1.00   46.31  ? 138 LYS C CE  1 
ATOM   6992  N NZ  . LYS C  1 138 ? 52.415  28.224  0.088   1.00   49.00  ? 138 LYS C NZ  1 
ATOM   6993  N N   . VAL C  1 139 ? 59.263  26.934  3.940   1.00   33.34  ? 139 VAL C N   1 
ATOM   6994  C CA  . VAL C  1 139 ? 60.204  27.945  4.412   1.00   32.30  ? 139 VAL C CA  1 
ATOM   6995  C C   . VAL C  1 139 ? 59.961  29.143  3.527   1.00   33.87  ? 139 VAL C C   1 
ATOM   6996  O O   . VAL C  1 139 ? 60.378  29.148  2.380   1.00   33.96  ? 139 VAL C O   1 
ATOM   6997  C CB  . VAL C  1 139 ? 61.691  27.501  4.307   1.00   35.99  ? 139 VAL C CB  1 
ATOM   6998  C CG1 . VAL C  1 139 ? 62.634  28.558  4.881   1.00   34.42  ? 139 VAL C CG1 1 
ATOM   6999  C CG2 . VAL C  1 139 ? 61.926  26.167  5.005   1.00   36.43  ? 139 VAL C CG2 1 
ATOM   7000  N N   . PRO C  1 140 ? 59.242  30.151  4.033   1.00   36.49  ? 140 PRO C N   1 
ATOM   7001  C CA  . PRO C  1 140 ? 58.807  31.251  3.165   1.00   39.58  ? 140 PRO C CA  1 
ATOM   7002  C C   . PRO C  1 140 ? 59.940  32.185  2.707   1.00   38.34  ? 140 PRO C C   1 
ATOM   7003  O O   . PRO C  1 140 ? 59.815  32.811  1.649   1.00   39.18  ? 140 PRO C O   1 
ATOM   7004  C CB  . PRO C  1 140 ? 57.795  32.002  4.033   1.00   42.36  ? 140 PRO C CB  1 
ATOM   7005  C CG  . PRO C  1 140 ? 57.478  31.066  5.163   1.00   41.02  ? 140 PRO C CG  1 
ATOM   7006  C CD  . PRO C  1 140 ? 58.702  30.281  5.392   1.00   36.62  ? 140 PRO C CD  1 
ATOM   7007  N N   . GLN C  1 141 ? 61.020  32.280  3.477   1.00   36.73  ? 141 GLN C N   1 
ATOM   7008  C CA  . GLN C  1 141 ? 62.157  33.095  3.053   1.00   39.03  ? 141 GLN C CA  1 
ATOM   7009  C C   . GLN C  1 141 ? 63.386  32.240  2.870   1.00   31.36  ? 141 GLN C C   1 
ATOM   7010  O O   . GLN C  1 141 ? 64.387  32.475  3.506   1.00   29.16  ? 141 GLN C O   1 
ATOM   7011  C CB  . GLN C  1 141 ? 62.488  34.222  4.055   1.00   43.88  ? 141 GLN C CB  1 
ATOM   7012  C CG  . GLN C  1 141 ? 61.492  35.356  4.198   1.00   50.27  ? 141 GLN C CG  1 
ATOM   7013  C CD  . GLN C  1 141 ? 60.459  35.099  5.255   1.00   59.64  ? 141 GLN C CD  1 
ATOM   7014  O OE1 . GLN C  1 141 ? 60.627  34.235  6.119   1.00   62.01  ? 141 GLN C OE1 1 
ATOM   7015  N NE2 . GLN C  1 141 ? 59.385  35.868  5.217   1.00   65.48  ? 141 GLN C NE2 1 
ATOM   7016  N N   . PHE C  1 142 ? 63.291  31.232  2.017   1.00   30.64  ? 142 PHE C N   1 
ATOM   7017  C CA  . PHE C  1 142 ? 64.414  30.345  1.739   1.00   27.10  ? 142 PHE C CA  1 
ATOM   7018  C C   . PHE C  1 142 ? 65.437  31.067  0.857   1.00   27.53  ? 142 PHE C C   1 
ATOM   7019  O O   . PHE C  1 142 ? 65.082  31.617  -0.176  1.00   27.43  ? 142 PHE C O   1 
ATOM   7020  C CB  . PHE C  1 142 ? 63.930  29.034  1.077   1.00   24.22  ? 142 PHE C CB  1 
ATOM   7021  C CG  . PHE C  1 142 ? 65.026  27.995  0.889   1.00   27.09  ? 142 PHE C CG  1 
ATOM   7022  C CD1 . PHE C  1 142 ? 65.421  27.169  1.943   1.00   24.12  ? 142 PHE C CD1 1 
ATOM   7023  C CD2 . PHE C  1 142 ? 65.677  27.854  -0.333  1.00   27.60  ? 142 PHE C CD2 1 
ATOM   7024  C CE1 . PHE C  1 142 ? 66.447  26.222  1.773   1.00   26.80  ? 142 PHE C CE1 1 
ATOM   7025  C CE2 . PHE C  1 142 ? 66.692  26.908  -0.502  1.00   25.60  ? 142 PHE C CE2 1 
ATOM   7026  C CZ  . PHE C  1 142 ? 67.079  26.098  0.556   1.00   26.37  ? 142 PHE C CZ  1 
ATOM   7027  N N   . LEU C  1 143 ? 66.705  31.046  1.273   1.00   27.28  ? 143 LEU C N   1 
ATOM   7028  C CA  . LEU C  1 143 ? 67.800  31.673  0.536   1.00   27.77  ? 143 LEU C CA  1 
ATOM   7029  C C   . LEU C  1 143 ? 68.548  30.719  -0.384  1.00   29.87  ? 143 LEU C C   1 
ATOM   7030  O O   . LEU C  1 143 ? 68.907  29.597  0.006   1.00   31.08  ? 143 LEU C O   1 
ATOM   7031  C CB  . LEU C  1 143 ? 68.797  32.324  1.511   1.00   28.32  ? 143 LEU C CB  1 
ATOM   7032  C CG  . LEU C  1 143 ? 68.278  33.459  2.411   1.00   29.52  ? 143 LEU C CG  1 
ATOM   7033  C CD1 . LEU C  1 143 ? 69.316  33.839  3.443   1.00   28.13  ? 143 LEU C CD1 1 
ATOM   7034  C CD2 . LEU C  1 143 ? 67.861  34.694  1.625   1.00   27.68  ? 143 LEU C CD2 1 
ATOM   7035  N N   . PHE C  1 144 ? 68.813  31.192  -1.599  1.00   31.36  ? 144 PHE C N   1 
ATOM   7036  C CA  . PHE C  1 144 ? 69.447  30.380  -2.627  1.00   28.96  ? 144 PHE C CA  1 
ATOM   7037  C C   . PHE C  1 144 ? 70.081  31.298  -3.667  1.00   29.96  ? 144 PHE C C   1 
ATOM   7038  O O   . PHE C  1 144 ? 69.974  32.520  -3.571  1.00   31.45  ? 144 PHE C O   1 
ATOM   7039  C CB  . PHE C  1 144 ? 68.409  29.455  -3.263  1.00   30.12  ? 144 PHE C CB  1 
ATOM   7040  C CG  . PHE C  1 144 ? 67.362  30.183  -4.033  1.00   30.40  ? 144 PHE C CG  1 
ATOM   7041  C CD1 . PHE C  1 144 ? 66.289  30.766  -3.384  1.00   29.87  ? 144 PHE C CD1 1 
ATOM   7042  C CD2 . PHE C  1 144 ? 67.452  30.299  -5.407  1.00   31.90  ? 144 PHE C CD2 1 
ATOM   7043  C CE1 . PHE C  1 144 ? 65.331  31.463  -4.084  1.00   30.73  ? 144 PHE C CE1 1 
ATOM   7044  C CE2 . PHE C  1 144 ? 66.484  30.994  -6.123  1.00   33.66  ? 144 PHE C CE2 1 
ATOM   7045  C CZ  . PHE C  1 144 ? 65.418  31.572  -5.461  1.00   33.03  ? 144 PHE C CZ  1 
ATOM   7046  N N   . SER C  1 145 ? 70.705  30.720  -4.680  1.00   29.01  ? 145 SER C N   1 
ATOM   7047  C CA  . SER C  1 145 ? 71.344  31.524  -5.698  1.00   29.47  ? 145 SER C CA  1 
ATOM   7048  C C   . SER C  1 145 ? 70.635  31.365  -7.048  1.00   33.64  ? 145 SER C C   1 
ATOM   7049  O O   . SER C  1 145 ? 70.286  30.257  -7.459  1.00   33.70  ? 145 SER C O   1 
ATOM   7050  C CB  . SER C  1 145 ? 72.827  31.153  -5.793  1.00   28.54  ? 145 SER C CB  1 
ATOM   7051  O OG  . SER C  1 145 ? 73.483  31.840  -6.842  1.00   30.50  ? 145 SER C OG  1 
ATOM   7052  N N   . CYS C  1 146 ? 70.374  32.492  -7.705  1.00   35.55  ? 146 CYS C N   1 
ATOM   7053  C CA  . CYS C  1 146 ? 69.977  32.504  -9.094  1.00   33.13  ? 146 CYS C CA  1 
ATOM   7054  C C   . CYS C  1 146 ? 71.247  32.501  -9.880  1.00   32.73  ? 146 CYS C C   1 
ATOM   7055  O O   . CYS C  1 146 ? 71.917  33.512  -9.922  1.00   33.40  ? 146 CYS C O   1 
ATOM   7056  C CB  . CYS C  1 146 ? 69.163  33.739  -9.443  1.00   31.62  ? 146 CYS C CB  1 
ATOM   7057  S SG  . CYS C  1 146 ? 67.422  33.672  -8.973  1.00   41.13  ? 146 CYS C SG  1 
ATOM   7058  N N   . ALA C  1 147 ? 71.604  31.365  -10.464 1.00   34.09  ? 147 ALA C N   1 
ATOM   7059  C CA  . ALA C  1 147 ? 72.893  31.213  -11.135 1.00   38.64  ? 147 ALA C CA  1 
ATOM   7060  C C   . ALA C  1 147 ? 72.826  31.547  -12.628 1.00   42.21  ? 147 ALA C C   1 
ATOM   7061  O O   . ALA C  1 147 ? 71.740  31.545  -13.229 1.00   44.77  ? 147 ALA C O   1 
ATOM   7062  C CB  . ALA C  1 147 ? 73.434  29.791  -10.927 1.00   38.81  ? 147 ALA C CB  1 
ATOM   7063  N N   . PRO C  1 148 ? 73.987  31.861  -13.227 1.00   39.40  ? 148 PRO C N   1 
ATOM   7064  C CA  . PRO C  1 148 ? 74.020  32.076  -14.674 1.00   40.93  ? 148 PRO C CA  1 
ATOM   7065  C C   . PRO C  1 148 ? 73.588  30.825  -15.386 1.00   43.69  ? 148 PRO C C   1 
ATOM   7066  O O   . PRO C  1 148 ? 73.978  29.743  -14.981 1.00   42.51  ? 148 PRO C O   1 
ATOM   7067  C CB  . PRO C  1 148 ? 75.486  32.364  -14.967 1.00   40.94  ? 148 PRO C CB  1 
ATOM   7068  C CG  . PRO C  1 148 ? 76.229  31.893  -13.736 1.00   38.64  ? 148 PRO C CG  1 
ATOM   7069  C CD  . PRO C  1 148 ? 75.305  32.047  -12.601 1.00   37.24  ? 148 PRO C CD  1 
ATOM   7070  N N   . SER C  1 149 ? 72.805  30.984  -16.443 1.00   47.69  ? 149 SER C N   1 
ATOM   7071  C CA  . SER C  1 149 ? 72.218  29.862  -17.162 1.00   51.05  ? 149 SER C CA  1 
ATOM   7072  C C   . SER C  1 149 ? 73.229  28.834  -17.686 1.00   47.63  ? 149 SER C C   1 
ATOM   7073  O O   . SER C  1 149 ? 72.928  27.647  -17.749 1.00   48.34  ? 149 SER C O   1 
ATOM   7074  C CB  . SER C  1 149 ? 71.384  30.403  -18.310 1.00   59.96  ? 149 SER C CB  1 
ATOM   7075  O OG  . SER C  1 149 ? 72.223  31.053  -19.248 1.00   66.92  ? 149 SER C OG  1 
ATOM   7076  N N   . PHE C  1 150 ? 74.412  29.285  -18.085 1.00   45.21  ? 150 PHE C N   1 
ATOM   7077  C CA  . PHE C  1 150 ? 75.390  28.394  -18.693 1.00   44.22  ? 150 PHE C CA  1 
ATOM   7078  C C   . PHE C  1 150 ? 75.831  27.307  -17.744 1.00   42.19  ? 150 PHE C C   1 
ATOM   7079  O O   . PHE C  1 150 ? 76.307  26.262  -18.161 1.00   47.12  ? 150 PHE C O   1 
ATOM   7080  C CB  . PHE C  1 150 ? 76.625  29.174  -19.134 1.00   51.73  ? 150 PHE C CB  1 
ATOM   7081  C CG  . PHE C  1 150 ? 77.570  29.473  -18.006 1.00   50.77  ? 150 PHE C CG  1 
ATOM   7082  C CD1 . PHE C  1 150 ? 78.522  28.542  -17.594 1.00   50.25  ? 150 PHE C CD1 1 
ATOM   7083  C CD2 . PHE C  1 150 ? 77.495  30.680  -17.335 1.00   49.66  ? 150 PHE C CD2 1 
ATOM   7084  C CE1 . PHE C  1 150 ? 79.365  28.814  -16.537 1.00   48.89  ? 150 PHE C CE1 1 
ATOM   7085  C CE2 . PHE C  1 150 ? 78.345  30.953  -16.283 1.00   46.83  ? 150 PHE C CE2 1 
ATOM   7086  C CZ  . PHE C  1 150 ? 79.280  30.019  -15.887 1.00   46.68  ? 150 PHE C CZ  1 
ATOM   7087  N N   . LEU C  1 151 ? 75.711  27.578  -16.456 1.00   41.89  ? 151 LEU C N   1 
ATOM   7088  C CA  . LEU C  1 151 ? 76.378  26.747  -15.466 1.00   43.38  ? 151 LEU C CA  1 
ATOM   7089  C C   . LEU C  1 151 ? 75.744  25.361  -15.445 1.00   47.30  ? 151 LEU C C   1 
ATOM   7090  O O   . LEU C  1 151 ? 76.422  24.353  -15.223 1.00   47.96  ? 151 LEU C O   1 
ATOM   7091  C CB  . LEU C  1 151 ? 76.327  27.412  -14.081 1.00   39.61  ? 151 LEU C CB  1 
ATOM   7092  C CG  . LEU C  1 151 ? 77.334  26.922  -13.037 1.00   37.68  ? 151 LEU C CG  1 
ATOM   7093  C CD1 . LEU C  1 151 ? 78.750  27.058  -13.534 1.00   35.00  ? 151 LEU C CD1 1 
ATOM   7094  C CD2 . LEU C  1 151 ? 77.156  27.660  -11.724 1.00   35.67  ? 151 LEU C CD2 1 
ATOM   7095  N N   . ALA C  1 152 ? 74.457  25.303  -15.760 1.00   48.51  ? 152 ALA C N   1 
ATOM   7096  C CA  . ALA C  1 152 ? 73.744  24.035  -15.725 1.00   49.07  ? 152 ALA C CA  1 
ATOM   7097  C C   . ALA C  1 152 ? 73.641  23.412  -17.109 1.00   52.36  ? 152 ALA C C   1 
ATOM   7098  O O   . ALA C  1 152 ? 72.984  22.384  -17.293 1.00   53.30  ? 152 ALA C O   1 
ATOM   7099  C CB  . ALA C  1 152 ? 72.365  24.218  -15.135 1.00   47.39  ? 152 ALA C CB  1 
ATOM   7100  N N   . GLN C  1 153 ? 74.289  24.020  -18.091 1.00   50.80  ? 153 GLN C N   1 
ATOM   7101  C CA  . GLN C  1 153 ? 74.107  23.541  -19.443 1.00   49.89  ? 153 GLN C CA  1 
ATOM   7102  C C   . GLN C  1 153 ? 74.927  22.296  -19.746 1.00   49.03  ? 153 GLN C C   1 
ATOM   7103  O O   . GLN C  1 153 ? 74.729  21.656  -20.780 1.00   51.46  ? 153 GLN C O   1 
ATOM   7104  C CB  . GLN C  1 153 ? 74.437  24.627  -20.448 1.00   50.85  ? 153 GLN C CB  1 
ATOM   7105  C CG  . GLN C  1 153 ? 73.296  25.573  -20.647 1.00   52.46  ? 153 GLN C CG  1 
ATOM   7106  C CD  . GLN C  1 153 ? 73.643  26.660  -21.609 1.00   58.33  ? 153 GLN C CD  1 
ATOM   7107  O OE1 . GLN C  1 153 ? 74.803  26.812  -22.008 1.00   61.15  ? 153 GLN C OE1 1 
ATOM   7108  N NE2 . GLN C  1 153 ? 72.641  27.423  -22.009 1.00   61.00  ? 153 GLN C NE2 1 
ATOM   7109  N N   . LYS C  1 154 ? 75.840  21.935  -18.854 1.00   47.66  ? 154 LYS C N   1 
ATOM   7110  C CA  . LYS C  1 154 ? 76.687  20.782  -19.132 1.00   51.35  ? 154 LYS C CA  1 
ATOM   7111  C C   . LYS C  1 154 ? 76.822  19.885  -17.944 1.00   50.12  ? 154 LYS C C   1 
ATOM   7112  O O   . LYS C  1 154 ? 77.034  20.347  -16.846 1.00   47.66  ? 154 LYS C O   1 
ATOM   7113  C CB  . LYS C  1 154 ? 78.090  21.208  -19.599 1.00   54.65  ? 154 LYS C CB  1 
ATOM   7114  C CG  . LYS C  1 154 ? 78.064  21.682  -21.037 1.00   61.48  ? 154 LYS C CG  1 
ATOM   7115  C CD  . LYS C  1 154 ? 79.411  21.828  -21.703 1.00   67.10  ? 154 LYS C CD  1 
ATOM   7116  C CE  . LYS C  1 154 ? 79.218  21.442  -23.182 1.00   74.41  ? 154 LYS C CE  1 
ATOM   7117  N NZ  . LYS C  1 154 ? 80.274  21.852  -24.160 1.00   78.55  ? 154 LYS C NZ  1 
ATOM   7118  N N   . GLY C  1 155 ? 76.702  18.589  -18.192 1.00   55.14  ? 155 GLY C N   1 
ATOM   7119  C CA  . GLY C  1 155 ? 77.046  17.578  -17.211 1.00   57.17  ? 155 GLY C CA  1 
ATOM   7120  C C   . GLY C  1 155 ? 75.956  16.976  -16.336 1.00   57.35  ? 155 GLY C C   1 
ATOM   7121  O O   . GLY C  1 155 ? 76.189  15.952  -15.693 1.00   61.10  ? 155 GLY C O   1 
ATOM   7122  N N   . LEU C  1 156 ? 74.775  17.586  -16.305 1.00   51.55  ? 156 LEU C N   1 
ATOM   7123  C CA  . LEU C  1 156 ? 73.722  17.157  -15.386 1.00   43.91  ? 156 LEU C CA  1 
ATOM   7124  C C   . LEU C  1 156 ? 72.687  16.203  -16.004 1.00   43.15  ? 156 LEU C C   1 
ATOM   7125  O O   . LEU C  1 156 ? 72.575  16.094  -17.233 1.00   44.53  ? 156 LEU C O   1 
ATOM   7126  C CB  . LEU C  1 156 ? 73.024  18.393  -14.809 1.00   42.49  ? 156 LEU C CB  1 
ATOM   7127  C CG  . LEU C  1 156 ? 73.924  19.506  -14.261 1.00   41.38  ? 156 LEU C CG  1 
ATOM   7128  C CD1 . LEU C  1 156 ? 73.075  20.601  -13.645 1.00   43.13  ? 156 LEU C CD1 1 
ATOM   7129  C CD2 . LEU C  1 156 ? 74.931  18.997  -13.250 1.00   39.22  ? 156 LEU C CD2 1 
ATOM   7130  N N   . PRO C  1 157 ? 71.933  15.488  -15.147 1.00   41.11  ? 157 PRO C N   1 
ATOM   7131  C CA  . PRO C  1 157 ? 70.842  14.681  -15.682 1.00   44.64  ? 157 PRO C CA  1 
ATOM   7132  C C   . PRO C  1 157 ? 69.880  15.530  -16.499 1.00   48.81  ? 157 PRO C C   1 
ATOM   7133  O O   . PRO C  1 157 ? 69.841  16.756  -16.378 1.00   47.19  ? 157 PRO C O   1 
ATOM   7134  C CB  . PRO C  1 157 ? 70.157  14.127  -14.433 1.00   42.52  ? 157 PRO C CB  1 
ATOM   7135  C CG  . PRO C  1 157 ? 71.210  14.110  -13.394 1.00   40.41  ? 157 PRO C CG  1 
ATOM   7136  C CD  . PRO C  1 157 ? 72.058  15.323  -13.684 1.00   41.42  ? 157 PRO C CD  1 
ATOM   7137  N N   . ASN C  1 158 ? 69.104  14.864  -17.331 1.00   52.57  ? 158 ASN C N   1 
ATOM   7138  C CA  . ASN C  1 158 ? 68.264  15.549  -18.280 1.00   58.38  ? 158 ASN C CA  1 
ATOM   7139  C C   . ASN C  1 158 ? 67.209  16.434  -17.576 1.00   55.66  ? 158 ASN C C   1 
ATOM   7140  O O   . ASN C  1 158 ? 66.607  16.011  -16.576 1.00   53.13  ? 158 ASN C O   1 
ATOM   7141  C CB  . ASN C  1 158 ? 67.625  14.487  -19.171 1.00   68.27  ? 158 ASN C CB  1 
ATOM   7142  C CG  . ASN C  1 158 ? 66.937  15.067  -20.368 1.00   78.78  ? 158 ASN C CG  1 
ATOM   7143  O OD1 . ASN C  1 158 ? 65.795  15.513  -20.282 1.00   82.58  ? 158 ASN C OD1 1 
ATOM   7144  N ND2 . ASN C  1 158 ? 67.628  15.077  -21.499 1.00   83.38  ? 158 ASN C ND2 1 
ATOM   7145  N N   . ASN C  1 159 ? 67.053  17.671  -18.073 1.00   56.08  ? 159 ASN C N   1 
ATOM   7146  C CA  . ASN C  1 159 ? 66.095  18.679  -17.570 1.00   58.92  ? 159 ASN C CA  1 
ATOM   7147  C C   . ASN C  1 159 ? 66.364  19.235  -16.152 1.00   53.80  ? 159 ASN C C   1 
ATOM   7148  O O   . ASN C  1 159 ? 65.566  20.014  -15.621 1.00   55.03  ? 159 ASN C O   1 
ATOM   7149  C CB  . ASN C  1 159 ? 64.655  18.165  -17.668 1.00   69.98  ? 159 ASN C CB  1 
ATOM   7150  C CG  . ASN C  1 159 ? 64.060  18.338  -19.080 1.00   84.99  ? 159 ASN C CG  1 
ATOM   7151  O OD1 . ASN C  1 159 ? 64.788  18.396  -20.080 1.00   91.04  ? 159 ASN C OD1 1 
ATOM   7152  N ND2 . ASN C  1 159 ? 62.730  18.393  -19.161 1.00   89.45  ? 159 ASN C ND2 1 
ATOM   7153  N N   . VAL C  1 160 ? 67.475  18.832  -15.545 1.00   47.64  ? 160 VAL C N   1 
ATOM   7154  C CA  . VAL C  1 160 ? 67.876  19.346  -14.240 1.00   42.22  ? 160 VAL C CA  1 
ATOM   7155  C C   . VAL C  1 160 ? 68.426  20.766  -14.394 1.00   43.49  ? 160 VAL C C   1 
ATOM   7156  O O   . VAL C  1 160 ? 69.192  21.048  -15.312 1.00   46.59  ? 160 VAL C O   1 
ATOM   7157  C CB  . VAL C  1 160 ? 68.926  18.431  -13.584 1.00   40.62  ? 160 VAL C CB  1 
ATOM   7158  C CG1 . VAL C  1 160 ? 69.675  19.152  -12.484 1.00   38.39  ? 160 VAL C CG1 1 
ATOM   7159  C CG2 . VAL C  1 160 ? 68.255  17.184  -13.040 1.00   40.62  ? 160 VAL C CG2 1 
ATOM   7160  N N   . GLN C  1 161 ? 68.008  21.671  -13.517 1.00   42.23  ? 161 GLN C N   1 
ATOM   7161  C CA  . GLN C  1 161 ? 68.296  23.088  -13.699 1.00   47.40  ? 161 GLN C CA  1 
ATOM   7162  C C   . GLN C  1 161 ? 69.138  23.722  -12.580 1.00   43.66  ? 161 GLN C C   1 
ATOM   7163  O O   . GLN C  1 161 ? 69.169  24.935  -12.433 1.00   41.58  ? 161 GLN C O   1 
ATOM   7164  C CB  . GLN C  1 161 ? 66.989  23.849  -13.822 1.00   54.60  ? 161 GLN C CB  1 
ATOM   7165  C CG  . GLN C  1 161 ? 66.325  23.675  -15.148 1.00   64.58  ? 161 GLN C CG  1 
ATOM   7166  C CD  . GLN C  1 161 ? 64.900  24.077  -15.059 1.00   74.01  ? 161 GLN C CD  1 
ATOM   7167  O OE1 . GLN C  1 161 ? 64.174  23.592  -14.193 1.00   76.63  ? 161 GLN C OE1 1 
ATOM   7168  N NE2 . GLN C  1 161 ? 64.476  24.981  -15.937 1.00   79.11  ? 161 GLN C NE2 1 
ATOM   7169  N N   . GLY C  1 162 ? 69.815  22.906  -11.788 1.00   42.16  ? 162 GLY C N   1 
ATOM   7170  C CA  . GLY C  1 162 ? 70.620  23.434  -10.716 1.00   31.11  ? 162 GLY C CA  1 
ATOM   7171  C C   . GLY C  1 162 ? 70.932  22.319  -9.782  1.00   29.85  ? 162 GLY C C   1 
ATOM   7172  O O   . GLY C  1 162 ? 70.767  21.167  -10.146 1.00   34.78  ? 162 GLY C O   1 
ATOM   7173  N N   . ALA C  1 163 ? 71.337  22.661  -8.568  1.00   28.01  ? 163 ALA C N   1 
ATOM   7174  C CA  . ALA C  1 163 ? 71.731  21.671  -7.586  1.00   28.45  ? 163 ALA C CA  1 
ATOM   7175  C C   . ALA C  1 163 ? 71.285  22.092  -6.227  1.00   27.23  ? 163 ALA C C   1 
ATOM   7176  O O   . ALA C  1 163 ? 71.113  23.254  -5.966  1.00   28.94  ? 163 ALA C O   1 
ATOM   7177  C CB  . ALA C  1 163 ? 73.245  21.465  -7.595  1.00   28.70  ? 163 ALA C CB  1 
ATOM   7178  N N   . LEU C  1 164 ? 71.034  21.128  -5.372  1.00   30.43  ? 164 LEU C N   1 
ATOM   7179  C CA  . LEU C  1 164 ? 70.828  21.449  -3.982  1.00   34.75  ? 164 LEU C CA  1 
ATOM   7180  C C   . LEU C  1 164 ? 72.013  20.963  -3.141  1.00   31.62  ? 164 LEU C C   1 
ATOM   7181  O O   . LEU C  1 164 ? 72.465  19.818  -3.244  1.00   30.50  ? 164 LEU C O   1 
ATOM   7182  C CB  . LEU C  1 164 ? 69.503  20.872  -3.515  1.00   40.81  ? 164 LEU C CB  1 
ATOM   7183  C CG  . LEU C  1 164 ? 69.390  19.370  -3.628  1.00   46.41  ? 164 LEU C CG  1 
ATOM   7184  C CD1 . LEU C  1 164 ? 69.428  18.808  -2.238  1.00   49.93  ? 164 LEU C CD1 1 
ATOM   7185  C CD2 . LEU C  1 164 ? 68.132  18.974  -4.321  1.00   49.21  ? 164 LEU C CD2 1 
ATOM   7186  N N   . GLY C  1 165 ? 72.549  21.847  -2.320  1.00   30.59  ? 165 GLY C N   1 
ATOM   7187  C CA  . GLY C  1 165 ? 73.738  21.497  -1.595  1.00   25.86  ? 165 GLY C CA  1 
ATOM   7188  C C   . GLY C  1 165 ? 73.374  21.171  -0.172  1.00   27.50  ? 165 GLY C C   1 
ATOM   7189  O O   . GLY C  1 165 ? 72.581  21.867  0.461   1.00   25.76  ? 165 GLY C O   1 
ATOM   7190  N N   . LEU C  1 166 ? 73.973  20.102  0.330   1.00   27.42  ? 166 LEU C N   1 
ATOM   7191  C CA  . LEU C  1 166 ? 73.752  19.653  1.694   1.00   27.91  ? 166 LEU C CA  1 
ATOM   7192  C C   . LEU C  1 166 ? 75.057  19.770  2.503   1.00   26.57  ? 166 LEU C C   1 
ATOM   7193  O O   . LEU C  1 166 ? 75.252  19.087  3.504   1.00   25.83  ? 166 LEU C O   1 
ATOM   7194  C CB  . LEU C  1 166 ? 73.239  18.209  1.701   1.00   29.96  ? 166 LEU C CB  1 
ATOM   7195  C CG  . LEU C  1 166 ? 71.910  17.835  1.048   1.00   30.90  ? 166 LEU C CG  1 
ATOM   7196  C CD1 . LEU C  1 166 ? 71.749  16.342  1.104   1.00   35.33  ? 166 LEU C CD1 1 
ATOM   7197  C CD2 . LEU C  1 166 ? 70.763  18.471  1.768   1.00   31.88  ? 166 LEU C CD2 1 
ATOM   7198  N N   . GLY C  1 167 ? 75.939  20.662  2.061   1.00   24.09  ? 167 GLY C N   1 
ATOM   7199  C CA  . GLY C  1 167 ? 77.246  20.828  2.666   1.00   22.48  ? 167 GLY C CA  1 
ATOM   7200  C C   . GLY C  1 167 ? 77.223  21.563  3.988   1.00   24.39  ? 167 GLY C C   1 
ATOM   7201  O O   . GLY C  1 167 ? 76.194  22.056  4.425   1.00   27.38  ? 167 GLY C O   1 
ATOM   7202  N N   . GLN C  1 168 ? 78.377  21.596  4.643   1.00   26.14  ? 168 GLN C N   1 
ATOM   7203  C CA  . GLN C  1 168 ? 78.558  22.309  5.893   1.00   25.46  ? 168 GLN C CA  1 
ATOM   7204  C C   . GLN C  1 168 ? 78.839  23.771  5.581   1.00   25.49  ? 168 GLN C C   1 
ATOM   7205  O O   . GLN C  1 168 ? 79.987  24.172  5.464   1.00   24.63  ? 168 GLN C O   1 
ATOM   7206  C CB  . GLN C  1 168 ? 79.694  21.676  6.695   1.00   25.44  ? 168 GLN C CB  1 
ATOM   7207  C CG  . GLN C  1 168 ? 79.301  20.358  7.279   1.00   24.11  ? 168 GLN C CG  1 
ATOM   7208  C CD  . GLN C  1 168 ? 78.196  20.537  8.274   1.00   28.77  ? 168 GLN C CD  1 
ATOM   7209  O OE1 . GLN C  1 168 ? 78.399  21.164  9.316   1.00   32.88  ? 168 GLN C OE1 1 
ATOM   7210  N NE2 . GLN C  1 168 ? 77.003  20.021  7.958   1.00   26.92  ? 168 GLN C NE2 1 
ATOM   7211  N N   . ALA C  1 169 ? 77.771  24.542  5.401   1.00   27.19  ? 169 ALA C N   1 
ATOM   7212  C CA  . ALA C  1 169 ? 77.846  25.936  4.967   1.00   26.76  ? 169 ALA C CA  1 
ATOM   7213  C C   . ALA C  1 169 ? 76.554  26.586  5.435   1.00   27.55  ? 169 ALA C C   1 
ATOM   7214  O O   . ALA C  1 169 ? 75.556  25.881  5.611   1.00   28.34  ? 169 ALA C O   1 
ATOM   7215  C CB  . ALA C  1 169 ? 78.024  26.046  3.437   1.00   24.39  ? 169 ALA C CB  1 
ATOM   7216  N N   . PRO C  1 170 ? 76.577  27.912  5.690   1.00   28.63  ? 170 PRO C N   1 
ATOM   7217  C CA  . PRO C  1 170 ? 75.499  28.633  6.383   1.00   28.31  ? 170 PRO C CA  1 
ATOM   7218  C C   . PRO C  1 170 ? 74.157  28.648  5.697   1.00   29.45  ? 170 PRO C C   1 
ATOM   7219  O O   . PRO C  1 170 ? 73.185  28.720  6.435   1.00   32.15  ? 170 PRO C O   1 
ATOM   7220  C CB  . PRO C  1 170 ? 76.029  30.065  6.481   1.00   28.94  ? 170 PRO C CB  1 
ATOM   7221  C CG  . PRO C  1 170 ? 77.119  30.157  5.489   1.00   29.74  ? 170 PRO C CG  1 
ATOM   7222  C CD  . PRO C  1 170 ? 77.736  28.789  5.461   1.00   29.79  ? 170 PRO C CD  1 
ATOM   7223  N N   . ILE C  1 171 ? 74.066  28.622  4.369   1.00   25.79  ? 171 ILE C N   1 
ATOM   7224  C CA  . ILE C  1 171 ? 72.739  28.504  3.770   1.00   23.01  ? 171 ILE C CA  1 
ATOM   7225  C C   . ILE C  1 171 ? 72.542  27.199  2.948   1.00   26.81  ? 171 ILE C C   1 
ATOM   7226  O O   . ILE C  1 171 ? 71.808  27.165  1.962   1.00   26.04  ? 171 ILE C O   1 
ATOM   7227  C CB  . ILE C  1 171 ? 72.382  29.752  2.904   1.00   23.50  ? 171 ILE C CB  1 
ATOM   7228  C CG1 . ILE C  1 171 ? 73.410  29.999  1.800   1.00   22.95  ? 171 ILE C CG1 1 
ATOM   7229  C CG2 . ILE C  1 171 ? 72.259  30.985  3.789   1.00   20.81  ? 171 ILE C CG2 1 
ATOM   7230  C CD1 . ILE C  1 171 ? 72.871  30.834  0.629   1.00   23.09  ? 171 ILE C CD1 1 
ATOM   7231  N N   . SER C  1 172 ? 73.166  26.116  3.392   1.00   28.58  ? 172 SER C N   1 
ATOM   7232  C CA  . SER C  1 172 ? 72.891  24.793  2.838   1.00   28.47  ? 172 SER C CA  1 
ATOM   7233  C C   . SER C  1 172 ? 71.436  24.444  3.105   1.00   29.49  ? 172 SER C C   1 
ATOM   7234  O O   . SER C  1 172 ? 70.793  25.060  3.955   1.00   30.22  ? 172 SER C O   1 
ATOM   7235  C CB  . SER C  1 172 ? 73.818  23.752  3.437   1.00   27.23  ? 172 SER C CB  1 
ATOM   7236  O OG  . SER C  1 172 ? 73.643  23.649  4.848   1.00   27.46  ? 172 SER C OG  1 
ATOM   7237  N N   . LEU C  1 173 ? 70.903  23.474  2.374   1.00   28.82  ? 173 LEU C N   1 
ATOM   7238  C CA  . LEU C  1 173 ? 69.493  23.138  2.514   1.00   28.82  ? 173 LEU C CA  1 
ATOM   7239  C C   . LEU C  1 173 ? 69.141  22.661  3.928   1.00   30.38  ? 173 LEU C C   1 
ATOM   7240  O O   . LEU C  1 173 ? 68.143  23.117  4.500   1.00   31.75  ? 173 LEU C O   1 
ATOM   7241  C CB  . LEU C  1 173 ? 69.094  22.091  1.478   1.00   27.64  ? 173 LEU C CB  1 
ATOM   7242  C CG  . LEU C  1 173 ? 67.713  21.465  1.690   1.00   27.24  ? 173 LEU C CG  1 
ATOM   7243  C CD1 . LEU C  1 173 ? 66.603  22.483  1.590   1.00   26.34  ? 173 LEU C CD1 1 
ATOM   7244  C CD2 . LEU C  1 173 ? 67.508  20.379  0.684   1.00   28.04  ? 173 LEU C CD2 1 
ATOM   7245  N N   . GLN C  1 174 ? 69.939  21.749  4.486   1.00   26.24  ? 174 GLN C N   1 
ATOM   7246  C CA  . GLN C  1 174 ? 69.619  21.195  5.790   1.00   25.07  ? 174 GLN C CA  1 
ATOM   7247  C C   . GLN C  1 174 ? 69.777  22.247  6.876   1.00   25.31  ? 174 GLN C C   1 
ATOM   7248  O O   . GLN C  1 174 ? 68.974  22.310  7.802   1.00   25.85  ? 174 GLN C O   1 
ATOM   7249  C CB  . GLN C  1 174 ? 70.471  19.934  6.106   1.00   25.08  ? 174 GLN C CB  1 
ATOM   7250  C CG  . GLN C  1 174 ? 71.895  20.150  6.689   1.00   27.87  ? 174 GLN C CG  1 
ATOM   7251  C CD  . GLN C  1 174 ? 72.922  20.484  5.645   1.00   25.64  ? 174 GLN C CD  1 
ATOM   7252  O OE1 . GLN C  1 174 ? 72.630  20.505  4.447   1.00   26.50  ? 174 GLN C OE1 1 
ATOM   7253  N NE2 . GLN C  1 174 ? 74.123  20.788  6.089   1.00   25.91  ? 174 GLN C NE2 1 
ATOM   7254  N N   . ASN C  1 175 ? 70.795  23.092  6.766   1.00   25.71  ? 175 ASN C N   1 
ATOM   7255  C CA  . ASN C  1 175 ? 71.002  24.088  7.801   1.00   28.82  ? 175 ASN C CA  1 
ATOM   7256  C C   . ASN C  1 175 ? 69.779  24.984  7.868   1.00   28.95  ? 175 ASN C C   1 
ATOM   7257  O O   . ASN C  1 175 ? 69.353  25.322  8.957   1.00   29.10  ? 175 ASN C O   1 
ATOM   7258  C CB  A ASN C  1 175 ? 72.310  24.885  7.570   0.70   31.11  ? 175 ASN C CB  1 
ATOM   7259  C CB  B ASN C  1 175 ? 72.250  24.939  7.543   0.30   30.74  ? 175 ASN C CB  1 
ATOM   7260  C CG  A ASN C  1 175 ? 73.585  24.074  7.949   0.70   41.93  ? 175 ASN C CG  1 
ATOM   7261  C CG  B ASN C  1 175 ? 72.384  26.090  8.531   0.30   31.09  ? 175 ASN C CG  1 
ATOM   7262  O OD1 A ASN C  1 175 ? 73.566  23.240  8.866   0.70   42.56  ? 175 ASN C OD1 1 
ATOM   7263  O OD1 B ASN C  1 175 ? 71.943  25.999  9.672   0.30   30.53  ? 175 ASN C OD1 1 
ATOM   7264  N ND2 A ASN C  1 175 ? 74.681  24.314  7.230   0.70   38.96  ? 175 ASN C ND2 1 
ATOM   7265  N ND2 B ASN C  1 175 ? 72.985  27.178  8.091   0.30   32.51  ? 175 ASN C ND2 1 
ATOM   7266  N N   . GLN C  1 176 ? 69.167  25.314  6.726   1.00   26.92  ? 176 GLN C N   1 
ATOM   7267  C CA  . GLN C  1 176 ? 67.972  26.169  6.726   1.00   24.08  ? 176 GLN C CA  1 
ATOM   7268  C C   . GLN C  1 176 ? 66.694  25.459  7.204   1.00   23.67  ? 176 GLN C C   1 
ATOM   7269  O O   . GLN C  1 176 ? 65.839  26.051  7.862   1.00   23.75  ? 176 GLN C O   1 
ATOM   7270  C CB  . GLN C  1 176 ? 67.741  26.757  5.342   1.00   23.14  ? 176 GLN C CB  1 
ATOM   7271  C CG  . GLN C  1 176 ? 68.760  27.833  4.944   1.00   21.86  ? 176 GLN C CG  1 
ATOM   7272  C CD  . GLN C  1 176 ? 68.359  28.605  3.694   1.00   22.46  ? 176 GLN C CD  1 
ATOM   7273  O OE1 . GLN C  1 176 ? 67.464  29.455  3.735   1.00   26.66  ? 176 GLN C OE1 1 
ATOM   7274  N NE2 . GLN C  1 176 ? 69.009  28.308  2.582   1.00   22.34  ? 176 GLN C NE2 1 
ATOM   7275  N N   . LEU C  1 177 ? 66.558  24.190  6.878   1.00   24.55  ? 177 LEU C N   1 
ATOM   7276  C CA  . LEU C  1 177 ? 65.441  23.411  7.385   1.00   26.39  ? 177 LEU C CA  1 
ATOM   7277  C C   . LEU C  1 177 ? 65.553  23.205  8.905   1.00   27.92  ? 177 LEU C C   1 
ATOM   7278  O O   . LEU C  1 177 ? 64.549  23.318  9.624   1.00   26.06  ? 177 LEU C O   1 
ATOM   7279  C CB  . LEU C  1 177 ? 65.381  22.072  6.645   1.00   26.35  ? 177 LEU C CB  1 
ATOM   7280  C CG  . LEU C  1 177 ? 65.058  22.144  5.146   1.00   25.78  ? 177 LEU C CG  1 
ATOM   7281  C CD1 . LEU C  1 177 ? 65.253  20.786  4.561   1.00   26.88  ? 177 LEU C CD1 1 
ATOM   7282  C CD2 . LEU C  1 177 ? 63.606  22.578  4.877   1.00   25.44  ? 177 LEU C CD2 1 
ATOM   7283  N N   . PHE C  1 178 ? 66.766  22.897  9.383   1.00   27.79  ? 178 PHE C N   1 
ATOM   7284  C CA  . PHE C  1 178 ? 67.025  22.709  10.813  1.00   25.96  ? 178 PHE C CA  1 
ATOM   7285  C C   . PHE C  1 178 ? 66.549  23.920  11.579  1.00   25.46  ? 178 PHE C C   1 
ATOM   7286  O O   . PHE C  1 178 ? 65.814  23.807  12.557  1.00   29.15  ? 178 PHE C O   1 
ATOM   7287  C CB  . PHE C  1 178 ? 68.511  22.494  11.117  1.00   26.94  ? 178 PHE C CB  1 
ATOM   7288  C CG  . PHE C  1 178 ? 69.087  21.209  10.588  1.00   26.55  ? 178 PHE C CG  1 
ATOM   7289  C CD1 . PHE C  1 178 ? 68.276  20.126  10.275  1.00   25.84  ? 178 PHE C CD1 1 
ATOM   7290  C CD2 . PHE C  1 178 ? 70.463  21.080  10.447  1.00   23.13  ? 178 PHE C CD2 1 
ATOM   7291  C CE1 . PHE C  1 178 ? 68.828  18.954  9.794   1.00   25.72  ? 178 PHE C CE1 1 
ATOM   7292  C CE2 . PHE C  1 178 ? 71.017  19.917  9.980   1.00   21.51  ? 178 PHE C CE2 1 
ATOM   7293  C CZ  . PHE C  1 178 ? 70.206  18.852  9.649   1.00   21.84  ? 178 PHE C CZ  1 
ATOM   7294  N N   . SER C  1 179 ? 66.969  25.090  11.121  1.00   24.98  ? 179 SER C N   1 
ATOM   7295  C CA  . SER C  1 179 ? 66.731  26.316  11.870  1.00   27.24  ? 179 SER C CA  1 
ATOM   7296  C C   . SER C  1 179 ? 65.281  26.861  11.750  1.00   30.89  ? 179 SER C C   1 
ATOM   7297  O O   . SER C  1 179 ? 64.755  27.405  12.729  1.00   30.80  ? 179 SER C O   1 
ATOM   7298  C CB  . SER C  1 179 ? 67.758  27.380  11.468  1.00   32.57  ? 179 SER C CB  1 
ATOM   7299  O OG  . SER C  1 179 ? 67.479  27.932  10.210  1.00   39.05  ? 179 SER C OG  1 
ATOM   7300  N N   . HIS C  1 180 ? 64.619  26.684  10.599  1.00   27.90  ? 180 HIS C N   1 
ATOM   7301  C CA  . HIS C  1 180 ? 63.239  27.152  10.451  1.00   27.45  ? 180 HIS C CA  1 
ATOM   7302  C C   . HIS C  1 180 ? 62.306  26.341  11.318  1.00   28.59  ? 180 HIS C C   1 
ATOM   7303  O O   . HIS C  1 180 ? 61.372  26.884  11.902  1.00   31.32  ? 180 HIS C O   1 
ATOM   7304  C CB  . HIS C  1 180 ? 62.769  27.076  8.989   1.00   27.09  ? 180 HIS C CB  1 
ATOM   7305  C CG  . HIS C  1 180 ? 61.422  27.694  8.745   1.00   26.68  ? 180 HIS C CG  1 
ATOM   7306  N ND1 . HIS C  1 180 ? 61.206  29.058  8.749   1.00   27.87  ? 180 HIS C ND1 1 
ATOM   7307  C CD2 . HIS C  1 180 ? 60.217  27.130  8.495   1.00   29.52  ? 180 HIS C CD2 1 
ATOM   7308  C CE1 . HIS C  1 180 ? 59.929  29.302  8.520   1.00   29.12  ? 180 HIS C CE1 1 
ATOM   7309  N NE2 . HIS C  1 180 ? 59.305  28.148  8.358   1.00   31.11  ? 180 HIS C NE2 1 
ATOM   7310  N N   . PHE C  1 181 ? 62.552  25.036  11.398  1.00   29.83  ? 181 PHE C N   1 
ATOM   7311  C CA  . PHE C  1 181 ? 61.609  24.133  12.061  1.00   28.41  ? 181 PHE C CA  1 
ATOM   7312  C C   . PHE C  1 181 ? 62.069  23.678  13.440  1.00   31.98  ? 181 PHE C C   1 
ATOM   7313  O O   . PHE C  1 181 ? 61.313  23.005  14.130  1.00   34.92  ? 181 PHE C O   1 
ATOM   7314  C CB  . PHE C  1 181 ? 61.309  22.905  11.181  1.00   24.49  ? 181 PHE C CB  1 
ATOM   7315  C CG  . PHE C  1 181 ? 60.542  23.232  9.925   1.00   28.03  ? 181 PHE C CG  1 
ATOM   7316  C CD1 . PHE C  1 181 ? 59.183  23.564  9.994   1.00   28.14  ? 181 PHE C CD1 1 
ATOM   7317  C CD2 . PHE C  1 181 ? 61.147  23.173  8.682   1.00   27.63  ? 181 PHE C CD2 1 
ATOM   7318  C CE1 . PHE C  1 181 ? 58.462  23.865  8.848   1.00   30.69  ? 181 PHE C CE1 1 
ATOM   7319  C CE2 . PHE C  1 181 ? 60.427  23.471  7.528   1.00   24.53  ? 181 PHE C CE2 1 
ATOM   7320  C CZ  . PHE C  1 181 ? 59.096  23.819  7.614   1.00   29.47  ? 181 PHE C CZ  1 
ATOM   7321  N N   . GLY C  1 182 ? 63.276  24.065  13.857  1.00   30.15  ? 182 GLY C N   1 
ATOM   7322  C CA  . GLY C  1 182 ? 63.800  23.647  15.146  1.00   26.99  ? 182 GLY C CA  1 
ATOM   7323  C C   . GLY C  1 182 ? 64.101  22.158  15.208  1.00   28.16  ? 182 GLY C C   1 
ATOM   7324  O O   . GLY C  1 182 ? 63.863  21.516  16.231  1.00   26.92  ? 182 GLY C O   1 
ATOM   7325  N N   . LEU C  1 183 ? 64.621  21.604  14.113  1.00   26.93  ? 183 LEU C N   1 
ATOM   7326  C CA  . LEU C  1 183 ? 64.929  20.176  14.044  1.00   26.26  ? 183 LEU C CA  1 
ATOM   7327  C C   . LEU C  1 183 ? 66.254  19.795  14.724  1.00   26.97  ? 183 LEU C C   1 
ATOM   7328  O O   . LEU C  1 183 ? 67.142  20.620  14.894  1.00   26.62  ? 183 LEU C O   1 
ATOM   7329  C CB  . LEU C  1 183 ? 64.996  19.709  12.592  1.00   25.51  ? 183 LEU C CB  1 
ATOM   7330  C CG  . LEU C  1 183 ? 63.812  19.980  11.670  1.00   28.40  ? 183 LEU C CG  1 
ATOM   7331  C CD1 . LEU C  1 183 ? 64.140  19.522  10.256  1.00   28.23  ? 183 LEU C CD1 1 
ATOM   7332  C CD2 . LEU C  1 183 ? 62.581  19.300  12.167  1.00   30.13  ? 183 LEU C CD2 1 
ATOM   7333  N N   . LYS C  1 184 ? 66.387  18.531  15.106  1.00   25.48  ? 184 LYS C N   1 
ATOM   7334  C CA  . LYS C  1 184 ? 67.679  18.015  15.481  1.00   27.12  ? 184 LYS C CA  1 
ATOM   7335  C C   . LYS C  1 184 ? 68.581  18.121  14.267  1.00   26.48  ? 184 LYS C C   1 
ATOM   7336  O O   . LYS C  1 184 ? 68.154  17.906  13.139  1.00   24.66  ? 184 LYS C O   1 
ATOM   7337  C CB  . LYS C  1 184 ? 67.574  16.568  16.009  1.00   32.54  ? 184 LYS C CB  1 
ATOM   7338  C CG  . LYS C  1 184 ? 68.895  15.789  16.084  1.00   39.04  ? 184 LYS C CG  1 
ATOM   7339  C CD  . LYS C  1 184 ? 68.827  14.597  17.023  1.00   46.32  ? 184 LYS C CD  1 
ATOM   7340  C CE  . LYS C  1 184 ? 70.093  13.722  16.991  1.00   51.66  ? 184 LYS C CE  1 
ATOM   7341  N NZ  . LYS C  1 184 ? 71.267  14.267  16.240  1.00   52.30  ? 184 LYS C NZ  1 
ATOM   7342  N N   . ARG C  1 185 ? 69.834  18.468  14.510  1.00   26.52  ? 185 ARG C N   1 
ATOM   7343  C CA  . ARG C  1 185 ? 70.792  18.623  13.445  1.00   25.39  ? 185 ARG C CA  1 
ATOM   7344  C C   . ARG C  1 185 ? 71.321  17.246  13.007  1.00   26.00  ? 185 ARG C C   1 
ATOM   7345  O O   . ARG C  1 185 ? 72.394  16.800  13.394  1.00   25.63  ? 185 ARG C O   1 
ATOM   7346  C CB  . ARG C  1 185 ? 71.921  19.542  13.904  1.00   25.76  ? 185 ARG C CB  1 
ATOM   7347  C CG  . ARG C  1 185 ? 71.434  20.885  14.399  1.00   25.32  ? 185 ARG C CG  1 
ATOM   7348  C CD  . ARG C  1 185 ? 72.591  21.853  14.670  1.00   25.34  ? 185 ARG C CD  1 
ATOM   7349  N NE  . ARG C  1 185 ? 73.170  22.347  13.434  1.00   28.80  ? 185 ARG C NE  1 
ATOM   7350  C CZ  . ARG C  1 185 ? 72.698  23.397  12.754  1.00   31.90  ? 185 ARG C CZ  1 
ATOM   7351  N NH1 . ARG C  1 185 ? 73.275  23.773  11.627  1.00   31.87  ? 185 ARG C NH1 1 
ATOM   7352  N NH2 . ARG C  1 185 ? 71.638  24.064  13.186  1.00   33.13  ? 185 ARG C NH2 1 
ATOM   7353  N N   . GLN C  1 186 ? 70.552  16.597  12.148  1.00   28.68  ? 186 GLN C N   1 
ATOM   7354  C CA  . GLN C  1 186 ? 70.845  15.258  11.692  1.00   27.34  ? 186 GLN C CA  1 
ATOM   7355  C C   . GLN C  1 186 ? 70.132  15.073  10.386  1.00   26.99  ? 186 GLN C C   1 
ATOM   7356  O O   . GLN C  1 186 ? 68.983  15.461  10.272  1.00   28.68  ? 186 GLN C O   1 
ATOM   7357  C CB  . GLN C  1 186 ? 70.362  14.240  12.716  1.00   29.84  ? 186 GLN C CB  1 
ATOM   7358  C CG  . GLN C  1 186 ? 70.619  12.807  12.363  1.00   32.94  ? 186 GLN C CG  1 
ATOM   7359  C CD  . GLN C  1 186 ? 69.850  11.896  13.264  1.00   36.84  ? 186 GLN C CD  1 
ATOM   7360  O OE1 . GLN C  1 186 ? 68.840  11.318  12.872  1.00   37.76  ? 186 GLN C OE1 1 
ATOM   7361  N NE2 . GLN C  1 186 ? 70.307  11.773  14.496  1.00   39.57  ? 186 GLN C NE2 1 
ATOM   7362  N N   . PHE C  1 187 ? 70.784  14.510  9.384   1.00   28.58  ? 187 PHE C N   1 
ATOM   7363  C CA  . PHE C  1 187 ? 70.023  14.099  8.207   1.00   28.37  ? 187 PHE C CA  1 
ATOM   7364  C C   . PHE C  1 187 ? 70.496  12.736  7.715   1.00   30.59  ? 187 PHE C C   1 
ATOM   7365  O O   . PHE C  1 187 ? 71.640  12.343  7.925   1.00   30.06  ? 187 PHE C O   1 
ATOM   7366  C CB  . PHE C  1 187 ? 70.080  15.163  7.088   1.00   26.81  ? 187 PHE C CB  1 
ATOM   7367  C CG  . PHE C  1 187 ? 71.441  15.362  6.480   1.00   28.24  ? 187 PHE C CG  1 
ATOM   7368  C CD1 . PHE C  1 187 ? 72.340  16.262  7.027   1.00   27.34  ? 187 PHE C CD1 1 
ATOM   7369  C CD2 . PHE C  1 187 ? 71.808  14.669  5.346   1.00   29.52  ? 187 PHE C CD2 1 
ATOM   7370  C CE1 . PHE C  1 187 ? 73.583  16.449  6.458   1.00   27.29  ? 187 PHE C CE1 1 
ATOM   7371  C CE2 . PHE C  1 187 ? 73.046  14.858  4.782   1.00   29.47  ? 187 PHE C CE2 1 
ATOM   7372  C CZ  . PHE C  1 187 ? 73.930  15.749  5.334   1.00   27.04  ? 187 PHE C CZ  1 
ATOM   7373  N N   . SER C  1 188 ? 69.594  12.019  7.052   1.00   31.98  ? 188 SER C N   1 
ATOM   7374  C CA  . SER C  1 188 ? 69.833  10.645  6.673   1.00   30.30  ? 188 SER C CA  1 
ATOM   7375  C C   . SER C  1 188 ? 69.630  10.467  5.195   1.00   30.70  ? 188 SER C C   1 
ATOM   7376  O O   . SER C  1 188 ? 68.716  11.021  4.615   1.00   32.19  ? 188 SER C O   1 
ATOM   7377  C CB  . SER C  1 188 ? 68.911  9.715   7.443   1.00   31.36  ? 188 SER C CB  1 
ATOM   7378  O OG  . SER C  1 188 ? 69.116  9.835   8.836   1.00   32.66  ? 188 SER C OG  1 
ATOM   7379  N N   . VAL C  1 189 ? 70.542  9.725   4.595   1.00   29.51  ? 189 VAL C N   1 
ATOM   7380  C CA  . VAL C  1 189 ? 70.550  9.495   3.172   1.00   29.26  ? 189 VAL C CA  1 
ATOM   7381  C C   . VAL C  1 189 ? 70.400  8.018   2.839   1.00   29.66  ? 189 VAL C C   1 
ATOM   7382  O O   . VAL C  1 189 ? 71.201  7.188   3.276   1.00   33.74  ? 189 VAL C O   1 
ATOM   7383  C CB  . VAL C  1 189 ? 71.852  9.996   2.561   1.00   28.08  ? 189 VAL C CB  1 
ATOM   7384  C CG1 . VAL C  1 189 ? 71.819  9.838   1.056   1.00   26.08  ? 189 VAL C CG1 1 
ATOM   7385  C CG2 . VAL C  1 189 ? 72.116  11.443  2.989   1.00   27.51  ? 189 VAL C CG2 1 
ATOM   7386  N N   . CYS C  1 190 ? 69.369  7.687   2.070   1.00   30.33  ? 190 CYS C N   1 
ATOM   7387  C CA  . CYS C  1 190 ? 69.171  6.335   1.557   1.00   30.37  ? 190 CYS C CA  1 
ATOM   7388  C C   . CYS C  1 190 ? 68.888  6.386   0.062   1.00   41.04  ? 190 CYS C C   1 
ATOM   7389  O O   . CYS C  1 190 ? 67.738  6.505   -0.358  1.00   41.45  ? 190 CYS C O   1 
ATOM   7390  C CB  . CYS C  1 190 ? 68.033  5.622   2.297   1.00   31.37  ? 190 CYS C CB  1 
ATOM   7391  S SG  . CYS C  1 190 ? 68.143  3.799   2.333   1.00   41.27  ? 190 CYS C SG  1 
ATOM   7392  N N   . LEU C  1 191 ? 69.934  6.324   -0.745  1.00   39.16  ? 191 LEU C N   1 
ATOM   7393  C CA  . LEU C  1 191 ? 69.758  6.344   -2.188  1.00   38.42  ? 191 LEU C CA  1 
ATOM   7394  C C   . LEU C  1 191 ? 69.298  4.980   -2.746  1.00   43.58  ? 191 LEU C C   1 
ATOM   7395  O O   . LEU C  1 191 ? 69.750  3.909   -2.292  1.00   42.77  ? 191 LEU C O   1 
ATOM   7396  C CB  . LEU C  1 191 ? 71.058  6.762   -2.859  1.00   34.99  ? 191 LEU C CB  1 
ATOM   7397  C CG  . LEU C  1 191 ? 71.647  8.073   -2.351  1.00   32.58  ? 191 LEU C CG  1 
ATOM   7398  C CD1 . LEU C  1 191 ? 72.891  8.431   -3.171  1.00   31.23  ? 191 LEU C CD1 1 
ATOM   7399  C CD2 . LEU C  1 191 ? 70.610  9.214   -2.338  1.00   33.55  ? 191 LEU C CD2 1 
ATOM   7400  N N   . SER C  1 192 ? 68.395  5.022   -3.730  1.00   45.25  ? 192 SER C N   1 
ATOM   7401  C CA  . SER C  1 192 ? 67.931  3.819   -4.424  1.00   44.96  ? 192 SER C CA  1 
ATOM   7402  C C   . SER C  1 192 ? 68.782  3.575   -5.659  1.00   46.74  ? 192 SER C C   1 
ATOM   7403  O O   . SER C  1 192 ? 69.026  4.480   -6.448  1.00   47.64  ? 192 SER C O   1 
ATOM   7404  C CB  . SER C  1 192 ? 66.461  3.944   -4.816  1.00   44.22  ? 192 SER C CB  1 
ATOM   7405  O OG  . SER C  1 192 ? 66.030  2.850   -5.600  1.00   42.79  ? 192 SER C OG  1 
ATOM   7406  N N   . ARG C  1 193 ? 69.225  2.334   -5.793  1.00   41.80  ? 193 ARG C N   1 
ATOM   7407  C CA  . ARG C  1 193 ? 70.060  1.848   -6.875  1.00   45.04  ? 193 ARG C CA  1 
ATOM   7408  C C   . ARG C  1 193 ? 69.364  1.878   -8.220  1.00   47.98  ? 193 ARG C C   1 
ATOM   7409  O O   . ARG C  1 193 ? 70.012  1.929   -9.263  1.00   46.45  ? 193 ARG C O   1 
ATOM   7410  C CB  . ARG C  1 193 ? 70.457  0.409   -6.554  1.00   55.29  ? 193 ARG C CB  1 
ATOM   7411  C CG  . ARG C  1 193 ? 71.441  -0.220  -7.489  1.00   65.49  ? 193 ARG C CG  1 
ATOM   7412  C CD  . ARG C  1 193 ? 71.326  -1.748  -7.529  1.00   75.84  ? 193 ARG C CD  1 
ATOM   7413  N NE  . ARG C  1 193 ? 71.202  -2.421  -6.232  1.00   84.34  ? 193 ARG C NE  1 
ATOM   7414  C CZ  . ARG C  1 193 ? 72.194  -2.633  -5.367  1.00   90.54  ? 193 ARG C CZ  1 
ATOM   7415  N NH1 . ARG C  1 193 ? 73.411  -2.162  -5.612  1.00   91.83  ? 193 ARG C NH1 1 
ATOM   7416  N NH2 . ARG C  1 193 ? 71.954  -3.289  -4.231  1.00   92.43  ? 193 ARG C NH2 1 
ATOM   7417  N N   . TYR C  1 194 ? 68.034  1.845   -8.159  1.00   50.80  ? 194 TYR C N   1 
ATOM   7418  C CA  . TYR C  1 194 ? 67.158  1.648   -9.312  1.00   55.23  ? 194 TYR C CA  1 
ATOM   7419  C C   . TYR C  1 194 ? 66.501  2.936   -9.806  1.00   54.23  ? 194 TYR C C   1 
ATOM   7420  O O   . TYR C  1 194 ? 65.981  3.721   -9.020  1.00   45.99  ? 194 TYR C O   1 
ATOM   7421  C CB  . TYR C  1 194 ? 66.075  0.606   -8.966  1.00   58.76  ? 194 TYR C CB  1 
ATOM   7422  C CG  . TYR C  1 194 ? 66.610  -0.574  -8.177  1.00   60.13  ? 194 TYR C CG  1 
ATOM   7423  C CD1 . TYR C  1 194 ? 67.328  -1.589  -8.803  1.00   64.19  ? 194 TYR C CD1 1 
ATOM   7424  C CD2 . TYR C  1 194 ? 66.407  -0.665  -6.801  1.00   57.78  ? 194 TYR C CD2 1 
ATOM   7425  C CE1 . TYR C  1 194 ? 67.835  -2.667  -8.077  1.00   66.92  ? 194 TYR C CE1 1 
ATOM   7426  C CE2 . TYR C  1 194 ? 66.910  -1.735  -6.066  1.00   60.44  ? 194 TYR C CE2 1 
ATOM   7427  C CZ  . TYR C  1 194 ? 67.625  -2.732  -6.707  1.00   66.91  ? 194 TYR C CZ  1 
ATOM   7428  O OH  . TYR C  1 194 ? 68.121  -3.799  -5.976  1.00   71.29  ? 194 TYR C OH  1 
ATOM   7429  N N   . SER C  1 195 ? 66.478  3.108   -11.121 1.00   57.24  ? 195 SER C N   1 
ATOM   7430  C CA  . SER C  1 195 ? 65.895  4.282   -11.744 1.00   58.34  ? 195 SER C CA  1 
ATOM   7431  C C   . SER C  1 195 ? 64.376  4.324   -11.576 1.00   55.36  ? 195 SER C C   1 
ATOM   7432  O O   . SER C  1 195 ? 63.769  5.389   -11.591 1.00   52.76  ? 195 SER C O   1 
ATOM   7433  C CB  . SER C  1 195 ? 66.259  4.270   -13.236 1.00   66.89  ? 195 SER C CB  1 
ATOM   7434  O OG  . SER C  1 195 ? 66.212  5.556   -13.826 1.00   70.66  ? 195 SER C OG  1 
ATOM   7435  N N   . THR C  1 196 ? 63.782  3.165   -11.326 1.00   55.77  ? 196 THR C N   1 
ATOM   7436  C CA  . THR C  1 196 ? 62.327  3.014   -11.287 1.00   58.28  ? 196 THR C CA  1 
ATOM   7437  C C   . THR C  1 196 ? 61.670  3.201   -9.929  1.00   54.86  ? 196 THR C C   1 
ATOM   7438  O O   . THR C  1 196 ? 60.449  3.131   -9.828  1.00   55.11  ? 196 THR C O   1 
ATOM   7439  C CB  . THR C  1 196 ? 61.921  1.623   -11.794 1.00   64.86  ? 196 THR C CB  1 
ATOM   7440  O OG1 . THR C  1 196 ? 62.446  0.619   -10.910 1.00   66.25  ? 196 THR C OG1 1 
ATOM   7441  C CG2 . THR C  1 196 ? 62.456  1.409   -13.207 1.00   59.08  ? 196 THR C CG2 1 
ATOM   7442  N N   . SER C  1 197 ? 62.463  3.420   -8.887  1.00   52.17  ? 197 SER C N   1 
ATOM   7443  C CA  . SER C  1 197 ? 61.896  3.685   -7.576  1.00   53.81  ? 197 SER C CA  1 
ATOM   7444  C C   . SER C  1 197 ? 62.764  4.665   -6.816  1.00   54.19  ? 197 SER C C   1 
ATOM   7445  O O   . SER C  1 197 ? 63.981  4.724   -7.001  1.00   54.44  ? 197 SER C O   1 
ATOM   7446  C CB  . SER C  1 197 ? 61.700  2.392   -6.774  1.00   57.16  ? 197 SER C CB  1 
ATOM   7447  O OG  . SER C  1 197 ? 62.911  1.697   -6.552  1.00   58.54  ? 197 SER C OG  1 
ATOM   7448  N N   . ASN C  1 198 ? 62.106  5.453   -5.977  1.00   51.43  ? 198 ASN C N   1 
ATOM   7449  C CA  . ASN C  1 198 ? 62.749  6.541   -5.263  1.00   48.64  ? 198 ASN C CA  1 
ATOM   7450  C C   . ASN C  1 198 ? 63.477  6.123   -4.003  1.00   44.23  ? 198 ASN C C   1 
ATOM   7451  O O   . ASN C  1 198 ? 63.098  5.156   -3.353  1.00   39.89  ? 198 ASN C O   1 
ATOM   7452  C CB  . ASN C  1 198 ? 61.706  7.589   -4.883  1.00   47.39  ? 198 ASN C CB  1 
ATOM   7453  C CG  . ASN C  1 198 ? 61.217  8.366   -6.057  1.00   48.51  ? 198 ASN C CG  1 
ATOM   7454  O OD1 . ASN C  1 198 ? 61.851  8.390   -7.101  1.00   49.63  ? 198 ASN C OD1 1 
ATOM   7455  N ND2 . ASN C  1 198 ? 60.046  8.959   -5.918  1.00   49.45  ? 198 ASN C ND2 1 
ATOM   7456  N N   . GLY C  1 199 ? 64.496  6.908   -3.661  1.00   38.27  ? 199 GLY C N   1 
ATOM   7457  C CA  . GLY C  1 199 ? 65.140  6.874   -2.359  1.00   37.26  ? 199 GLY C CA  1 
ATOM   7458  C C   . GLY C  1 199 ? 64.759  8.121   -1.582  1.00   35.59  ? 199 GLY C C   1 
ATOM   7459  O O   . GLY C  1 199 ? 63.901  8.888   -2.014  1.00   38.20  ? 199 GLY C O   1 
ATOM   7460  N N   . ALA C  1 200 ? 65.416  8.376   -0.465  1.00   34.90  ? 200 ALA C N   1 
ATOM   7461  C CA  . ALA C  1 200 ? 64.989  9.501   0.341   1.00   33.80  ? 200 ALA C CA  1 
ATOM   7462  C C   . ALA C  1 200 ? 66.118  10.158  1.076   1.00   31.05  ? 200 ALA C C   1 
ATOM   7463  O O   . ALA C  1 200 ? 67.165  9.559   1.280   1.00   30.55  ? 200 ALA C O   1 
ATOM   7464  C CB  . ALA C  1 200 ? 63.951  9.052   1.333   1.00   30.67  ? 200 ALA C CB  1 
ATOM   7465  N N   . ILE C  1 201 ? 65.886  11.423  1.425   1.00   31.51  ? 201 ILE C N   1 
ATOM   7466  C CA  . ILE C  1 201 ? 66.646  12.147  2.425   1.00   28.91  ? 201 ILE C CA  1 
ATOM   7467  C C   . ILE C  1 201 ? 65.709  12.506  3.555   1.00   27.02  ? 201 ILE C C   1 
ATOM   7468  O O   . ILE C  1 201 ? 64.602  12.985  3.330   1.00   28.84  ? 201 ILE C O   1 
ATOM   7469  C CB  . ILE C  1 201 ? 67.260  13.438  1.905   1.00   32.26  ? 201 ILE C CB  1 
ATOM   7470  C CG1 . ILE C  1 201 ? 67.937  13.213  0.569   1.00   35.07  ? 201 ILE C CG1 1 
ATOM   7471  C CG2 . ILE C  1 201 ? 68.240  13.991  2.928   1.00   30.07  ? 201 ILE C CG2 1 
ATOM   7472  C CD1 . ILE C  1 201 ? 69.186  12.438  0.671   1.00   36.73  ? 201 ILE C CD1 1 
ATOM   7473  N N   . LEU C  1 202 ? 66.162  12.286  4.777   1.00   28.26  ? 202 LEU C N   1 
ATOM   7474  C CA  . LEU C  1 202 ? 65.345  12.559  5.944   1.00   29.15  ? 202 LEU C CA  1 
ATOM   7475  C C   . LEU C  1 202 ? 65.996  13.632  6.780   1.00   27.36  ? 202 LEU C C   1 
ATOM   7476  O O   . LEU C  1 202 ? 67.200  13.591  6.966   1.00   25.61  ? 202 LEU C O   1 
ATOM   7477  C CB  . LEU C  1 202 ? 65.149  11.276  6.768   1.00   31.13  ? 202 LEU C CB  1 
ATOM   7478  C CG  . LEU C  1 202 ? 64.007  10.318  6.379   1.00   33.91  ? 202 LEU C CG  1 
ATOM   7479  C CD1 . LEU C  1 202 ? 64.209  9.671   5.013   1.00   33.69  ? 202 LEU C CD1 1 
ATOM   7480  C CD2 . LEU C  1 202 ? 63.886  9.250   7.410   1.00   34.42  ? 202 LEU C CD2 1 
ATOM   7481  N N   . PHE C  1 203 ? 65.211  14.602  7.252   1.00   28.00  ? 203 PHE C N   1 
ATOM   7482  C CA  . PHE C  1 203 ? 65.730  15.703  8.061   1.00   26.88  ? 203 PHE C CA  1 
ATOM   7483  C C   . PHE C  1 203 ? 65.102  15.695  9.446   1.00   27.47  ? 203 PHE C C   1 
ATOM   7484  O O   . PHE C  1 203 ? 63.884  15.733  9.601   1.00   28.70  ? 203 PHE C O   1 
ATOM   7485  C CB  . PHE C  1 203 ? 65.483  17.052  7.396   1.00   28.99  ? 203 PHE C CB  1 
ATOM   7486  C CG  . PHE C  1 203 ? 66.054  17.155  6.029   1.00   28.46  ? 203 PHE C CG  1 
ATOM   7487  C CD1 . PHE C  1 203 ? 65.334  16.694  4.934   1.00   28.85  ? 203 PHE C CD1 1 
ATOM   7488  C CD2 . PHE C  1 203 ? 67.305  17.718  5.834   1.00   28.96  ? 203 PHE C CD2 1 
ATOM   7489  C CE1 . PHE C  1 203 ? 65.851  16.764  3.667   1.00   30.08  ? 203 PHE C CE1 1 
ATOM   7490  C CE2 . PHE C  1 203 ? 67.835  17.806  4.566   1.00   29.30  ? 203 PHE C CE2 1 
ATOM   7491  C CZ  . PHE C  1 203 ? 67.105  17.323  3.479   1.00   30.93  ? 203 PHE C CZ  1 
ATOM   7492  N N   . GLY C  1 204 ? 65.951  15.620  10.459  1.00   28.13  ? 204 GLY C N   1 
ATOM   7493  C CA  . GLY C  1 204 ? 65.481  15.554  11.821  1.00   28.86  ? 204 GLY C CA  1 
ATOM   7494  C C   . GLY C  1 204 ? 65.919  14.259  12.435  1.00   30.03  ? 204 GLY C C   1 
ATOM   7495  O O   . GLY C  1 204 ? 66.589  13.459  11.789  1.00   28.69  ? 204 GLY C O   1 
ATOM   7496  N N   . ASP C  1 205 ? 65.529  14.063  13.689  1.00   34.82  ? 205 ASP C N   1 
ATOM   7497  C CA  . ASP C  1 205 ? 65.928  12.895  14.466  1.00   38.51  ? 205 ASP C CA  1 
ATOM   7498  C C   . ASP C  1 205 ? 65.153  11.655  14.077  1.00   38.42  ? 205 ASP C C   1 
ATOM   7499  O O   . ASP C  1 205 ? 63.944  11.582  14.279  1.00   38.96  ? 205 ASP C O   1 
ATOM   7500  C CB  . ASP C  1 205 ? 65.727  13.156  15.951  1.00   43.15  ? 205 ASP C CB  1 
ATOM   7501  C CG  . ASP C  1 205 ? 66.357  12.087  16.829  1.00   45.91  ? 205 ASP C CG  1 
ATOM   7502  O OD1 . ASP C  1 205 ? 67.077  11.187  16.322  1.00   44.21  ? 205 ASP C OD1 1 
ATOM   7503  O OD2 . ASP C  1 205 ? 66.110  12.156  18.041  1.00   49.10  1 205 ASP C OD2 1 
ATOM   7504  N N   . ILE C  1 206 ? 65.845  10.614  13.672  1.00   38.34  ? 206 ILE C N   1 
ATOM   7505  C CA  . ILE C  1 206 ? 65.102  9.452   13.263  1.00   42.95  ? 206 ILE C CA  1 
ATOM   7506  C C   . ILE C  1 206 ? 64.771  8.588   14.461  1.00   48.00  ? 206 ILE C C   1 
ATOM   7507  O O   . ILE C  1 206 ? 64.034  7.638   14.354  1.00   52.72  ? 206 ILE C O   1 
ATOM   7508  C CB  . ILE C  1 206 ? 65.919  8.652   12.267  1.00   42.66  ? 206 ILE C CB  1 
ATOM   7509  C CG1 . ILE C  1 206 ? 67.328  8.529   12.811  1.00   44.80  ? 206 ILE C CG1 1 
ATOM   7510  C CG2 . ILE C  1 206 ? 66.017  9.372   10.947  1.00   43.05  ? 206 ILE C CG2 1 
ATOM   7511  C CD1 . ILE C  1 206 ? 68.218  7.770   11.911  1.00   47.18  ? 206 ILE C CD1 1 
ATOM   7512  N N   . ASN C  1 207 ? 65.235  8.993   15.626  1.00   50.34  ? 207 ASN C N   1 
ATOM   7513  C CA  . ASN C  1 207 ? 65.052  8.210   16.835  1.00   54.15  ? 207 ASN C CA  1 
ATOM   7514  C C   . ASN C  1 207 ? 64.093  8.863   17.802  1.00   54.95  ? 207 ASN C C   1 
ATOM   7515  O O   . ASN C  1 207 ? 64.161  8.645   19.007  1.00   57.09  ? 207 ASN C O   1 
ATOM   7516  C CB  . ASN C  1 207 ? 66.405  7.963   17.491  1.00   61.41  ? 207 ASN C CB  1 
ATOM   7517  C CG  . ASN C  1 207 ? 67.331  7.146   16.603  1.00   66.81  ? 207 ASN C CG  1 
ATOM   7518  O OD1 . ASN C  1 207 ? 66.941  6.092   16.089  1.00   71.23  ? 207 ASN C OD1 1 
ATOM   7519  N ND2 . ASN C  1 207 ? 68.546  7.649   16.379  1.00   65.77  ? 207 ASN C ND2 1 
ATOM   7520  N N   . ASP C  1 208 ? 63.163  9.625   17.252  1.00   55.12  ? 208 ASP C N   1 
ATOM   7521  C CA  . ASP C  1 208 ? 62.192  10.378  18.033  1.00   59.24  ? 208 ASP C CA  1 
ATOM   7522  C C   . ASP C  1 208 ? 60.862  9.655   18.032  1.00   63.96  ? 208 ASP C C   1 
ATOM   7523  O O   . ASP C  1 208 ? 60.267  9.468   16.972  1.00   66.77  ? 208 ASP C O   1 
ATOM   7524  C CB  . ASP C  1 208 ? 62.036  11.803  17.465  1.00   57.25  ? 208 ASP C CB  1 
ATOM   7525  C CG  . ASP C  1 208 ? 61.038  12.683  18.254  1.00   59.34  ? 208 ASP C CG  1 
ATOM   7526  O OD1 . ASP C  1 208 ? 60.268  12.201  19.114  1.00   62.61  ? 208 ASP C OD1 1 
ATOM   7527  O OD2 . ASP C  1 208 ? 61.026  13.901  18.006  1.00   59.18  ? 208 ASP C OD2 1 
ATOM   7528  N N   . PRO C  1 209 ? 60.439  9.168   19.220  1.00   65.21  ? 209 PRO C N   1 
ATOM   7529  C CA  . PRO C  1 209 ? 59.163  8.474   19.444  1.00   66.37  ? 209 PRO C CA  1 
ATOM   7530  C C   . PRO C  1 209 ? 57.980  9.187   18.768  1.00   66.35  ? 209 PRO C C   1 
ATOM   7531  O O   . PRO C  1 209 ? 56.988  8.544   18.441  1.00   71.02  ? 209 PRO C O   1 
ATOM   7532  C CB  . PRO C  1 209 ? 59.013  8.489   20.971  1.00   68.76  ? 209 PRO C CB  1 
ATOM   7533  C CG  . PRO C  1 209 ? 60.388  8.696   21.518  1.00   67.21  ? 209 PRO C CG  1 
ATOM   7534  C CD  . PRO C  1 209 ? 61.316  9.097   20.405  1.00   64.36  ? 209 PRO C CD  1 
ATOM   7535  N N   . ASN C  1 210 ? 58.053  10.502  18.601  1.00   62.28  ? 210 ASN C N   1 
ATOM   7536  C CA  . ASN C  1 210 ? 57.002  11.174  17.865  1.00   63.60  ? 210 ASN C CA  1 
ATOM   7537  C C   . ASN C  1 210 ? 57.016  10.704  16.427  1.00   63.15  ? 210 ASN C C   1 
ATOM   7538  O O   . ASN C  1 210 ? 55.967  10.499  15.817  1.00   65.98  ? 210 ASN C O   1 
ATOM   7539  C CB  . ASN C  1 210 ? 57.177  12.696  17.901  1.00   64.79  ? 210 ASN C CB  1 
ATOM   7540  C CG  . ASN C  1 210 ? 56.907  13.289  19.267  1.00   71.92  ? 210 ASN C CG  1 
ATOM   7541  O OD1 . ASN C  1 210 ? 55.902  13.974  19.466  1.00   74.89  ? 210 ASN C OD1 1 
ATOM   7542  N ND2 . ASN C  1 210 ? 57.812  13.054  20.208  1.00   74.50  ? 210 ASN C ND2 1 
ATOM   7543  N N   . ASN C  1 211 ? 58.208  10.392  15.933  1.00   62.25  ? 211 ASN C N   1 
ATOM   7544  C CA  . ASN C  1 211 ? 58.370  10.019  14.535  1.00   62.21  ? 211 ASN C CA  1 
ATOM   7545  C C   . ASN C  1 211 ? 58.368  8.528   14.415  1.00   63.98  ? 211 ASN C C   1 
ATOM   7546  O O   . ASN C  1 211 ? 58.621  7.992   13.340  1.00   64.44  ? 211 ASN C O   1 
ATOM   7547  C CB  . ASN C  1 211 ? 59.700  10.524  13.952  1.00   59.98  ? 211 ASN C CB  1 
ATOM   7548  C CG  . ASN C  1 211 ? 59.878  12.024  14.062  1.00   60.72  ? 211 ASN C CG  1 
ATOM   7549  O OD1 . ASN C  1 211 ? 58.927  12.808  13.915  1.00   60.69  ? 211 ASN C OD1 1 
ATOM   7550  N ND2 . ASN C  1 211 ? 61.128  12.440  14.279  1.00   58.92  ? 211 ASN C ND2 1 
ATOM   7551  N N   . ASN C  1 212 ? 58.013  7.863   15.504  1.00   65.53  ? 212 ASN C N   1 
ATOM   7552  C CA  . ASN C  1 212 ? 58.156  6.425   15.569  1.00   66.14  ? 212 ASN C CA  1 
ATOM   7553  C C   . ASN C  1 212 ? 57.198  5.786   14.584  1.00   62.71  ? 212 ASN C C   1 
ATOM   7554  O O   . ASN C  1 212 ? 57.428  4.687   14.098  1.00   61.99  ? 212 ASN C O   1 
ATOM   7555  C CB  . ASN C  1 212 ? 57.893  5.932   16.995  1.00   72.63  ? 212 ASN C CB  1 
ATOM   7556  C CG  . ASN C  1 212 ? 58.462  4.549   17.258  1.00   76.19  ? 212 ASN C CG  1 
ATOM   7557  O OD1 . ASN C  1 212 ? 59.651  4.310   17.053  1.00   73.48  ? 212 ASN C OD1 1 
ATOM   7558  N ND2 . ASN C  1 212 ? 57.610  3.627   17.709  1.00   81.82  ? 212 ASN C ND2 1 
ATOM   7559  N N   . ASN C  1 213 ? 56.149  6.509   14.237  1.00   60.60  ? 213 ASN C N   1 
ATOM   7560  C CA  . ASN C  1 213 ? 55.180  5.922   13.364  1.00   60.24  ? 213 ASN C CA  1 
ATOM   7561  C C   . ASN C  1 213 ? 55.755  5.832   11.966  1.00   53.20  ? 213 ASN C C   1 
ATOM   7562  O O   . ASN C  1 213 ? 55.574  4.829   11.298  1.00   53.68  ? 213 ASN C O   1 
ATOM   7563  C CB  . ASN C  1 213 ? 53.903  6.755   13.365  1.00   66.91  ? 213 ASN C CB  1 
ATOM   7564  C CG  . ASN C  1 213 ? 53.137  6.656   14.672  1.00   74.88  ? 213 ASN C CG  1 
ATOM   7565  O OD1 . ASN C  1 213 ? 53.024  5.584   15.264  1.00   79.85  ? 213 ASN C OD1 1 
ATOM   7566  N ND2 . ASN C  1 213 ? 52.619  7.787   15.136  1.00   76.70  ? 213 ASN C ND2 1 
ATOM   7567  N N   . TYR C  1 214 ? 56.494  6.853   11.544  1.00   47.05  ? 214 TYR C N   1 
ATOM   7568  C CA  . TYR C  1 214 ? 57.067  6.877   10.195  1.00   44.11  ? 214 TYR C CA  1 
ATOM   7569  C C   . TYR C  1 214 ? 58.307  6.004   9.983   1.00   45.13  ? 214 TYR C C   1 
ATOM   7570  O O   . TYR C  1 214 ? 58.533  5.455   8.898   1.00   46.30  ? 214 TYR C O   1 
ATOM   7571  C CB  . TYR C  1 214 ? 57.406  8.307   9.785   1.00   39.59  ? 214 TYR C CB  1 
ATOM   7572  C CG  . TYR C  1 214 ? 57.776  8.411   8.323   1.00   36.54  ? 214 TYR C CG  1 
ATOM   7573  C CD1 . TYR C  1 214 ? 56.788  8.396   7.351   1.00   37.21  ? 214 TYR C CD1 1 
ATOM   7574  C CD2 . TYR C  1 214 ? 59.110  8.501   7.910   1.00   36.15  ? 214 TYR C CD2 1 
ATOM   7575  C CE1 . TYR C  1 214 ? 57.103  8.468   6.018   1.00   37.11  ? 214 TYR C CE1 1 
ATOM   7576  C CE2 . TYR C  1 214 ? 59.442  8.580   6.563   1.00   33.51  ? 214 TYR C CE2 1 
ATOM   7577  C CZ  . TYR C  1 214 ? 58.428  8.569   5.627   1.00   37.15  ? 214 TYR C CZ  1 
ATOM   7578  O OH  . TYR C  1 214 ? 58.715  8.639   4.286   1.00   38.55  ? 214 TYR C OH  1 
ATOM   7579  N N   . ILE C  1 215 ? 59.133  5.900   11.012  1.00   44.15  ? 215 ILE C N   1 
ATOM   7580  C CA  . ILE C  1 215 ? 60.394  5.192   10.883  1.00   42.91  ? 215 ILE C CA  1 
ATOM   7581  C C   . ILE C  1 215 ? 60.262  3.774   11.386  1.00   44.77  ? 215 ILE C C   1 
ATOM   7582  O O   . ILE C  1 215 ? 61.219  3.040   11.455  1.00   44.68  ? 215 ILE C O   1 
ATOM   7583  C CB  . ILE C  1 215 ? 61.504  5.920   11.653  1.00   40.01  ? 215 ILE C CB  1 
ATOM   7584  C CG1 . ILE C  1 215 ? 61.088  6.114   13.106  1.00   44.17  ? 215 ILE C CG1 1 
ATOM   7585  C CG2 . ILE C  1 215 ? 61.751  7.281   11.043  1.00   35.64  ? 215 ILE C CG2 1 
ATOM   7586  C CD1 . ILE C  1 215 ? 61.676  5.140   14.049  1.00   46.75  ? 215 ILE C CD1 1 
ATOM   7587  N N   . HIS C  1 216 ? 59.047  3.390   11.711  1.00   51.02  ? 216 HIS C N   1 
ATOM   7588  C CA  . HIS C  1 216 ? 58.819  2.107   12.331  1.00   57.88  ? 216 HIS C CA  1 
ATOM   7589  C C   . HIS C  1 216 ? 59.360  0.967   11.485  1.00   57.15  ? 216 HIS C C   1 
ATOM   7590  O O   . HIS C  1 216 ? 59.909  0.002   12.014  1.00   54.79  ? 216 HIS C O   1 
ATOM   7591  C CB  . HIS C  1 216 ? 57.334  1.883   12.584  1.00   64.88  ? 216 HIS C CB  1 
ATOM   7592  C CG  . HIS C  1 216 ? 57.052  0.637   13.359  1.00   72.26  ? 216 HIS C CG  1 
ATOM   7593  N ND1 . HIS C  1 216 ? 56.781  -0.571  12.755  1.00   76.47  ? 216 HIS C ND1 1 
ATOM   7594  C CD2 . HIS C  1 216 ? 57.011  0.411   14.694  1.00   76.52  ? 216 HIS C CD2 1 
ATOM   7595  C CE1 . HIS C  1 216 ? 56.586  -1.490  13.686  1.00   81.66  ? 216 HIS C CE1 1 
ATOM   7596  N NE2 . HIS C  1 216 ? 56.715  -0.918  14.870  1.00   81.86  ? 216 HIS C NE2 1 
ATOM   7597  N N   . ASN C  1 217 ? 59.205  1.075   10.172  1.00   59.57  ? 217 ASN C N   1 
ATOM   7598  C CA  . ASN C  1 217 ? 59.681  0.022   9.289   1.00   63.80  ? 217 ASN C CA  1 
ATOM   7599  C C   . ASN C  1 217 ? 61.209  -0.069  9.229   1.00   60.58  ? 217 ASN C C   1 
ATOM   7600  O O   . ASN C  1 217 ? 61.763  -1.057  8.739   1.00   62.40  ? 217 ASN C O   1 
ATOM   7601  C CB  . ASN C  1 217 ? 59.129  0.216   7.880   1.00   68.33  ? 217 ASN C CB  1 
ATOM   7602  C CG  . ASN C  1 217 ? 59.548  -0.895  6.939   1.00   71.73  ? 217 ASN C CG  1 
ATOM   7603  O OD1 . ASN C  1 217 ? 59.111  -2.045  7.072   1.00   73.97  ? 217 ASN C OD1 1 
ATOM   7604  N ND2 . ASN C  1 217 ? 60.459  -0.571  6.023   1.00   71.97  ? 217 ASN C ND2 1 
ATOM   7605  N N   . SER C  1 218 ? 61.902  0.947   9.724   1.00   53.27  ? 218 SER C N   1 
ATOM   7606  C CA  . SER C  1 218 ? 63.353  0.902   9.681   1.00   44.17  ? 218 SER C CA  1 
ATOM   7607  C C   . SER C  1 218 ? 64.002  0.596   11.028  1.00   42.41  ? 218 SER C C   1 
ATOM   7608  O O   . SER C  1 218 ? 65.201  0.662   11.145  1.00   41.70  ? 218 SER C O   1 
ATOM   7609  C CB  . SER C  1 218 ? 63.896  2.209   9.172   1.00   38.86  ? 218 SER C CB  1 
ATOM   7610  O OG  . SER C  1 218 ? 63.869  3.133   10.224  1.00   38.67  ? 218 SER C OG  1 
ATOM   7611  N N   . LEU C  1 219 ? 63.223  0.260   12.045  1.00   44.72  ? 219 LEU C N   1 
ATOM   7612  C CA  . LEU C  1 219 ? 63.762  0.145   13.400  1.00   45.03  ? 219 LEU C CA  1 
ATOM   7613  C C   . LEU C  1 219 ? 64.829  -0.948  13.582  1.00   46.07  ? 219 LEU C C   1 
ATOM   7614  O O   . LEU C  1 219 ? 65.699  -0.808  14.445  1.00   43.86  ? 219 LEU C O   1 
ATOM   7615  C CB  . LEU C  1 219 ? 62.626  -0.074  14.400  1.00   49.92  ? 219 LEU C CB  1 
ATOM   7616  C CG  . LEU C  1 219 ? 61.869  1.203   14.783  1.00   48.64  ? 219 LEU C CG  1 
ATOM   7617  C CD1 . LEU C  1 219 ? 60.695  0.886   15.670  1.00   50.86  ? 219 LEU C CD1 1 
ATOM   7618  C CD2 . LEU C  1 219 ? 62.812  2.153   15.467  1.00   45.17  ? 219 LEU C CD2 1 
ATOM   7619  N N   . ASP C  1 220 ? 64.768  -2.045  12.827  1.00   47.29  ? 220 ASP C N   1 
ATOM   7620  C CA  . ASP C  1 220 ? 65.812  -3.052  12.979  1.00   51.23  ? 220 ASP C CA  1 
ATOM   7621  C C   . ASP C  1 220 ? 67.131  -2.559  12.454  1.00   44.75  ? 220 ASP C C   1 
ATOM   7622  O O   . ASP C  1 220 ? 68.181  -2.786  13.064  1.00   44.39  ? 220 ASP C O   1 
ATOM   7623  C CB  . ASP C  1 220 ? 65.496  -4.341  12.231  1.00   61.26  ? 220 ASP C CB  1 
ATOM   7624  C CG  . ASP C  1 220 ? 64.328  -5.066  12.784  1.00   71.86  ? 220 ASP C CG  1 
ATOM   7625  O OD1 . ASP C  1 220 ? 64.199  -5.146  14.024  1.00   76.03  ? 220 ASP C OD1 1 
ATOM   7626  O OD2 . ASP C  1 220 ? 63.546  -5.575  11.963  1.00   75.37  ? 220 ASP C OD2 1 
ATOM   7627  N N   . VAL C  1 221 ? 67.067  -1.873  11.321  1.00   39.31  ? 221 VAL C N   1 
ATOM   7628  C CA  . VAL C  1 221 ? 68.253  -1.335  10.693  1.00   37.15  ? 221 VAL C CA  1 
ATOM   7629  C C   . VAL C  1 221 ? 68.912  -0.353  11.614  1.00   39.94  ? 221 VAL C C   1 
ATOM   7630  O O   . VAL C  1 221 ? 70.126  -0.320  11.716  1.00   42.10  ? 221 VAL C O   1 
ATOM   7631  C CB  . VAL C  1 221 ? 67.934  -0.682  9.341   1.00   36.56  ? 221 VAL C CB  1 
ATOM   7632  C CG1 . VAL C  1 221 ? 69.179  -0.076  8.706   1.00   29.15  ? 221 VAL C CG1 1 
ATOM   7633  C CG2 . VAL C  1 221 ? 67.293  -1.716  8.421   1.00   38.90  ? 221 VAL C CG2 1 
ATOM   7634  N N   . LEU C  1 222 ? 68.108  0.472   12.263  1.00   41.79  ? 222 LEU C N   1 
ATOM   7635  C CA  . LEU C  1 222 ? 68.628  1.488   13.168  1.00   40.01  ? 222 LEU C CA  1 
ATOM   7636  C C   . LEU C  1 222 ? 69.341  0.896   14.377  1.00   43.95  ? 222 LEU C C   1 
ATOM   7637  O O   . LEU C  1 222 ? 70.351  1.444   14.829  1.00   42.57  ? 222 LEU C O   1 
ATOM   7638  C CB  . LEU C  1 222 ? 67.503  2.398   13.652  1.00   38.99  ? 222 LEU C CB  1 
ATOM   7639  C CG  . LEU C  1 222 ? 66.814  3.260   12.608  1.00   35.33  ? 222 LEU C CG  1 
ATOM   7640  C CD1 . LEU C  1 222 ? 65.804  4.169   13.299  1.00   34.96  ? 222 LEU C CD1 1 
ATOM   7641  C CD2 . LEU C  1 222 ? 67.829  4.044   11.817  1.00   32.17  ? 222 LEU C CD2 1 
ATOM   7642  N N   . HIS C  1 223 ? 68.827  -0.231  14.873  1.00   48.89  ? 223 HIS C N   1 
ATOM   7643  C CA  . HIS C  1 223 ? 69.364  -0.925  16.043  1.00   56.42  ? 223 HIS C CA  1 
ATOM   7644  C C   . HIS C  1 223 ? 70.816  -1.336  15.799  1.00   54.50  ? 223 HIS C C   1 
ATOM   7645  O O   . HIS C  1 223 ? 71.627  -1.378  16.720  1.00   56.42  ? 223 HIS C O   1 
ATOM   7646  C CB  . HIS C  1 223 ? 68.485  -2.157  16.351  1.00   66.08  ? 223 HIS C CB  1 
ATOM   7647  C CG  . HIS C  1 223 ? 68.891  -2.954  17.565  1.00   73.68  ? 223 HIS C CG  1 
ATOM   7648  N ND1 . HIS C  1 223 ? 68.684  -2.519  18.859  1.00   76.38  ? 223 HIS C ND1 1 
ATOM   7649  C CD2 . HIS C  1 223 ? 69.476  -4.176  17.674  1.00   76.26  ? 223 HIS C CD2 1 
ATOM   7650  C CE1 . HIS C  1 223 ? 69.122  -3.433  19.709  1.00   78.59  ? 223 HIS C CE1 1 
ATOM   7651  N NE2 . HIS C  1 223 ? 69.611  -4.446  19.015  1.00   78.44  ? 223 HIS C NE2 1 
ATOM   7652  N N   . ASP C  1 224 ? 71.134  -1.609  14.539  1.00   50.87  ? 224 ASP C N   1 
ATOM   7653  C CA  . ASP C  1 224 ? 72.428  -2.152  14.148  1.00   48.73  ? 224 ASP C CA  1 
ATOM   7654  C C   . ASP C  1 224 ? 73.377  -1.132  13.506  1.00   42.36  ? 224 ASP C C   1 
ATOM   7655  O O   . ASP C  1 224 ? 74.378  -1.516  12.926  1.00   41.16  ? 224 ASP C O   1 
ATOM   7656  C CB  . ASP C  1 224 ? 72.213  -3.313  13.176  1.00   52.47  ? 224 ASP C CB  1 
ATOM   7657  C CG  . ASP C  1 224 ? 71.464  -4.481  13.798  1.00   55.42  ? 224 ASP C CG  1 
ATOM   7658  O OD1 . ASP C  1 224 ? 71.525  -4.671  15.036  1.00   54.77  ? 224 ASP C OD1 1 
ATOM   7659  O OD2 . ASP C  1 224 ? 70.779  -5.190  13.033  1.00   56.03  1 224 ASP C OD2 1 
ATOM   7660  N N   . LEU C  1 225 ? 73.053  0.154   13.573  1.00   37.33  ? 225 LEU C N   1 
ATOM   7661  C CA  . LEU C  1 225 ? 73.930  1.153   12.995  1.00   33.77  ? 225 LEU C CA  1 
ATOM   7662  C C   . LEU C  1 225 ? 75.316  1.144   13.633  1.00   33.88  ? 225 LEU C C   1 
ATOM   7663  O O   . LEU C  1 225 ? 75.473  1.000   14.841  1.00   33.17  ? 225 LEU C O   1 
ATOM   7664  C CB  . LEU C  1 225 ? 73.331  2.556   13.114  1.00   32.66  ? 225 LEU C CB  1 
ATOM   7665  C CG  . LEU C  1 225 ? 72.209  3.014   12.183  1.00   31.14  ? 225 LEU C CG  1 
ATOM   7666  C CD1 . LEU C  1 225 ? 72.031  4.516   12.319  1.00   32.04  ? 225 LEU C CD1 1 
ATOM   7667  C CD2 . LEU C  1 225 ? 72.488  2.653   10.754  1.00   28.56  ? 225 LEU C CD2 1 
ATOM   7668  N N   . VAL C  1 226 ? 76.313  1.332   12.783  1.00   33.71  ? 226 VAL C N   1 
ATOM   7669  C CA  . VAL C  1 226 ? 77.693  1.427   13.180  1.00   32.62  ? 226 VAL C CA  1 
ATOM   7670  C C   . VAL C  1 226 ? 78.154  2.842   12.866  1.00   31.46  ? 226 VAL C C   1 
ATOM   7671  O O   . VAL C  1 226 ? 77.798  3.386   11.825  1.00   30.09  ? 226 VAL C O   1 
ATOM   7672  C CB  . VAL C  1 226 ? 78.536  0.374   12.430  1.00   32.82  ? 226 VAL C CB  1 
ATOM   7673  C CG1 . VAL C  1 226 ? 79.994  0.702   12.463  1.00   36.01  ? 226 VAL C CG1 1 
ATOM   7674  C CG2 . VAL C  1 226 ? 78.324  -0.939  13.045  1.00   36.63  ? 226 VAL C CG2 1 
ATOM   7675  N N   . TYR C  1 227 ? 78.935  3.439   13.760  1.00   33.16  ? 227 TYR C N   1 
ATOM   7676  C CA  . TYR C  1 227 ? 79.353  4.840   13.592  1.00   35.18  ? 227 TYR C CA  1 
ATOM   7677  C C   . TYR C  1 227 ? 80.856  5.054   13.457  1.00   32.04  ? 227 TYR C C   1 
ATOM   7678  O O   . TYR C  1 227 ? 81.652  4.273   13.988  1.00   32.20  ? 227 TYR C O   1 
ATOM   7679  C CB  . TYR C  1 227 ? 78.869  5.661   14.765  1.00   38.95  ? 227 TYR C CB  1 
ATOM   7680  C CG  . TYR C  1 227 ? 77.381  5.708   14.863  1.00   40.48  ? 227 TYR C CG  1 
ATOM   7681  C CD1 . TYR C  1 227 ? 76.648  6.634   14.140  1.00   40.59  ? 227 TYR C CD1 1 
ATOM   7682  C CD2 . TYR C  1 227 ? 76.707  4.810   15.673  1.00   45.26  ? 227 TYR C CD2 1 
ATOM   7683  C CE1 . TYR C  1 227 ? 75.280  6.683   14.241  1.00   44.25  ? 227 TYR C CE1 1 
ATOM   7684  C CE2 . TYR C  1 227 ? 75.351  4.842   15.779  1.00   48.09  ? 227 TYR C CE2 1 
ATOM   7685  C CZ  . TYR C  1 227 ? 74.642  5.775   15.063  1.00   49.04  ? 227 TYR C CZ  1 
ATOM   7686  O OH  . TYR C  1 227 ? 73.283  5.788   15.181  1.00   53.44  ? 227 TYR C OH  1 
ATOM   7687  N N   . THR C  1 228 ? 81.229  6.136   12.781  1.00   26.86  ? 228 THR C N   1 
ATOM   7688  C CA  . THR C  1 228 ? 82.626  6.518   12.653  1.00   27.92  ? 228 THR C CA  1 
ATOM   7689  C C   . THR C  1 228 ? 82.710  8.050   12.701  1.00   26.37  ? 228 THR C C   1 
ATOM   7690  O O   . THR C  1 228 ? 81.777  8.737   12.297  1.00   27.73  ? 228 THR C O   1 
ATOM   7691  C CB  . THR C  1 228 ? 83.233  5.961   11.346  1.00   27.28  ? 228 THR C CB  1 
ATOM   7692  O OG1 . THR C  1 228 ? 84.660  6.109   11.358  1.00   30.71  ? 228 THR C OG1 1 
ATOM   7693  C CG2 . THR C  1 228 ? 82.664  6.671   10.155  1.00   24.81  ? 228 THR C CG2 1 
ATOM   7694  N N   . PRO C  1 229 ? 83.816  8.602   13.223  1.00   24.42  ? 229 PRO C N   1 
ATOM   7695  C CA  . PRO C  1 229 ? 83.814  10.065  13.330  1.00   26.09  ? 229 PRO C CA  1 
ATOM   7696  C C   . PRO C  1 229 ? 83.766  10.770  11.985  1.00   24.17  ? 229 PRO C C   1 
ATOM   7697  O O   . PRO C  1 229 ? 84.314  10.335  10.977  1.00   26.20  ? 229 PRO C O   1 
ATOM   7698  C CB  . PRO C  1 229 ? 85.112  10.365  14.085  1.00   24.67  ? 229 PRO C CB  1 
ATOM   7699  C CG  . PRO C  1 229 ? 85.368  9.101   14.863  1.00   27.07  ? 229 PRO C CG  1 
ATOM   7700  C CD  . PRO C  1 229 ? 84.935  7.997   13.947  1.00   25.63  ? 229 PRO C CD  1 
ATOM   7701  N N   . LEU C  1 230 ? 83.048  11.870  11.990  1.00   24.67  ? 230 LEU C N   1 
ATOM   7702  C CA  . LEU C  1 230 ? 82.895  12.690  10.813  1.00   23.72  ? 230 LEU C CA  1 
ATOM   7703  C C   . LEU C  1 230 ? 83.761  13.947  10.950  1.00   24.80  ? 230 LEU C C   1 
ATOM   7704  O O   . LEU C  1 230 ? 83.767  14.619  11.984  1.00   25.11  ? 230 LEU C O   1 
ATOM   7705  C CB  . LEU C  1 230 ? 81.426  13.054  10.630  1.00   25.81  ? 230 LEU C CB  1 
ATOM   7706  C CG  . LEU C  1 230 ? 80.980  13.960  9.492   1.00   24.41  ? 230 LEU C CG  1 
ATOM   7707  C CD1 . LEU C  1 230 ? 81.265  13.327  8.157   1.00   22.57  ? 230 LEU C CD1 1 
ATOM   7708  C CD2 . LEU C  1 230 ? 79.501  14.204  9.653   1.00   24.41  ? 230 LEU C CD2 1 
ATOM   7709  N N   . THR C  1 231 ? 84.543  14.235  9.919   1.00   27.67  ? 231 THR C N   1 
ATOM   7710  C CA  . THR C  1 231 ? 85.307  15.468  9.870   1.00   29.15  ? 231 THR C CA  1 
ATOM   7711  C C   . THR C  1 231 ? 84.938  16.236  8.630   1.00   28.97  ? 231 THR C C   1 
ATOM   7712  O O   . THR C  1 231 ? 84.448  15.685  7.641   1.00   27.28  ? 231 THR C O   1 
ATOM   7713  C CB  . THR C  1 231 ? 86.825  15.252  9.891   1.00   28.24  ? 231 THR C CB  1 
ATOM   7714  O OG1 . THR C  1 231 ? 87.150  14.164  9.013   1.00   26.88  ? 231 THR C OG1 1 
ATOM   7715  C CG2 . THR C  1 231 ? 87.311  14.953  11.297  1.00   27.01  ? 231 THR C CG2 1 
ATOM   7716  N N   . ILE C  1 232 ? 85.155  17.537  8.728   1.00   29.83  ? 232 ILE C N   1 
ATOM   7717  C CA  . ILE C  1 232 ? 84.696  18.472  7.734   1.00   29.25  ? 232 ILE C CA  1 
ATOM   7718  C C   . ILE C  1 232 ? 85.847  19.315  7.211   1.00   28.20  ? 232 ILE C C   1 
ATOM   7719  O O   . ILE C  1 232 ? 86.627  19.825  7.995   1.00   28.21  ? 232 ILE C O   1 
ATOM   7720  C CB  . ILE C  1 232 ? 83.606  19.378  8.330   1.00   28.37  ? 232 ILE C CB  1 
ATOM   7721  C CG1 . ILE C  1 232 ? 82.507  18.516  8.966   1.00   25.69  ? 232 ILE C CG1 1 
ATOM   7722  C CG2 . ILE C  1 232 ? 83.067  20.327  7.276   1.00   29.27  ? 232 ILE C CG2 1 
ATOM   7723  C CD1 . ILE C  1 232 ? 81.788  17.593  7.977   1.00   22.52  ? 232 ILE C CD1 1 
ATOM   7724  N N   . SER C  1 233 ? 85.976  19.447  5.895   1.00   29.14  ? 233 SER C N   1 
ATOM   7725  C CA  . SER C  1 233 ? 87.010  20.326  5.333   1.00   31.19  ? 233 SER C CA  1 
ATOM   7726  C C   . SER C  1 233 ? 86.657  21.812  5.436   1.00   35.88  ? 233 SER C C   1 
ATOM   7727  O O   . SER C  1 233 ? 85.525  22.179  5.769   1.00   36.32  ? 233 SER C O   1 
ATOM   7728  C CB  . SER C  1 233 ? 87.271  19.991  3.865   1.00   32.15  ? 233 SER C CB  1 
ATOM   7729  O OG  . SER C  1 233 ? 86.194  20.398  3.038   1.00   33.48  ? 233 SER C OG  1 
ATOM   7730  N N   . LYS C  1 234 ? 87.630  22.666  5.127   1.00   35.85  ? 234 LYS C N   1 
ATOM   7731  C CA  . LYS C  1 234 ? 87.423  24.100  5.173   1.00   38.64  ? 234 LYS C CA  1 
ATOM   7732  C C   . LYS C  1 234 ? 86.414  24.513  4.126   1.00   37.39  ? 234 LYS C C   1 
ATOM   7733  O O   . LYS C  1 234 ? 85.810  25.568  4.225   1.00   34.88  ? 234 LYS C O   1 
ATOM   7734  C CB  . LYS C  1 234 ? 88.737  24.868  4.943   1.00   45.02  ? 234 LYS C CB  1 
ATOM   7735  C CG  . LYS C  1 234 ? 89.831  24.687  6.003   1.00   51.29  ? 234 LYS C CG  1 
ATOM   7736  C CD  . LYS C  1 234 ? 91.092  25.472  5.608   1.00   60.70  ? 234 LYS C CD  1 
ATOM   7737  C CE  . LYS C  1 234 ? 92.305  25.140  6.483   1.00   66.62  ? 234 LYS C CE  1 
ATOM   7738  N NZ  . LYS C  1 234 ? 93.602  25.568  5.861   1.00   72.07  ? 234 LYS C NZ  1 
ATOM   7739  N N   . GLN C  1 235 ? 86.180  23.642  3.157   1.00   37.34  ? 235 GLN C N   1 
ATOM   7740  C CA  . GLN C  1 235 ? 85.253  23.955  2.091   1.00   37.18  ? 235 GLN C CA  1 
ATOM   7741  C C   . GLN C  1 235 ? 83.888  23.351  2.374   1.00   35.48  ? 235 GLN C C   1 
ATOM   7742  O O   . GLN C  1 235 ? 82.985  23.443  1.556   1.00   35.55  ? 235 GLN C O   1 
ATOM   7743  C CB  . GLN C  1 235 ? 85.788  23.417  0.774   1.00   41.68  ? 235 GLN C CB  1 
ATOM   7744  C CG  . GLN C  1 235 ? 87.033  24.132  0.313   1.00   54.06  ? 235 GLN C CG  1 
ATOM   7745  C CD  . GLN C  1 235 ? 86.814  25.628  0.095   1.00   66.83  ? 235 GLN C CD  1 
ATOM   7746  O OE1 . GLN C  1 235 ? 85.767  26.057  -0.403  1.00   69.06  ? 235 GLN C OE1 1 
ATOM   7747  N NE2 . GLN C  1 235 ? 87.809  26.432  0.481   1.00   72.37  ? 235 GLN C NE2 1 
ATOM   7748  N N   . GLY C  1 236 ? 83.747  22.732  3.544   1.00   32.06  ? 236 GLY C N   1 
ATOM   7749  C CA  . GLY C  1 236 ? 82.475  22.192  3.986   1.00   30.82  ? 236 GLY C CA  1 
ATOM   7750  C C   . GLY C  1 236 ? 82.149  20.770  3.544   1.00   25.70  ? 236 GLY C C   1 
ATOM   7751  O O   . GLY C  1 236 ? 80.992  20.341  3.601   1.00   24.82  ? 236 GLY C O   1 
ATOM   7752  N N   . GLU C  1 237 ? 83.168  20.024  3.140   1.00   25.61  ? 237 GLU C N   1 
ATOM   7753  C CA  . GLU C  1 237 ? 82.990  18.651  2.668   1.00   24.19  ? 237 GLU C CA  1 
ATOM   7754  C C   . GLU C  1 237 ? 83.035  17.606  3.773   1.00   24.69  ? 237 GLU C C   1 
ATOM   7755  O O   . GLU C  1 237 ? 83.715  17.799  4.779   1.00   26.84  ? 237 GLU C O   1 
ATOM   7756  C CB  . GLU C  1 237 ? 84.066  18.309  1.650   1.00   25.42  ? 237 GLU C CB  1 
ATOM   7757  C CG  . GLU C  1 237 ? 84.156  19.278  0.513   1.00   29.73  ? 237 GLU C CG  1 
ATOM   7758  C CD  . GLU C  1 237 ? 85.546  19.300  -0.079  1.00   40.25  ? 237 GLU C CD  1 
ATOM   7759  O OE1 . GLU C  1 237 ? 86.504  19.631  0.656   1.00   40.77  ? 237 GLU C OE1 1 
ATOM   7760  O OE2 . GLU C  1 237 ? 85.681  19.018  -1.285  1.00   46.17  1 237 GLU C OE2 1 
ATOM   7761  N N   . TYR C  1 238 ? 82.332  16.490  3.540   1.00   25.83  ? 238 TYR C N   1 
ATOM   7762  C CA  . TYR C  1 238 ? 82.228  15.375  4.479   1.00   26.07  ? 238 TYR C CA  1 
ATOM   7763  C C   . TYR C  1 238 ? 83.312  14.342  4.219   1.00   26.17  ? 238 TYR C C   1 
ATOM   7764  O O   . TYR C  1 238 ? 83.426  13.824  3.102   1.00   24.53  ? 238 TYR C O   1 
ATOM   7765  C CB  . TYR C  1 238 ? 80.842  14.720  4.383   1.00   24.46  ? 238 TYR C CB  1 
ATOM   7766  C CG  . TYR C  1 238 ? 79.694  15.652  4.718   1.00   24.90  ? 238 TYR C CG  1 
ATOM   7767  C CD1 . TYR C  1 238 ? 79.396  15.982  6.033   1.00   24.02  ? 238 TYR C CD1 1 
ATOM   7768  C CD2 . TYR C  1 238 ? 78.922  16.214  3.729   1.00   26.77  ? 238 TYR C CD2 1 
ATOM   7769  C CE1 . TYR C  1 238 ? 78.349  16.852  6.343   1.00   23.51  ? 238 TYR C CE1 1 
ATOM   7770  C CE2 . TYR C  1 238 ? 77.883  17.085  4.039   1.00   25.74  ? 238 TYR C CE2 1 
ATOM   7771  C CZ  . TYR C  1 238 ? 77.605  17.386  5.342   1.00   23.76  ? 238 TYR C CZ  1 
ATOM   7772  O OH  . TYR C  1 238 ? 76.575  18.241  5.639   1.00   26.23  ? 238 TYR C OH  1 
ATOM   7773  N N   . PHE C  1 239 ? 84.081  14.043  5.266   1.00   26.53  ? 239 PHE C N   1 
ATOM   7774  C CA  . PHE C  1 239 ? 85.190  13.086  5.235   1.00   24.89  ? 239 PHE C CA  1 
ATOM   7775  C C   . PHE C  1 239 ? 85.066  12.044  6.332   1.00   26.55  ? 239 PHE C C   1 
ATOM   7776  O O   . PHE C  1 239 ? 84.529  12.328  7.403   1.00   28.30  ? 239 PHE C O   1 
ATOM   7777  C CB  . PHE C  1 239 ? 86.533  13.819  5.393   1.00   24.91  ? 239 PHE C CB  1 
ATOM   7778  C CG  . PHE C  1 239 ? 87.025  14.447  4.128   1.00   25.13  ? 239 PHE C CG  1 
ATOM   7779  C CD1 . PHE C  1 239 ? 86.559  15.671  3.719   1.00   24.00  ? 239 PHE C CD1 1 
ATOM   7780  C CD2 . PHE C  1 239 ? 87.976  13.820  3.355   1.00   27.10  ? 239 PHE C CD2 1 
ATOM   7781  C CE1 . PHE C  1 239 ? 86.997  16.236  2.544   1.00   26.13  ? 239 PHE C CE1 1 
ATOM   7782  C CE2 . PHE C  1 239 ? 88.417  14.395  2.175   1.00   27.29  ? 239 PHE C CE2 1 
ATOM   7783  C CZ  . PHE C  1 239 ? 87.929  15.593  1.781   1.00   27.23  ? 239 PHE C CZ  1 
ATOM   7784  N N   . ILE C  1 240 ? 85.528  10.828  6.063   1.00   26.50  ? 240 ILE C N   1 
ATOM   7785  C CA  . ILE C  1 240 ? 85.799  9.885   7.150   1.00   28.13  ? 240 ILE C CA  1 
ATOM   7786  C C   . ILE C  1 240 ? 87.229  9.342   7.028   1.00   27.92  ? 240 ILE C C   1 
ATOM   7787  O O   . ILE C  1 240 ? 87.915  9.581   6.047   1.00   30.57  ? 240 ILE C O   1 
ATOM   7788  C CB  . ILE C  1 240 ? 84.800  8.674   7.191   1.00   31.11  ? 240 ILE C CB  1 
ATOM   7789  C CG1 . ILE C  1 240 ? 84.816  7.893   5.879   1.00   30.03  ? 240 ILE C CG1 1 
ATOM   7790  C CG2 . ILE C  1 240 ? 83.382  9.118   7.558   1.00   29.63  ? 240 ILE C CG2 1 
ATOM   7791  C CD1 . ILE C  1 240 ? 84.056  6.614   5.947   1.00   27.49  ? 240 ILE C CD1 1 
ATOM   7792  N N   . GLN C  1 241 ? 87.678  8.629   8.047   1.00   28.27  ? 241 GLN C N   1 
ATOM   7793  C CA  . GLN C  1 241 ? 89.017  8.084   8.042   1.00   28.78  ? 241 GLN C CA  1 
ATOM   7794  C C   . GLN C  1 241 ? 89.001  6.595   7.754   1.00   32.91  ? 241 GLN C C   1 
ATOM   7795  O O   . GLN C  1 241 ? 88.488  5.790   8.547   1.00   34.13  ? 241 GLN C O   1 
ATOM   7796  C CB  . GLN C  1 241 ? 89.710  8.325   9.373   1.00   25.75  ? 241 GLN C CB  1 
ATOM   7797  C CG  . GLN C  1 241 ? 91.063  7.637   9.436   1.00   29.68  ? 241 GLN C CG  1 
ATOM   7798  C CD  . GLN C  1 241 ? 92.005  8.134   8.338   1.00   36.29  ? 241 GLN C CD  1 
ATOM   7799  O OE1 . GLN C  1 241 ? 91.877  9.255   7.860   1.00   36.31  ? 241 GLN C OE1 1 
ATOM   7800  N NE2 . GLN C  1 241 ? 92.928  7.287   7.915   1.00   39.71  ? 241 GLN C NE2 1 
ATOM   7801  N N   . VAL C  1 242 ? 89.603  6.238   6.630   1.00   31.91  ? 242 VAL C N   1 
ATOM   7802  C CA  . VAL C  1 242 ? 89.793  4.858   6.218   1.00   27.92  ? 242 VAL C CA  1 
ATOM   7803  C C   . VAL C  1 242 ? 91.276  4.481   6.367   1.00   31.78  ? 242 VAL C C   1 
ATOM   7804  O O   . VAL C  1 242 ? 92.137  5.044   5.673   1.00   32.56  ? 242 VAL C O   1 
ATOM   7805  C CB  . VAL C  1 242 ? 89.334  4.672   4.771   1.00   24.80  ? 242 VAL C CB  1 
ATOM   7806  C CG1 . VAL C  1 242 ? 89.675  3.324   4.291   1.00   24.42  ? 242 VAL C CG1 1 
ATOM   7807  C CG2 . VAL C  1 242 ? 87.855  4.911   4.652   1.00   24.36  ? 242 VAL C CG2 1 
ATOM   7808  N N   . ASN C  1 243 ? 91.586  3.573   7.289   1.00   29.04  ? 243 ASN C N   1 
ATOM   7809  C CA  . ASN C  1 243 ? 92.979  3.150   7.510   1.00   31.98  ? 243 ASN C CA  1 
ATOM   7810  C C   . ASN C  1 243 ? 93.527  2.172   6.454   1.00   33.80  ? 243 ASN C C   1 
ATOM   7811  O O   . ASN C  1 243 ? 94.723  2.160   6.163   1.00   35.45  ? 243 ASN C O   1 
ATOM   7812  C CB  . ASN C  1 243 ? 93.114  2.526   8.896   1.00   33.32  ? 243 ASN C CB  1 
ATOM   7813  C CG  . ASN C  1 243 ? 93.291  3.558   9.996   1.00   34.19  ? 243 ASN C CG  1 
ATOM   7814  O OD1 . ASN C  1 243 ? 93.305  4.752   9.742   1.00   35.10  ? 243 ASN C OD1 1 
ATOM   7815  N ND2 . ASN C  1 243 ? 93.412  3.091   11.235  1.00   35.85  ? 243 ASN C ND2 1 
ATOM   7816  N N   . ALA C  1 244 ? 92.641  1.362   5.883   1.00   31.48  ? 244 ALA C N   1 
ATOM   7817  C CA  . ALA C  1 244 ? 93.020  0.384   4.885   1.00   30.18  ? 244 ALA C CA  1 
ATOM   7818  C C   . ALA C  1 244 ? 91.826  -0.057  4.080   1.00   28.66  ? 244 ALA C C   1 
ATOM   7819  O O   . ALA C  1 244 ? 90.690  0.011   4.531   1.00   27.39  ? 244 ALA C O   1 
ATOM   7820  C CB  . ALA C  1 244 ? 93.658  -0.809  5.530   1.00   31.01  ? 244 ALA C CB  1 
ATOM   7821  N N   . ILE C  1 245 ? 92.104  -0.507  2.869   1.00   32.42  ? 245 ILE C N   1 
ATOM   7822  C CA  . ILE C  1 245 ? 91.128  -1.236  2.101   1.00   32.61  ? 245 ILE C CA  1 
ATOM   7823  C C   . ILE C  1 245 ? 91.567  -2.657  2.159   1.00   33.20  ? 245 ILE C C   1 
ATOM   7824  O O   . ILE C  1 245 ? 92.696  -2.955  1.833   1.00   36.89  ? 245 ILE C O   1 
ATOM   7825  C CB  . ILE C  1 245 ? 91.041  -0.793  0.658   1.00   34.40  ? 245 ILE C CB  1 
ATOM   7826  C CG1 . ILE C  1 245 ? 90.784  0.699   0.594   1.00   34.78  ? 245 ILE C CG1 1 
ATOM   7827  C CG2 . ILE C  1 245 ? 89.932  -1.532  -0.044  1.00   33.28  ? 245 ILE C CG2 1 
ATOM   7828  C CD1 . ILE C  1 245 ? 91.021  1.251   -0.773  1.00   40.04  ? 245 ILE C CD1 1 
ATOM   7829  N N   . ARG C  1 246 ? 90.694  -3.525  2.639   1.00   33.47  ? 246 ARG C N   1 
ATOM   7830  C CA  . ARG C  1 246 ? 91.010  -4.930  2.775   1.00   36.08  ? 246 ARG C CA  1 
ATOM   7831  C C   . ARG C  1 246 ? 90.461  -5.715  1.599   1.00   38.11  ? 246 ARG C C   1 
ATOM   7832  O O   . ARG C  1 246 ? 89.314  -5.564  1.245   1.00   41.59  ? 246 ARG C O   1 
ATOM   7833  C CB  . ARG C  1 246 ? 90.419  -5.497  4.066   1.00   41.33  ? 246 ARG C CB  1 
ATOM   7834  C CG  . ARG C  1 246 ? 90.691  -6.995  4.268   1.00   46.43  ? 246 ARG C CG  1 
ATOM   7835  C CD  . ARG C  1 246 ? 89.641  -7.678  5.153   1.00   52.98  ? 246 ARG C CD  1 
ATOM   7836  N NE  . ARG C  1 246 ? 89.759  -7.379  6.583   1.00   58.24  ? 246 ARG C NE  1 
ATOM   7837  C CZ  . ARG C  1 246 ? 88.718  -7.323  7.422   1.00   63.05  ? 246 ARG C CZ  1 
ATOM   7838  N NH1 . ARG C  1 246 ? 87.481  -7.556  6.985   1.00   64.17  ? 246 ARG C NH1 1 
ATOM   7839  N NH2 . ARG C  1 246 ? 88.910  -7.041  8.704   1.00   64.90  ? 246 ARG C NH2 1 
ATOM   7840  N N   . VAL C  1 247 ? 91.286  -6.541  0.979   1.00   41.00  ? 247 VAL C N   1 
ATOM   7841  C CA  . VAL C  1 247 ? 90.800  -7.511  0.023   1.00   43.74  ? 247 VAL C CA  1 
ATOM   7842  C C   . VAL C  1 247 ? 91.262  -8.890  0.497   1.00   49.25  ? 247 VAL C C   1 
ATOM   7843  O O   . VAL C  1 247 ? 92.448  -9.212  0.451   1.00   48.39  ? 247 VAL C O   1 
ATOM   7844  C CB  . VAL C  1 247 ? 91.302  -7.224  -1.384  1.00   45.34  ? 247 VAL C CB  1 
ATOM   7845  C CG1 . VAL C  1 247 ? 90.718  -8.225  -2.350  1.00   48.58  ? 247 VAL C CG1 1 
ATOM   7846  C CG2 . VAL C  1 247 ? 90.931  -5.803  -1.772  1.00   42.70  ? 247 VAL C CG2 1 
ATOM   7847  N N   . ASN C  1 248 ? 90.318  -9.684  0.992   1.00   40.10  ? 248 ASN C N   1 
ATOM   7848  C CA  . ASN C  1 248 ? 90.644  -10.932 1.655   1.00   42.94  ? 248 ASN C CA  1 
ATOM   7849  C C   . ASN C  1 248 ? 91.700  -10.736 2.764   1.00   39.95  ? 248 ASN C C   1 
ATOM   7850  O O   . ASN C  1 248 ? 91.395  -10.156 3.794   1.00   38.55  ? 248 ASN C O   1 
ATOM   7851  C CB  . ASN C  1 248 ? 91.072  -11.979 0.617   1.00   45.55  ? 248 ASN C CB  1 
ATOM   7852  C CG  . ASN C  1 248 ? 89.899  -12.461 -0.237  1.00   46.12  ? 248 ASN C CG  1 
ATOM   7853  O OD1 . ASN C  1 248 ? 88.743  -12.327 0.152   1.00   44.79  ? 248 ASN C OD1 1 
ATOM   7854  N ND2 . ASN C  1 248 ? 90.200  -13.037 -1.390  1.00   48.09  ? 248 ASN C ND2 1 
ATOM   7855  N N   . LYS C  1 249 ? 92.922  -11.219 2.579   1.00   41.66  ? 249 LYS C N   1 
ATOM   7856  C CA  . LYS C  1 249 ? 93.937  -10.998 3.611   1.00   42.77  ? 249 LYS C CA  1 
ATOM   7857  C C   . LYS C  1 249 ? 95.036  -9.997  3.202   1.00   38.56  ? 249 LYS C C   1 
ATOM   7858  O O   . LYS C  1 249 ? 96.113  -9.952  3.818   1.00   37.81  ? 249 LYS C O   1 
ATOM   7859  C CB  . LYS C  1 249 ? 94.586  -12.328 3.979   1.00   47.39  ? 249 LYS C CB  1 
ATOM   7860  C CG  . LYS C  1 249 ? 93.612  -13.462 4.175   1.00   52.98  ? 249 LYS C CG  1 
ATOM   7861  C CD  . LYS C  1 249 ? 94.317  -14.682 4.730   1.00   57.13  ? 249 LYS C CD  1 
ATOM   7862  C CE  . LYS C  1 249 ? 93.476  -15.933 4.540   1.00   61.36  ? 249 LYS C CE  1 
ATOM   7863  N NZ  . LYS C  1 249 ? 92.059  -15.627 4.839   1.00   61.00  ? 249 LYS C NZ  1 
ATOM   7864  N N   . HIS C  1 250 ? 94.755  -9.196  2.177   1.00   34.22  ? 250 HIS C N   1 
ATOM   7865  C CA  . HIS C  1 250 ? 95.690  -8.169  1.762   1.00   35.92  ? 250 HIS C CA  1 
ATOM   7866  C C   . HIS C  1 250 ? 95.171  -6.787  2.120   1.00   34.80  ? 250 HIS C C   1 
ATOM   7867  O O   . HIS C  1 250 ? 94.074  -6.415  1.715   1.00   35.50  ? 250 HIS C O   1 
ATOM   7868  C CB  . HIS C  1 250 ? 95.947  -8.323  0.271   1.00   33.35  ? 250 HIS C CB  1 
ATOM   7869  C CG  . HIS C  1 250 ? 96.644  -9.604  -0.052  1.00   34.89  ? 250 HIS C CG  1 
ATOM   7870  N ND1 . HIS C  1 250 ? 96.843  -10.053 -1.337  1.00   35.40  ? 250 HIS C ND1 1 
ATOM   7871  C CD2 . HIS C  1 250 ? 97.150  -10.556 0.766   1.00   35.62  ? 250 HIS C CD2 1 
ATOM   7872  C CE1 . HIS C  1 250 ? 97.466  -11.217 -1.297  1.00   40.55  ? 250 HIS C CE1 1 
ATOM   7873  N NE2 . HIS C  1 250 ? 97.666  -11.544 -0.032  1.00   38.54  ? 250 HIS C NE2 1 
ATOM   7874  N N   . LEU C  1 251 ? 95.972  -6.002  2.833   1.00   35.08  ? 251 LEU C N   1 
ATOM   7875  C CA  . LEU C  1 251 ? 95.520  -4.672  3.241   1.00   32.96  ? 251 LEU C CA  1 
ATOM   7876  C C   . LEU C  1 251 ? 96.309  -3.558  2.571   1.00   31.32  ? 251 LEU C C   1 
ATOM   7877  O O   . LEU C  1 251 ? 97.524  -3.461  2.731   1.00   32.30  ? 251 LEU C O   1 
ATOM   7878  C CB  . LEU C  1 251 ? 95.587  -4.531  4.762   1.00   33.57  ? 251 LEU C CB  1 
ATOM   7879  C CG  . LEU C  1 251 ? 94.548  -5.409  5.467   1.00   34.85  ? 251 LEU C CG  1 
ATOM   7880  C CD1 . LEU C  1 251 ? 95.104  -6.737  5.890   1.00   34.71  ? 251 LEU C CD1 1 
ATOM   7881  C CD2 . LEU C  1 251 ? 93.936  -4.689  6.635   1.00   36.80  ? 251 LEU C CD2 1 
ATOM   7882  N N   . VAL C  1 252 ? 95.578  -2.704  1.850   1.00   29.13  ? 252 VAL C N   1 
ATOM   7883  C CA  . VAL C  1 252 ? 96.133  -1.548  1.157   1.00   29.13  ? 252 VAL C CA  1 
ATOM   7884  C C   . VAL C  1 252 ? 95.974  -0.313  2.032   1.00   29.64  ? 252 VAL C C   1 
ATOM   7885  O O   . VAL C  1 252 ? 94.876  0.057   2.408   1.00   32.10  ? 252 VAL C O   1 
ATOM   7886  C CB  . VAL C  1 252 ? 95.452  -1.360  -0.225  1.00   27.37  ? 252 VAL C CB  1 
ATOM   7887  C CG1 . VAL C  1 252 ? 96.036  -0.190  -0.982  1.00   28.66  ? 252 VAL C CG1 1 
ATOM   7888  C CG2 . VAL C  1 252 ? 95.573  -2.638  -1.062  1.00   26.81  ? 252 VAL C CG2 1 
ATOM   7889  N N   . ILE C  1 253 ? 97.092  0.287   2.403   1.00   32.44  ? 253 ILE C N   1 
ATOM   7890  C CA  . ILE C  1 253 ? 97.111  1.405   3.328   1.00   35.35  ? 253 ILE C CA  1 
ATOM   7891  C C   . ILE C  1 253 ? 97.267  2.677   2.506   1.00   40.80  ? 253 ILE C C   1 
ATOM   7892  O O   . ILE C  1 253 ? 98.309  2.873   1.879   1.00   41.64  ? 253 ILE C O   1 
ATOM   7893  C CB  . ILE C  1 253 ? 98.288  1.366   4.337   1.00   36.30  ? 253 ILE C CB  1 
ATOM   7894  C CG1 . ILE C  1 253 ? 98.444  0.003   5.006   1.00   41.15  ? 253 ILE C CG1 1 
ATOM   7895  C CG2 . ILE C  1 253 ? 98.156  2.470   5.361   1.00   36.37  ? 253 ILE C CG2 1 
ATOM   7896  C CD1 . ILE C  1 253 ? 97.203  -0.522  5.613   1.00   43.00  ? 253 ILE C CD1 1 
ATOM   7897  N N   . PRO C  1 254 ? 96.219  3.522   2.461   1.00   46.00  ? 254 PRO C N   1 
ATOM   7898  C CA  . PRO C  1 254 ? 96.318  4.780   1.711   1.00   52.23  ? 254 PRO C CA  1 
ATOM   7899  C C   . PRO C  1 254 ? 97.416  5.689   2.304   1.00   66.32  ? 254 PRO C C   1 
ATOM   7900  O O   . PRO C  1 254 ? 97.191  6.377   3.306   1.00   70.23  ? 254 PRO C O   1 
ATOM   7901  C CB  . PRO C  1 254 ? 94.927  5.401   1.881   1.00   47.95  ? 254 PRO C CB  1 
ATOM   7902  C CG  . PRO C  1 254 ? 94.045  4.278   2.317   1.00   43.55  ? 254 PRO C CG  1 
ATOM   7903  C CD  . PRO C  1 254 ? 94.909  3.382   3.121   1.00   44.68  ? 254 PRO C CD  1 
ATOM   7904  N N   . THR C  1 255 ? 98.598  5.630   1.669   1.00   73.84  ? 255 THR C N   1 
ATOM   7905  C CA  . THR C  1 255 ? 99.815  6.429   1.936   1.00   78.89  ? 255 THR C CA  1 
ATOM   7906  C C   . THR C  1 255 ? 100.382 6.172   3.339   1.00   83.64  ? 255 THR C C   1 
ATOM   7907  O O   . THR C  1 255 ? 101.157 5.224   3.553   1.00   84.21  ? 255 THR C O   1 
ATOM   7908  C CB  . THR C  1 255 ? 99.582  7.936   1.749   1.00   77.71  ? 255 THR C CB  1 
ATOM   7909  O OG1 . THR C  1 255 ? 98.596  8.396   2.679   1.00   75.58  ? 255 THR C OG1 1 
ATOM   7910  C CG2 . THR C  1 255 ? 99.106  8.215   0.327   1.00   76.22  ? 255 THR C CG2 1 
ATOM   7911  N N   . GLY C  1 271 ? 92.678  13.668  15.731  1.00   94.93  ? 271 GLY C N   1 
ATOM   7912  C CA  . GLY C  1 271 ? 91.734  14.687  15.283  1.00   92.93  ? 271 GLY C CA  1 
ATOM   7913  C C   . GLY C  1 271 ? 92.286  15.595  14.195  1.00   88.18  ? 271 GLY C C   1 
ATOM   7914  O O   . GLY C  1 271 ? 92.558  16.782  14.395  1.00   86.81  ? 271 GLY C O   1 
ATOM   7915  N N   . GLU C  1 272 ? 92.432  14.994  13.022  1.00   84.20  ? 272 GLU C N   1 
ATOM   7916  C CA  . GLU C  1 272 ? 92.922  15.626  11.801  1.00   80.47  ? 272 GLU C CA  1 
ATOM   7917  C C   . GLU C  1 272 ? 91.903  15.107  10.788  1.00   65.22  ? 272 GLU C C   1 
ATOM   7918  O O   . GLU C  1 272 ? 91.240  14.117  11.086  1.00   62.15  ? 272 GLU C O   1 
ATOM   7919  C CB  . GLU C  1 272 ? 94.391  15.237  11.525  1.00   86.27  ? 272 GLU C CB  1 
ATOM   7920  C CG  . GLU C  1 272 ? 94.810  14.900  10.084  1.00   86.34  ? 272 GLU C CG  1 
ATOM   7921  C CD  . GLU C  1 272 ? 94.707  16.058  9.093   1.00   91.29  ? 272 GLU C CD  1 
ATOM   7922  O OE1 . GLU C  1 272 ? 94.462  17.212  9.510   1.00   95.18  ? 272 GLU C OE1 1 
ATOM   7923  O OE2 . GLU C  1 272 ? 94.874  15.801  7.879   1.00   90.69  ? 272 GLU C OE2 1 
ATOM   7924  N N   . ILE C  1 273 ? 91.722  15.766  9.642   1.00   59.51  ? 273 ILE C N   1 
ATOM   7925  C CA  . ILE C  1 273 ? 90.661  15.357  8.711   1.00   54.42  ? 273 ILE C CA  1 
ATOM   7926  C C   . ILE C  1 273 ? 90.929  14.003  8.089   1.00   52.53  ? 273 ILE C C   1 
ATOM   7927  O O   . ILE C  1 273 ? 92.070  13.664  7.790   1.00   53.86  ? 273 ILE C O   1 
ATOM   7928  C CB  . ILE C  1 273 ? 90.458  16.390  7.564   1.00   54.95  ? 273 ILE C CB  1 
ATOM   7929  C CG1 . ILE C  1 273 ? 90.163  17.771  8.119   1.00   60.71  ? 273 ILE C CG1 1 
ATOM   7930  C CG2 . ILE C  1 273 ? 89.285  16.039  6.672   1.00   47.45  ? 273 ILE C CG2 1 
ATOM   7931  C CD1 . ILE C  1 273 ? 89.815  18.745  7.044   1.00   61.24  ? 273 ILE C CD1 1 
ATOM   7932  N N   . GLY C  1 274 ? 89.857  13.230  7.924   1.00   49.92  ? 274 GLY C N   1 
ATOM   7933  C CA  . GLY C  1 274 ? 89.901  11.926  7.293   1.00   49.59  ? 274 GLY C CA  1 
ATOM   7934  C C   . GLY C  1 274 ? 90.349  11.983  5.852   1.00   47.57  ? 274 GLY C C   1 
ATOM   7935  O O   . GLY C  1 274 ? 90.307  13.035  5.229   1.00   52.22  ? 274 GLY C O   1 
ATOM   7936  N N   . GLY C  1 275 ? 90.755  10.845  5.318   1.00   39.86  ? 275 GLY C N   1 
ATOM   7937  C CA  . GLY C  1 275 ? 91.273  10.786  3.976   1.00   35.65  ? 275 GLY C CA  1 
ATOM   7938  C C   . GLY C  1 275 ? 90.241  10.379  2.958   1.00   32.78  ? 275 GLY C C   1 
ATOM   7939  O O   . GLY C  1 275 ? 90.526  10.416  1.769   1.00   35.44  ? 275 GLY C O   1 
ATOM   7940  N N   . ALA C  1 276 ? 89.051  9.981   3.406   1.00   28.26  ? 276 ALA C N   1 
ATOM   7941  C CA  . ALA C  1 276 ? 88.034  9.535   2.473   1.00   24.37  ? 276 ALA C CA  1 
ATOM   7942  C C   . ALA C  1 276 ? 86.877  10.522  2.381   1.00   27.07  ? 276 ALA C C   1 
ATOM   7943  O O   . ALA C  1 276 ? 86.114  10.722  3.321   1.00   26.55  ? 276 ALA C O   1 
ATOM   7944  C CB  . ALA C  1 276 ? 87.527  8.159   2.863   1.00   23.59  ? 276 ALA C CB  1 
ATOM   7945  N N   . LEU C  1 277 ? 86.752  11.117  1.207   1.00   26.27  ? 277 LEU C N   1 
ATOM   7946  C CA  . LEU C  1 277 ? 85.680  12.034  0.928   1.00   26.92  ? 277 LEU C CA  1 
ATOM   7947  C C   . LEU C  1 277 ? 84.407  11.250  0.682   1.00   29.13  ? 277 LEU C C   1 
ATOM   7948  O O   . LEU C  1 277 ? 84.427  10.206  0.031   1.00   28.39  ? 277 LEU C O   1 
ATOM   7949  C CB  . LEU C  1 277 ? 86.017  12.876  -0.296  1.00   27.23  ? 277 LEU C CB  1 
ATOM   7950  C CG  . LEU C  1 277 ? 84.921  13.773  -0.842  1.00   19.76  ? 277 LEU C CG  1 
ATOM   7951  C CD1 . LEU C  1 277 ? 84.765  14.958  0.053   1.00   21.16  ? 277 LEU C CD1 1 
ATOM   7952  C CD2 . LEU C  1 277 ? 85.215  14.201  -2.228  1.00   23.35  ? 277 LEU C CD2 1 
ATOM   7953  N N   . ILE C  1 278 ? 83.292  11.775  1.172   1.00   30.18  ? 278 ILE C N   1 
ATOM   7954  C CA  . ILE C  1 278 ? 81.992  11.261  0.798   1.00   28.33  ? 278 ILE C CA  1 
ATOM   7955  C C   . ILE C  1 278 ? 81.306  12.272  -0.106  1.00   28.26  ? 278 ILE C C   1 
ATOM   7956  O O   . ILE C  1 278 ? 81.239  13.438  0.220   1.00   27.45  ? 278 ILE C O   1 
ATOM   7957  C CB  . ILE C  1 278 ? 81.136  10.980  2.022   1.00   28.82  ? 278 ILE C CB  1 
ATOM   7958  C CG1 . ILE C  1 278 ? 81.842  9.988   2.948   1.00   23.59  ? 278 ILE C CG1 1 
ATOM   7959  C CG2 . ILE C  1 278 ? 79.817  10.399  1.587   1.00   31.14  ? 278 ILE C CG2 1 
ATOM   7960  C CD1 . ILE C  1 278 ? 81.190  9.869   4.293   1.00   25.84  ? 278 ILE C CD1 1 
ATOM   7961  N N   . THR C  1 279 ? 80.841  11.822  -1.269  1.00   30.17  ? 279 THR C N   1 
ATOM   7962  C CA  . THR C  1 279 ? 80.257  12.718  -2.259  1.00   31.43  ? 279 THR C CA  1 
ATOM   7963  C C   . THR C  1 279 ? 79.173  12.004  -3.071  1.00   33.04  ? 279 THR C C   1 
ATOM   7964  O O   . THR C  1 279 ? 79.174  10.778  -3.147  1.00   32.38  ? 279 THR C O   1 
ATOM   7965  C CB  . THR C  1 279 ? 81.320  13.273  -3.223  1.00   30.78  ? 279 THR C CB  1 
ATOM   7966  O OG1 . THR C  1 279 ? 80.689  14.142  -4.175  1.00   32.45  ? 279 THR C OG1 1 
ATOM   7967  C CG2 . THR C  1 279 ? 81.984  12.147  -3.978  1.00   27.89  ? 279 THR C CG2 1 
ATOM   7968  N N   . THR C  1 280 ? 78.250  12.772  -3.666  1.00   32.48  ? 280 THR C N   1 
ATOM   7969  C CA  . THR C  1 280 ? 77.202  12.204  -4.527  1.00   30.42  ? 280 THR C CA  1 
ATOM   7970  C C   . THR C  1 280 ? 77.313  12.634  -5.968  1.00   31.95  ? 280 THR C C   1 
ATOM   7971  O O   . THR C  1 280 ? 76.410  12.343  -6.776  1.00   35.79  ? 280 THR C O   1 
ATOM   7972  C CB  . THR C  1 280 ? 75.782  12.581  -4.091  1.00   28.79  ? 280 THR C CB  1 
ATOM   7973  O OG1 . THR C  1 280 ? 75.683  14.004  -3.969  1.00   30.30  ? 280 THR C OG1 1 
ATOM   7974  C CG2 . THR C  1 280 ? 75.437  11.942  -2.785  1.00   28.14  ? 280 THR C CG2 1 
ATOM   7975  N N   . THR C  1 281 ? 78.385  13.344  -6.301  1.00   28.83  ? 281 THR C N   1 
ATOM   7976  C CA  . THR C  1 281 ? 78.427  13.966  -7.608  1.00   31.66  ? 281 THR C CA  1 
ATOM   7977  C C   . THR C  1 281 ? 79.288  13.196  -8.617  1.00   33.95  ? 281 THR C C   1 
ATOM   7978  O O   . THR C  1 281 ? 79.580  13.707  -9.691  1.00   36.58  ? 281 THR C O   1 
ATOM   7979  C CB  . THR C  1 281 ? 78.856  15.436  -7.518  1.00   30.71  ? 281 THR C CB  1 
ATOM   7980  O OG1 . THR C  1 281 ? 80.058  15.564  -6.761  1.00   29.66  ? 281 THR C OG1 1 
ATOM   7981  C CG2 . THR C  1 281 ? 77.768  16.202  -6.830  1.00   31.81  ? 281 THR C CG2 1 
ATOM   7982  N N   . HIS C  1 282 ? 79.681  11.969  -8.281  1.00   31.89  ? 282 HIS C N   1 
ATOM   7983  C CA  . HIS C  1 282 ? 80.135  11.023  -9.305  1.00   34.08  ? 282 HIS C CA  1 
ATOM   7984  C C   . HIS C  1 282 ? 79.694  9.627   -8.913  1.00   33.18  ? 282 HIS C C   1 
ATOM   7985  O O   . HIS C  1 282 ? 79.550  9.343   -7.721  1.00   34.85  ? 282 HIS C O   1 
ATOM   7986  C CB  . HIS C  1 282 ? 81.651  11.100  -9.529  1.00   40.05  ? 282 HIS C CB  1 
ATOM   7987  C CG  . HIS C  1 282 ? 82.478  10.938  -8.287  1.00   45.45  ? 282 HIS C CG  1 
ATOM   7988  N ND1 . HIS C  1 282 ? 82.560  9.752   -7.590  1.00   48.34  ? 282 HIS C ND1 1 
ATOM   7989  C CD2 . HIS C  1 282 ? 83.291  11.811  -7.641  1.00   45.90  ? 282 HIS C CD2 1 
ATOM   7990  C CE1 . HIS C  1 282 ? 83.368  9.906   -6.553  1.00   47.09  ? 282 HIS C CE1 1 
ATOM   7991  N NE2 . HIS C  1 282 ? 83.827  11.144  -6.566  1.00   46.06  ? 282 HIS C NE2 1 
ATOM   7992  N N   . PRO C  1 283 ? 79.408  8.767   -9.910  1.00   34.39  ? 283 PRO C N   1 
ATOM   7993  C CA  . PRO C  1 283 ? 78.878  7.441   -9.586  1.00   33.39  ? 283 PRO C CA  1 
ATOM   7994  C C   . PRO C  1 283 ? 79.870  6.491   -8.936  1.00   33.37  ? 283 PRO C C   1 
ATOM   7995  O O   . PRO C  1 283 ? 79.596  6.002   -7.861  1.00   34.71  ? 283 PRO C O   1 
ATOM   7996  C CB  . PRO C  1 283 ? 78.463  6.890   -10.948 1.00   36.43  ? 283 PRO C CB  1 
ATOM   7997  C CG  . PRO C  1 283 ? 79.231  7.663   -11.934 1.00   38.27  ? 283 PRO C CG  1 
ATOM   7998  C CD  . PRO C  1 283 ? 79.385  9.025   -11.356 1.00   36.19  ? 283 PRO C CD  1 
ATOM   7999  N N   . TYR C  1 284 ? 81.032  6.291   -9.520  1.00   33.11  ? 284 TYR C N   1 
ATOM   8000  C CA  . TYR C  1 284 ? 81.916  5.258   -9.021  1.00   33.82  ? 284 TYR C CA  1 
ATOM   8001  C C   . TYR C  1 284 ? 82.889  5.821   -7.988  1.00   34.80  ? 284 TYR C C   1 
ATOM   8002  O O   . TYR C  1 284 ? 83.081  7.026   -7.899  1.00   36.57  ? 284 TYR C O   1 
ATOM   8003  C CB  . TYR C  1 284 ? 82.654  4.609   -10.201 1.00   35.79  ? 284 TYR C CB  1 
ATOM   8004  C CG  . TYR C  1 284 ? 81.697  4.150   -11.285 1.00   38.87  ? 284 TYR C CG  1 
ATOM   8005  C CD1 . TYR C  1 284 ? 80.691  3.230   -11.012 1.00   40.83  ? 284 TYR C CD1 1 
ATOM   8006  C CD2 . TYR C  1 284 ? 81.774  4.660   -12.574 1.00   41.66  ? 284 TYR C CD2 1 
ATOM   8007  C CE1 . TYR C  1 284 ? 79.801  2.824   -11.995 1.00   44.71  ? 284 TYR C CE1 1 
ATOM   8008  C CE2 . TYR C  1 284 ? 80.882  4.251   -13.564 1.00   47.03  ? 284 TYR C CE2 1 
ATOM   8009  C CZ  . TYR C  1 284 ? 79.902  3.335   -13.267 1.00   48.35  ? 284 TYR C CZ  1 
ATOM   8010  O OH  . TYR C  1 284 ? 79.020  2.933   -14.246 1.00   55.70  ? 284 TYR C OH  1 
ATOM   8011  N N   . THR C  1 285 ? 83.475  4.954   -7.174  1.00   34.52  ? 285 THR C N   1 
ATOM   8012  C CA  . THR C  1 285 ? 84.474  5.382   -6.193  1.00   31.38  ? 285 THR C CA  1 
ATOM   8013  C C   . THR C  1 285 ? 85.824  5.680   -6.850  1.00   30.86  ? 285 THR C C   1 
ATOM   8014  O O   . THR C  1 285 ? 86.353  4.874   -7.597  1.00   33.78  ? 285 THR C O   1 
ATOM   8015  C CB  . THR C  1 285 ? 84.659  4.318   -5.108  1.00   28.64  ? 285 THR C CB  1 
ATOM   8016  O OG1 . THR C  1 285 ? 83.424  4.162   -4.406  1.00   29.60  ? 285 THR C OG1 1 
ATOM   8017  C CG2 . THR C  1 285 ? 85.747  4.709   -4.142  1.00   23.70  ? 285 THR C CG2 1 
ATOM   8018  N N   . VAL C  1 286 ? 86.394  6.832   -6.528  1.00   30.01  ? 286 VAL C N   1 
ATOM   8019  C CA  . VAL C  1 286 ? 87.582  7.316   -7.206  1.00   32.63  ? 286 VAL C CA  1 
ATOM   8020  C C   . VAL C  1 286 ? 88.795  7.215   -6.278  1.00   34.00  ? 286 VAL C C   1 
ATOM   8021  O O   . VAL C  1 286 ? 88.746  7.631   -5.118  1.00   33.28  ? 286 VAL C O   1 
ATOM   8022  C CB  . VAL C  1 286 ? 87.372  8.781   -7.688  1.00   28.61  ? 286 VAL C CB  1 
ATOM   8023  C CG1 . VAL C  1 286 ? 88.630  9.348   -8.347  1.00   30.23  ? 286 VAL C CG1 1 
ATOM   8024  C CG2 . VAL C  1 286 ? 86.182  8.863   -8.662  1.00   30.02  ? 286 VAL C CG2 1 
ATOM   8025  N N   . LEU C  1 287 ? 89.873  6.632   -6.791  1.00   35.29  ? 287 LEU C N   1 
ATOM   8026  C CA  . LEU C  1 287 ? 91.110  6.481   -6.033  1.00   35.13  ? 287 LEU C CA  1 
ATOM   8027  C C   . LEU C  1 287 ? 92.247  7.278   -6.657  1.00   37.79  ? 287 LEU C C   1 
ATOM   8028  O O   . LEU C  1 287 ? 92.370  7.355   -7.889  1.00   40.72  ? 287 LEU C O   1 
ATOM   8029  C CB  . LEU C  1 287 ? 91.501  5.007   -5.963  1.00   32.71  ? 287 LEU C CB  1 
ATOM   8030  C CG  . LEU C  1 287 ? 90.401  4.062   -5.495  1.00   28.74  ? 287 LEU C CG  1 
ATOM   8031  C CD1 . LEU C  1 287 ? 90.853  2.650   -5.684  1.00   30.89  ? 287 LEU C CD1 1 
ATOM   8032  C CD2 . LEU C  1 287 ? 90.115  4.320   -4.055  1.00   24.67  ? 287 LEU C CD2 1 
ATOM   8033  N N   . SER C  1 288 ? 93.089  7.866   -5.819  1.00   37.59  ? 288 SER C N   1 
ATOM   8034  C CA  . SER C  1 288 ? 94.256  8.535   -6.343  1.00   39.82  ? 288 SER C CA  1 
ATOM   8035  C C   . SER C  1 288 ? 95.116  7.487   -7.018  1.00   41.20  ? 288 SER C C   1 
ATOM   8036  O O   . SER C  1 288 ? 95.099  6.327   -6.637  1.00   37.62  ? 288 SER C O   1 
ATOM   8037  C CB  . SER C  1 288 ? 95.025  9.228   -5.238  1.00   41.13  ? 288 SER C CB  1 
ATOM   8038  O OG  . SER C  1 288 ? 95.478  8.248   -4.337  1.00   41.17  ? 288 SER C OG  1 
ATOM   8039  N N   . HIS C  1 289 ? 95.897  7.921   -7.996  1.00   45.50  ? 289 HIS C N   1 
ATOM   8040  C CA  . HIS C  1 289 ? 96.585  7.006   -8.885  1.00   47.97  ? 289 HIS C CA  1 
ATOM   8041  C C   . HIS C  1 289 ? 97.450  5.993   -8.156  1.00   50.53  ? 289 HIS C C   1 
ATOM   8042  O O   . HIS C  1 289 ? 97.404  4.804   -8.454  1.00   48.94  ? 289 HIS C O   1 
ATOM   8043  C CB  . HIS C  1 289 ? 97.422  7.783   -9.873  1.00   50.71  ? 289 HIS C CB  1 
ATOM   8044  C CG  . HIS C  1 289 ? 98.132  6.914   -10.850 1.00   52.11  ? 289 HIS C CG  1 
ATOM   8045  N ND1 . HIS C  1 289 ? 97.466  6.190   -11.811 1.00   52.48  ? 289 HIS C ND1 1 
ATOM   8046  C CD2 . HIS C  1 289 ? 99.446  6.654   -11.022 1.00   55.00  ? 289 HIS C CD2 1 
ATOM   8047  C CE1 . HIS C  1 289 ? 98.339  5.511   -12.529 1.00   56.72  ? 289 HIS C CE1 1 
ATOM   8048  N NE2 . HIS C  1 289 ? 99.547  5.777   -12.071 1.00   58.44  ? 289 HIS C NE2 1 
ATOM   8049  N N   . SER C  1 290 ? 98.214  6.455   -7.177  1.00   53.92  ? 290 SER C N   1 
ATOM   8050  C CA  . SER C  1 290 ? 99.097  5.558   -6.447  1.00   55.71  ? 290 SER C CA  1 
ATOM   8051  C C   . SER C  1 290 ? 98.262  4.497   -5.709  1.00   49.94  ? 290 SER C C   1 
ATOM   8052  O O   . SER C  1 290 ? 98.641  3.331   -5.639  1.00   50.25  ? 290 SER C O   1 
ATOM   8053  C CB  . SER C  1 290 ? 100.001 6.333   -5.472  1.00   59.15  ? 290 SER C CB  1 
ATOM   8054  O OG  . SER C  1 290 ? 99.240  7.007   -4.484  1.00   58.49  ? 290 SER C OG  1 
ATOM   8055  N N   . ILE C  1 291 ? 97.128  4.903   -5.160  1.00   43.01  ? 291 ILE C N   1 
ATOM   8056  C CA  . ILE C  1 291 ? 96.251  3.962   -4.491  1.00   39.72  ? 291 ILE C CA  1 
ATOM   8057  C C   . ILE C  1 291 ? 95.570  3.046   -5.498  1.00   37.53  ? 291 ILE C C   1 
ATOM   8058  O O   . ILE C  1 291 ? 95.426  1.855   -5.276  1.00   35.34  ? 291 ILE C O   1 
ATOM   8059  C CB  . ILE C  1 291 ? 95.190  4.698   -3.650  1.00   38.34  ? 291 ILE C CB  1 
ATOM   8060  C CG1 . ILE C  1 291 ? 95.877  5.534   -2.566  1.00   39.02  ? 291 ILE C CG1 1 
ATOM   8061  C CG2 . ILE C  1 291 ? 94.207  3.703   -3.050  1.00   36.51  ? 291 ILE C CG2 1 
ATOM   8062  C CD1 . ILE C  1 291 ? 94.931  6.355   -1.732  1.00   39.88  ? 291 ILE C CD1 1 
ATOM   8063  N N   . PHE C  1 292 ? 95.134  3.627   -6.601  1.00   37.75  ? 292 PHE C N   1 
ATOM   8064  C CA  . PHE C  1 292 ? 94.479  2.869   -7.638  1.00   35.94  ? 292 PHE C CA  1 
ATOM   8065  C C   . PHE C  1 292 ? 95.381  1.732   -8.134  1.00   40.31  ? 292 PHE C C   1 
ATOM   8066  O O   . PHE C  1 292 ? 94.938  0.597   -8.284  1.00   42.98  ? 292 PHE C O   1 
ATOM   8067  C CB  . PHE C  1 292 ? 94.077  3.790   -8.788  1.00   35.65  ? 292 PHE C CB  1 
ATOM   8068  C CG  . PHE C  1 292 ? 93.514  3.064   -9.968  1.00   38.22  ? 292 PHE C CG  1 
ATOM   8069  C CD1 . PHE C  1 292 ? 92.187  2.681   -9.999  1.00   36.87  ? 292 PHE C CD1 1 
ATOM   8070  C CD2 . PHE C  1 292 ? 94.323  2.723   -11.037 1.00   43.60  ? 292 PHE C CD2 1 
ATOM   8071  C CE1 . PHE C  1 292 ? 91.673  1.976   -11.099 1.00   39.01  ? 292 PHE C CE1 1 
ATOM   8072  C CE2 . PHE C  1 292 ? 93.811  2.024   -12.124 1.00   46.72  ? 292 PHE C CE2 1 
ATOM   8073  C CZ  . PHE C  1 292 ? 92.484  1.657   -12.145 1.00   42.78  ? 292 PHE C CZ  1 
ATOM   8074  N N   . GLU C  1 293 ? 96.655  2.026   -8.355  1.00   42.88  ? 293 GLU C N   1 
ATOM   8075  C CA  . GLU C  1 293 ? 97.573  1.052   -8.927  1.00   45.46  ? 293 GLU C CA  1 
ATOM   8076  C C   . GLU C  1 293 ? 97.712  -0.181  -8.047  1.00   43.54  ? 293 GLU C C   1 
ATOM   8077  O O   . GLU C  1 293 ? 97.629  -1.317  -8.520  1.00   44.41  ? 293 GLU C O   1 
ATOM   8078  C CB  . GLU C  1 293 ? 98.959  1.675   -9.085  1.00   53.08  ? 293 GLU C CB  1 
ATOM   8079  C CG  . GLU C  1 293 ? 99.104  2.656   -10.196 1.00   62.26  ? 293 GLU C CG  1 
ATOM   8080  C CD  . GLU C  1 293 ? 99.184  2.005   -11.544 1.00   71.54  ? 293 GLU C CD  1 
ATOM   8081  O OE1 . GLU C  1 293 ? 100.315 1.730   -12.010 1.00   76.39  ? 293 GLU C OE1 1 
ATOM   8082  O OE2 . GLU C  1 293 ? 98.109  1.789   -12.142 1.00   73.87  1 293 GLU C OE2 1 
ATOM   8083  N N   . VAL C  1 294 ? 97.872  0.055   -6.753  1.00   39.18  ? 294 VAL C N   1 
ATOM   8084  C CA  . VAL C  1 294 ? 98.079  -1.008  -5.791  1.00   34.54  ? 294 VAL C CA  1 
ATOM   8085  C C   . VAL C  1 294 ? 96.828  -1.820  -5.577  1.00   33.23  ? 294 VAL C C   1 
ATOM   8086  O O   . VAL C  1 294 ? 96.847  -3.038  -5.630  1.00   38.64  ? 294 VAL C O   1 
ATOM   8087  C CB  . VAL C  1 294 ? 98.548  -0.420  -4.453  1.00   33.57  ? 294 VAL C CB  1 
ATOM   8088  C CG1 . VAL C  1 294 ? 98.658  -1.483  -3.412  1.00   34.73  ? 294 VAL C CG1 1 
ATOM   8089  C CG2 . VAL C  1 294 ? 99.885  0.215   -4.646  1.00   34.04  ? 294 VAL C CG2 1 
ATOM   8090  N N   . PHE C  1 295 ? 95.723  -1.134  -5.383  1.00   33.20  ? 295 PHE C N   1 
ATOM   8091  C CA  . PHE C  1 295 ? 94.481  -1.804  -5.106  1.00   32.57  ? 295 PHE C CA  1 
ATOM   8092  C C   . PHE C  1 295 ? 94.024  -2.699  -6.271  1.00   36.12  ? 295 PHE C C   1 
ATOM   8093  O O   . PHE C  1 295 ? 93.649  -3.841  -6.042  1.00   40.74  ? 295 PHE C O   1 
ATOM   8094  C CB  . PHE C  1 295 ? 93.399  -0.757  -4.767  1.00   31.79  ? 295 PHE C CB  1 
ATOM   8095  C CG  . PHE C  1 295 ? 92.013  -1.330  -4.650  1.00   33.87  ? 295 PHE C CG  1 
ATOM   8096  C CD1 . PHE C  1 295 ? 91.619  -1.988  -3.499  1.00   34.93  ? 295 PHE C CD1 1 
ATOM   8097  C CD2 . PHE C  1 295 ? 91.122  -1.261  -5.711  1.00   35.29  ? 295 PHE C CD2 1 
ATOM   8098  C CE1 . PHE C  1 295 ? 90.357  -2.533  -3.387  1.00   34.92  ? 295 PHE C CE1 1 
ATOM   8099  C CE2 . PHE C  1 295 ? 89.858  -1.823  -5.616  1.00   36.66  ? 295 PHE C CE2 1 
ATOM   8100  C CZ  . PHE C  1 295 ? 89.474  -2.460  -4.450  1.00   36.23  ? 295 PHE C CZ  1 
ATOM   8101  N N   . THR C  1 296 ? 94.055  -2.212  -7.511  1.00   37.43  ? 296 THR C N   1 
ATOM   8102  C CA  . THR C  1 296 ? 93.523  -3.010  -8.619  1.00   40.53  ? 296 THR C CA  1 
ATOM   8103  C C   . THR C  1 296 ? 94.350  -4.250  -8.852  1.00   44.09  ? 296 THR C C   1 
ATOM   8104  O O   . THR C  1 296 ? 93.845  -5.268  -9.314  1.00   47.60  ? 296 THR C O   1 
ATOM   8105  C CB  . THR C  1 296 ? 93.425  -2.218  -9.924  1.00   48.13  ? 296 THR C CB  1 
ATOM   8106  O OG1 . THR C  1 296 ? 94.711  -1.726  -10.281 1.00   54.53  ? 296 THR C OG1 1 
ATOM   8107  C CG2 . THR C  1 296 ? 92.484  -1.045  -9.756  1.00   47.69  ? 296 THR C CG2 1 
ATOM   8108  N N   . GLN C  1 297 ? 95.642  -4.140  -8.585  1.00   43.40  ? 297 GLN C N   1 
ATOM   8109  C CA  . GLN C  1 297 ? 96.549  -5.256  -8.714  1.00   44.00  ? 297 GLN C CA  1 
ATOM   8110  C C   . GLN C  1 297 ? 96.323  -6.245  -7.569  1.00   43.32  ? 297 GLN C C   1 
ATOM   8111  O O   . GLN C  1 297 ? 96.275  -7.447  -7.796  1.00   45.67  ? 297 GLN C O   1 
ATOM   8112  C CB  . GLN C  1 297 ? 97.991  -4.751  -8.750  1.00   50.23  ? 297 GLN C CB  1 
ATOM   8113  C CG  . GLN C  1 297 ? 99.084  -5.801  -8.993  1.00   59.42  ? 297 GLN C CG  1 
ATOM   8114  C CD  . GLN C  1 297 ? 98.946  -6.555  -10.317 1.00   67.42  ? 297 GLN C CD  1 
ATOM   8115  O OE1 . GLN C  1 297 ? 98.858  -5.948  -11.385 1.00   73.09  ? 297 GLN C OE1 1 
ATOM   8116  N NE2 . GLN C  1 297 ? 98.999  -7.888  -10.251 1.00   67.77  ? 297 GLN C NE2 1 
ATOM   8117  N N   . VAL C  1 298 ? 96.196  -5.752  -6.338  1.00   40.01  ? 298 VAL C N   1 
ATOM   8118  C CA  . VAL C  1 298 ? 95.899  -6.631  -5.206  1.00   37.10  ? 298 VAL C CA  1 
ATOM   8119  C C   . VAL C  1 298 ? 94.608  -7.386  -5.468  1.00   38.40  ? 298 VAL C C   1 
ATOM   8120  O O   . VAL C  1 298 ? 94.471  -8.565  -5.159  1.00   36.81  ? 298 VAL C O   1 
ATOM   8121  C CB  . VAL C  1 298 ? 95.762  -5.854  -3.899  1.00   36.52  ? 298 VAL C CB  1 
ATOM   8122  C CG1 . VAL C  1 298 ? 95.109  -6.742  -2.817  1.00   36.23  ? 298 VAL C CG1 1 
ATOM   8123  C CG2 . VAL C  1 298 ? 97.122  -5.354  -3.454  1.00   36.59  ? 298 VAL C CG2 1 
ATOM   8124  N N   . PHE C  1 299 ? 93.648  -6.674  -6.037  1.00   42.45  ? 299 PHE C N   1 
ATOM   8125  C CA  . PHE C  1 299 ? 92.387  -7.278  -6.378  1.00   44.36  ? 299 PHE C CA  1 
ATOM   8126  C C   . PHE C  1 299 ? 92.593  -8.341  -7.441  1.00   50.12  ? 299 PHE C C   1 
ATOM   8127  O O   . PHE C  1 299 ? 92.099  -9.460  -7.307  1.00   54.66  ? 299 PHE C O   1 
ATOM   8128  C CB  . PHE C  1 299 ? 91.386  -6.231  -6.858  1.00   43.99  ? 299 PHE C CB  1 
ATOM   8129  C CG  . PHE C  1 299 ? 90.003  -6.777  -7.006  1.00   49.17  ? 299 PHE C CG  1 
ATOM   8130  C CD1 . PHE C  1 299 ? 89.605  -7.387  -8.183  1.00   55.94  ? 299 PHE C CD1 1 
ATOM   8131  C CD2 . PHE C  1 299 ? 89.111  -6.742  -5.948  1.00   46.38  ? 299 PHE C CD2 1 
ATOM   8132  C CE1 . PHE C  1 299 ? 88.334  -7.923  -8.307  1.00   58.34  ? 299 PHE C CE1 1 
ATOM   8133  C CE2 . PHE C  1 299 ? 87.845  -7.268  -6.071  1.00   48.56  ? 299 PHE C CE2 1 
ATOM   8134  C CZ  . PHE C  1 299 ? 87.455  -7.861  -7.249  1.00   54.58  ? 299 PHE C CZ  1 
ATOM   8135  N N   . ALA C  1 300 ? 93.342  -8.017  -8.488  1.00   49.88  ? 300 ALA C N   1 
ATOM   8136  C CA  . ALA C  1 300 ? 93.574  -8.977  -9.569  1.00   51.13  ? 300 ALA C CA  1 
ATOM   8137  C C   . ALA C  1 300 ? 94.219  -10.255 -9.076  1.00   54.66  ? 300 ALA C C   1 
ATOM   8138  O O   . ALA C  1 300 ? 94.014  -11.319 -9.657  1.00   59.25  ? 300 ALA C O   1 
ATOM   8139  C CB  . ALA C  1 300 ? 94.427  -8.362  -10.652 1.00   52.63  ? 300 ALA C CB  1 
ATOM   8140  N N   . ASN C  1 301 ? 95.038  -10.134 -8.034  1.00   53.27  ? 301 ASN C N   1 
ATOM   8141  C CA  . ASN C  1 301 ? 95.700  -11.280 -7.397  1.00   52.70  ? 301 ASN C CA  1 
ATOM   8142  C C   . ASN C  1 301 ? 94.766  -12.165 -6.575  1.00   50.92  ? 301 ASN C C   1 
ATOM   8143  O O   . ASN C  1 301 ? 95.138  -13.267 -6.219  1.00   52.23  ? 301 ASN C O   1 
ATOM   8144  C CB  . ASN C  1 301 ? 96.843  -10.812 -6.494  1.00   50.68  ? 301 ASN C CB  1 
ATOM   8145  C CG  . ASN C  1 301 ? 98.003  -10.223 -7.266  1.00   52.22  ? 301 ASN C CG  1 
ATOM   8146  O OD1 . ASN C  1 301 ? 98.112  -10.385 -8.483  1.00   56.09  ? 301 ASN C OD1 1 
ATOM   8147  N ND2 . ASN C  1 301 ? 98.884  -9.533  -6.553  1.00   49.39  ? 301 ASN C ND2 1 
ATOM   8148  N N   . ASN C  1 302 ? 93.590  -11.662 -6.222  1.00   50.54  ? 302 ASN C N   1 
ATOM   8149  C CA  . ASN C  1 302 ? 92.630  -12.448 -5.457  1.00   53.68  ? 302 ASN C CA  1 
ATOM   8150  C C   . ASN C  1 302 ? 91.473  -12.972 -6.340  1.00   61.18  ? 302 ASN C C   1 
ATOM   8151  O O   . ASN C  1 302 ? 90.377  -13.300 -5.857  1.00   64.79  ? 302 ASN C O   1 
ATOM   8152  C CB  . ASN C  1 302 ? 92.094  -11.608 -4.291  1.00   48.29  ? 302 ASN C CB  1 
ATOM   8153  C CG  . ASN C  1 302 ? 93.107  -11.451 -3.168  1.00   43.52  ? 302 ASN C CG  1 
ATOM   8154  O OD1 . ASN C  1 302 ? 93.126  -12.226 -2.207  1.00   42.47  ? 302 ASN C OD1 1 
ATOM   8155  N ND2 . ASN C  1 302 ? 93.954  -10.449 -3.288  1.00   37.71  ? 302 ASN C ND2 1 
ATOM   8156  N N   . MET C  1 303 ? 91.742  -13.058 -7.640  1.00   54.92  ? 303 MET C N   1 
ATOM   8157  C CA  . MET C  1 303 ? 90.763  -13.513 -8.623  1.00   55.33  ? 303 MET C CA  1 
ATOM   8158  C C   . MET C  1 303 ? 91.444  -14.419 -9.654  1.00   60.84  ? 303 MET C C   1 
ATOM   8159  O O   . MET C  1 303 ? 92.665  -14.415 -9.764  1.00   62.31  ? 303 MET C O   1 
ATOM   8160  C CB  . MET C  1 303 ? 90.078  -12.317 -9.300  1.00   48.87  ? 303 MET C CB  1 
ATOM   8161  C CG  . MET C  1 303 ? 89.161  -11.516 -8.386  1.00   43.04  ? 303 MET C CG  1 
ATOM   8162  S SD  . MET C  1 303 ? 87.725  -12.509 -7.935  1.00   61.44  ? 303 MET C SD  1 
ATOM   8163  C CE  . MET C  1 303 ? 86.778  -12.431 -9.439  1.00   58.72  ? 303 MET C CE  1 
ATOM   8164  N N   . PRO C  1 304 ? 90.662  -15.212 -10.399 1.00   63.97  ? 304 PRO C N   1 
ATOM   8165  C CA  . PRO C  1 304 ? 91.255  -16.013 -11.475 1.00   65.45  ? 304 PRO C CA  1 
ATOM   8166  C C   . PRO C  1 304 ? 91.794  -15.105 -12.568 1.00   62.72  ? 304 PRO C C   1 
ATOM   8167  O O   . PRO C  1 304 ? 91.010  -14.418 -13.227 1.00   57.95  ? 304 PRO C O   1 
ATOM   8168  C CB  . PRO C  1 304 ? 90.086  -16.865 -11.968 1.00   68.08  ? 304 PRO C CB  1 
ATOM   8169  C CG  . PRO C  1 304 ? 88.876  -16.116 -11.539 1.00   67.83  ? 304 PRO C CG  1 
ATOM   8170  C CD  . PRO C  1 304 ? 89.226  -15.476 -10.243 1.00   65.35  ? 304 PRO C CD  1 
ATOM   8171  N N   . LYS C  1 305 ? 93.119  -15.098 -12.731 1.00   65.14  ? 305 LYS C N   1 
ATOM   8172  C CA  . LYS C  1 305 ? 93.797  -14.180 -13.640 1.00   64.05  ? 305 LYS C CA  1 
ATOM   8173  C C   . LYS C  1 305 ? 93.465  -14.414 -15.089 1.00   67.52  ? 305 LYS C C   1 
ATOM   8174  O O   . LYS C  1 305 ? 93.637  -13.519 -15.918 1.00   68.88  ? 305 LYS C O   1 
ATOM   8175  C CB  . LYS C  1 305 ? 95.320  -14.257 -13.451 0.0000 63.06  ? 305 LYS C CB  1 
ATOM   8176  C CG  . LYS C  1 305 ? 95.775  -13.549 -12.202 0.0000 58.15  ? 305 LYS C CG  1 
ATOM   8177  C CD  . LYS C  1 305 ? 97.288  -13.525 -12.096 0.0000 58.71  ? 305 LYS C CD  1 
ATOM   8178  C CE  . LYS C  1 305 ? 97.724  -12.800 -10.826 0.0000 55.48  ? 305 LYS C CE  1 
ATOM   8179  N NZ  . LYS C  1 305 ? 97.268  -11.381 -10.814 0.0000 51.54  ? 305 LYS C NZ  1 
ATOM   8180  N N   . GLN C  1 306 ? 93.046  -15.628 -15.411 1.00   69.21  ? 306 GLN C N   1 
ATOM   8181  C CA  . GLN C  1 306 ? 92.685  -15.895 -16.784 1.00   71.51  ? 306 GLN C CA  1 
ATOM   8182  C C   . GLN C  1 306 ? 91.174  -15.877 -16.925 1.00   71.13  ? 306 GLN C C   1 
ATOM   8183  O O   . GLN C  1 306 ? 90.622  -16.611 -17.727 1.00   76.09  ? 306 GLN C O   1 
ATOM   8184  C CB  . GLN C  1 306 ? 93.304  -17.194 -17.284 0.0000 74.51  ? 306 GLN C CB  1 
ATOM   8185  C CG  . GLN C  1 306 ? 94.666  -17.423 -16.645 0.0000 73.26  ? 306 GLN C CG  1 
ATOM   8186  C CD  . GLN C  1 306 ? 95.788  -16.539 -17.217 0.0000 71.35  ? 306 GLN C CD  1 
ATOM   8187  O OE1 . GLN C  1 306 ? 95.531  -15.557 -17.913 0.0000 69.22  ? 306 GLN C OE1 1 
ATOM   8188  N NE2 . GLN C  1 306 ? 97.042  -16.916 -16.943 0.0000 72.95  ? 306 GLN C NE2 1 
ATOM   8189  N N   . ALA C  1 307 ? 90.516  -15.115 -16.060 1.00   66.98  ? 307 ALA C N   1 
ATOM   8190  C CA  . ALA C  1 307 ? 89.100  -14.859 -16.161 1.00   65.64  ? 307 ALA C CA  1 
ATOM   8191  C C   . ALA C  1 307 ? 88.918  -13.430 -16.590 1.00   64.47  ? 307 ALA C C   1 
ATOM   8192  O O   . ALA C  1 307 ? 87.800  -13.009 -16.871 1.00   64.85  ? 307 ALA C O   1 
ATOM   8193  C CB  . ALA C  1 307 ? 88.417  -15.116 -14.819 1.00   62.00  ? 307 ALA C CB  1 
ATOM   8194  N N   . GLN C  1 308 ? 90.038  -12.711 -16.634 1.00   63.68  ? 308 GLN C N   1 
ATOM   8195  C CA  . GLN C  1 308 ? 90.054  -11.304 -16.975 1.00   63.07  ? 308 GLN C CA  1 
ATOM   8196  C C   . GLN C  1 308 ? 89.745  -11.096 -18.446 1.00   66.68  ? 308 GLN C C   1 
ATOM   8197  O O   . GLN C  1 308 ? 90.036  -11.952 -19.264 1.00   71.80  ? 308 GLN C O   1 
ATOM   8198  C CB  . GLN C  1 308 ? 91.413  -10.700 -16.648 1.00   63.14  ? 308 GLN C CB  1 
ATOM   8199  C CG  . GLN C  1 308 ? 91.866  -10.935 -15.220 1.00   63.96  ? 308 GLN C CG  1 
ATOM   8200  C CD  . GLN C  1 308 ? 93.200  -10.297 -14.898 1.00   66.97  ? 308 GLN C CD  1 
ATOM   8201  O OE1 . GLN C  1 308 ? 93.792  -9.624  -15.739 1.00   69.83  ? 308 GLN C OE1 1 
ATOM   8202  N NE2 . GLN C  1 308 ? 93.676  -10.493 -13.666 1.00   65.96  ? 308 GLN C NE2 1 
ATOM   8203  N N   . VAL C  1 309 ? 89.147  -9.952  -18.768 1.00   64.99  ? 309 VAL C N   1 
ATOM   8204  C CA  . VAL C  1 309 ? 88.841  -9.550  -20.143 1.00   65.12  ? 309 VAL C CA  1 
ATOM   8205  C C   . VAL C  1 309 ? 89.305  -8.124  -20.345 1.00   62.80  ? 309 VAL C C   1 
ATOM   8206  O O   . VAL C  1 309 ? 89.579  -7.427  -19.364 1.00   59.79  ? 309 VAL C O   1 
ATOM   8207  C CB  . VAL C  1 309 ? 87.344  -9.643  -20.457 1.00   66.88  ? 309 VAL C CB  1 
ATOM   8208  C CG1 . VAL C  1 309 ? 86.852  -11.067 -20.268 1.00   71.09  ? 309 VAL C CG1 1 
ATOM   8209  C CG2 . VAL C  1 309 ? 86.563  -8.677  -19.580 1.00   63.67  ? 309 VAL C CG2 1 
ATOM   8210  N N   . LYS C  1 310 ? 89.391  -7.688  -21.600 1.00   66.31  ? 310 LYS C N   1 
ATOM   8211  C CA  . LYS C  1 310 ? 89.723  -6.297  -21.866 1.00   67.96  ? 310 LYS C CA  1 
ATOM   8212  C C   . LYS C  1 310 ? 88.804  -5.410  -21.073 1.00   65.20  ? 310 LYS C C   1 
ATOM   8213  O O   . LYS C  1 310 ? 87.579  -5.565  -21.126 1.00   65.99  ? 310 LYS C O   1 
ATOM   8214  C CB  . LYS C  1 310 ? 89.583  -5.901  -23.339 1.00   74.73  ? 310 LYS C CB  1 
ATOM   8215  C CG  . LYS C  1 310 ? 90.056  -4.448  -23.575 1.00   77.10  ? 310 LYS C CG  1 
ATOM   8216  C CD  . LYS C  1 310 ? 89.937  -3.938  -25.012 1.00   81.23  ? 310 LYS C CD  1 
ATOM   8217  C CE  . LYS C  1 310 ? 88.486  -3.653  -25.406 1.00   82.45  ? 310 LYS C CE  1 
ATOM   8218  N NZ  . LYS C  1 310 ? 88.416  -2.969  -26.726 1.00   88.98  ? 310 LYS C NZ  1 
ATOM   8219  N N   . ALA C  1 311 ? 89.403  -4.540  -20.275 1.00   63.32  ? 311 ALA C N   1 
ATOM   8220  C CA  . ALA C  1 311 ? 88.653  -3.542  -19.529 1.00   62.05  ? 311 ALA C CA  1 
ATOM   8221  C C   . ALA C  1 311 ? 87.903  -2.620  -20.497 1.00   64.42  ? 311 ALA C C   1 
ATOM   8222  O O   . ALA C  1 311 ? 88.399  -2.293  -21.584 1.00   64.75  ? 311 ALA C O   1 
ATOM   8223  C CB  . ALA C  1 311 ? 89.568  -2.747  -18.623 1.00   60.67  ? 311 ALA C CB  1 
ATOM   8224  N N   . VAL C  1 312 ? 86.707  -2.206  -20.096 1.00   65.81  ? 312 VAL C N   1 
ATOM   8225  C CA  . VAL C  1 312 ? 85.842  -1.395  -20.946 1.00   69.47  ? 312 VAL C CA  1 
ATOM   8226  C C   . VAL C  1 312 ? 85.319  -0.213  -20.135 1.00   65.75  ? 312 VAL C C   1 
ATOM   8227  O O   . VAL C  1 312 ? 85.212  -0.294  -18.908 1.00   60.12  ? 312 VAL C O   1 
ATOM   8228  C CB  . VAL C  1 312 ? 84.658  -2.221  -21.539 1.00   83.92  ? 312 VAL C CB  1 
ATOM   8229  C CG1 . VAL C  1 312 ? 85.166  -3.317  -22.470 1.00   89.44  ? 312 VAL C CG1 1 
ATOM   8230  C CG2 . VAL C  1 312 ? 83.808  -2.818  -20.441 1.00   78.75  ? 312 VAL C CG2 1 
ATOM   8231  N N   . GLY C  1 313 ? 85.063  0.904   -20.813 1.00   68.29  ? 313 GLY C N   1 
ATOM   8232  C CA  . GLY C  1 313 ? 84.522  2.074   -20.152 1.00   64.82  ? 313 GLY C CA  1 
ATOM   8233  C C   . GLY C  1 313 ? 85.588  2.766   -19.326 1.00   60.02  ? 313 GLY C C   1 
ATOM   8234  O O   . GLY C  1 313 ? 86.741  2.865   -19.741 1.00   59.76  ? 313 GLY C O   1 
ATOM   8235  N N   . PRO C  1 314 ? 85.200  3.263   -18.146 1.00   57.78  ? 314 PRO C N   1 
ATOM   8236  C CA  . PRO C  1 314 ? 86.131  3.938   -17.239 1.00   56.59  ? 314 PRO C CA  1 
ATOM   8237  C C   . PRO C  1 314 ? 86.925  2.969   -16.368 1.00   55.48  ? 314 PRO C C   1 
ATOM   8238  O O   . PRO C  1 314 ? 87.844  3.394   -15.668 1.00   55.74  ? 314 PRO C O   1 
ATOM   8239  C CB  . PRO C  1 314 ? 85.194  4.771   -16.360 1.00   54.68  ? 314 PRO C CB  1 
ATOM   8240  C CG  . PRO C  1 314 ? 83.952  3.915   -16.267 1.00   53.75  ? 314 PRO C CG  1 
ATOM   8241  C CD  . PRO C  1 314 ? 83.823  3.242   -17.611 1.00   57.86  ? 314 PRO C CD  1 
ATOM   8242  N N   . PHE C  1 315 ? 86.595  1.683   -16.446 1.00   55.14  ? 315 PHE C N   1 
ATOM   8243  C CA  . PHE C  1 315 ? 87.117  0.700   -15.507 1.00   53.19  ? 315 PHE C CA  1 
ATOM   8244  C C   . PHE C  1 315 ? 88.420  0.140   -15.981 1.00   57.21  ? 315 PHE C C   1 
ATOM   8245  O O   . PHE C  1 315 ? 88.680  0.100   -17.180 1.00   61.88  ? 315 PHE C O   1 
ATOM   8246  C CB  . PHE C  1 315 ? 86.126  -0.441  -15.320 1.00   52.15  ? 315 PHE C CB  1 
ATOM   8247  C CG  . PHE C  1 315 ? 84.774  0.012   -14.901 1.00   50.82  ? 315 PHE C CG  1 
ATOM   8248  C CD1 . PHE C  1 315 ? 84.587  0.617   -13.669 1.00   47.01  ? 315 PHE C CD1 1 
ATOM   8249  C CD2 . PHE C  1 315 ? 83.691  -0.138  -15.746 1.00   53.92  ? 315 PHE C CD2 1 
ATOM   8250  C CE1 . PHE C  1 315 ? 83.349  1.047   -13.287 1.00   46.99  ? 315 PHE C CE1 1 
ATOM   8251  C CE2 . PHE C  1 315 ? 82.447  0.297   -15.365 1.00   55.89  ? 315 PHE C CE2 1 
ATOM   8252  C CZ  . PHE C  1 315 ? 82.276  0.890   -14.134 1.00   52.52  ? 315 PHE C CZ  1 
ATOM   8253  N N   . GLY C  1 316 ? 89.221  -0.334  -15.037 1.00   55.33  ? 316 GLY C N   1 
ATOM   8254  C CA  . GLY C  1 316 ? 90.542  -0.836  -15.357 1.00   54.85  ? 316 GLY C CA  1 
ATOM   8255  C C   . GLY C  1 316 ? 90.697  -2.341  -15.300 1.00   52.76  ? 316 GLY C C   1 
ATOM   8256  O O   . GLY C  1 316 ? 91.622  -2.912  -15.874 1.00   52.68  ? 316 GLY C O   1 
ATOM   8257  N N   . LEU C  1 317 ? 89.779  -2.992  -14.610 1.00   50.36  ? 317 LEU C N   1 
ATOM   8258  C CA  . LEU C  1 317 ? 89.890  -4.416  -14.420 1.00   48.98  ? 317 LEU C CA  1 
ATOM   8259  C C   . LEU C  1 317 ? 88.530  -5.056  -14.642 1.00   52.06  ? 317 LEU C C   1 
ATOM   8260  O O   . LEU C  1 317 ? 87.613  -4.902  -13.835 1.00   51.36  ? 317 LEU C O   1 
ATOM   8261  C CB  . LEU C  1 317 ? 90.424  -4.698  -13.023 1.00   45.38  ? 317 LEU C CB  1 
ATOM   8262  C CG  . LEU C  1 317 ? 90.692  -6.129  -12.630 1.00   45.08  ? 317 LEU C CG  1 
ATOM   8263  C CD1 . LEU C  1 317 ? 91.689  -6.700  -13.602 1.00   46.62  ? 317 LEU C CD1 1 
ATOM   8264  C CD2 . LEU C  1 317 ? 91.238  -6.138  -11.221 1.00   44.15  ? 317 LEU C CD2 1 
ATOM   8265  N N   . CYS C  1 318 ? 88.388  -5.744  -15.767 1.00   55.58  ? 318 CYS C N   1 
ATOM   8266  C CA  . CYS C  1 318 ? 87.120  -6.366  -16.097 1.00   57.09  ? 318 CYS C CA  1 
ATOM   8267  C C   . CYS C  1 318 ? 87.283  -7.837  -16.326 1.00   56.85  ? 318 CYS C C   1 
ATOM   8268  O O   . CYS C  1 318 ? 88.351  -8.299  -16.713 1.00   57.69  ? 318 CYS C O   1 
ATOM   8269  C CB  . CYS C  1 318 ? 86.507  -5.708  -17.315 1.00   60.29  ? 318 CYS C CB  1 
ATOM   8270  S SG  . CYS C  1 318 ? 86.110  -4.026  -16.944 1.00   59.17  ? 318 CYS C SG  1 
ATOM   8271  N N   . TYR C  1 319 ? 86.206  -8.566  -16.081 1.00   57.58  ? 319 TYR C N   1 
ATOM   8272  C CA  . TYR C  1 319 ? 86.214  -10.011 -16.187 1.00   59.33  ? 319 TYR C CA  1 
ATOM   8273  C C   . TYR C  1 319 ? 85.107  -10.531 -17.071 1.00   64.65  ? 319 TYR C C   1 
ATOM   8274  O O   . TYR C  1 319 ? 84.161  -9.803  -17.374 1.00   66.34  ? 319 TYR C O   1 
ATOM   8275  C CB  . TYR C  1 319 ? 86.066  -10.637 -14.800 1.00   58.28  ? 319 TYR C CB  1 
ATOM   8276  C CG  . TYR C  1 319 ? 87.242  -10.421 -13.881 1.00   56.87  ? 319 TYR C CG  1 
ATOM   8277  C CD1 . TYR C  1 319 ? 87.348  -9.272  -13.106 1.00   52.13  ? 319 TYR C CD1 1 
ATOM   8278  C CD2 . TYR C  1 319 ? 88.247  -11.376 -13.783 1.00   61.16  ? 319 TYR C CD2 1 
ATOM   8279  C CE1 . TYR C  1 319 ? 88.425  -9.077  -12.266 1.00   51.32  ? 319 TYR C CE1 1 
ATOM   8280  C CE2 . TYR C  1 319 ? 89.319  -11.195 -12.952 1.00   61.23  ? 319 TYR C CE2 1 
ATOM   8281  C CZ  . TYR C  1 319 ? 89.411  -10.043 -12.195 1.00   57.86  ? 319 TYR C CZ  1 
ATOM   8282  O OH  . TYR C  1 319 ? 90.500  -9.877  -11.368 1.00   59.06  ? 319 TYR C OH  1 
ATOM   8283  N N   . ASP C  1 320 ? 85.245  -11.789 -17.499 1.00   68.84  ? 320 ASP C N   1 
ATOM   8284  C CA  . ASP C  1 320 ? 84.129  -12.506 -18.101 1.00   73.85  ? 320 ASP C CA  1 
ATOM   8285  C C   . ASP C  1 320 ? 83.167  -12.854 -16.956 1.00   71.54  ? 320 ASP C C   1 
ATOM   8286  O O   . ASP C  1 320 ? 83.544  -13.501 -15.974 1.00   68.11  ? 320 ASP C O   1 
ATOM   8287  C CB  . ASP C  1 320 ? 84.620  -13.754 -18.843 1.00   80.13  ? 320 ASP C CB  1 
ATOM   8288  C CG  . ASP C  1 320 ? 83.505  -14.729 -19.160 1.00   86.03  ? 320 ASP C CG  1 
ATOM   8289  O OD1 . ASP C  1 320 ? 82.448  -14.301 -19.678 1.00   89.51  ? 320 ASP C OD1 1 
ATOM   8290  O OD2 . ASP C  1 320 ? 83.700  -15.932 -18.893 1.00   87.99  ? 320 ASP C OD2 1 
ATOM   8291  N N   . SER C  1 321 ? 81.908  -12.478 -17.125 1.00   73.46  ? 321 SER C N   1 
ATOM   8292  C CA  . SER C  1 321 ? 80.932  -12.561 -16.050 1.00   75.43  ? 321 SER C CA  1 
ATOM   8293  C C   . SER C  1 321 ? 80.576  -14.024 -15.733 1.00   82.17  ? 321 SER C C   1 
ATOM   8294  O O   . SER C  1 321 ? 80.052  -14.325 -14.663 1.00   84.23  ? 321 SER C O   1 
ATOM   8295  C CB  . SER C  1 321 ? 79.700  -11.714 -16.407 1.00   78.07  ? 321 SER C CB  1 
ATOM   8296  O OG  . SER C  1 321 ? 78.723  -11.719 -15.387 1.00   79.40  ? 321 SER C OG  1 
ATOM   8297  N N   . ARG C  1 322 ? 80.845  -14.922 -16.679 1.00   86.15  ? 322 ARG C N   1 
ATOM   8298  C CA  . ARG C  1 322 ? 80.577  -16.356 -16.516 1.00   91.75  ? 322 ARG C CA  1 
ATOM   8299  C C   . ARG C  1 322 ? 81.573  -17.089 -15.589 1.00   92.00  ? 322 ARG C C   1 
ATOM   8300  O O   . ARG C  1 322 ? 81.171  -17.960 -14.810 1.00   96.39  ? 322 ARG C O   1 
ATOM   8301  C CB  . ARG C  1 322 ? 80.572  -17.022 -17.899 0.0000 95.49  ? 322 ARG C CB  1 
ATOM   8302  C CG  . ARG C  1 322 ? 79.615  -18.197 -18.071 0.0000 101.81 ? 322 ARG C CG  1 
ATOM   8303  C CD  . ARG C  1 322 ? 79.498  -18.550 -19.555 0.0000 106.12 ? 322 ARG C CD  1 
ATOM   8304  N NE  . ARG C  1 322 ? 78.836  -19.829 -19.801 0.0000 112.63 ? 322 ARG C NE  1 
ATOM   8305  C CZ  . ARG C  1 322 ? 78.457  -20.248 -21.005 0.0000 117.74 ? 322 ARG C CZ  1 
ATOM   8306  N NH1 . ARG C  1 322 ? 77.859  -21.423 -21.146 0.0000 124.72 ? 322 ARG C NH1 1 
ATOM   8307  N NH2 . ARG C  1 322 ? 78.670  -19.487 -22.070 0.0000 116.70 ? 322 ARG C NH2 1 
ATOM   8308  N N   . LYS C  1 323 ? 82.858  -16.739 -15.683 1.00   86.72  ? 323 LYS C N   1 
ATOM   8309  C CA  . LYS C  1 323 ? 83.929  -17.370 -14.897 1.00   84.00  ? 323 LYS C CA  1 
ATOM   8310  C C   . LYS C  1 323 ? 84.045  -16.815 -13.476 1.00   82.79  ? 323 LYS C C   1 
ATOM   8311  O O   . LYS C  1 323 ? 84.366  -17.537 -12.532 1.00   84.42  ? 323 LYS C O   1 
ATOM   8312  C CB  . LYS C  1 323 ? 85.254  -17.220 -15.639 0.0000 80.49  ? 323 LYS C CB  1 
ATOM   8313  C CG  . LYS C  1 323 ? 85.198  -17.850 -17.012 0.0000 83.99  ? 323 LYS C CG  1 
ATOM   8314  C CD  . LYS C  1 323 ? 86.512  -17.771 -17.747 0.0000 82.48  ? 323 LYS C CD  1 
ATOM   8315  C CE  . LYS C  1 323 ? 86.261  -17.820 -19.252 0.0000 85.56  ? 323 LYS C CE  1 
ATOM   8316  N NZ  . LYS C  1 323 ? 87.083  -16.826 -19.999 0.0000 83.01  ? 323 LYS C NZ  1 
ATOM   8317  N N   . ILE C  1 324 ? 83.770  -15.528 -13.325 1.00   82.27  ? 324 ILE C N   1 
ATOM   8318  C CA  . ILE C  1 324 ? 83.745  -14.929 -12.006 1.00   80.16  ? 324 ILE C CA  1 
ATOM   8319  C C   . ILE C  1 324 ? 82.293  -15.060 -11.610 1.00   86.20  ? 324 ILE C C   1 
ATOM   8320  O O   . ILE C  1 324 ? 81.406  -14.840 -12.427 1.00   91.06  ? 324 ILE C O   1 
ATOM   8321  C CB  . ILE C  1 324 ? 84.231  -13.465 -11.995 0.0000 74.64  ? 324 ILE C CB  1 
ATOM   8322  C CG1 . ILE C  1 324 ? 83.143  -12.507 -12.498 0.0000 74.10  ? 324 ILE C CG1 1 
ATOM   8323  C CG2 . ILE C  1 324 ? 85.494  -13.341 -12.812 0.0000 73.46  ? 324 ILE C CG2 1 
ATOM   8324  C CD1 . ILE C  1 324 ? 83.462  -11.049 -12.308 0.0000 69.46  ? 324 ILE C CD1 1 
ATOM   8325  N N   . SER C  1 325 ? 82.045  -15.508 -10.388 1.00   86.50  ? 325 SER C N   1 
ATOM   8326  C CA  . SER C  1 325 ? 80.675  -15.689 -9.911  1.00   88.38  ? 325 SER C CA  1 
ATOM   8327  C C   . SER C  1 325 ? 80.678  -16.081 -8.452  1.00   89.65  ? 325 SER C C   1 
ATOM   8328  O O   . SER C  1 325 ? 80.586  -15.224 -7.590  1.00   87.91  ? 325 SER C O   1 
ATOM   8329  C CB  . SER C  1 325 ? 79.949  -16.741 -10.725 1.00   90.29  ? 325 SER C CB  1 
ATOM   8330  O OG  . SER C  1 325 ? 79.564  -16.205 -11.977 1.00   88.78  ? 325 SER C OG  1 
ATOM   8331  N N   . GLY C  1 326 ? 80.770  -17.376 -8.176  1.00   92.01  ? 326 GLY C N   1 
ATOM   8332  C CA  . GLY C  1 326 ? 81.045  -17.817 -6.823  1.00   91.01  ? 326 GLY C CA  1 
ATOM   8333  C C   . GLY C  1 326 ? 82.540  -18.067 -6.807  1.00   86.77  ? 326 GLY C C   1 
ATOM   8334  O O   . GLY C  1 326 ? 82.972  -19.144 -7.218  1.00   90.87  ? 326 GLY C O   1 
ATOM   8335  N N   . GLY C  1 327 ? 83.342  -17.073 -6.413  1.00   77.60  ? 327 GLY C N   1 
ATOM   8336  C CA  . GLY C  1 327 ? 82.863  -15.779 -5.953  1.00   70.66  ? 327 GLY C CA  1 
ATOM   8337  C C   . GLY C  1 327 ? 83.846  -14.627 -6.130  1.00   62.56  ? 327 GLY C C   1 
ATOM   8338  O O   . GLY C  1 327 ? 84.899  -14.781 -6.755  1.00   63.46  ? 327 GLY C O   1 
ATOM   8339  N N   . ALA C  1 328 ? 83.453  -13.454 -5.639  1.00   57.18  ? 328 ALA C N   1 
ATOM   8340  C CA  . ALA C  1 328 ? 84.315  -12.269 -5.543  1.00   52.32  ? 328 ALA C CA  1 
ATOM   8341  C C   . ALA C  1 328 ? 84.906  -12.185 -4.128  1.00   54.06  ? 328 ALA C C   1 
ATOM   8342  O O   . ALA C  1 328 ? 84.345  -12.752 -3.187  1.00   61.07  ? 328 ALA C O   1 
ATOM   8343  C CB  . ALA C  1 328 ? 83.554  -11.006 -5.892  1.00   50.15  ? 328 ALA C CB  1 
ATOM   8344  N N   . PRO C  1 329 ? 86.061  -11.533 -3.969  1.00   49.93  ? 329 PRO C N   1 
ATOM   8345  C CA  . PRO C  1 329 ? 86.674  -11.552 -2.634  1.00   50.09  ? 329 PRO C CA  1 
ATOM   8346  C C   . PRO C  1 329 ? 86.026  -10.588 -1.642  1.00   47.86  ? 329 PRO C C   1 
ATOM   8347  O O   . PRO C  1 329 ? 85.266  -9.725  -2.076  1.00   47.92  ? 329 PRO C O   1 
ATOM   8348  C CB  . PRO C  1 329 ? 88.120  -11.133 -2.910  1.00   48.78  ? 329 PRO C CB  1 
ATOM   8349  C CG  . PRO C  1 329 ? 88.067  -10.365 -4.159  1.00   45.89  ? 329 PRO C CG  1 
ATOM   8350  C CD  . PRO C  1 329 ? 86.930  -10.911 -4.977  1.00   47.22  ? 329 PRO C CD  1 
ATOM   8351  N N   . SER C  1 330 ? 86.289  -10.765 -0.340  1.00   48.74  ? 330 SER C N   1 
ATOM   8352  C CA  . SER C  1 330 ? 85.914  -9.786  0.702   1.00   48.43  ? 330 SER C CA  1 
ATOM   8353  C C   . SER C  1 330 ? 86.593  -8.437  0.498   1.00   43.85  ? 330 SER C C   1 
ATOM   8354  O O   . SER C  1 330 ? 87.817  -8.363  0.543   1.00   41.90  ? 330 SER C O   1 
ATOM   8355  C CB  . SER C  1 330 ? 86.271  -10.289 2.103   1.00   50.15  ? 330 SER C CB  1 
ATOM   8356  O OG  . SER C  1 330 ? 85.934  -11.648 2.253   1.00   55.57  ? 330 SER C OG  1 
ATOM   8357  N N   . VAL C  1 331 ? 85.799  -7.379  0.327   1.00   43.09  ? 331 VAL C N   1 
ATOM   8358  C CA  . VAL C  1 331 ? 86.308  -6.002  0.288   1.00   42.16  ? 331 VAL C CA  1 
ATOM   8359  C C   . VAL C  1 331 ? 85.745  -5.124  1.403   1.00   40.07  ? 331 VAL C C   1 
ATOM   8360  O O   . VAL C  1 331 ? 84.542  -4.936  1.483   1.00   43.48  ? 331 VAL C O   1 
ATOM   8361  C CB  . VAL C  1 331 ? 85.989  -5.312  -1.022  1.00   40.76  ? 331 VAL C CB  1 
ATOM   8362  C CG1 . VAL C  1 331 ? 86.550  -3.905  -0.981  1.00   38.61  ? 331 VAL C CG1 1 
ATOM   8363  C CG2 . VAL C  1 331 ? 86.589  -6.084  -2.160  1.00   44.29  ? 331 VAL C CG2 1 
ATOM   8364  N N   . ASP C  1 332 ? 86.614  -4.669  2.299   1.00   34.20  ? 332 ASP C N   1 
ATOM   8365  C CA  . ASP C  1 332 ? 86.218  -3.905  3.470   1.00   30.27  ? 332 ASP C CA  1 
ATOM   8366  C C   . ASP C  1 332 ? 87.046  -2.637  3.610   1.00   29.20  ? 332 ASP C C   1 
ATOM   8367  O O   . ASP C  1 332 ? 88.241  -2.643  3.371   1.00   30.29  ? 332 ASP C O   1 
ATOM   8368  C CB  . ASP C  1 332 ? 86.359  -4.732  4.764   1.00   35.83  ? 332 ASP C CB  1 
ATOM   8369  C CG  . ASP C  1 332 ? 85.543  -6.046  4.763   1.00   40.07  ? 332 ASP C CG  1 
ATOM   8370  O OD1 . ASP C  1 332 ? 84.503  -6.150  4.084   1.00   42.33  ? 332 ASP C OD1 1 
ATOM   8371  O OD2 . ASP C  1 332 ? 85.947  -6.997  5.468   1.00   43.27  ? 332 ASP C OD2 1 
ATOM   8372  N N   . LEU C  1 333 ? 86.400  -1.555  4.012   1.00   31.33  ? 333 LEU C N   1 
ATOM   8373  C CA  . LEU C  1 333 ? 87.087  -0.362  4.447   1.00   27.15  ? 333 LEU C CA  1 
ATOM   8374  C C   . LEU C  1 333 ? 87.326  -0.501  5.910   1.00   32.47  ? 333 LEU C C   1 
ATOM   8375  O O   . LEU C  1 333 ? 86.393  -0.654  6.689   1.00   27.56  ? 333 LEU C O   1 
ATOM   8376  C CB  . LEU C  1 333 ? 86.284  0.891   4.188   1.00   26.15  ? 333 LEU C CB  1 
ATOM   8377  C CG  . LEU C  1 333 ? 85.795  1.065   2.758   1.00   27.55  ? 333 LEU C CG  1 
ATOM   8378  C CD1 . LEU C  1 333 ? 85.003  2.360   2.626   1.00   30.48  ? 333 LEU C CD1 1 
ATOM   8379  C CD2 . LEU C  1 333 ? 86.966  1.053   1.803   1.00   27.15  ? 333 LEU C CD2 1 
ATOM   8380  N N   . ILE C  1 334 ? 88.595  -0.455  6.272   1.00   33.72  ? 334 ILE C N   1 
ATOM   8381  C CA  . ILE C  1 334 ? 89.001  -0.496  7.664   1.00   35.37  ? 334 ILE C CA  1 
ATOM   8382  C C   . ILE C  1 334 ? 89.048  0.909   8.275   1.00   32.96  ? 334 ILE C C   1 
ATOM   8383  O O   . ILE C  1 334 ? 89.712  1.812   7.785   1.00   30.42  ? 334 ILE C O   1 
ATOM   8384  C CB  . ILE C  1 334 ? 90.364  -1.197  7.814   1.00   37.94  ? 334 ILE C CB  1 
ATOM   8385  C CG1 . ILE C  1 334 ? 90.380  -2.535  7.049   1.00   39.89  ? 334 ILE C CG1 1 
ATOM   8386  C CG2 . ILE C  1 334 ? 90.666  -1.451  9.284   1.00   41.68  ? 334 ILE C CG2 1 
ATOM   8387  C CD1 . ILE C  1 334 ? 89.338  -3.553  7.502   1.00   33.79  ? 334 ILE C CD1 1 
ATOM   8388  N N   . LEU C  1 335 ? 88.277  1.090   9.328   1.00   33.92  ? 335 LEU C N   1 
ATOM   8389  C CA  . LEU C  1 335 ? 88.084  2.396   9.889   1.00   34.44  ? 335 LEU C CA  1 
ATOM   8390  C C   . LEU C  1 335 ? 88.967  2.527   11.118  1.00   40.18  ? 335 LEU C C   1 
ATOM   8391  O O   . LEU C  1 335 ? 89.184  1.539   11.812  1.00   45.68  ? 335 LEU C O   1 
ATOM   8392  C CB  . LEU C  1 335 ? 86.619  2.574   10.236  1.00   33.81  ? 335 LEU C CB  1 
ATOM   8393  C CG  . LEU C  1 335 ? 85.723  2.290   9.040   1.00   33.03  ? 335 LEU C CG  1 
ATOM   8394  C CD1 . LEU C  1 335 ? 84.299  2.438   9.446   1.00   36.60  ? 335 LEU C CD1 1 
ATOM   8395  C CD2 . LEU C  1 335 ? 86.030  3.243   7.900   1.00   30.75  ? 335 LEU C CD2 1 
ATOM   8396  N N   . ASP C  1 336 ? 89.529  3.707   11.353  1.00   42.72  ? 336 ASP C N   1 
ATOM   8397  C CA  . ASP C  1 336 ? 90.446  3.912   12.481  1.00   47.69  ? 336 ASP C CA  1 
ATOM   8398  C C   . ASP C  1 336 ? 89.818  3.634   13.835  1.00   48.00  ? 336 ASP C C   1 
ATOM   8399  O O   . ASP C  1 336 ? 88.694  4.065   14.100  1.00   44.02  ? 336 ASP C O   1 
ATOM   8400  C CB  . ASP C  1 336 ? 91.036  5.326   12.501  1.00   53.13  ? 336 ASP C CB  1 
ATOM   8401  C CG  . ASP C  1 336 ? 92.128  5.497   13.582  1.00   60.38  ? 336 ASP C CG  1 
ATOM   8402  O OD1 . ASP C  1 336 ? 93.005  4.611   13.732  1.00   60.13  ? 336 ASP C OD1 1 
ATOM   8403  O OD2 . ASP C  1 336 ? 92.098  6.516   14.300  1.00   65.88  ? 336 ASP C OD2 1 
ATOM   8404  N N   . LYS C  1 337 ? 90.543  2.876   14.660  1.00   57.18  ? 337 LYS C N   1 
ATOM   8405  C CA  . LYS C  1 337 ? 90.184  2.668   16.063  1.00   65.80  ? 337 LYS C CA  1 
ATOM   8406  C C   . LYS C  1 337 ? 88.878  1.949   16.229  1.00   69.57  ? 337 LYS C C   1 
ATOM   8407  O O   . LYS C  1 337 ? 88.236  2.009   17.274  1.00   74.26  ? 337 LYS C O   1 
ATOM   8408  C CB  . LYS C  1 337 ? 90.126  4.009   16.807  1.00   68.88  ? 337 LYS C CB  1 
ATOM   8409  C CG  . LYS C  1 337 ? 91.353  4.297   17.672  1.00   73.05  ? 337 LYS C CG  1 
ATOM   8410  C CD  . LYS C  1 337 ? 91.856  2.978   18.320  1.00   77.41  ? 337 LYS C CD  1 
ATOM   8411  C CE  . LYS C  1 337 ? 93.131  3.173   19.148  1.00   78.11  ? 337 LYS C CE  1 
ATOM   8412  N NZ  . LYS C  1 337 ? 93.764  1.864   19.523  1.00   77.90  ? 337 LYS C NZ  1 
ATOM   8413  N N   . ASN C  1 338 ? 88.456  1.279   15.184  1.00   67.25  ? 338 ASN C N   1 
ATOM   8414  C CA  . ASN C  1 338 ? 87.141  0.741   15.264  1.00   66.74  ? 338 ASN C CA  1 
ATOM   8415  C C   . ASN C  1 338 ? 87.241  -0.737  15.393  1.00   70.32  ? 338 ASN C C   1 
ATOM   8416  O O   . ASN C  1 338 ? 88.211  -1.363  14.944  1.00   73.27  ? 338 ASN C O   1 
ATOM   8417  C CB  . ASN C  1 338 ? 86.320  1.103   14.033  1.00   62.64  ? 338 ASN C CB  1 
ATOM   8418  C CG  . ASN C  1 338 ? 84.846  1.060   14.291  1.00   60.27  ? 338 ASN C CG  1 
ATOM   8419  O OD1 . ASN C  1 338 ? 84.378  0.294   15.115  1.00   62.29  ? 338 ASN C OD1 1 
ATOM   8420  N ND2 . ASN C  1 338 ? 84.101  1.925   13.609  1.00   57.57  ? 338 ASN C ND2 1 
ATOM   8421  N N   . ASP C  1 339 ? 86.219  -1.281  16.025  1.00   72.09  ? 339 ASP C N   1 
ATOM   8422  C CA  . ASP C  1 339 ? 86.027  -2.702  16.116  1.00   77.33  ? 339 ASP C CA  1 
ATOM   8423  C C   . ASP C  1 339 ? 85.446  -3.073  14.782  1.00   75.03  ? 339 ASP C C   1 
ATOM   8424  O O   . ASP C  1 339 ? 85.312  -4.251  14.438  1.00   75.00  ? 339 ASP C O   1 
ATOM   8425  C CB  . ASP C  1 339 ? 85.072  -3.082  17.233  1.00   85.90  ? 339 ASP C CB  1 
ATOM   8426  C CG  . ASP C  1 339 ? 85.691  -2.957  18.592  1.00   96.21  ? 339 ASP C CG  1 
ATOM   8427  O OD1 . ASP C  1 339 ? 86.938  -2.877  18.683  1.00   99.45  ? 339 ASP C OD1 1 
ATOM   8428  O OD2 . ASP C  1 339 ? 84.924  -2.945  19.574  1.00   101.89 ? 339 ASP C OD2 1 
ATOM   8429  N N   . ALA C  1 340 ? 85.104  -2.033  14.028  1.00   72.54  ? 340 ALA C N   1 
ATOM   8430  C CA  . ALA C  1 340 ? 84.269  -2.196  12.860  1.00   68.66  ? 340 ALA C CA  1 
ATOM   8431  C C   . ALA C  1 340 ? 84.743  -1.491  11.585  1.00   59.43  ? 340 ALA C C   1 
ATOM   8432  O O   . ALA C  1 340 ? 85.690  -0.684  11.528  1.00   58.91  ? 340 ALA C O   1 
ATOM   8433  C CB  . ALA C  1 340 ? 82.818  -1.767  13.196  1.00   75.94  ? 340 ALA C CB  1 
ATOM   8434  N N   . VAL C  1 341 ? 84.031  -1.927  10.565  1.00   49.42  ? 341 VAL C N   1 
ATOM   8435  C CA  . VAL C  1 341 ? 84.435  -2.009  9.201   1.00   39.86  ? 341 VAL C CA  1 
ATOM   8436  C C   . VAL C  1 341 ? 83.270  -1.581  8.346   1.00   33.26  ? 341 VAL C C   1 
ATOM   8437  O O   . VAL C  1 341 ? 82.136  -1.813  8.737   1.00   34.44  ? 341 VAL C O   1 
ATOM   8438  C CB  . VAL C  1 341 ? 84.872  -3.455  8.923   1.00   37.75  ? 341 VAL C CB  1 
ATOM   8439  C CG1 . VAL C  1 341 ? 84.852  -3.788  7.489   1.00   37.49  ? 341 VAL C CG1 1 
ATOM   8440  C CG2 . VAL C  1 341 ? 86.228  -3.705  9.552   1.00   37.86  ? 341 VAL C CG2 1 
ATOM   8441  N N   . TRP C  1 342 ? 83.516  -0.911  7.225   1.00   29.55  ? 342 TRP C N   1 
ATOM   8442  C CA  . TRP C  1 342 ? 82.432  -0.686  6.281   1.00   28.03  ? 342 TRP C CA  1 
ATOM   8443  C C   . TRP C  1 342 ? 82.578  -1.699  5.158   1.00   30.09  ? 342 TRP C C   1 
ATOM   8444  O O   . TRP C  1 342 ? 83.350  -1.516  4.231   1.00   30.45  ? 342 TRP C O   1 
ATOM   8445  C CB  . TRP C  1 342 ? 82.449  0.726   5.726   1.00   28.98  ? 342 TRP C CB  1 
ATOM   8446  C CG  . TRP C  1 342 ? 81.129  1.150   5.206   1.00   28.33  ? 342 TRP C CG  1 
ATOM   8447  C CD1 . TRP C  1 342 ? 80.075  0.351   4.934   1.00   31.12  ? 342 TRP C CD1 1 
ATOM   8448  C CD2 . TRP C  1 342 ? 80.723  2.477   4.868   1.00   30.73  ? 342 TRP C CD2 1 
ATOM   8449  N NE1 . TRP C  1 342 ? 79.016  1.091   4.474   1.00   32.88  ? 342 TRP C NE1 1 
ATOM   8450  C CE2 . TRP C  1 342 ? 79.393  2.403   4.414   1.00   31.94  ? 342 TRP C CE2 1 
ATOM   8451  C CE3 . TRP C  1 342 ? 81.349  3.723   4.921   1.00   31.72  ? 342 TRP C CE3 1 
ATOM   8452  C CZ2 . TRP C  1 342 ? 78.667  3.528   4.016   1.00   35.42  ? 342 TRP C CZ2 1 
ATOM   8453  C CZ3 . TRP C  1 342 ? 80.617  4.851   4.519   1.00   34.94  ? 342 TRP C CZ3 1 
ATOM   8454  C CH2 . TRP C  1 342 ? 79.292  4.740   4.077   1.00   35.36  ? 342 TRP C CH2 1 
ATOM   8455  N N   . ARG C  1 343 ? 81.827  -2.785  5.268   1.00   29.93  ? 343 ARG C N   1 
ATOM   8456  C CA  . ARG C  1 343 ? 81.910  -3.896  4.335   1.00   30.55  ? 343 ARG C CA  1 
ATOM   8457  C C   . ARG C  1 343 ? 81.239  -3.538  3.033   1.00   31.29  ? 343 ARG C C   1 
ATOM   8458  O O   . ARG C  1 343 ? 80.218  -2.874  3.039   1.00   34.75  ? 343 ARG C O   1 
ATOM   8459  C CB  . ARG C  1 343 ? 81.298  -5.151  4.956   1.00   33.60  ? 343 ARG C CB  1 
ATOM   8460  C CG  . ARG C  1 343 ? 81.462  -6.385  4.118   1.00   36.65  ? 343 ARG C CG  1 
ATOM   8461  C CD  . ARG C  1 343 ? 81.439  -7.607  4.988   1.00   40.28  ? 343 ARG C CD  1 
ATOM   8462  N NE  . ARG C  1 343 ? 82.630  -7.710  5.816   1.00   42.51  ? 343 ARG C NE  1 
ATOM   8463  C CZ  . ARG C  1 343 ? 82.685  -8.419  6.939   1.00   48.67  ? 343 ARG C CZ  1 
ATOM   8464  N NH1 . ARG C  1 343 ? 81.606  -9.072  7.368   1.00   52.82  ? 343 ARG C NH1 1 
ATOM   8465  N NH2 . ARG C  1 343 ? 83.814  -8.475  7.640   1.00   50.39  ? 343 ARG C NH2 1 
ATOM   8466  N N   . ILE C  1 344 ? 81.849  -3.878  1.909   1.00   29.75  ? 344 ILE C N   1 
ATOM   8467  C CA  . ILE C  1 344 ? 81.229  -3.593  0.625   1.00   34.57  ? 344 ILE C CA  1 
ATOM   8468  C C   . ILE C  1 344 ? 80.841  -4.881  -0.091  1.00   37.21  ? 344 ILE C C   1 
ATOM   8469  O O   . ILE C  1 344 ? 81.678  -5.769  -0.289  1.00   39.26  ? 344 ILE C O   1 
ATOM   8470  C CB  . ILE C  1 344 ? 82.145  -2.779  -0.285  1.00   38.19  ? 344 ILE C CB  1 
ATOM   8471  C CG1 . ILE C  1 344 ? 82.713  -1.580  0.467   1.00   39.65  ? 344 ILE C CG1 1 
ATOM   8472  C CG2 . ILE C  1 344 ? 81.384  -2.360  -1.531  1.00   37.61  ? 344 ILE C CG2 1 
ATOM   8473  C CD1 . ILE C  1 344 ? 83.722  -0.805  -0.323  1.00   40.27  ? 344 ILE C CD1 1 
ATOM   8474  N N   . SER C  1 345 ? 79.563  -4.991  -0.444  1.00   36.72  ? 345 SER C N   1 
ATOM   8475  C CA  . SER C  1 345 ? 79.021  -6.175  -1.116  1.00   38.61  ? 345 SER C CA  1 
ATOM   8476  C C   . SER C  1 345 ? 79.551  -6.281  -2.542  1.00   40.29  ? 345 SER C C   1 
ATOM   8477  O O   . SER C  1 345 ? 79.720  -5.266  -3.213  1.00   42.59  ? 345 SER C O   1 
ATOM   8478  C CB  . SER C  1 345 ? 77.494  -6.107  -1.111  1.00   36.79  ? 345 SER C CB  1 
ATOM   8479  O OG  . SER C  1 345 ? 76.937  -6.884  -2.144  1.00   41.55  ? 345 SER C OG  1 
ATOM   8480  N N   . SER C  1 346 ? 79.803  -7.495  -3.015  1.00   41.15  ? 346 SER C N   1 
ATOM   8481  C CA  . SER C  1 346 ? 80.329  -7.674  -4.363  1.00   41.84  ? 346 SER C CA  1 
ATOM   8482  C C   . SER C  1 346 ? 79.259  -7.306  -5.377  1.00   46.53  ? 346 SER C C   1 
ATOM   8483  O O   . SER C  1 346 ? 79.529  -7.062  -6.549  1.00   48.23  ? 346 SER C O   1 
ATOM   8484  C CB  . SER C  1 346 ? 80.814  -9.111  -4.575  1.00   42.81  ? 346 SER C CB  1 
ATOM   8485  O OG  . SER C  1 346 ? 79.725  -9.998  -4.750  1.00   44.83  ? 346 SER C OG  1 
ATOM   8486  N N   . GLU C  1 347 ? 78.053  -7.131  -4.872  1.00   50.50  ? 347 GLU C N   1 
ATOM   8487  C CA  . GLU C  1 347 ? 76.919  -6.780  -5.696  1.00   55.35  ? 347 GLU C CA  1 
ATOM   8488  C C   . GLU C  1 347 ? 76.959  -5.270  -5.886  1.00   53.73  ? 347 GLU C C   1 
ATOM   8489  O O   . GLU C  1 347 ? 76.313  -4.707  -6.766  1.00   55.37  ? 347 GLU C O   1 
ATOM   8490  C CB  . GLU C  1 347 ? 75.638  -7.240  -4.970  1.00   59.84  ? 347 GLU C CB  1 
ATOM   8491  C CG  . GLU C  1 347 ? 74.531  -7.885  -5.796  1.00   69.63  ? 347 GLU C CG  1 
ATOM   8492  C CD  . GLU C  1 347 ? 73.283  -8.227  -4.955  1.00   77.93  ? 347 GLU C CD  1 
ATOM   8493  O OE1 . GLU C  1 347 ? 73.436  -8.831  -3.860  1.00   77.36  ? 347 GLU C OE1 1 
ATOM   8494  O OE2 . GLU C  1 347 ? 72.149  -7.915  -5.392  1.00   84.70  ? 347 GLU C OE2 1 
ATOM   8495  N N   . ASN C  1 348 ? 77.762  -4.617  -5.061  1.00   50.30  ? 348 ASN C N   1 
ATOM   8496  C CA  . ASN C  1 348 ? 77.955  -3.190  -5.190  1.00   50.33  ? 348 ASN C CA  1 
ATOM   8497  C C   . ASN C  1 348 ? 79.166  -2.809  -6.039  1.00   49.89  ? 348 ASN C C   1 
ATOM   8498  O O   . ASN C  1 348 ? 79.056  -1.997  -6.953  1.00   53.39  ? 348 ASN C O   1 
ATOM   8499  C CB  . ASN C  1 348 ? 78.052  -2.568  -3.791  1.00   51.14  ? 348 ASN C CB  1 
ATOM   8500  C CG  . ASN C  1 348 ? 78.058  -1.050  -3.817  1.00   53.22  ? 348 ASN C CG  1 
ATOM   8501  O OD1 . ASN C  1 348 ? 78.889  -0.416  -4.475  1.00   54.21  ? 348 ASN C OD1 1 
ATOM   8502  N ND2 . ASN C  1 348 ? 77.095  -0.457  -3.116  1.00   53.21  ? 348 ASN C ND2 1 
ATOM   8503  N N   . PHE C  1 349 ? 80.313  -3.418  -5.772  1.00   45.57  ? 349 PHE C N   1 
ATOM   8504  C CA  . PHE C  1 349 ? 81.533  -2.943  -6.404  1.00   45.03  ? 349 PHE C CA  1 
ATOM   8505  C C   . PHE C  1 349 ? 81.865  -3.587  -7.743  1.00   49.42  ? 349 PHE C C   1 
ATOM   8506  O O   . PHE C  1 349 ? 82.785  -3.132  -8.412  1.00   50.57  ? 349 PHE C O   1 
ATOM   8507  C CB  . PHE C  1 349 ? 82.713  -3.068  -5.426  1.00   43.79  ? 349 PHE C CB  1 
ATOM   8508  C CG  . PHE C  1 349 ? 83.033  -4.479  -4.977  1.00   45.96  ? 349 PHE C CG  1 
ATOM   8509  C CD1 . PHE C  1 349 ? 83.644  -5.381  -5.819  1.00   51.44  ? 349 PHE C CD1 1 
ATOM   8510  C CD2 . PHE C  1 349 ? 82.772  -4.871  -3.676  1.00   46.07  ? 349 PHE C CD2 1 
ATOM   8511  C CE1 . PHE C  1 349 ? 83.956  -6.680  -5.383  1.00   56.13  ? 349 PHE C CE1 1 
ATOM   8512  C CE2 . PHE C  1 349 ? 83.080  -6.152  -3.229  1.00   50.69  ? 349 PHE C CE2 1 
ATOM   8513  C CZ  . PHE C  1 349 ? 83.676  -7.063  -4.086  1.00   54.91  ? 349 PHE C CZ  1 
ATOM   8514  N N   . MET C  1 350 ? 81.105  -4.607  -8.143  1.00   46.40  ? 350 MET C N   1 
ATOM   8515  C CA  . MET C  1 350 ? 81.215  -5.186  -9.485  1.00   49.16  ? 350 MET C CA  1 
ATOM   8516  C C   . MET C  1 350 ? 80.203  -4.538  -10.428 1.00   50.90  ? 350 MET C C   1 
ATOM   8517  O O   . MET C  1 350 ? 79.012  -4.479  -10.120 1.00   52.15  ? 350 MET C O   1 
ATOM   8518  C CB  . MET C  1 350 ? 80.983  -6.686  -9.449  1.00   52.62  ? 350 MET C CB  1 
ATOM   8519  C CG  . MET C  1 350 ? 82.025  -7.455  -8.662  1.00   54.46  ? 350 MET C CG  1 
ATOM   8520  S SD  . MET C  1 350 ? 83.752  -7.189  -9.113  1.00   51.75  ? 350 MET C SD  1 
ATOM   8521  C CE  . MET C  1 350 ? 83.785  -7.695  -10.824 1.00   40.30  ? 350 MET C CE  1 
ATOM   8522  N N   . VAL C  1 351 ? 80.675  -4.033  -11.563 1.00   50.38  ? 351 VAL C N   1 
ATOM   8523  C CA  . VAL C  1 351 ? 79.815  -3.314  -12.488 1.00   50.39  ? 351 VAL C CA  1 
ATOM   8524  C C   . VAL C  1 351 ? 79.594  -4.094  -13.772 1.00   54.05  ? 351 VAL C C   1 
ATOM   8525  O O   . VAL C  1 351 ? 80.519  -4.671  -14.317 1.00   54.20  ? 351 VAL C O   1 
ATOM   8526  C CB  . VAL C  1 351 ? 80.409  -1.917  -12.827 1.00   38.25  ? 351 VAL C CB  1 
ATOM   8527  C CG1 . VAL C  1 351 ? 79.474  -1.118  -13.718 1.00   39.60  ? 351 VAL C CG1 1 
ATOM   8528  C CG2 . VAL C  1 351 ? 80.706  -1.127  -11.553 1.00   37.14  ? 351 VAL C CG2 1 
ATOM   8529  N N   . GLN C  1 352 ? 78.372  -4.021  -14.286 1.00   58.30  ? 352 GLN C N   1 
ATOM   8530  C CA  . GLN C  1 352 ? 77.957  -4.738  -15.476 1.00   62.82  ? 352 GLN C CA  1 
ATOM   8531  C C   . GLN C  1 352 ? 78.093  -3.865  -16.719 1.00   65.19  ? 352 GLN C C   1 
ATOM   8532  O O   . GLN C  1 352 ? 77.121  -3.594  -17.410 1.00   69.80  ? 352 GLN C O   1 
ATOM   8533  C CB  . GLN C  1 352 ? 76.529  -5.254  -15.309 1.00   68.14  ? 352 GLN C CB  1 
ATOM   8534  C CG  . GLN C  1 352 ? 76.058  -6.113  -16.458 1.00   78.82  ? 352 GLN C CG  1 
ATOM   8535  C CD  . GLN C  1 352 ? 76.867  -7.388  -16.549 1.00   88.23  ? 352 GLN C CD  1 
ATOM   8536  O OE1 . GLN C  1 352 ? 76.912  -8.177  -15.606 1.00   90.53  ? 352 GLN C OE1 1 
ATOM   8537  N NE2 . GLN C  1 352 ? 77.517  -7.598  -17.691 1.00   93.73  ? 352 GLN C NE2 1 
ATOM   8538  N N   . ALA C  1 353 ? 79.307  -3.357  -16.922 1.00   63.98  ? 353 ALA C N   1 
ATOM   8539  C CA  . ALA C  1 353 ? 79.711  -2.591  -18.110 1.00   64.36  ? 353 ALA C CA  1 
ATOM   8540  C C   . ALA C  1 353 ? 79.099  -3.050  -19.441 1.00   69.60  ? 353 ALA C C   1 
ATOM   8541  O O   . ALA C  1 353 ? 78.629  -2.231  -20.230 1.00   72.67  ? 353 ALA C O   1 
ATOM   8542  C CB  . ALA C  1 353 ? 81.214  -2.613  -18.223 1.00   61.61  ? 353 ALA C CB  1 
ATOM   8543  N N   . GLN C  1 354 ? 79.160  -4.348  -19.710 1.00   71.03  ? 354 GLN C N   1 
ATOM   8544  C CA  . GLN C  1 354 ? 78.643  -4.902  -20.951 1.00   73.43  ? 354 GLN C CA  1 
ATOM   8545  C C   . GLN C  1 354 ? 78.014  -6.248  -20.616 1.00   73.31  ? 354 GLN C C   1 
ATOM   8546  O O   . GLN C  1 354 ? 78.323  -6.803  -19.573 1.00   72.40  ? 354 GLN C O   1 
ATOM   8547  C CB  . GLN C  1 354 ? 79.762  -5.037  -21.962 1.00   76.66  ? 354 GLN C CB  1 
ATOM   8548  C CG  . GLN C  1 354 ? 79.973  -3.785  -22.787 1.00   79.01  ? 354 GLN C CG  1 
ATOM   8549  C CD  . GLN C  1 354 ? 81.268  -3.850  -23.559 1.00   82.34  ? 354 GLN C CD  1 
ATOM   8550  O OE1 . GLN C  1 354 ? 81.771  -4.936  -23.839 1.00   84.61  ? 354 GLN C OE1 1 
ATOM   8551  N NE2 . GLN C  1 354 ? 81.821  -2.690  -23.906 1.00   82.12  ? 354 GLN C NE2 1 
ATOM   8552  N N   . ASP C  1 355 ? 77.182  -6.798  -21.496 1.00   75.95  ? 355 ASP C N   1 
ATOM   8553  C CA  . ASP C  1 355 ? 76.654  -8.155  -21.300 1.00   80.51  ? 355 ASP C CA  1 
ATOM   8554  C C   . ASP C  1 355 ? 77.761  -9.187  -21.133 1.00   81.35  ? 355 ASP C C   1 
ATOM   8555  O O   . ASP C  1 355 ? 78.712  -9.236  -21.921 1.00   82.83  ? 355 ASP C O   1 
ATOM   8556  C CB  . ASP C  1 355 ? 75.769  -8.561  -22.466 1.00   88.54  ? 355 ASP C CB  1 
ATOM   8557  C CG  . ASP C  1 355 ? 76.470  -8.399  -23.784 1.00   96.34  ? 355 ASP C CG  1 
ATOM   8558  O OD1 . ASP C  1 355 ? 77.489  -7.669  -23.821 1.00   96.47  ? 355 ASP C OD1 1 
ATOM   8559  O OD2 . ASP C  1 355 ? 76.014  -9.007  -24.775 1.00   102.59 ? 355 ASP C OD2 1 
ATOM   8560  N N   . GLY C  1 356 ? 77.612  -10.013 -20.100 1.00   80.38  ? 356 GLY C N   1 
ATOM   8561  C CA  . GLY C  1 356 ? 78.594  -11.018 -19.731 1.00   79.75  ? 356 GLY C CA  1 
ATOM   8562  C C   . GLY C  1 356 ? 79.980  -10.457 -19.443 1.00   74.84  ? 356 GLY C C   1 
ATOM   8563  O O   . GLY C  1 356 ? 80.985  -11.162 -19.534 1.00   75.56  ? 356 GLY C O   1 
ATOM   8564  N N   . VAL C  1 357 ? 80.038  -9.174  -19.110 1.00   69.01  ? 357 VAL C N   1 
ATOM   8565  C CA  . VAL C  1 357 ? 81.278  -8.561  -18.675 1.00   62.84  ? 357 VAL C CA  1 
ATOM   8566  C C   . VAL C  1 357 ? 81.018  -7.867  -17.361 1.00   56.37  ? 357 VAL C C   1 
ATOM   8567  O O   . VAL C  1 357 ? 80.127  -7.039  -17.276 1.00   54.42  ? 357 VAL C O   1 
ATOM   8568  C CB  . VAL C  1 357 ? 81.826  -7.578  -19.696 1.00   64.27  ? 357 VAL C CB  1 
ATOM   8569  C CG1 . VAL C  1 357 ? 83.111  -6.948  -19.159 1.00   55.54  ? 357 VAL C CG1 1 
ATOM   8570  C CG2 . VAL C  1 357 ? 82.083  -8.304  -21.026 1.00   62.60  ? 357 VAL C CG2 1 
ATOM   8571  N N   . SER C  1 358 ? 81.765  -8.221  -16.328 1.00   53.25  ? 358 SER C N   1 
ATOM   8572  C CA  . SER C  1 358 ? 81.560  -7.628  -15.017 1.00   53.84  ? 358 SER C CA  1 
ATOM   8573  C C   . SER C  1 358 ? 82.836  -6.892  -14.532 1.00   55.55  ? 358 SER C C   1 
ATOM   8574  O O   . SER C  1 358 ? 83.901  -7.497  -14.433 1.00   55.58  ? 358 SER C O   1 
ATOM   8575  C CB  . SER C  1 358 ? 81.112  -8.720  -14.042 1.00   58.54  ? 358 SER C CB  1 
ATOM   8576  O OG  . SER C  1 358 ? 80.893  -8.213  -12.740 1.00   60.35  ? 358 SER C OG  1 
ATOM   8577  N N   . CYS C  1 359 ? 82.736  -5.597  -14.227 1.00   52.08  ? 359 CYS C N   1 
ATOM   8578  C CA  . CYS C  1 359 ? 83.943  -4.788  -13.968 1.00   46.68  ? 359 CYS C CA  1 
ATOM   8579  C C   . CYS C  1 359 ? 84.148  -4.319  -12.532 1.00   42.95  ? 359 CYS C C   1 
ATOM   8580  O O   . CYS C  1 359 ? 83.202  -4.077  -11.798 1.00   40.09  ? 359 CYS C O   1 
ATOM   8581  C CB  . CYS C  1 359 ? 83.942  -3.557  -14.873 1.00   44.10  ? 359 CYS C CB  1 
ATOM   8582  S SG  . CYS C  1 359 ? 84.099  -3.952  -16.621 1.00   57.93  ? 359 CYS C SG  1 
ATOM   8583  N N   . LEU C  1 360 ? 85.406  -4.196  -12.138 1.00   42.49  ? 360 LEU C N   1 
ATOM   8584  C CA  . LEU C  1 360 ? 85.741  -3.642  -10.840 1.00   42.54  ? 360 LEU C CA  1 
ATOM   8585  C C   . LEU C  1 360 ? 85.490  -2.154  -10.841 1.00   46.29  ? 360 LEU C C   1 
ATOM   8586  O O   . LEU C  1 360 ? 86.134  -1.415  -11.590 1.00   47.96  ? 360 LEU C O   1 
ATOM   8587  C CB  . LEU C  1 360 ? 87.190  -3.949  -10.487 1.00   44.81  ? 360 LEU C CB  1 
ATOM   8588  C CG  . LEU C  1 360 ? 87.717  -3.402  -9.164  1.00   43.75  ? 360 LEU C CG  1 
ATOM   8589  C CD1 . LEU C  1 360 ? 86.915  -3.934  -7.973  1.00   42.08  ? 360 LEU C CD1 1 
ATOM   8590  C CD2 . LEU C  1 360 ? 89.182  -3.801  -9.021  1.00   43.23  ? 360 LEU C CD2 1 
ATOM   8591  N N   . GLY C  1 361 ? 84.535  -1.736  -10.009 1.00   45.65  ? 361 GLY C N   1 
ATOM   8592  C CA  . GLY C  1 361 ? 83.989  -0.392  -10.018 1.00   44.88  ? 361 GLY C CA  1 
ATOM   8593  C C   . GLY C  1 361 ? 84.746  0.675   -9.252  1.00   43.70  ? 361 GLY C C   1 
ATOM   8594  O O   . GLY C  1 361 ? 84.149  1.487   -8.547  1.00   42.39  ? 361 GLY C O   1 
ATOM   8595  N N   . PHE C  1 362 ? 86.062  0.695   -9.420  1.00   44.41  ? 362 PHE C N   1 
ATOM   8596  C CA  . PHE C  1 362 ? 86.891  1.770   -8.900  1.00   41.53  ? 362 PHE C CA  1 
ATOM   8597  C C   . PHE C  1 362 ? 87.646  2.363   -10.070 1.00   43.22  ? 362 PHE C C   1 
ATOM   8598  O O   . PHE C  1 362 ? 88.131  1.636   -10.933 1.00   47.56  ? 362 PHE C O   1 
ATOM   8599  C CB  . PHE C  1 362 ? 87.881  1.287   -7.858  1.00   40.17  ? 362 PHE C CB  1 
ATOM   8600  C CG  . PHE C  1 362 ? 87.252  0.700   -6.640  1.00   38.69  ? 362 PHE C CG  1 
ATOM   8601  C CD1 . PHE C  1 362 ? 86.714  -0.581  -6.668  1.00   38.73  ? 362 PHE C CD1 1 
ATOM   8602  C CD2 . PHE C  1 362 ? 87.225  1.413   -5.450  1.00   36.03  ? 362 PHE C CD2 1 
ATOM   8603  C CE1 . PHE C  1 362 ? 86.155  -1.134  -5.534  1.00   35.85  ? 362 PHE C CE1 1 
ATOM   8604  C CE2 . PHE C  1 362 ? 86.664  0.863   -4.321  1.00   33.59  ? 362 PHE C CE2 1 
ATOM   8605  C CZ  . PHE C  1 362 ? 86.134  -0.411  -4.363  1.00   34.30  ? 362 PHE C CZ  1 
ATOM   8606  N N   . VAL C  1 363 ? 87.760  3.683   -10.093 1.00   40.70  ? 363 VAL C N   1 
ATOM   8607  C CA  . VAL C  1 363 ? 88.389  4.361   -11.208 1.00   37.04  ? 363 VAL C CA  1 
ATOM   8608  C C   . VAL C  1 363 ? 89.579  5.197   -10.734 1.00   36.19  ? 363 VAL C C   1 
ATOM   8609  O O   . VAL C  1 363 ? 89.654  5.596   -9.569  1.00   35.24  ? 363 VAL C O   1 
ATOM   8610  C CB  . VAL C  1 363 ? 87.370  5.213   -11.942 1.00   37.60  ? 363 VAL C CB  1 
ATOM   8611  C CG1 . VAL C  1 363 ? 86.206  4.335   -12.402 1.00   37.25  ? 363 VAL C CG1 1 
ATOM   8612  C CG2 . VAL C  1 363 ? 86.851  6.285   -11.036 1.00   36.81  ? 363 VAL C CG2 1 
ATOM   8613  N N   . ASP C  1 364 ? 90.543  5.380   -11.630 1.00   37.95  ? 364 ASP C N   1 
ATOM   8614  C CA  . ASP C  1 364 ? 91.770  6.105   -11.350 1.00   38.46  ? 364 ASP C CA  1 
ATOM   8615  C C   . ASP C  1 364 ? 91.514  7.599   -11.366 1.00   41.20  ? 364 ASP C C   1 
ATOM   8616  O O   . ASP C  1 364 ? 91.091  8.154   -12.383 1.00   41.82  ? 364 ASP C O   1 
ATOM   8617  C CB  . ASP C  1 364 ? 92.841  5.725   -12.374 1.00   40.80  ? 364 ASP C CB  1 
ATOM   8618  C CG  . ASP C  1 364 ? 94.225  6.232   -12.005 1.00   41.87  ? 364 ASP C CG  1 
ATOM   8619  O OD1 . ASP C  1 364 ? 94.340  7.129   -11.136 1.00   41.63  ? 364 ASP C OD1 1 
ATOM   8620  O OD2 . ASP C  1 364 ? 95.200  5.716   -12.585 1.00   43.27  1 364 ASP C OD2 1 
ATOM   8621  N N   . GLY C  1 365 ? 91.746  8.238   -10.220 1.00   41.80  ? 365 GLY C N   1 
ATOM   8622  C CA  . GLY C  1 365 ? 91.585  9.678   -10.074 1.00   41.94  ? 365 GLY C CA  1 
ATOM   8623  C C   . GLY C  1 365 ? 92.779  10.526  -10.477 1.00   45.36  ? 365 GLY C C   1 
ATOM   8624  O O   . GLY C  1 365 ? 92.729  11.749  -10.416 1.00   48.68  ? 365 GLY C O   1 
ATOM   8625  N N   . GLY C  1 366 ? 93.854  9.873   -10.889 1.00   47.09  ? 366 GLY C N   1 
ATOM   8626  C CA  . GLY C  1 366 ? 95.056  10.557  -11.301 1.00   48.76  ? 366 GLY C CA  1 
ATOM   8627  C C   . GLY C  1 366 ? 95.937  10.927  -10.130 1.00   51.46  ? 366 GLY C C   1 
ATOM   8628  O O   . GLY C  1 366 ? 95.669  10.559  -8.989  1.00   47.12  ? 366 GLY C O   1 
ATOM   8629  N N   . VAL C  1 367 ? 96.979  11.698  -10.430 1.00   60.83  ? 367 VAL C N   1 
ATOM   8630  C CA  . VAL C  1 367 ? 98.019  12.029  -9.464  1.00   67.54  ? 367 VAL C CA  1 
ATOM   8631  C C   . VAL C  1 367 ? 97.711  13.336  -8.739  1.00   71.64  ? 367 VAL C C   1 
ATOM   8632  O O   . VAL C  1 367 ? 98.333  13.652  -7.721  1.00   76.36  ? 367 VAL C O   1 
ATOM   8633  C CB  . VAL C  1 367 ? 99.406  12.150  -10.143 1.00   72.08  ? 367 VAL C CB  1 
ATOM   8634  C CG1 . VAL C  1 367 ? 100.517 11.879  -9.135  1.00   74.39  ? 367 VAL C CG1 1 
ATOM   8635  C CG2 . VAL C  1 367 ? 99.507  11.194  -11.324 1.00   71.38  ? 367 VAL C CG2 1 
ATOM   8636  N N   . HIS C  1 368 ? 96.754  14.097  -9.261  1.00   68.72  ? 368 HIS C N   1 
ATOM   8637  C CA  . HIS C  1 368 ? 96.351  15.313  -8.583  1.00   66.65  ? 368 HIS C CA  1 
ATOM   8638  C C   . HIS C  1 368 ? 94.912  15.152  -8.147  1.00   63.83  ? 368 HIS C C   1 
ATOM   8639  O O   . HIS C  1 368 ? 94.112  16.062  -8.277  1.00   65.73  ? 368 HIS C O   1 
ATOM   8640  C CB  . HIS C  1 368 ? 96.501  16.515  -9.503  1.00   70.22  ? 368 HIS C CB  1 
ATOM   8641  C CG  . HIS C  1 368 ? 97.839  16.595  -10.164 1.00   77.16  ? 368 HIS C CG  1 
ATOM   8642  N ND1 . HIS C  1 368 ? 99.017  16.745  -9.463  1.00   80.13  ? 368 HIS C ND1 1 
ATOM   8643  C CD2 . HIS C  1 368 ? 98.185  16.506  -11.471 1.00   81.32  ? 368 HIS C CD2 1 
ATOM   8644  C CE1 . HIS C  1 368 ? 100.031 16.763  -10.312 1.00   84.47  ? 368 HIS C CE1 1 
ATOM   8645  N NE2 . HIS C  1 368 ? 99.553  16.620  -11.537 1.00   85.17  ? 368 HIS C NE2 1 
ATOM   8646  N N   . ALA C  1 369 ? 94.572  13.964  -7.670  1.00   59.74  ? 369 ALA C N   1 
ATOM   8647  C CA  . ALA C  1 369 ? 93.236  13.702  -7.176  1.00   53.19  ? 369 ALA C CA  1 
ATOM   8648  C C   . ALA C  1 369 ? 92.989  14.497  -5.905  1.00   55.85  ? 369 ALA C C   1 
ATOM   8649  O O   . ALA C  1 369 ? 93.925  14.784  -5.157  1.00   58.06  ? 369 ALA C O   1 
ATOM   8650  C CB  . ALA C  1 369 ? 93.039  12.216  -6.932  1.00   47.48  ? 369 ALA C CB  1 
ATOM   8651  N N   . ARG C  1 370 ? 91.721  14.837  -5.669  1.00   57.50  ? 370 ARG C N   1 
ATOM   8652  C CA  . ARG C  1 370 ? 91.287  15.676  -4.546  1.00   58.32  ? 370 ARG C CA  1 
ATOM   8653  C C   . ARG C  1 370 ? 91.528  14.991  -3.203  1.00   50.15  ? 370 ARG C C   1 
ATOM   8654  O O   . ARG C  1 370 ? 92.048  15.612  -2.280  1.00   49.56  ? 370 ARG C O   1 
ATOM   8655  C CB  . ARG C  1 370 ? 89.791  16.019  -4.712  1.00   64.51  ? 370 ARG C CB  1 
ATOM   8656  C CG  . ARG C  1 370 ? 89.039  16.574  -3.478  1.00   68.89  ? 370 ARG C CG  1 
ATOM   8657  C CD  . ARG C  1 370 ? 89.644  17.872  -2.967  1.00   74.17  ? 370 ARG C CD  1 
ATOM   8658  N NE  . ARG C  1 370 ? 88.992  18.400  -1.763  1.00   75.05  ? 370 ARG C NE  1 
ATOM   8659  C CZ  . ARG C  1 370 ? 89.482  18.313  -0.525  1.00   75.83  ? 370 ARG C CZ  1 
ATOM   8660  N NH1 . ARG C  1 370 ? 90.633  17.698  -0.293  1.00   76.75  ? 370 ARG C NH1 1 
ATOM   8661  N NH2 . ARG C  1 370 ? 88.815  18.844  0.490   1.00   74.81  ? 370 ARG C NH2 1 
ATOM   8662  N N   . ALA C  1 371 ? 91.186  13.703  -3.128  1.00   42.67  ? 371 ALA C N   1 
ATOM   8663  C CA  . ALA C  1 371 ? 91.418  12.877  -1.946  1.00   36.38  ? 371 ALA C CA  1 
ATOM   8664  C C   . ALA C  1 371 ? 91.918  11.516  -2.401  1.00   36.40  ? 371 ALA C C   1 
ATOM   8665  O O   . ALA C  1 371 ? 91.841  11.205  -3.591  1.00   38.37  ? 371 ALA C O   1 
ATOM   8666  C CB  . ALA C  1 371 ? 90.152  12.749  -1.109  1.00   33.60  ? 371 ALA C CB  1 
ATOM   8667  N N   . GLY C  1 372 ? 92.475  10.735  -1.471  1.00   36.32  ? 372 GLY C N   1 
ATOM   8668  C CA  . GLY C  1 372 ? 93.000  9.392   -1.744  1.00   35.75  ? 372 GLY C CA  1 
ATOM   8669  C C   . GLY C  1 372 ? 91.894  8.438   -2.118  1.00   33.20  ? 372 GLY C C   1 
ATOM   8670  O O   . GLY C  1 372 ? 92.030  7.595   -3.000  1.00   32.68  ? 372 GLY C O   1 
ATOM   8671  N N   . ILE C  1 373 ? 90.785  8.607   -1.407  1.00   33.01  ? 373 ILE C N   1 
ATOM   8672  C CA  . ILE C  1 373 ? 89.541  7.890   -1.640  1.00   30.73  ? 373 ILE C CA  1 
ATOM   8673  C C   . ILE C  1 373 ? 88.378  8.873   -1.711  1.00   28.19  ? 373 ILE C C   1 
ATOM   8674  O O   . ILE C  1 373 ? 88.212  9.724   -0.853  1.00   27.95  ? 373 ILE C O   1 
ATOM   8675  C CB  . ILE C  1 373 ? 89.268  6.870   -0.525  1.00   28.65  ? 373 ILE C CB  1 
ATOM   8676  C CG1 . ILE C  1 373 ? 90.430  5.907   -0.392  1.00   28.43  ? 373 ILE C CG1 1 
ATOM   8677  C CG2 . ILE C  1 373 ? 88.002  6.107   -0.801  1.00   28.34  ? 373 ILE C CG2 1 
ATOM   8678  C CD1 . ILE C  1 373 ? 90.346  5.047   0.844   1.00   27.57  ? 373 ILE C CD1 1 
ATOM   8679  N N   . ALA C  1 374 ? 87.583  8.773   -2.761  1.00   29.12  ? 374 ALA C N   1 
ATOM   8680  C CA  . ALA C  1 374 ? 86.334  9.513   -2.801  1.00   29.77  ? 374 ALA C CA  1 
ATOM   8681  C C   . ALA C  1 374 ? 85.161  8.564   -3.059  1.00   29.93  ? 374 ALA C C   1 
ATOM   8682  O O   . ALA C  1 374 ? 84.948  8.094   -4.177  1.00   29.68  ? 374 ALA C O   1 
ATOM   8683  C CB  . ALA C  1 374 ? 86.384  10.623  -3.857  1.00   28.39  ? 374 ALA C CB  1 
ATOM   8684  N N   . LEU C  1 375 ? 84.404  8.294   -2.003  1.00   30.53  ? 375 LEU C N   1 
ATOM   8685  C CA  . LEU C  1 375 ? 83.266  7.407   -2.071  1.00   28.51  ? 375 LEU C CA  1 
ATOM   8686  C C   . LEU C  1 375 ? 82.089  8.131   -2.732  1.00   35.21  ? 375 LEU C C   1 
ATOM   8687  O O   . LEU C  1 375 ? 81.679  9.200   -2.279  1.00   36.25  ? 375 LEU C O   1 
ATOM   8688  C CB  . LEU C  1 375 ? 82.893  6.910   -0.666  1.00   25.35  ? 375 LEU C CB  1 
ATOM   8689  C CG  . LEU C  1 375 ? 84.041  6.320   0.162   1.00   24.68  ? 375 LEU C CG  1 
ATOM   8690  C CD1 . LEU C  1 375 ? 83.642  6.103   1.606   1.00   23.84  ? 375 LEU C CD1 1 
ATOM   8691  C CD2 . LEU C  1 375 ? 84.538  5.032   -0.435  1.00   25.71  ? 375 LEU C CD2 1 
ATOM   8692  N N   . GLY C  1 376 ? 81.546  7.541   -3.800  1.00   37.64  ? 376 GLY C N   1 
ATOM   8693  C CA  . GLY C  1 376 ? 80.553  8.199   -4.639  1.00   37.07  ? 376 GLY C CA  1 
ATOM   8694  C C   . GLY C  1 376 ? 79.151  7.645   -4.509  1.00   33.80  ? 376 GLY C C   1 
ATOM   8695  O O   . GLY C  1 376 ? 78.834  6.968   -3.531  1.00   31.17  ? 376 GLY C O   1 
ATOM   8696  N N   . ALA C  1 377 ? 78.318  7.926   -5.508  1.00   33.68  ? 377 ALA C N   1 
ATOM   8697  C CA  . ALA C  1 377 ? 76.897  7.569   -5.471  1.00   31.58  ? 377 ALA C CA  1 
ATOM   8698  C C   . ALA C  1 377 ? 76.642  6.073   -5.403  1.00   33.68  ? 377 ALA C C   1 
ATOM   8699  O O   . ALA C  1 377 ? 75.814  5.621   -4.612  1.00   35.04  ? 377 ALA C O   1 
ATOM   8700  C CB  . ALA C  1 377 ? 76.196  8.132   -6.687  1.00   31.11  ? 377 ALA C CB  1 
ATOM   8701  N N   A HIS C  1 378 ? 77.372  5.300   -6.197  0.50   34.09  ? 378 HIS C N   1 
ATOM   8702  N N   B HIS C  1 378 ? 77.350  5.323   -6.248  0.50   34.13  ? 378 HIS C N   1 
ATOM   8703  C CA  A HIS C  1 378 ? 77.156  3.859   -6.240  0.50   33.34  ? 378 HIS C CA  1 
ATOM   8704  C CA  B HIS C  1 378 ? 77.284  3.858   -6.305  0.50   33.40  ? 378 HIS C CA  1 
ATOM   8705  C C   A HIS C  1 378 ? 77.519  3.201   -4.909  0.50   32.13  ? 378 HIS C C   1 
ATOM   8706  C C   B HIS C  1 378 ? 77.539  3.213   -4.944  0.50   32.49  ? 378 HIS C C   1 
ATOM   8707  O O   A HIS C  1 378 ? 76.895  2.220   -4.526  0.50   32.61  ? 378 HIS C O   1 
ATOM   8708  O O   B HIS C  1 378 ? 76.860  2.264   -4.573  0.50   32.57  ? 378 HIS C O   1 
ATOM   8709  C CB  A HIS C  1 378 ? 77.911  3.230   -7.412  0.50   34.55  ? 378 HIS C CB  1 
ATOM   8710  C CB  B HIS C  1 378 ? 78.301  3.331   -7.327  0.50   34.40  ? 378 HIS C CB  1 
ATOM   8711  C CG  A HIS C  1 378 ? 77.208  3.406   -8.723  0.50   35.07  ? 378 HIS C CG  1 
ATOM   8712  C CG  B HIS C  1 378 ? 78.008  1.957   -7.844  0.50   36.06  ? 378 HIS C CG  1 
ATOM   8713  N ND1 A HIS C  1 378 ? 77.430  2.593   -9.813  0.50   39.03  ? 378 HIS C ND1 1 
ATOM   8714  N ND1 B HIS C  1 378 ? 76.795  1.608   -8.394  0.50   39.13  ? 378 HIS C ND1 1 
ATOM   8715  C CD2 A HIS C  1 378 ? 76.281  4.310   -9.116  0.50   33.60  ? 378 HIS C CD2 1 
ATOM   8716  C CD2 B HIS C  1 378 ? 78.788  0.852   -7.923  0.50   36.09  ? 378 HIS C CD2 1 
ATOM   8717  C CE1 A HIS C  1 378 ? 76.666  2.988   -10.818 0.50   38.38  ? 378 HIS C CE1 1 
ATOM   8718  C CE1 B HIS C  1 378 ? 76.833  0.343   -8.774  0.50   38.78  ? 378 HIS C CE1 1 
ATOM   8719  N NE2 A HIS C  1 378 ? 75.959  4.029   -10.421 0.50   33.30  ? 378 HIS C NE2 1 
ATOM   8720  N NE2 B HIS C  1 378 ? 78.031  -0.138  -8.499  0.50   36.80  ? 378 HIS C NE2 1 
ATOM   8721  N N   . HIS C  1 379 ? 78.524  3.731   -4.214  1.00   31.33  ? 379 HIS C N   1 
ATOM   8722  C CA  . HIS C  1 379 ? 78.867  3.238   -2.872  1.00   31.22  ? 379 HIS C CA  1 
ATOM   8723  C C   . HIS C  1 379 ? 77.703  3.417   -1.891  1.00   32.39  ? 379 HIS C C   1 
ATOM   8724  O O   . HIS C  1 379 ? 77.413  2.519   -1.088  1.00   34.01  ? 379 HIS C O   1 
ATOM   8725  C CB  . HIS C  1 379 ? 80.123  3.961   -2.313  1.00   30.09  ? 379 HIS C CB  1 
ATOM   8726  C CG  . HIS C  1 379 ? 80.502  3.547   -0.917  1.00   28.68  ? 379 HIS C CG  1 
ATOM   8727  N ND1 . HIS C  1 379 ? 81.322  2.472   -0.650  1.00   30.61  ? 379 HIS C ND1 1 
ATOM   8728  C CD2 . HIS C  1 379 ? 80.169  4.068   0.289   1.00   28.86  ? 379 HIS C CD2 1 
ATOM   8729  C CE1 . HIS C  1 379 ? 81.464  2.338   0.656   1.00   30.62  ? 379 HIS C CE1 1 
ATOM   8730  N NE2 . HIS C  1 379 ? 80.774  3.294   1.248   1.00   31.43  ? 379 HIS C NE2 1 
ATOM   8731  N N   . LEU C  1 380 ? 77.050  4.575   -1.956  1.00   28.96  ? 380 LEU C N   1 
ATOM   8732  C CA  . LEU C  1 380 ? 75.975  4.941   -1.030  1.00   27.57  ? 380 LEU C CA  1 
ATOM   8733  C C   . LEU C  1 380 ? 74.630  4.250   -1.289  1.00   27.47  ? 380 LEU C C   1 
ATOM   8734  O O   . LEU C  1 380 ? 73.801  4.106   -0.395  1.00   30.25  ? 380 LEU C O   1 
ATOM   8735  C CB  . LEU C  1 380 ? 75.768  6.458   -1.061  1.00   27.40  ? 380 LEU C CB  1 
ATOM   8736  C CG  . LEU C  1 380 ? 76.945  7.348   -0.659  1.00   25.02  ? 380 LEU C CG  1 
ATOM   8737  C CD1 . LEU C  1 380 ? 76.604  8.771   -1.000  1.00   25.48  ? 380 LEU C CD1 1 
ATOM   8738  C CD2 . LEU C  1 380 ? 77.282  7.225   0.817   1.00   22.99  ? 380 LEU C CD2 1 
ATOM   8739  N N   . GLU C  1 381 ? 74.397  3.875   -2.532  1.00   29.40  ? 381 GLU C N   1 
ATOM   8740  C CA  . GLU C  1 381 ? 73.133  3.288   -2.924  1.00   31.87  ? 381 GLU C CA  1 
ATOM   8741  C C   . GLU C  1 381 ? 72.824  2.003   -2.144  1.00   32.99  ? 381 GLU C C   1 
ATOM   8742  O O   . GLU C  1 381 ? 73.705  1.151   -1.934  1.00   33.06  ? 381 GLU C O   1 
ATOM   8743  C CB  . GLU C  1 381 ? 73.139  3.028   -4.427  1.00   29.78  ? 381 GLU C CB  1 
ATOM   8744  C CG  . GLU C  1 381 ? 72.966  4.286   -5.228  1.00   31.26  ? 381 GLU C CG  1 
ATOM   8745  C CD  . GLU C  1 381 ? 73.347  4.141   -6.684  1.00   35.33  ? 381 GLU C CD  1 
ATOM   8746  O OE1 . GLU C  1 381 ? 73.728  3.036   -7.111  1.00   36.85  ? 381 GLU C OE1 1 
ATOM   8747  O OE2 . GLU C  1 381 ? 73.262  5.153   -7.411  1.00   38.38  1 381 GLU C OE2 1 
ATOM   8748  N N   . GLU C  1 382 ? 71.565  1.899   -1.709  1.00   33.42  ? 382 GLU C N   1 
ATOM   8749  C CA  . GLU C  1 382 ? 71.060  0.764   -0.931  1.00   35.48  ? 382 GLU C CA  1 
ATOM   8750  C C   . GLU C  1 382 ? 71.753  0.602   0.427   1.00   31.78  ? 382 GLU C C   1 
ATOM   8751  O O   . GLU C  1 382 ? 71.810  -0.493  0.991   1.00   33.12  ? 382 GLU C O   1 
ATOM   8752  C CB  . GLU C  1 382 ? 71.173  -0.526  -1.753  1.00   37.72  ? 382 GLU C CB  1 
ATOM   8753  C CG  . GLU C  1 382 ? 70.337  -0.499  -3.022  1.00   39.71  ? 382 GLU C CG  1 
ATOM   8754  C CD  . GLU C  1 382 ? 68.878  -0.146  -2.767  1.00   40.58  ? 382 GLU C CD  1 
ATOM   8755  O OE1 . GLU C  1 382 ? 68.315  -0.588  -1.746  1.00   42.21  ? 382 GLU C OE1 1 
ATOM   8756  O OE2 . GLU C  1 382 ? 68.277  0.541   -3.608  1.00   39.49  1 382 GLU C OE2 1 
ATOM   8757  N N   . ASN C  1 383 ? 72.271  1.713   0.937   1.00   31.54  ? 383 ASN C N   1 
ATOM   8758  C CA  . ASN C  1 383 ? 72.744  1.799   2.308   1.00   32.30  ? 383 ASN C CA  1 
ATOM   8759  C C   . ASN C  1 383 ? 72.024  2.954   2.984   1.00   29.37  ? 383 ASN C C   1 
ATOM   8760  O O   . ASN C  1 383 ? 71.766  3.962   2.356   1.00   29.40  ? 383 ASN C O   1 
ATOM   8761  C CB  . ASN C  1 383 ? 74.268  2.009   2.375   1.00   32.98  ? 383 ASN C CB  1 
ATOM   8762  C CG  . ASN C  1 383 ? 75.071  0.791   1.917   1.00   33.97  ? 383 ASN C CG  1 
ATOM   8763  O OD1 . ASN C  1 383 ? 75.075  -0.253  2.572   1.00   34.40  ? 383 ASN C OD1 1 
ATOM   8764  N ND2 . ASN C  1 383 ? 75.802  0.948   0.822   1.00   34.68  ? 383 ASN C ND2 1 
ATOM   8765  N N   . LEU C  1 384 ? 71.717  2.811   4.267   1.00   31.29  ? 384 LEU C N   1 
ATOM   8766  C CA  . LEU C  1 384 ? 71.202  3.922   5.046   1.00   30.11  ? 384 LEU C CA  1 
ATOM   8767  C C   . LEU C  1 384 ? 72.355  4.628   5.777   1.00   32.77  ? 384 LEU C C   1 
ATOM   8768  O O   . LEU C  1 384 ? 73.036  4.029   6.604   1.00   35.10  ? 384 LEU C O   1 
ATOM   8769  C CB  . LEU C  1 384 ? 70.128  3.447   6.031   1.00   29.50  ? 384 LEU C CB  1 
ATOM   8770  C CG  . LEU C  1 384 ? 69.605  4.569   6.941   1.00   29.75  ? 384 LEU C CG  1 
ATOM   8771  C CD1 . LEU C  1 384 ? 68.800  5.607   6.145   1.00   28.27  ? 384 LEU C CD1 1 
ATOM   8772  C CD2 . LEU C  1 384 ? 68.753  3.988   8.051   1.00   30.16  ? 384 LEU C CD2 1 
ATOM   8773  N N   . VAL C  1 385 ? 72.583  5.895   5.444   1.00   32.38  ? 385 VAL C N   1 
ATOM   8774  C CA  . VAL C  1 385 ? 73.714  6.645   5.983   1.00   29.84  ? 385 VAL C CA  1 
ATOM   8775  C C   . VAL C  1 385 ? 73.260  7.875   6.767   1.00   27.77  ? 385 VAL C C   1 
ATOM   8776  O O   . VAL C  1 385 ? 72.679  8.785   6.216   1.00   27.73  ? 385 VAL C O   1 
ATOM   8777  C CB  . VAL C  1 385 ? 74.641  7.060   4.861   1.00   28.05  ? 385 VAL C CB  1 
ATOM   8778  C CG1 . VAL C  1 385 ? 75.863  7.772   5.420   1.00   27.62  ? 385 VAL C CG1 1 
ATOM   8779  C CG2 . VAL C  1 385 ? 75.047  5.832   4.064   1.00   27.19  ? 385 VAL C CG2 1 
ATOM   8780  N N   . VAL C  1 386 ? 73.529  7.875   8.063   1.00   28.15  ? 386 VAL C N   1 
ATOM   8781  C CA  . VAL C  1 386 ? 73.038  8.909   8.949   1.00   25.93  ? 386 VAL C CA  1 
ATOM   8782  C C   . VAL C  1 386 ? 74.128  9.901   9.267   1.00   26.54  ? 386 VAL C C   1 
ATOM   8783  O O   . VAL C  1 386 ? 75.145  9.538   9.841   1.00   28.92  ? 386 VAL C O   1 
ATOM   8784  C CB  . VAL C  1 386 ? 72.524  8.316   10.254  1.00   26.19  ? 386 VAL C CB  1 
ATOM   8785  C CG1 . VAL C  1 386 ? 72.013  9.437   11.174  1.00   26.74  ? 386 VAL C CG1 1 
ATOM   8786  C CG2 . VAL C  1 386 ? 71.441  7.326   9.954   1.00   26.05  ? 386 VAL C CG2 1 
ATOM   8787  N N   . PHE C  1 387 ? 73.909  11.157  8.917   1.00   25.41  ? 387 PHE C N   1 
ATOM   8788  C CA  . PHE C  1 387 ? 74.859  12.204  9.222   1.00   27.18  ? 387 PHE C CA  1 
ATOM   8789  C C   . PHE C  1 387 ? 74.434  12.846  10.527  1.00   28.72  ? 387 PHE C C   1 
ATOM   8790  O O   . PHE C  1 387 ? 73.537  13.682  10.554  1.00   28.68  ? 387 PHE C O   1 
ATOM   8791  C CB  . PHE C  1 387 ? 74.939  13.227  8.082   1.00   26.74  ? 387 PHE C CB  1 
ATOM   8792  C CG  . PHE C  1 387 ? 75.565  12.672  6.827   1.00   29.49  ? 387 PHE C CG  1 
ATOM   8793  C CD1 . PHE C  1 387 ? 74.837  11.879  5.963   1.00   28.69  ? 387 PHE C CD1 1 
ATOM   8794  C CD2 . PHE C  1 387 ? 76.884  12.938  6.518   1.00   31.12  ? 387 PHE C CD2 1 
ATOM   8795  C CE1 . PHE C  1 387 ? 75.422  11.353  4.820   1.00   27.15  ? 387 PHE C CE1 1 
ATOM   8796  C CE2 . PHE C  1 387 ? 77.473  12.423  5.373   1.00   29.39  ? 387 PHE C CE2 1 
ATOM   8797  C CZ  . PHE C  1 387 ? 76.737  11.626  4.528   1.00   28.69  ? 387 PHE C CZ  1 
ATOM   8798  N N   . ASP C  1 388 ? 75.062  12.402  11.611  1.00   28.14  ? 388 ASP C N   1 
ATOM   8799  C CA  . ASP C  1 388 ? 74.741  12.893  12.928  1.00   29.66  ? 388 ASP C CA  1 
ATOM   8800  C C   . ASP C  1 388 ? 75.625  14.100  13.251  1.00   32.01  ? 388 ASP C C   1 
ATOM   8801  O O   . ASP C  1 388 ? 76.697  13.967  13.824  1.00   35.71  ? 388 ASP C O   1 
ATOM   8802  C CB  . ASP C  1 388 ? 74.932  11.778  13.949  1.00   32.98  ? 388 ASP C CB  1 
ATOM   8803  C CG  . ASP C  1 388 ? 74.402  12.144  15.312  1.00   38.54  ? 388 ASP C CG  1 
ATOM   8804  O OD1 . ASP C  1 388 ? 74.054  13.328  15.526  1.00   42.70  ? 388 ASP C OD1 1 
ATOM   8805  O OD2 . ASP C  1 388 ? 74.321  11.247  16.169  1.00   39.79  1 388 ASP C OD2 1 
ATOM   8806  N N   . LEU C  1 389 ? 75.152  15.287  12.915  1.00   28.91  ? 389 LEU C N   1 
ATOM   8807  C CA  . LEU C  1 389 ? 75.989  16.450  13.014  1.00   30.01  ? 389 LEU C CA  1 
ATOM   8808  C C   . LEU C  1 389 ? 76.163  16.877  14.460  1.00   32.27  ? 389 LEU C C   1 
ATOM   8809  O O   . LEU C  1 389 ? 77.142  17.524  14.791  1.00   35.96  ? 389 LEU C O   1 
ATOM   8810  C CB  . LEU C  1 389 ? 75.430  17.593  12.146  1.00   31.20  ? 389 LEU C CB  1 
ATOM   8811  C CG  . LEU C  1 389 ? 75.083  17.157  10.715  1.00   28.72  ? 389 LEU C CG  1 
ATOM   8812  C CD1 . LEU C  1 389 ? 74.240  18.154  10.043  1.00   29.71  ? 389 LEU C CD1 1 
ATOM   8813  C CD2 . LEU C  1 389 ? 76.324  16.945  9.905   1.00   26.96  ? 389 LEU C CD2 1 
ATOM   8814  N N   . GLU C  1 390 ? 75.233  16.504  15.324  1.00   31.27  ? 390 GLU C N   1 
ATOM   8815  C CA  . GLU C  1 390 ? 75.320  16.914  16.720  1.00   32.69  ? 390 GLU C CA  1 
ATOM   8816  C C   . GLU C  1 390 ? 76.440  16.201  17.424  1.00   31.97  ? 390 GLU C C   1 
ATOM   8817  O O   . GLU C  1 390 ? 77.033  16.735  18.366  1.00   33.38  ? 390 GLU C O   1 
ATOM   8818  C CB  . GLU C  1 390 ? 74.003  16.681  17.457  1.00   34.07  ? 390 GLU C CB  1 
ATOM   8819  C CG  . GLU C  1 390 ? 72.901  17.554  16.939  1.00   38.46  ? 390 GLU C CG  1 
ATOM   8820  C CD  . GLU C  1 390 ? 71.723  17.640  17.883  1.00   47.47  ? 390 GLU C CD  1 
ATOM   8821  O OE1 . GLU C  1 390 ? 71.600  16.741  18.756  1.00   47.29  ? 390 GLU C OE1 1 
ATOM   8822  O OE2 . GLU C  1 390 ? 70.927  18.616  17.749  1.00   52.87  ? 390 GLU C OE2 1 
ATOM   8823  N N   . ARG C  1 391 ? 76.730  14.995  16.966  1.00   31.68  ? 391 ARG C N   1 
ATOM   8824  C CA  . ARG C  1 391 ? 77.795  14.223  17.575  1.00   32.43  ? 391 ARG C CA  1 
ATOM   8825  C C   . ARG C  1 391 ? 78.984  14.088  16.649  1.00   31.62  ? 391 ARG C C   1 
ATOM   8826  O O   . ARG C  1 391 ? 79.935  13.414  16.988  1.00   32.89  ? 391 ARG C O   1 
ATOM   8827  C CB  . ARG C  1 391 ? 77.305  12.836  18.004  1.00   32.47  ? 391 ARG C CB  1 
ATOM   8828  C CG  . ARG C  1 391 ? 76.179  12.857  19.043  1.00   37.04  ? 391 ARG C CG  1 
ATOM   8829  C CD  . ARG C  1 391 ? 76.000  11.503  19.710  1.00   44.17  ? 391 ARG C CD  1 
ATOM   8830  N NE  . ARG C  1 391 ? 77.308  11.049  20.190  1.00   58.05  ? 391 ARG C NE  1 
ATOM   8831  C CZ  . ARG C  1 391 ? 77.539  9.999   20.982  1.00   67.69  ? 391 ARG C CZ  1 
ATOM   8832  N NH1 . ARG C  1 391 ? 76.536  9.255   21.424  1.00   69.77  ? 391 ARG C NH1 1 
ATOM   8833  N NH2 . ARG C  1 391 ? 78.787  9.703   21.347  1.00   71.02  ? 391 ARG C NH2 1 
ATOM   8834  N N   . SER C  1 392 ? 78.931  14.735  15.492  1.00   29.99  ? 392 SER C N   1 
ATOM   8835  C CA  . SER C  1 392 ? 80.017  14.685  14.503  1.00   28.08  ? 392 SER C CA  1 
ATOM   8836  C C   . SER C  1 392 ? 80.449  13.264  14.119  1.00   27.72  ? 392 SER C C   1 
ATOM   8837  O O   . SER C  1 392 ? 81.610  12.900  14.210  1.00   29.42  ? 392 SER C O   1 
ATOM   8838  C CB  . SER C  1 392 ? 81.223  15.466  15.020  1.00   28.47  ? 392 SER C CB  1 
ATOM   8839  O OG  . SER C  1 392 ? 82.103  15.790  13.962  1.00   27.94  ? 392 SER C OG  1 
ATOM   8840  N N   . ARG C  1 393 ? 79.511  12.468  13.657  1.00   26.05  ? 393 ARG C N   1 
ATOM   8841  C CA  . ARG C  1 393 ? 79.795  11.100  13.277  1.00   25.30  ? 393 ARG C CA  1 
ATOM   8842  C C   . ARG C  1 393 ? 78.871  10.682  12.156  1.00   27.46  ? 393 ARG C C   1 
ATOM   8843  O O   . ARG C  1 393 ? 77.802  11.278  11.942  1.00   27.81  ? 393 ARG C O   1 
ATOM   8844  C CB  . ARG C  1 393 ? 79.632  10.165  14.467  1.00   26.40  ? 393 ARG C CB  1 
ATOM   8845  C CG  . ARG C  1 393 ? 78.207  10.141  14.979  1.00   26.82  ? 393 ARG C CG  1 
ATOM   8846  C CD  . ARG C  1 393 ? 78.087  9.361   16.282  1.00   31.09  ? 393 ARG C CD  1 
ATOM   8847  N NE  . ARG C  1 393 ? 76.680  9.214   16.643  1.00   33.81  ? 393 ARG C NE  1 
ATOM   8848  C CZ  . ARG C  1 393 ? 76.190  8.334   17.516  1.00   35.41  ? 393 ARG C CZ  1 
ATOM   8849  N NH1 . ARG C  1 393 ? 76.981  7.486   18.169  1.00   34.88  ? 393 ARG C NH1 1 
ATOM   8850  N NH2 . ARG C  1 393 ? 74.884  8.303   17.729  1.00   37.87  ? 393 ARG C NH2 1 
ATOM   8851  N N   . VAL C  1 394 ? 79.293  9.659   11.433  1.00   28.00  ? 394 VAL C N   1 
ATOM   8852  C CA  . VAL C  1 394 ? 78.483  9.073   10.390  1.00   30.54  ? 394 VAL C CA  1 
ATOM   8853  C C   . VAL C  1 394 ? 78.121  7.673   10.810  1.00   27.82  ? 394 VAL C C   1 
ATOM   8854  O O   . VAL C  1 394 ? 78.960  6.958   11.325  1.00   27.37  ? 394 VAL C O   1 
ATOM   8855  C CB  . VAL C  1 394 ? 79.215  9.060   9.036   1.00   36.46  ? 394 VAL C CB  1 
ATOM   8856  C CG1 . VAL C  1 394 ? 78.388  8.379   7.975   1.00   38.86  ? 394 VAL C CG1 1 
ATOM   8857  C CG2 . VAL C  1 394 ? 79.492  10.448  8.608   1.00   39.39  ? 394 VAL C CG2 1 
ATOM   8858  N N   . GLY C  1 395 ? 76.859  7.305   10.615  1.00   28.00  ? 395 GLY C N   1 
ATOM   8859  C CA  . GLY C  1 395 ? 76.379  5.957   10.894  1.00   26.97  ? 395 GLY C CA  1 
ATOM   8860  C C   . GLY C  1 395 ? 75.939  5.240   9.635   1.00   25.12  ? 395 GLY C C   1 
ATOM   8861  O O   . GLY C  1 395 ? 75.516  5.878   8.695   1.00   26.43  ? 395 GLY C O   1 
ATOM   8862  N N   . PHE C  1 396 ? 76.057  3.922   9.596   1.00   26.28  ? 396 PHE C N   1 
ATOM   8863  C CA  . PHE C  1 396 ? 75.609  3.174   8.417   1.00   28.65  ? 396 PHE C CA  1 
ATOM   8864  C C   . PHE C  1 396 ? 75.137  1.804   8.850   1.00   30.50  ? 396 PHE C C   1 
ATOM   8865  O O   . PHE C  1 396 ? 75.451  1.362   9.953   1.00   32.51  ? 396 PHE C O   1 
ATOM   8866  C CB  . PHE C  1 396 ? 76.710  3.064   7.364   1.00   30.08  ? 396 PHE C CB  1 
ATOM   8867  C CG  . PHE C  1 396 ? 78.020  2.533   7.905   1.00   31.81  ? 396 PHE C CG  1 
ATOM   8868  C CD1 . PHE C  1 396 ? 78.265  1.169   7.969   1.00   32.80  ? 396 PHE C CD1 1 
ATOM   8869  C CD2 . PHE C  1 396 ? 78.993  3.405   8.377   1.00   28.97  ? 396 PHE C CD2 1 
ATOM   8870  C CE1 . PHE C  1 396 ? 79.451  0.690   8.476   1.00   32.76  ? 396 PHE C CE1 1 
ATOM   8871  C CE2 . PHE C  1 396 ? 80.187  2.925   8.880   1.00   28.61  ? 396 PHE C CE2 1 
ATOM   8872  C CZ  . PHE C  1 396 ? 80.410  1.562   8.931   1.00   30.62  ? 396 PHE C CZ  1 
ATOM   8873  N N   . ASN C  1 397 ? 74.345  1.147   8.016   1.00   29.55  ? 397 ASN C N   1 
ATOM   8874  C CA  . ASN C  1 397 ? 73.843  -0.163  8.389   1.00   32.24  ? 397 ASN C CA  1 
ATOM   8875  C C   . ASN C  1 397 ? 74.968  -1.200  8.436   1.00   30.75  ? 397 ASN C C   1 
ATOM   8876  O O   . ASN C  1 397 ? 75.800  -1.255  7.542   1.00   32.48  ? 397 ASN C O   1 
ATOM   8877  C CB  . ASN C  1 397 ? 72.720  -0.578  7.437   1.00   33.80  ? 397 ASN C CB  1 
ATOM   8878  C CG  . ASN C  1 397 ? 73.064  -0.323  5.989   1.00   30.59  ? 397 ASN C CG  1 
ATOM   8879  O OD1 . ASN C  1 397 ? 73.229  0.807   5.581   1.00   29.93  ? 397 ASN C OD1 1 
ATOM   8880  N ND2 . ASN C  1 397 ? 73.151  -1.381  5.201   1.00   32.14  ? 397 ASN C ND2 1 
ATOM   8881  N N   . SER C  1 398 ? 75.022  -1.987  9.503   1.00   30.86  ? 398 SER C N   1 
ATOM   8882  C CA  . SER C  1 398 ? 76.098  -2.952  9.648   1.00   30.23  ? 398 SER C CA  1 
ATOM   8883  C C   . SER C  1 398 ? 75.769  -4.284  8.987   1.00   35.90  ? 398 SER C C   1 
ATOM   8884  O O   . SER C  1 398 ? 76.591  -5.187  8.952   1.00   40.66  ? 398 SER C O   1 
ATOM   8885  C CB  . SER C  1 398 ? 76.437  -3.174  11.111  1.00   29.86  ? 398 SER C CB  1 
ATOM   8886  O OG  . SER C  1 398 ? 75.317  -3.608  11.838  1.00   34.52  ? 398 SER C OG  1 
ATOM   8887  N N   . ASN C  1 399 ? 74.541  -4.450  8.538   1.00   36.52  ? 399 ASN C N   1 
ATOM   8888  C CA  . ASN C  1 399 ? 74.195  -5.598  7.718   1.00   37.13  ? 399 ASN C CA  1 
ATOM   8889  C C   . ASN C  1 399 ? 73.554  -5.037  6.465   1.00   39.34  ? 399 ASN C C   1 
ATOM   8890  O O   . ASN C  1 399 ? 73.132  -3.890  6.477   1.00   40.19  ? 399 ASN C O   1 
ATOM   8891  C CB  . ASN C  1 399 ? 73.260  -6.541  8.479   1.00   37.68  ? 399 ASN C CB  1 
ATOM   8892  C CG  . ASN C  1 399 ? 73.880  -7.077  9.766   1.00   36.86  ? 399 ASN C CG  1 
ATOM   8893  O OD1 . ASN C  1 399 ? 74.712  -7.988  9.748   1.00   37.12  ? 399 ASN C OD1 1 
ATOM   8894  N ND2 . ASN C  1 399 ? 73.497  -6.495  10.884  1.00   37.46  ? 399 ASN C ND2 1 
ATOM   8895  N N   . SER C  1 400 ? 73.502  -5.803  5.380   1.00   40.28  ? 400 SER C N   1 
ATOM   8896  C CA  . SER C  1 400 ? 72.902  -5.285  4.154   1.00   38.08  ? 400 SER C CA  1 
ATOM   8897  C C   . SER C  1 400 ? 71.440  -5.026  4.393   1.00   39.62  ? 400 SER C C   1 
ATOM   8898  O O   . SER C  1 400 ? 70.794  -5.697  5.209   1.00   39.65  ? 400 SER C O   1 
ATOM   8899  C CB  . SER C  1 400 ? 73.061  -6.245  2.979   1.00   37.99  ? 400 SER C CB  1 
ATOM   8900  O OG  . SER C  1 400 ? 72.211  -7.367  3.108   1.00   43.25  ? 400 SER C OG  1 
ATOM   8901  N N   . LEU C  1 401 ? 70.910  -4.033  3.702   1.00   40.01  ? 401 LEU C N   1 
ATOM   8902  C CA  . LEU C  1 401 ? 69.487  -3.793  3.810   1.00   41.26  ? 401 LEU C CA  1 
ATOM   8903  C C   . LEU C  1 401 ? 68.714  -5.036  3.377   1.00   44.53  ? 401 LEU C C   1 
ATOM   8904  O O   . LEU C  1 401 ? 67.719  -5.428  3.997   1.00   44.58  ? 401 LEU C O   1 
ATOM   8905  C CB  . LEU C  1 401 ? 69.082  -2.577  2.977   1.00   39.92  ? 401 LEU C CB  1 
ATOM   8906  C CG  . LEU C  1 401 ? 69.521  -1.195  3.429   1.00   36.51  ? 401 LEU C CG  1 
ATOM   8907  C CD1 . LEU C  1 401 ? 68.789  -0.191  2.587   1.00   35.13  ? 401 LEU C CD1 1 
ATOM   8908  C CD2 . LEU C  1 401 ? 69.158  -0.994  4.901   1.00   33.72  ? 401 LEU C CD2 1 
ATOM   8909  N N   . LYS C  1 402 ? 69.224  -5.690  2.346   1.00   45.44  ? 402 LYS C N   1 
ATOM   8910  C CA  . LYS C  1 402 ? 68.557  -6.826  1.765   1.00   38.99  ? 402 LYS C CA  1 
ATOM   8911  C C   . LYS C  1 402 ? 68.471  -7.949  2.800   1.00   47.03  ? 402 LYS C C   1 
ATOM   8912  O O   . LYS C  1 402 ? 67.502  -8.714  2.796   1.00   48.75  ? 402 LYS C O   1 
ATOM   8913  C CB  . LYS C  1 402 ? 69.298  -7.241  0.484   1.00   39.41  ? 402 LYS C CB  1 
ATOM   8914  C CG  . LYS C  1 402 ? 68.875  -8.515  -0.197  1.00   49.04  ? 402 LYS C CG  1 
ATOM   8915  C CD  . LYS C  1 402 ? 69.663  -8.700  -1.522  1.00   69.01  ? 402 LYS C CD  1 
ATOM   8916  C CE  . LYS C  1 402 ? 69.393  -10.021 -2.268  1.00   73.43  ? 402 LYS C CE  1 
ATOM   8917  N NZ  . LYS C  1 402 ? 69.061  -11.223 -1.453  1.00   76.95  ? 402 LYS C NZ  1 
ATOM   8918  N N   . SER C  1 403 ? 69.426  -8.020  3.734   1.00   45.38  ? 403 SER C N   1 
ATOM   8919  C CA  . SER C  1 403 ? 69.364  -9.062  4.786   1.00   45.80  ? 403 SER C CA  1 
ATOM   8920  C C   . SER C  1 403 ? 68.233  -8.811  5.791   1.00   46.41  ? 403 SER C C   1 
ATOM   8921  O O   . SER C  1 403 ? 67.794  -9.736  6.483   1.00   45.78  ? 403 SER C O   1 
ATOM   8922  C CB  . SER C  1 403 ? 70.703  -9.182  5.537   1.00   41.68  ? 403 SER C CB  1 
ATOM   8923  O OG  . SER C  1 403 ? 70.801  -8.221  6.580   1.00   40.92  ? 403 SER C OG  1 
ATOM   8924  N N   . TYR C  1 404 ? 67.732  -7.575  5.823   1.00   45.62  ? 404 TYR C N   1 
ATOM   8925  C CA  . TYR C  1 404 ? 66.585  -7.217  6.654   1.00   45.67  ? 404 TYR C CA  1 
ATOM   8926  C C   . TYR C  1 404 ? 65.292  -7.329  5.862   1.00   49.12  ? 404 TYR C C   1 
ATOM   8927  O O   . TYR C  1 404 ? 64.214  -7.074  6.384   1.00   50.32  ? 404 TYR C O   1 
ATOM   8928  C CB  . TYR C  1 404 ? 66.715  -5.792  7.179   1.00   38.48  ? 404 TYR C CB  1 
ATOM   8929  C CG  . TYR C  1 404 ? 67.880  -5.511  8.110   1.00   42.15  ? 404 TYR C CG  1 
ATOM   8930  C CD1 . TYR C  1 404 ? 67.767  -5.729  9.483   1.00   42.39  ? 404 TYR C CD1 1 
ATOM   8931  C CD2 . TYR C  1 404 ? 69.084  -5.024  7.624   1.00   34.14  ? 404 TYR C CD2 1 
ATOM   8932  C CE1 . TYR C  1 404 ? 68.829  -5.462  10.343  1.00   39.43  ? 404 TYR C CE1 1 
ATOM   8933  C CE2 . TYR C  1 404 ? 70.137  -4.752  8.470   1.00   36.40  ? 404 TYR C CE2 1 
ATOM   8934  C CZ  . TYR C  1 404 ? 70.003  -4.973  9.828   1.00   37.39  ? 404 TYR C CZ  1 
ATOM   8935  O OH  . TYR C  1 404 ? 71.045  -4.702  10.686  1.00   36.97  ? 404 TYR C OH  1 
ATOM   8936  N N   . GLY C  1 405 ? 65.409  -7.694  4.593   1.00   44.25  ? 405 GLY C N   1 
ATOM   8937  C CA  . GLY C  1 405 ? 64.275  -7.702  3.692   1.00   46.52  ? 405 GLY C CA  1 
ATOM   8938  C C   . GLY C  1 405 ? 63.898  -6.307  3.205   1.00   54.76  ? 405 GLY C C   1 
ATOM   8939  O O   . GLY C  1 405 ? 62.788  -6.100  2.707   1.00   46.75  ? 405 GLY C O   1 
ATOM   8940  N N   . LYS C  1 406 ? 64.833  -5.359  3.305   1.00   49.89  ? 406 LYS C N   1 
ATOM   8941  C CA  . LYS C  1 406 ? 64.540  -3.956  2.993   1.00   45.52  ? 406 LYS C CA  1 
ATOM   8942  C C   . LYS C  1 406 ? 65.314  -3.434  1.785   1.00   44.55  ? 406 LYS C C   1 
ATOM   8943  O O   . LYS C  1 406 ? 66.305  -4.020  1.349   1.00   43.63  ? 406 LYS C O   1 
ATOM   8944  C CB  . LYS C  1 406 ? 64.833  -3.039  4.200   1.00   39.70  ? 406 LYS C CB  1 
ATOM   8945  C CG  . LYS C  1 406 ? 64.194  -3.516  5.476   1.00   41.44  ? 406 LYS C CG  1 
ATOM   8946  C CD  . LYS C  1 406 ? 62.696  -3.332  5.439   1.00   45.82  ? 406 LYS C CD  1 
ATOM   8947  C CE  . LYS C  1 406 ? 62.042  -4.097  6.565   1.00   50.55  ? 406 LYS C CE  1 
ATOM   8948  N NZ  . LYS C  1 406 ? 62.849  -3.913  7.797   1.00   50.67  ? 406 LYS C NZ  1 
ATOM   8949  N N   . THR C  1 407 ? 64.807  -2.325  1.254   1.00   45.86  ? 407 THR C N   1 
ATOM   8950  C CA  . THR C  1 407 ? 65.449  -1.529  0.221   1.00   41.17  ? 407 THR C CA  1 
ATOM   8951  C C   . THR C  1 407 ? 65.377  -0.055  0.617   1.00   39.01  ? 407 THR C C   1 
ATOM   8952  O O   . THR C  1 407 ? 64.687  0.322   1.559   1.00   37.35  ? 407 THR C O   1 
ATOM   8953  C CB  . THR C  1 407 ? 64.778  -1.709  -1.148  1.00   39.19  ? 407 THR C CB  1 
ATOM   8954  O OG1 . THR C  1 407 ? 63.493  -1.079  -1.140  1.00   49.27  ? 407 THR C OG1 1 
ATOM   8955  C CG2 . THR C  1 407 ? 64.598  -3.182  -1.469  1.00   41.83  ? 407 THR C CG2 1 
ATOM   8956  N N   . CYS C  1 408 ? 66.103  0.782   -0.104  1.00   39.70  ? 408 CYS C N   1 
ATOM   8957  C CA  . CYS C  1 408 ? 66.052  2.215   0.147   1.00   40.19  ? 408 CYS C CA  1 
ATOM   8958  C C   . CYS C  1 408 ? 64.728  2.809   -0.293  1.00   41.59  ? 408 CYS C C   1 
ATOM   8959  O O   . CYS C  1 408 ? 64.360  3.899   0.147   1.00   39.53  ? 408 CYS C O   1 
ATOM   8960  C CB  . CYS C  1 408 ? 67.232  2.925   -0.534  1.00   39.39  ? 408 CYS C CB  1 
ATOM   8961  S SG  . CYS C  1 408 ? 68.732  3.046   0.528   1.00   34.75  ? 408 CYS C SG  1 
ATOM   8962  N N   . SER C  1 409 ? 64.011  2.083   -1.153  1.00   47.51  ? 409 SER C N   1 
ATOM   8963  C CA  . SER C  1 409 ? 62.682  2.495   -1.611  1.00   49.58  ? 409 SER C CA  1 
ATOM   8964  C C   . SER C  1 409 ? 61.585  2.163   -0.618  1.00   47.97  ? 409 SER C C   1 
ATOM   8965  O O   . SER C  1 409 ? 60.578  2.846   -0.575  1.00   51.32  ? 409 SER C O   1 
ATOM   8966  C CB  . SER C  1 409 ? 62.331  1.844   -2.952  1.00   55.84  ? 409 SER C CB  1 
ATOM   8967  O OG  . SER C  1 409 ? 63.240  2.203   -3.975  1.00   56.80  ? 409 SER C OG  1 
ATOM   8968  N N   . ASN C  1 410 ? 61.747  1.093   0.147   1.00   46.39  ? 410 ASN C N   1 
ATOM   8969  C CA  . ASN C  1 410 ? 60.694  0.700   1.069   1.00   41.89  ? 410 ASN C CA  1 
ATOM   8970  C C   . ASN C  1 410 ? 61.064  0.756   2.555   1.00   42.13  ? 410 ASN C C   1 
ATOM   8971  O O   . ASN C  1 410 ? 60.289  0.351   3.387   1.00   46.81  ? 410 ASN C O   1 
ATOM   8972  C CB  . ASN C  1 410 ? 60.173  -0.694  0.702   1.00   44.98  ? 410 ASN C CB  1 
ATOM   8973  C CG  . ASN C  1 410 ? 61.209  -1.778  0.855   1.00   50.13  ? 410 ASN C CG  1 
ATOM   8974  O OD1 . ASN C  1 410 ? 62.058  -1.735  1.748   1.00   46.59  ? 410 ASN C OD1 1 
ATOM   8975  N ND2 . ASN C  1 410 ? 61.142  -2.776  -0.027  1.00   53.18  ? 410 ASN C ND2 1 
ATOM   8976  N N   . LEU C  1 411 ? 62.224  1.274   2.903   1.00   40.51  ? 411 LEU C N   1 
ATOM   8977  C CA  . LEU C  1 411 ? 62.538  1.410   4.314   1.00   40.29  ? 411 LEU C CA  1 
ATOM   8978  C C   . LEU C  1 411 ? 61.515  2.313   4.969   1.00   40.97  ? 411 LEU C C   1 
ATOM   8979  O O   . LEU C  1 411 ? 61.064  2.061   6.086   1.00   41.79  ? 411 LEU C O   1 
ATOM   8980  C CB  . LEU C  1 411 ? 63.933  1.986   4.496   1.00   38.82  ? 411 LEU C CB  1 
ATOM   8981  C CG  . LEU C  1 411 ? 65.038  1.148   5.120   1.00   40.90  ? 411 LEU C CG  1 
ATOM   8982  C CD1 . LEU C  1 411 ? 66.202  2.053   5.564   1.00   38.90  ? 411 LEU C CD1 1 
ATOM   8983  C CD2 . LEU C  1 411 ? 64.516  0.336   6.279   1.00   41.93  ? 411 LEU C CD2 1 
ATOM   8984  N N   . PHE C  1 412 ? 61.138  3.350   4.222   1.00   43.28  ? 412 PHE C N   1 
ATOM   8985  C CA  . PHE C  1 412 ? 60.140  4.347   4.617   1.00   41.46  ? 412 PHE C CA  1 
ATOM   8986  C C   . PHE C  1 412 ? 59.030  4.456   3.589   1.00   41.64  ? 412 PHE C C   1 
ATOM   8987  O O   . PHE C  1 412 ? 59.234  4.150   2.431   1.00   44.38  ? 412 PHE C O   1 
ATOM   8988  C CB  . PHE C  1 412 ? 60.829  5.698   4.782   1.00   37.12  ? 412 PHE C CB  1 
ATOM   8989  C CG  . PHE C  1 412 ? 62.039  5.629   5.628   1.00   32.68  ? 412 PHE C CG  1 
ATOM   8990  C CD1 . PHE C  1 412 ? 61.930  5.568   7.003   1.00   34.18  ? 412 PHE C CD1 1 
ATOM   8991  C CD2 . PHE C  1 412 ? 63.295  5.567   5.054   1.00   31.33  ? 412 PHE C CD2 1 
ATOM   8992  C CE1 . PHE C  1 412 ? 63.055  5.464   7.792   1.00   31.57  ? 412 PHE C CE1 1 
ATOM   8993  C CE2 . PHE C  1 412 ? 64.420  5.478   5.827   1.00   30.84  ? 412 PHE C CE2 1 
ATOM   8994  C CZ  . PHE C  1 412 ? 64.306  5.425   7.204   1.00   31.92  ? 412 PHE C CZ  1 
ATOM   8995  N N   . ASP C  1 413 ? 57.852  4.899   3.993   1.00   45.32  ? 413 ASP C N   1 
ATOM   8996  C CA  . ASP C  1 413 ? 56.775  5.072   3.024   1.00   54.76  ? 413 ASP C CA  1 
ATOM   8997  C C   . ASP C  1 413 ? 56.959  6.353   2.205   1.00   59.45  ? 413 ASP C C   1 
ATOM   8998  O O   . ASP C  1 413 ? 56.796  7.460   2.727   1.00   62.10  ? 413 ASP C O   1 
ATOM   8999  C CB  . ASP C  1 413 ? 55.412  5.106   3.720   1.00   56.89  ? 413 ASP C CB  1 
ATOM   9000  C CG  . ASP C  1 413 ? 54.256  4.961   2.749   1.00   62.92  ? 413 ASP C CG  1 
ATOM   9001  O OD1 . ASP C  1 413 ? 54.365  5.398   1.588   1.00   63.17  ? 413 ASP C OD1 1 
ATOM   9002  O OD2 . ASP C  1 413 ? 53.214  4.411   3.154   1.00   68.53  1 413 ASP C OD2 1 
ATOM   9003  N N   . LEU C  1 414 ? 57.250  6.202   0.915   1.00   58.18  ? 414 LEU C N   1 
ATOM   9004  C CA  . LEU C  1 414 ? 57.481  7.355   0.043   1.00   54.73  ? 414 LEU C CA  1 
ATOM   9005  C C   . LEU C  1 414 ? 56.357  7.574   -0.970  1.00   60.29  ? 414 LEU C C   1 
ATOM   9006  O O   . LEU C  1 414 ? 56.549  8.277   -1.959  1.00   60.91  ? 414 LEU C O   1 
ATOM   9007  C CB  . LEU C  1 414 ? 58.824  7.209   -0.699  1.00   49.72  ? 414 LEU C CB  1 
ATOM   9008  C CG  . LEU C  1 414 ? 60.116  7.090   0.105   1.00   38.36  ? 414 LEU C CG  1 
ATOM   9009  C CD1 . LEU C  1 414 ? 61.314  6.841   -0.782  1.00   37.10  ? 414 LEU C CD1 1 
ATOM   9010  C CD2 . LEU C  1 414 ? 60.331  8.358   0.877   1.00   36.63  ? 414 LEU C CD2 1 
ATOM   9011  N N   . ASN C  1 415 ? 55.185  6.996   -0.722  1.00   64.50  ? 415 ASN C N   1 
ATOM   9012  C CA  . ASN C  1 415 ? 54.045  7.190   -1.612  1.00   71.63  ? 415 ASN C CA  1 
ATOM   9013  C C   . ASN C  1 415 ? 53.403  8.553   -1.326  1.00   71.83  ? 415 ASN C C   1 
ATOM   9014  O O   . ASN C  1 415 ? 53.256  8.917   -0.160  1.00   69.91  ? 415 ASN C O   1 
ATOM   9015  C CB  . ASN C  1 415 ? 53.021  6.063   -1.427  1.00   78.02  ? 415 ASN C CB  1 
ATOM   9016  C CG  . ASN C  1 415 ? 53.603  4.682   -1.677  1.00   79.69  ? 415 ASN C CG  1 
ATOM   9017  O OD1 . ASN C  1 415 ? 54.316  4.460   -2.652  1.00   78.61  ? 415 ASN C OD1 1 
ATOM   9018  N ND2 . ASN C  1 415 ? 53.294  3.744   -0.791  1.00   82.18  ? 415 ASN C ND2 1 
ATOM   9019  N N   . ASN C  1 416 ? 52.999  9.278   -2.378  1.00   74.90  ? 416 ASN C N   1 
ATOM   9020  C CA  . ASN C  1 416 ? 52.659  10.701  -2.253  1.00   78.16  ? 416 ASN C CA  1 
ATOM   9021  C C   . ASN C  1 416 ? 51.214  11.040  -2.036  1.00   79.36  ? 416 ASN C C   1 
ATOM   9022  O O   . ASN C  1 416 ? 50.319  10.453  -2.656  1.00   83.50  ? 416 ASN C O   1 
ATOM   9023  C CB  . ASN C  1 416 ? 53.091  11.494  -3.484  1.00   85.23  ? 416 ASN C CB  1 
ATOM   9024  C CG  . ASN C  1 416 ? 54.364  10.987  -4.079  1.00   91.39  ? 416 ASN C CG  1 
ATOM   9025  O OD1 . ASN C  1 416 ? 54.343  10.077  -4.907  1.00   96.50  ? 416 ASN C OD1 1 
ATOM   9026  N ND2 . ASN C  1 416 ? 55.497  11.543  -3.641  1.00   89.87  ? 416 ASN C ND2 1 
ATOM   9027  N N   . PRO C  1 417 ? 50.989  11.999  -1.134  1.00   76.78  ? 417 PRO C N   1 
ATOM   9028  C CA  . PRO C  1 417 ? 49.669  12.593  -0.966  1.00   81.92  ? 417 PRO C CA  1 
ATOM   9029  C C   . PRO C  1 417 ? 49.356  13.582  -2.134  1.00   87.35  ? 417 PRO C C   1 
ATOM   9030  O O   . PRO C  1 417 ? 48.887  13.162  -3.191  1.00   90.41  ? 417 PRO C O   1 
ATOM   9031  C CB  . PRO C  1 417 ? 49.774  13.304  0.374   1.00   78.78  ? 417 PRO C CB  1 
ATOM   9032  C CG  . PRO C  1 417 ? 51.214  13.618  0.531   1.00   72.72  ? 417 PRO C CG  1 
ATOM   9033  C CD  . PRO C  1 417 ? 52.007  12.680  -0.329  1.00   70.78  ? 417 PRO C CD  1 
ATOM   9034  N N   . SER D  1 10  ? 151.930 -0.101  5.563   1.00   91.84  ? 10  SER D N   1 
ATOM   9035  C CA  . SER D  1 10  ? 151.581 -0.734  4.290   1.00   92.33  ? 10  SER D CA  1 
ATOM   9036  C C   . SER D  1 10  ? 150.109 -0.420  3.960   1.00   88.72  ? 10  SER D C   1 
ATOM   9037  O O   . SER D  1 10  ? 149.569 -0.903  2.961   1.00   92.15  ? 10  SER D O   1 
ATOM   9038  C CB  . SER D  1 10  ? 151.822 -2.265  4.360   1.00   89.30  ? 10  SER D CB  1 
ATOM   9039  O OG  . SER D  1 10  ? 151.594 -2.923  3.115   1.00   89.37  ? 10  SER D OG  1 
ATOM   9040  N N   . LYS D  1 11  ? 149.479 0.403   4.802   1.00   80.83  ? 11  LYS D N   1 
ATOM   9041  C CA  . LYS D  1 11  ? 148.046 0.744   4.700   1.00   72.63  ? 11  LYS D CA  1 
ATOM   9042  C C   . LYS D  1 11  ? 147.100 -0.486  4.687   1.00   52.34  ? 11  LYS D C   1 
ATOM   9043  O O   . LYS D  1 11  ? 147.116 -1.326  3.778   1.00   53.97  ? 11  LYS D O   1 
ATOM   9044  C CB  . LYS D  1 11  ? 147.807 1.658   3.488   1.00   66.72  ? 11  LYS D CB  1 
ATOM   9045  C CG  . LYS D  1 11  ? 147.101 2.940   3.892   1.00   62.33  ? 11  LYS D CG  1 
ATOM   9046  C CD  . LYS D  1 11  ? 147.600 4.186   3.168   1.00   62.48  ? 11  LYS D CD  1 
ATOM   9047  C CE  . LYS D  1 11  ? 147.827 3.942   1.699   1.00   67.26  ? 11  LYS D CE  1 
ATOM   9048  N NZ  . LYS D  1 11  ? 148.463 5.130   1.063   1.00   70.46  ? 11  LYS D NZ  1 
ATOM   9049  N N   . PRO D  1 12  ? 146.311 -0.609  5.761   1.00   45.60  ? 12  PRO D N   1 
ATOM   9050  C CA  . PRO D  1 12  ? 145.398 -1.713  6.033   1.00   44.31  ? 12  PRO D CA  1 
ATOM   9051  C C   . PRO D  1 12  ? 144.226 -1.683  5.056   1.00   42.55  ? 12  PRO D C   1 
ATOM   9052  O O   . PRO D  1 12  ? 143.911 -0.627  4.481   1.00   38.29  ? 12  PRO D O   1 
ATOM   9053  C CB  . PRO D  1 12  ? 144.945 -1.447  7.468   1.00   41.85  ? 12  PRO D CB  1 
ATOM   9054  C CG  . PRO D  1 12  ? 145.048 -0.007  7.611   1.00   40.61  ? 12  PRO D CG  1 
ATOM   9055  C CD  . PRO D  1 12  ? 146.210 0.434   6.792   1.00   41.42  ? 12  PRO D CD  1 
ATOM   9056  N N   . ASN D  1 13  ? 143.612 -2.844  4.857   1.00   43.80  ? 13  ASN D N   1 
ATOM   9057  C CA  . ASN D  1 13  ? 142.484 -2.967  3.949   1.00   44.47  ? 13  ASN D CA  1 
ATOM   9058  C C   . ASN D  1 13  ? 141.133 -3.083  4.669   1.00   39.61  ? 13  ASN D C   1 
ATOM   9059  O O   . ASN D  1 13  ? 140.081 -3.079  4.031   1.00   38.14  ? 13  ASN D O   1 
ATOM   9060  C CB  . ASN D  1 13  ? 142.709 -4.173  3.053   1.00   51.18  ? 13  ASN D CB  1 
ATOM   9061  C CG  . ASN D  1 13  ? 143.724 -3.894  1.976   1.00   58.02  ? 13  ASN D CG  1 
ATOM   9062  O OD1 . ASN D  1 13  ? 143.689 -2.836  1.339   1.00   58.12  ? 13  ASN D OD1 1 
ATOM   9063  N ND2 . ASN D  1 13  ? 144.681 -4.813  1.806   1.00   61.13  ? 13  ASN D ND2 1 
ATOM   9064  N N   . LEU D  1 14  ? 141.177 -3.122  5.999   1.00   35.41  ? 14  LEU D N   1 
ATOM   9065  C CA  . LEU D  1 14  ? 139.992 -3.263  6.823   1.00   30.02  ? 14  LEU D CA  1 
ATOM   9066  C C   . LEU D  1 14  ? 140.234 -2.690  8.195   1.00   29.77  ? 14  LEU D C   1 
ATOM   9067  O O   . LEU D  1 14  ? 141.274 -2.913  8.772   1.00   30.94  ? 14  LEU D O   1 
ATOM   9068  C CB  . LEU D  1 14  ? 139.589 -4.737  6.926   1.00   31.46  ? 14  LEU D CB  1 
ATOM   9069  C CG  . LEU D  1 14  ? 138.232 -5.126  7.516   1.00   30.68  ? 14  LEU D CG  1 
ATOM   9070  C CD1 . LEU D  1 14  ? 137.067 -4.779  6.615   1.00   29.79  ? 14  LEU D CD1 1 
ATOM   9071  C CD2 . LEU D  1 14  ? 138.262 -6.611  7.744   1.00   33.28  ? 14  LEU D CD2 1 
ATOM   9072  N N   . LEU D  1 15  ? 139.274 -1.921  8.700   1.00   32.28  ? 15  LEU D N   1 
ATOM   9073  C CA  . LEU D  1 15  ? 139.355 -1.317  10.022  1.00   29.24  ? 15  LEU D CA  1 
ATOM   9074  C C   . LEU D  1 15  ? 138.173 -1.784  10.839  1.00   32.62  ? 15  LEU D C   1 
ATOM   9075  O O   . LEU D  1 15  ? 137.101 -1.998  10.293  1.00   35.38  ? 15  LEU D O   1 
ATOM   9076  C CB  . LEU D  1 15  ? 139.336 0.199   9.925   1.00   27.14  ? 15  LEU D CB  1 
ATOM   9077  C CG  . LEU D  1 15  ? 140.319 0.769   8.908   1.00   27.50  ? 15  LEU D CG  1 
ATOM   9078  C CD1 . LEU D  1 15  ? 140.054 2.259   8.753   1.00   27.43  ? 15  LEU D CD1 1 
ATOM   9079  C CD2 . LEU D  1 15  ? 141.757 0.474   9.338   1.00   27.41  ? 15  LEU D CD2 1 
ATOM   9080  N N   . VAL D  1 16  ? 138.349 -1.911  12.147  1.00   32.37  ? 16  VAL D N   1 
ATOM   9081  C CA  . VAL D  1 16  ? 137.298 -2.461  12.981  1.00   33.03  ? 16  VAL D CA  1 
ATOM   9082  C C   . VAL D  1 16  ? 137.075 -1.586  14.221  1.00   34.12  ? 16  VAL D C   1 
ATOM   9083  O O   . VAL D  1 16  ? 138.024 -1.231  14.937  1.00   33.94  ? 16  VAL D O   1 
ATOM   9084  C CB  . VAL D  1 16  ? 137.624 -3.919  13.408  1.00   36.29  ? 16  VAL D CB  1 
ATOM   9085  C CG1 . VAL D  1 16  ? 136.483 -4.525  14.214  1.00   33.23  ? 16  VAL D CG1 1 
ATOM   9086  C CG2 . VAL D  1 16  ? 137.904 -4.784  12.193  1.00   35.27  ? 16  VAL D CG2 1 
ATOM   9087  N N   . LEU D  1 17  ? 135.811 -1.241  14.454  1.00   34.06  ? 17  LEU D N   1 
ATOM   9088  C CA  . LEU D  1 17  ? 135.418 -0.470  15.623  1.00   34.83  ? 17  LEU D CA  1 
ATOM   9089  C C   . LEU D  1 17  ? 134.427 -1.238  16.489  1.00   32.42  ? 17  LEU D C   1 
ATOM   9090  O O   . LEU D  1 17  ? 133.277 -1.414  16.132  1.00   33.41  ? 17  LEU D O   1 
ATOM   9091  C CB  . LEU D  1 17  ? 134.795 0.857   15.202  1.00   35.64  ? 17  LEU D CB  1 
ATOM   9092  C CG  . LEU D  1 17  ? 134.325 1.672   16.396  1.00   38.57  ? 17  LEU D CG  1 
ATOM   9093  C CD1 . LEU D  1 17  ? 135.498 2.209   17.177  1.00   38.02  ? 17  LEU D CD1 1 
ATOM   9094  C CD2 . LEU D  1 17  ? 133.451 2.794   15.907  1.00   39.89  ? 17  LEU D CD2 1 
ATOM   9095  N N   . PRO D  1 18  ? 134.882 -1.697  17.645  1.00   32.55  ? 18  PRO D N   1 
ATOM   9096  C CA  . PRO D  1 18  ? 133.970 -2.389  18.548  1.00   34.07  ? 18  PRO D CA  1 
ATOM   9097  C C   . PRO D  1 18  ? 132.949 -1.421  19.165  1.00   36.60  ? 18  PRO D C   1 
ATOM   9098  O O   . PRO D  1 18  ? 133.326 -0.288  19.514  1.00   36.86  ? 18  PRO D O   1 
ATOM   9099  C CB  . PRO D  1 18  ? 134.909 -2.956  19.606  1.00   34.28  ? 18  PRO D CB  1 
ATOM   9100  C CG  . PRO D  1 18  ? 136.285 -2.929  18.972  1.00   32.24  ? 18  PRO D CG  1 
ATOM   9101  C CD  . PRO D  1 18  ? 136.268 -1.720  18.141  1.00   31.85  ? 18  PRO D CD  1 
ATOM   9102  N N   . VAL D  1 19  ? 131.687 -1.853  19.272  1.00   34.19  ? 19  VAL D N   1 
ATOM   9103  C CA  . VAL D  1 19  ? 130.600 -1.023  19.805  1.00   33.99  ? 19  VAL D CA  1 
ATOM   9104  C C   . VAL D  1 19  ? 129.837 -1.801  20.860  1.00   36.98  ? 19  VAL D C   1 
ATOM   9105  O O   . VAL D  1 19  ? 129.860 -3.028  20.841  1.00   38.44  ? 19  VAL D O   1 
ATOM   9106  C CB  . VAL D  1 19  ? 129.615 -0.533  18.699  1.00   39.47  ? 19  VAL D CB  1 
ATOM   9107  C CG1 . VAL D  1 19  ? 130.340 0.271   17.649  1.00   35.96  ? 19  VAL D CG1 1 
ATOM   9108  C CG2 . VAL D  1 19  ? 128.897 -1.689  18.055  1.00   41.40  ? 19  VAL D CG2 1 
ATOM   9109  N N   . GLN D  1 20  ? 129.188 -1.099  21.793  1.00   37.57  ? 20  GLN D N   1 
ATOM   9110  C CA  . GLN D  1 20  ? 128.469 -1.765  22.884  1.00   39.57  ? 20  GLN D CA  1 
ATOM   9111  C C   . GLN D  1 20  ? 127.039 -1.278  23.102  1.00   40.23  ? 20  GLN D C   1 
ATOM   9112  O O   . GLN D  1 20  ? 126.778 -0.091  23.013  1.00   41.84  ? 20  GLN D O   1 
ATOM   9113  C CB  . GLN D  1 20  ? 129.237 -1.605  24.175  1.00   42.63  ? 20  GLN D CB  1 
ATOM   9114  C CG  . GLN D  1 20  ? 128.692 -2.472  25.265  1.00   50.67  ? 20  GLN D CG  1 
ATOM   9115  C CD  . GLN D  1 20  ? 129.595 -2.491  26.456  1.00   60.01  ? 20  GLN D CD  1 
ATOM   9116  O OE1 . GLN D  1 20  ? 129.337 -1.826  27.459  1.00   64.66  ? 20  GLN D OE1 1 
ATOM   9117  N NE2 . GLN D  1 20  ? 130.678 -3.252  26.356  1.00   62.82  ? 20  GLN D NE2 1 
ATOM   9118  N N   . GLU D  1 21  ? 126.124 -2.187  23.425  1.00   41.05  ? 21  GLU D N   1 
ATOM   9119  C CA  . GLU D  1 21  ? 124.748 -1.803  23.710  1.00   44.18  ? 21  GLU D CA  1 
ATOM   9120  C C   . GLU D  1 21  ? 124.607 -1.277  25.122  1.00   47.46  ? 21  GLU D C   1 
ATOM   9121  O O   . GLU D  1 21  ? 125.174 -1.832  26.052  1.00   49.23  ? 21  GLU D O   1 
ATOM   9122  C CB  . GLU D  1 21  ? 123.807 -2.987  23.512  1.00   47.35  ? 21  GLU D CB  1 
ATOM   9123  C CG  . GLU D  1 21  ? 122.333 -2.610  23.289  1.00   52.41  ? 21  GLU D CG  1 
ATOM   9124  C CD  . GLU D  1 21  ? 121.446 -2.763  24.532  1.00   58.67  ? 21  GLU D CD  1 
ATOM   9125  O OE1 . GLU D  1 21  ? 121.959 -3.118  25.616  1.00   61.41  ? 21  GLU D OE1 1 
ATOM   9126  O OE2 . GLU D  1 21  ? 120.219 -2.554  24.412  1.00   58.79  ? 21  GLU D OE2 1 
ATOM   9127  N N   . ASP D  1 22  ? 123.863 -0.187  25.272  1.00   48.76  ? 22  ASP D N   1 
ATOM   9128  C CA  . ASP D  1 22  ? 123.557 0.361   26.596  1.00   51.40  ? 22  ASP D CA  1 
ATOM   9129  C C   . ASP D  1 22  ? 122.183 -0.117  27.026  1.00   53.04  ? 22  ASP D C   1 
ATOM   9130  O O   . ASP D  1 22  ? 121.186 0.191   26.376  1.00   47.65  ? 22  ASP D O   1 
ATOM   9131  C CB  . ASP D  1 22  ? 123.609 1.894   26.601  1.00   50.20  ? 22  ASP D CB  1 
ATOM   9132  C CG  . ASP D  1 22  ? 123.252 2.487   27.954  1.00   55.87  ? 22  ASP D CG  1 
ATOM   9133  O OD1 . ASP D  1 22  ? 123.991 2.229   28.931  1.00   59.87  ? 22  ASP D OD1 1 
ATOM   9134  O OD2 . ASP D  1 22  ? 122.235 3.210   28.051  1.00   57.14  1 22  ASP D OD2 1 
ATOM   9135  N N   . ALA D  1 23  ? 122.134 -0.865  28.121  1.00   53.33  ? 23  ALA D N   1 
ATOM   9136  C CA  . ALA D  1 23  ? 120.912 -1.523  28.542  1.00   57.52  ? 23  ALA D CA  1 
ATOM   9137  C C   . ALA D  1 23  ? 119.770 -0.546  28.820  1.00   60.52  ? 23  ALA D C   1 
ATOM   9138  O O   . ALA D  1 23  ? 118.641 -0.756  28.377  1.00   59.56  ? 23  ALA D O   1 
ATOM   9139  C CB  . ALA D  1 23  ? 121.190 -2.349  29.771  1.00   60.49  ? 23  ALA D CB  1 
ATOM   9140  N N   . SER D  1 24  ? 120.084 0.540   29.515  1.00   62.19  ? 24  SER D N   1 
ATOM   9141  C CA  . SER D  1 24  ? 119.090 1.531   29.908  1.00   64.30  ? 24  SER D CA  1 
ATOM   9142  C C   . SER D  1 24  ? 118.337 2.159   28.728  1.00   63.16  ? 24  SER D C   1 
ATOM   9143  O O   . SER D  1 24  ? 117.107 2.193   28.718  1.00   64.68  ? 24  SER D O   1 
ATOM   9144  C CB  . SER D  1 24  ? 119.779 2.625   30.726  1.00   66.15  ? 24  SER D CB  1 
ATOM   9145  O OG  . SER D  1 24  ? 118.907 3.697   31.013  1.00   69.26  ? 24  SER D OG  1 
ATOM   9146  N N   . THR D  1 25  ? 119.084 2.628   27.729  1.00   59.18  ? 25  THR D N   1 
ATOM   9147  C CA  . THR D  1 25  ? 118.533 3.388   26.611  1.00   54.77  ? 25  THR D CA  1 
ATOM   9148  C C   . THR D  1 25  ? 118.257 2.546   25.368  1.00   51.68  ? 25  THR D C   1 
ATOM   9149  O O   . THR D  1 25  ? 117.468 2.936   24.510  1.00   49.98  ? 25  THR D O   1 
ATOM   9150  C CB  . THR D  1 25  ? 119.493 4.508   26.204  1.00   50.24  ? 25  THR D CB  1 
ATOM   9151  O OG1 . THR D  1 25  ? 120.708 3.924   25.724  1.00   47.40  ? 25  THR D OG1 1 
ATOM   9152  C CG2 . THR D  1 25  ? 119.806 5.414   27.385  1.00   52.86  ? 25  THR D CG2 1 
ATOM   9153  N N   . GLY D  1 26  ? 118.911 1.395   25.265  1.00   51.01  ? 26  GLY D N   1 
ATOM   9154  C CA  . GLY D  1 26  ? 118.750 0.531   24.109  1.00   48.76  ? 26  GLY D CA  1 
ATOM   9155  C C   . GLY D  1 26  ? 119.561 0.991   22.922  1.00   46.90  ? 26  GLY D C   1 
ATOM   9156  O O   . GLY D  1 26  ? 119.446 0.437   21.821  1.00   44.37  ? 26  GLY D O   1 
ATOM   9157  N N   . LEU D  1 27  ? 120.397 2.002   23.165  1.00   47.98  ? 27  LEU D N   1 
ATOM   9158  C CA  . LEU D  1 27  ? 121.267 2.594   22.151  1.00   45.65  ? 27  LEU D CA  1 
ATOM   9159  C C   . LEU D  1 27  ? 122.658 1.963   22.221  1.00   42.09  ? 27  LEU D C   1 
ATOM   9160  O O   . LEU D  1 27  ? 122.975 1.247   23.168  1.00   41.55  ? 27  LEU D O   1 
ATOM   9161  C CB  . LEU D  1 27  ? 121.359 4.110   22.346  1.00   46.57  ? 27  LEU D CB  1 
ATOM   9162  C CG  . LEU D  1 27  ? 120.012 4.836   22.299  1.00   49.70  ? 27  LEU D CG  1 
ATOM   9163  C CD1 . LEU D  1 27  ? 120.184 6.303   22.631  1.00   51.99  ? 27  LEU D CD1 1 
ATOM   9164  C CD2 . LEU D  1 27  ? 119.390 4.673   20.936  1.00   46.66  ? 27  LEU D CD2 1 
ATOM   9165  N N   . HIS D  1 28  ? 123.471 2.205   21.198  1.00   41.62  ? 28  HIS D N   1 
ATOM   9166  C CA  . HIS D  1 28  ? 124.811 1.634   21.116  1.00   40.02  ? 28  HIS D CA  1 
ATOM   9167  C C   . HIS D  1 28  ? 125.851 2.741   21.130  1.00   42.63  ? 28  HIS D C   1 
ATOM   9168  O O   . HIS D  1 28  ? 125.599 3.817   20.626  1.00   44.74  ? 28  HIS D O   1 
ATOM   9169  C CB  . HIS D  1 28  ? 124.947 0.776   19.859  1.00   35.20  ? 28  HIS D CB  1 
ATOM   9170  C CG  . HIS D  1 28  ? 124.109 -0.463  19.895  1.00   35.16  ? 28  HIS D CG  1 
ATOM   9171  N ND1 . HIS D  1 28  ? 124.650 -1.722  19.994  1.00   33.99  ? 28  HIS D ND1 1 
ATOM   9172  C CD2 . HIS D  1 28  ? 122.766 -0.632  19.876  1.00   38.14  ? 28  HIS D CD2 1 
ATOM   9173  C CE1 . HIS D  1 28  ? 123.677 -2.614  20.023  1.00   37.38  ? 28  HIS D CE1 1 
ATOM   9174  N NE2 . HIS D  1 28  ? 122.522 -1.979  19.960  1.00   37.91  ? 28  HIS D NE2 1 
ATOM   9175  N N   . TRP D  1 29  ? 127.021 2.468   21.705  1.00   44.04  ? 29  TRP D N   1 
ATOM   9176  C CA  . TRP D  1 29  ? 128.100 3.458   21.855  1.00   40.60  ? 29  TRP D CA  1 
ATOM   9177  C C   . TRP D  1 29  ? 129.460 2.772   21.627  1.00   41.80  ? 29  TRP D C   1 
ATOM   9178  O O   . TRP D  1 29  ? 129.574 1.542   21.658  1.00   42.18  ? 29  TRP D O   1 
ATOM   9179  C CB  . TRP D  1 29  ? 128.049 4.121   23.252  1.00   39.90  ? 29  TRP D CB  1 
ATOM   9180  C CG  . TRP D  1 29  ? 128.274 3.142   24.403  1.00   41.86  ? 29  TRP D CG  1 
ATOM   9181  C CD1 . TRP D  1 29  ? 127.352 2.308   24.961  1.00   41.25  ? 29  TRP D CD1 1 
ATOM   9182  C CD2 . TRP D  1 29  ? 129.501 2.903   25.110  1.00   46.86  ? 29  TRP D CD2 1 
ATOM   9183  N NE1 . TRP D  1 29  ? 127.923 1.561   25.957  1.00   41.45  ? 29  TRP D NE1 1 
ATOM   9184  C CE2 . TRP D  1 29  ? 129.240 1.906   26.072  1.00   46.64  ? 29  TRP D CE2 1 
ATOM   9185  C CE3 . TRP D  1 29  ? 130.802 3.426   25.012  1.00   50.27  ? 29  TRP D CE3 1 
ATOM   9186  C CZ2 . TRP D  1 29  ? 130.221 1.429   26.942  1.00   49.36  ? 29  TRP D CZ2 1 
ATOM   9187  C CZ3 . TRP D  1 29  ? 131.782 2.949   25.888  1.00   51.77  ? 29  TRP D CZ3 1 
ATOM   9188  C CH2 . TRP D  1 29  ? 131.480 1.962   26.836  1.00   50.70  ? 29  TRP D CH2 1 
ATOM   9189  N N   . ALA D  1 30  ? 130.488 3.576   21.388  1.00   43.33  ? 30  ALA D N   1 
ATOM   9190  C CA  . ALA D  1 30  ? 131.845 3.070   21.197  1.00   41.20  ? 30  ALA D CA  1 
ATOM   9191  C C   . ALA D  1 30  ? 132.838 3.961   21.907  1.00   39.67  ? 30  ALA D C   1 
ATOM   9192  O O   . ALA D  1 30  ? 132.636 5.158   22.012  1.00   38.50  ? 30  ALA D O   1 
ATOM   9193  C CB  . ALA D  1 30  ? 132.195 2.977   19.703  1.00   37.01  ? 30  ALA D CB  1 
ATOM   9194  N N   . ASN D  1 31  ? 133.903 3.358   22.407  1.00   42.82  ? 31  ASN D N   1 
ATOM   9195  C CA  . ASN D  1 31  ? 135.063 4.105   22.852  1.00   47.04  ? 31  ASN D CA  1 
ATOM   9196  C C   . ASN D  1 31  ? 135.916 4.440   21.634  1.00   47.20  ? 31  ASN D C   1 
ATOM   9197  O O   . ASN D  1 31  ? 136.361 3.544   20.924  1.00   47.90  ? 31  ASN D O   1 
ATOM   9198  C CB  . ASN D  1 31  ? 135.869 3.309   23.876  1.00   50.38  ? 31  ASN D CB  1 
ATOM   9199  C CG  . ASN D  1 31  ? 135.320 3.440   25.276  1.00   54.69  ? 31  ASN D CG  1 
ATOM   9200  O OD1 . ASN D  1 31  ? 134.902 2.455   25.882  1.00   57.78  ? 31  ASN D OD1 1 
ATOM   9201  N ND2 . ASN D  1 31  ? 135.312 4.656   25.799  1.00   55.87  ? 31  ASN D ND2 1 
ATOM   9202  N N   . ILE D  1 32  ? 136.084 5.732   21.366  1.00   48.96  ? 32  ILE D N   1 
ATOM   9203  C CA  . ILE D  1 32  ? 136.929 6.225   20.272  1.00   47.75  ? 32  ILE D CA  1 
ATOM   9204  C C   . ILE D  1 32  ? 138.281 6.722   20.791  1.00   49.65  ? 32  ILE D C   1 
ATOM   9205  O O   . ILE D  1 32  ? 138.349 7.439   21.796  1.00   55.82  ? 32  ILE D O   1 
ATOM   9206  C CB  . ILE D  1 32  ? 136.235 7.372   19.494  1.00   58.55  ? 32  ILE D CB  1 
ATOM   9207  C CG1 . ILE D  1 32  ? 134.864 6.922   18.995  1.00   58.35  ? 32  ILE D CG1 1 
ATOM   9208  C CG2 . ILE D  1 32  ? 137.072 7.830   18.295  1.00   56.20  ? 32  ILE D CG2 1 
ATOM   9209  C CD1 . ILE D  1 32  ? 134.935 5.908   17.876  1.00   57.20  ? 32  ILE D CD1 1 
ATOM   9210  N N   . HIS D  1 33  ? 139.359 6.338   20.118  1.00   43.63  ? 33  HIS D N   1 
ATOM   9211  C CA  . HIS D  1 33  ? 140.678 6.802   20.516  1.00   41.43  ? 33  HIS D CA  1 
ATOM   9212  C C   . HIS D  1 33  ? 141.022 8.091   19.798  1.00   40.96  ? 33  HIS D C   1 
ATOM   9213  O O   . HIS D  1 33  ? 140.946 8.161   18.575  1.00   39.77  ? 33  HIS D O   1 
ATOM   9214  C CB  . HIS D  1 33  ? 141.720 5.732   20.256  1.00   41.51  ? 33  HIS D CB  1 
ATOM   9215  C CG  . HIS D  1 33  ? 141.562 4.528   21.128  1.00   44.50  ? 33  HIS D CG  1 
ATOM   9216  N ND1 . HIS D  1 33  ? 140.504 3.652   21.007  1.00   44.40  ? 33  HIS D ND1 1 
ATOM   9217  C CD2 . HIS D  1 33  ? 142.331 4.054   22.136  1.00   48.14  ? 33  HIS D CD2 1 
ATOM   9218  C CE1 . HIS D  1 33  ? 140.623 2.695   21.910  1.00   45.73  ? 33  HIS D CE1 1 
ATOM   9219  N NE2 . HIS D  1 33  ? 141.725 2.914   22.604  1.00   48.62  ? 33  HIS D NE2 1 
ATOM   9220  N N   . LYS D  1 34  ? 141.356 9.119   20.578  1.00   43.02  ? 34  LYS D N   1 
ATOM   9221  C CA  . LYS D  1 34  ? 141.658 10.454  20.060  1.00   39.52  ? 34  LYS D CA  1 
ATOM   9222  C C   . LYS D  1 34  ? 142.833 11.092  20.796  1.00   39.52  ? 34  LYS D C   1 
ATOM   9223  O O   . LYS D  1 34  ? 143.138 10.714  21.937  1.00   40.07  ? 34  LYS D O   1 
ATOM   9224  C CB  . LYS D  1 34  ? 140.439 11.361  20.224  1.00   39.68  ? 34  LYS D CB  1 
ATOM   9225  C CG  . LYS D  1 34  ? 139.107 10.832  19.671  1.00   40.79  ? 34  LYS D CG  1 
ATOM   9226  C CD  . LYS D  1 34  ? 138.781 11.368  18.298  1.00   43.79  ? 34  LYS D CD  1 
ATOM   9227  C CE  . LYS D  1 34  ? 138.610 12.872  18.368  1.00   48.76  ? 34  LYS D CE  1 
ATOM   9228  N NZ  . LYS D  1 34  ? 137.915 13.439  17.203  1.00   51.44  ? 34  LYS D NZ  1 
ATOM   9229  N N   . ARG D  1 35  ? 143.438 12.089  20.146  1.00   39.59  ? 35  ARG D N   1 
ATOM   9230  C CA  . ARG D  1 35  ? 144.421 13.008  20.742  1.00   41.84  ? 35  ARG D CA  1 
ATOM   9231  C C   . ARG D  1 35  ? 145.835 12.471  20.934  1.00   44.56  ? 35  ARG D C   1 
ATOM   9232  O O   . ARG D  1 35  ? 146.102 11.280  20.781  1.00   44.57  ? 35  ARG D O   1 
ATOM   9233  C CB  . ARG D  1 35  ? 143.904 13.518  22.093  1.00   45.88  ? 35  ARG D CB  1 
ATOM   9234  C CG  . ARG D  1 35  ? 142.576 14.214  21.961  1.00   47.33  ? 35  ARG D CG  1 
ATOM   9235  C CD  . ARG D  1 35  ? 141.894 14.410  23.280  1.00   51.31  ? 35  ARG D CD  1 
ATOM   9236  N NE  . ARG D  1 35  ? 140.471 14.618  23.041  1.00   53.89  ? 35  ARG D NE  1 
ATOM   9237  C CZ  . ARG D  1 35  ? 139.574 14.892  23.984  1.00   58.94  ? 35  ARG D CZ  1 
ATOM   9238  N NH1 . ARG D  1 35  ? 139.945 14.973  25.260  1.00   63.54  ? 35  ARG D NH1 1 
ATOM   9239  N NH2 . ARG D  1 35  ? 138.300 15.067  23.650  1.00   57.26  ? 35  ARG D NH2 1 
ATOM   9240  N N   . THR D  1 36  ? 146.735 13.391  21.273  1.00   49.72  ? 36  THR D N   1 
ATOM   9241  C CA  . THR D  1 36  ? 148.101 13.064  21.667  1.00   53.27  ? 36  THR D CA  1 
ATOM   9242  C C   . THR D  1 36  ? 148.356 13.714  23.026  1.00   56.40  ? 36  THR D C   1 
ATOM   9243  O O   . THR D  1 36  ? 148.418 14.941  23.131  1.00   59.42  ? 36  THR D O   1 
ATOM   9244  C CB  . THR D  1 36  ? 149.141 13.554  20.621  1.00   45.05  ? 36  THR D CB  1 
ATOM   9245  O OG1 . THR D  1 36  ? 148.820 13.033  19.322  1.00   43.46  ? 36  THR D OG1 1 
ATOM   9246  C CG2 . THR D  1 36  ? 150.509 13.085  20.990  1.00   45.85  ? 36  THR D CG2 1 
ATOM   9247  N N   . PRO D  1 37  ? 148.505 12.900  24.080  1.00   56.23  ? 37  PRO D N   1 
ATOM   9248  C CA  . PRO D  1 37  ? 148.507 11.431  24.120  1.00   55.71  ? 37  PRO D CA  1 
ATOM   9249  C C   . PRO D  1 37  ? 147.150 10.830  23.812  1.00   55.12  ? 37  PRO D C   1 
ATOM   9250  O O   . PRO D  1 37  ? 146.138 11.465  24.076  1.00   59.38  ? 37  PRO D O   1 
ATOM   9251  C CB  . PRO D  1 37  ? 148.889 11.128  25.563  1.00   58.59  ? 37  PRO D CB  1 
ATOM   9252  C CG  . PRO D  1 37  ? 148.427 12.319  26.321  1.00   59.21  ? 37  PRO D CG  1 
ATOM   9253  C CD  . PRO D  1 37  ? 148.633 13.485  25.424  1.00   57.48  ? 37  PRO D CD  1 
ATOM   9254  N N   . LEU D  1 38  ? 147.136 9.627   23.254  1.00   50.28  ? 38  LEU D N   1 
ATOM   9255  C CA  . LEU D  1 38  ? 145.899 8.994   22.808  1.00   46.61  ? 38  LEU D CA  1 
ATOM   9256  C C   . LEU D  1 38  ? 145.006 8.653   24.006  1.00   47.34  ? 38  LEU D C   1 
ATOM   9257  O O   . LEU D  1 38  ? 145.518 8.223   25.047  1.00   49.21  ? 38  LEU D O   1 
ATOM   9258  C CB  . LEU D  1 38  ? 146.220 7.734   22.006  1.00   46.20  ? 38  LEU D CB  1 
ATOM   9259  C CG  . LEU D  1 38  ? 145.289 7.275   20.884  1.00   43.67  ? 38  LEU D CG  1 
ATOM   9260  C CD1 . LEU D  1 38  ? 145.251 8.304   19.768  1.00   41.67  ? 38  LEU D CD1 1 
ATOM   9261  C CD2 . LEU D  1 38  ? 145.667 5.892   20.361  1.00   42.54  ? 38  LEU D CD2 1 
ATOM   9262  N N   . MET D  1 39  ? 143.691 8.869   23.895  1.00   44.61  ? 39  MET D N   1 
ATOM   9263  C CA  . MET D  1 39  ? 142.785 8.438   24.968  1.00   47.06  ? 39  MET D CA  1 
ATOM   9264  C C   . MET D  1 39  ? 141.405 8.043   24.448  1.00   47.86  ? 39  MET D C   1 
ATOM   9265  O O   . MET D  1 39  ? 141.126 8.184   23.270  1.00   47.41  ? 39  MET D O   1 
ATOM   9266  C CB  . MET D  1 39  ? 142.675 9.512   26.055  1.00   50.43  ? 39  MET D CB  1 
ATOM   9267  C CG  . MET D  1 39  ? 142.448 10.915  25.557  1.00   50.87  ? 39  MET D CG  1 
ATOM   9268  S SD  . MET D  1 39  ? 140.751 11.251  25.094  1.00   82.28  ? 39  MET D SD  1 
ATOM   9269  C CE  . MET D  1 39  ? 139.962 11.241  26.703  1.00   54.80  ? 39  MET D CE  1 
ATOM   9270  N N   . GLN D  1 40  ? 140.557 7.514   25.329  1.00   50.58  ? 40  GLN D N   1 
ATOM   9271  C CA  . GLN D  1 40  ? 139.244 7.007   24.934  1.00   46.67  ? 40  GLN D CA  1 
ATOM   9272  C C   . GLN D  1 40  ? 138.123 7.969   25.283  1.00   45.11  ? 40  GLN D C   1 
ATOM   9273  O O   . GLN D  1 40  ? 138.031 8.447   26.408  1.00   47.62  ? 40  GLN D O   1 
ATOM   9274  C CB  . GLN D  1 40  ? 138.964 5.679   25.610  1.00   50.20  ? 40  GLN D CB  1 
ATOM   9275  C CG  . GLN D  1 40  ? 139.872 4.567   25.173  1.00   55.62  ? 40  GLN D CG  1 
ATOM   9276  C CD  . GLN D  1 40  ? 139.540 3.262   25.867  1.00   61.46  ? 40  GLN D CD  1 
ATOM   9277  O OE1 . GLN D  1 40  ? 138.965 2.359   25.263  1.00   62.97  ? 40  GLN D OE1 1 
ATOM   9278  N NE2 . GLN D  1 40  ? 139.889 3.161   27.146  1.00   65.07  ? 40  GLN D NE2 1 
ATOM   9279  N N   . VAL D  1 41  ? 137.270 8.231   24.303  1.00   42.52  ? 41  VAL D N   1 
ATOM   9280  C CA  . VAL D  1 41  ? 136.106 9.081   24.470  1.00   45.92  ? 41  VAL D CA  1 
ATOM   9281  C C   . VAL D  1 41  ? 134.858 8.302   24.162  1.00   42.71  ? 41  VAL D C   1 
ATOM   9282  O O   . VAL D  1 41  ? 134.665 7.924   23.014  1.00   41.87  ? 41  VAL D O   1 
ATOM   9283  C CB  . VAL D  1 41  ? 136.129 10.267  23.510  1.00   51.94  ? 41  VAL D CB  1 
ATOM   9284  C CG1 . VAL D  1 41  ? 135.055 11.264  23.903  1.00   58.59  ? 41  VAL D CG1 1 
ATOM   9285  C CG2 . VAL D  1 41  ? 137.501 10.911  23.473  1.00   52.75  ? 41  VAL D CG2 1 
ATOM   9286  N N   . PRO D  1 42  ? 133.975 8.104   25.148  1.00   43.71  ? 42  PRO D N   1 
ATOM   9287  C CA  . PRO D  1 42  ? 132.734 7.387   24.827  1.00   41.53  ? 42  PRO D CA  1 
ATOM   9288  C C   . PRO D  1 42  ? 131.749 8.262   24.039  1.00   40.54  ? 42  PRO D C   1 
ATOM   9289  O O   . PRO D  1 42  ? 131.422 9.365   24.486  1.00   42.75  ? 42  PRO D O   1 
ATOM   9290  C CB  . PRO D  1 42  ? 132.202 6.991   26.203  1.00   43.93  ? 42  PRO D CB  1 
ATOM   9291  C CG  . PRO D  1 42  ? 132.789 7.976   27.133  1.00   47.09  ? 42  PRO D CG  1 
ATOM   9292  C CD  . PRO D  1 42  ? 134.113 8.373   26.590  1.00   46.70  ? 42  PRO D CD  1 
ATOM   9293  N N   . LEU D  1 43  ? 131.328 7.768   22.870  1.00   38.18  ? 43  LEU D N   1 
ATOM   9294  C CA  . LEU D  1 43  ? 130.461 8.491   21.917  1.00   37.91  ? 43  LEU D CA  1 
ATOM   9295  C C   . LEU D  1 43  ? 129.278 7.655   21.426  1.00   37.00  ? 43  LEU D C   1 
ATOM   9296  O O   . LEU D  1 43  ? 129.397 6.449   21.265  1.00   37.39  ? 43  LEU D O   1 
ATOM   9297  C CB  . LEU D  1 43  ? 131.257 8.956   20.683  1.00   37.42  ? 43  LEU D CB  1 
ATOM   9298  C CG  . LEU D  1 43  ? 132.441 9.908   20.876  1.00   38.12  ? 43  LEU D CG  1 
ATOM   9299  C CD1 . LEU D  1 43  ? 133.159 10.141  19.598  1.00   29.16  ? 43  LEU D CD1 1 
ATOM   9300  C CD2 . LEU D  1 43  ? 131.963 11.227  21.457  1.00   40.64  ? 43  LEU D CD2 1 
ATOM   9301  N N   . LEU D  1 44  ? 128.136 8.301   21.201  1.00   36.78  ? 44  LEU D N   1 
ATOM   9302  C CA  . LEU D  1 44  ? 126.952 7.629   20.670  1.00   38.31  ? 44  LEU D CA  1 
ATOM   9303  C C   . LEU D  1 44  ? 127.091 7.249   19.184  1.00   37.71  ? 44  LEU D C   1 
ATOM   9304  O O   . LEU D  1 44  ? 127.626 8.009   18.383  1.00   36.15  ? 44  LEU D O   1 
ATOM   9305  C CB  . LEU D  1 44  ? 125.712 8.498   20.865  1.00   41.83  ? 44  LEU D CB  1 
ATOM   9306  C CG  . LEU D  1 44  ? 124.368 7.918   20.412  1.00   43.14  ? 44  LEU D CG  1 
ATOM   9307  C CD1 . LEU D  1 44  ? 123.782 6.979   21.441  1.00   42.29  ? 44  LEU D CD1 1 
ATOM   9308  C CD2 . LEU D  1 44  ? 123.379 9.012   20.071  1.00   48.23  ? 44  LEU D CD2 1 
ATOM   9309  N N   . LEU D  1 45  ? 126.618 6.053   18.839  1.00   37.20  ? 45  LEU D N   1 
ATOM   9310  C CA  . LEU D  1 45  ? 126.562 5.589   17.458  1.00   34.75  ? 45  LEU D CA  1 
ATOM   9311  C C   . LEU D  1 45  ? 125.354 6.161   16.727  1.00   33.65  ? 45  LEU D C   1 
ATOM   9312  O O   . LEU D  1 45  ? 124.223 5.806   17.010  1.00   32.82  ? 45  LEU D O   1 
ATOM   9313  C CB  . LEU D  1 45  ? 126.544 4.052   17.419  1.00   34.88  ? 45  LEU D CB  1 
ATOM   9314  C CG  . LEU D  1 45  ? 126.327 3.456   16.035  1.00   32.69  ? 45  LEU D CG  1 
ATOM   9315  C CD1 . LEU D  1 45  ? 127.491 3.837   15.173  1.00   32.37  ? 45  LEU D CD1 1 
ATOM   9316  C CD2 . LEU D  1 45  ? 126.206 1.970   16.101  1.00   31.55  ? 45  LEU D CD2 1 
ATOM   9317  N N   . ASP D  1 46  ? 125.610 7.031   15.765  1.00   35.13  ? 46  ASP D N   1 
ATOM   9318  C CA  . ASP D  1 46  ? 124.542 7.694   15.049  1.00   37.85  ? 46  ASP D CA  1 
ATOM   9319  C C   . ASP D  1 46  ? 124.728 7.363   13.586  1.00   35.75  ? 46  ASP D C   1 
ATOM   9320  O O   . ASP D  1 46  ? 125.487 8.011   12.881  1.00   30.16  ? 46  ASP D O   1 
ATOM   9321  C CB  . ASP D  1 46  ? 124.577 9.209   15.308  1.00   39.69  ? 46  ASP D CB  1 
ATOM   9322  C CG  . ASP D  1 46  ? 123.418 9.958   14.662  1.00   40.55  ? 46  ASP D CG  1 
ATOM   9323  O OD1 . ASP D  1 46  ? 122.514 9.299   14.111  1.00   42.01  ? 46  ASP D OD1 1 
ATOM   9324  O OD2 . ASP D  1 46  ? 123.402 11.206  14.727  1.00   38.77  1 46  ASP D OD2 1 
ATOM   9325  N N   . LEU D  1 47  ? 124.026 6.335   13.144  1.00   36.06  ? 47  LEU D N   1 
ATOM   9326  C CA  . LEU D  1 47  ? 124.182 5.834   11.796  1.00   34.96  ? 47  LEU D CA  1 
ATOM   9327  C C   . LEU D  1 47  ? 124.024 6.915   10.735  1.00   34.94  ? 47  LEU D C   1 
ATOM   9328  O O   . LEU D  1 47  ? 124.762 6.929   9.765   1.00   34.46  ? 47  LEU D O   1 
ATOM   9329  C CB  . LEU D  1 47  ? 123.161 4.729   11.540  1.00   34.33  ? 47  LEU D CB  1 
ATOM   9330  C CG  . LEU D  1 47  ? 123.176 4.219   10.105  1.00   32.19  ? 47  LEU D CG  1 
ATOM   9331  C CD1 . LEU D  1 47  ? 124.489 3.513   9.808   1.00   29.65  ? 47  LEU D CD1 1 
ATOM   9332  C CD2 . LEU D  1 47  ? 121.991 3.341   9.829   1.00   33.20  ? 47  LEU D CD2 1 
ATOM   9333  N N   . ASN D  1 48  ? 123.043 7.803   10.912  1.00   35.69  ? 48  ASN D N   1 
ATOM   9334  C CA  . ASN D  1 48  ? 122.742 8.820   9.918   1.00   31.99  ? 48  ASN D CA  1 
ATOM   9335  C C   . ASN D  1 48  ? 123.400 10.170  10.194  1.00   33.10  ? 48  ASN D C   1 
ATOM   9336  O O   . ASN D  1 48  ? 123.220 11.128  9.443   1.00   35.28  ? 48  ASN D O   1 
ATOM   9337  C CB  . ASN D  1 48  ? 121.234 9.008   9.808   1.00   34.46  ? 48  ASN D CB  1 
ATOM   9338  C CG  . ASN D  1 48  ? 120.559 7.808   9.261   1.00   34.66  ? 48  ASN D CG  1 
ATOM   9339  O OD1 . ASN D  1 48  ? 120.992 7.280   8.261   1.00   35.59  ? 48  ASN D OD1 1 
ATOM   9340  N ND2 . ASN D  1 48  ? 119.480 7.385   9.880   1.00   35.93  ? 48  ASN D ND2 1 
ATOM   9341  N N   . GLY D  1 49  ? 124.178 10.240  11.261  1.00   33.98  ? 49  GLY D N   1 
ATOM   9342  C CA  . GLY D  1 49  ? 124.828 11.473  11.650  1.00   33.99  ? 49  GLY D CA  1 
ATOM   9343  C C   . GLY D  1 49  ? 125.835 11.939  10.619  1.00   32.44  ? 49  GLY D C   1 
ATOM   9344  O O   . GLY D  1 49  ? 126.594 11.163  10.039  1.00   30.68  ? 49  GLY D O   1 
ATOM   9345  N N   . LYS D  1 50  ? 125.844 13.245  10.405  1.00   33.64  ? 50  LYS D N   1 
ATOM   9346  C CA  . LYS D  1 50  ? 126.634 13.828  9.356   1.00   31.42  ? 50  LYS D CA  1 
ATOM   9347  C C   . LYS D  1 50  ? 128.088 13.926  9.765   1.00   31.37  ? 50  LYS D C   1 
ATOM   9348  O O   . LYS D  1 50  ? 128.947 14.040  8.911   1.00   30.43  ? 50  LYS D O   1 
ATOM   9349  C CB  . LYS D  1 50  ? 126.097 15.205  9.008   1.00   31.13  ? 50  LYS D CB  1 
ATOM   9350  C CG  . LYS D  1 50  ? 124.734 15.204  8.363   1.00   33.54  ? 50  LYS D CG  1 
ATOM   9351  C CD  . LYS D  1 50  ? 124.389 16.616  8.007   1.00   38.51  ? 50  LYS D CD  1 
ATOM   9352  C CE  . LYS D  1 50  ? 122.966 16.747  7.575   1.00   46.52  ? 50  LYS D CE  1 
ATOM   9353  N NZ  . LYS D  1 50  ? 122.645 18.189  7.382   1.00   52.82  ? 50  LYS D NZ  1 
ATOM   9354  N N   . HIS D  1 51  ? 128.364 13.914  11.067  1.00   30.75  ? 51  HIS D N   1 
ATOM   9355  C CA  . HIS D  1 51  ? 129.746 14.004  11.535  1.00   29.22  ? 51  HIS D CA  1 
ATOM   9356  C C   . HIS D  1 51  ? 129.931 13.521  12.966  1.00   30.45  ? 51  HIS D C   1 
ATOM   9357  O O   . HIS D  1 51  ? 128.976 13.184  13.667  1.00   34.03  ? 51  HIS D O   1 
ATOM   9358  C CB  . HIS D  1 51  ? 130.278 15.448  11.439  1.00   30.81  ? 51  HIS D CB  1 
ATOM   9359  C CG  . HIS D  1 51  ? 129.584 16.421  12.344  1.00   30.16  ? 51  HIS D CG  1 
ATOM   9360  N ND1 . HIS D  1 51  ? 128.650 17.325  11.891  1.00   32.24  ? 51  HIS D ND1 1 
ATOM   9361  C CD2 . HIS D  1 51  ? 129.708 16.644  13.675  1.00   29.38  ? 51  HIS D CD2 1 
ATOM   9362  C CE1 . HIS D  1 51  ? 128.213 18.047  12.908  1.00   32.90  ? 51  HIS D CE1 1 
ATOM   9363  N NE2 . HIS D  1 51  ? 128.838 17.649  14.001  1.00   32.60  ? 51  HIS D NE2 1 
ATOM   9364  N N   . LEU D  1 52  ? 131.187 13.458  13.378  1.00   28.55  ? 52  LEU D N   1 
ATOM   9365  C CA  . LEU D  1 52  ? 131.517 13.207  14.765  1.00   31.63  ? 52  LEU D CA  1 
ATOM   9366  C C   . LEU D  1 52  ? 131.562 14.503  15.536  1.00   36.33  ? 52  LEU D C   1 
ATOM   9367  O O   . LEU D  1 52  ? 132.242 15.434  15.132  1.00   38.44  ? 52  LEU D O   1 
ATOM   9368  C CB  . LEU D  1 52  ? 132.868 12.507  14.876  1.00   31.55  ? 52  LEU D CB  1 
ATOM   9369  C CG  . LEU D  1 52  ? 133.330 12.035  16.251  1.00   34.47  ? 52  LEU D CG  1 
ATOM   9370  C CD1 . LEU D  1 52  ? 134.234 10.868  16.018  1.00   33.78  ? 52  LEU D CD1 1 
ATOM   9371  C CD2 . LEU D  1 52  ? 134.067 13.103  17.019  1.00   36.98  ? 52  LEU D CD2 1 
ATOM   9372  N N   . TRP D  1 53  ? 130.904 14.549  16.682  1.00   40.68  ? 53  TRP D N   1 
ATOM   9373  C CA  . TRP D  1 53  ? 131.005 15.727  17.532  1.00   42.97  ? 53  TRP D CA  1 
ATOM   9374  C C   . TRP D  1 53  ? 131.272 15.311  18.973  1.00   42.81  ? 53  TRP D C   1 
ATOM   9375  O O   . TRP D  1 53  ? 130.841 14.252  19.409  1.00   39.86  ? 53  TRP D O   1 
ATOM   9376  C CB  . TRP D  1 53  ? 129.743 16.601  17.422  1.00   41.42  ? 53  TRP D CB  1 
ATOM   9377  C CG  . TRP D  1 53  ? 128.417 15.960  17.805  1.00   39.72  ? 53  TRP D CG  1 
ATOM   9378  C CD1 . TRP D  1 53  ? 127.548 15.331  16.969  1.00   38.21  ? 53  TRP D CD1 1 
ATOM   9379  C CD2 . TRP D  1 53  ? 127.799 15.944  19.106  1.00   39.53  ? 53  TRP D CD2 1 
ATOM   9380  N NE1 . TRP D  1 53  ? 126.439 14.914  17.660  1.00   39.22  ? 53  TRP D NE1 1 
ATOM   9381  C CE2 . TRP D  1 53  ? 126.569 15.277  18.974  1.00   40.63  ? 53  TRP D CE2 1 
ATOM   9382  C CE3 . TRP D  1 53  ? 128.178 16.411  20.370  1.00   38.32  ? 53  TRP D CE3 1 
ATOM   9383  C CZ2 . TRP D  1 53  ? 125.714 15.066  20.056  1.00   41.52  ? 53  TRP D CZ2 1 
ATOM   9384  C CZ3 . TRP D  1 53  ? 127.331 16.203  21.434  1.00   39.05  ? 53  TRP D CZ3 1 
ATOM   9385  C CH2 . TRP D  1 53  ? 126.114 15.536  21.273  1.00   39.32  ? 53  TRP D CH2 1 
ATOM   9386  N N   . VAL D  1 54  ? 132.009 16.149  19.692  1.00   44.32  ? 54  VAL D N   1 
ATOM   9387  C CA  . VAL D  1 54  ? 132.395 15.857  21.065  1.00   46.71  ? 54  VAL D CA  1 
ATOM   9388  C C   . VAL D  1 54  ? 132.350 17.126  21.908  1.00   49.92  ? 54  VAL D C   1 
ATOM   9389  O O   . VAL D  1 54  ? 132.555 18.218  21.381  1.00   51.00  ? 54  VAL D O   1 
ATOM   9390  C CB  . VAL D  1 54  ? 133.812 15.235  21.114  1.00   44.12  ? 54  VAL D CB  1 
ATOM   9391  C CG1 . VAL D  1 54  ? 134.854 16.248  20.691  1.00   44.13  ? 54  VAL D CG1 1 
ATOM   9392  C CG2 . VAL D  1 54  ? 134.111 14.719  22.498  1.00   46.79  ? 54  VAL D CG2 1 
ATOM   9393  N N   . THR D  1 55  ? 132.093 16.995  23.210  1.00   54.42  ? 55  THR D N   1 
ATOM   9394  C CA  . THR D  1 55  ? 132.205 18.148  24.097  1.00   57.18  ? 55  THR D CA  1 
ATOM   9395  C C   . THR D  1 55  ? 133.684 18.419  24.285  1.00   58.11  ? 55  THR D C   1 
ATOM   9396  O O   . THR D  1 55  ? 134.463 17.538  24.691  1.00   59.13  ? 55  THR D O   1 
ATOM   9397  C CB  . THR D  1 55  ? 131.520 17.940  25.493  1.00   54.01  ? 55  THR D CB  1 
ATOM   9398  O OG1 . THR D  1 55  ? 130.112 17.703  25.336  1.00   53.49  ? 55  THR D OG1 1 
ATOM   9399  C CG2 . THR D  1 55  ? 131.689 19.182  26.366  1.00   58.03  ? 55  THR D CG2 1 
ATOM   9400  N N   . CYS D  1 56  ? 134.049 19.658  24.004  1.00   58.71  ? 56  CYS D N   1 
ATOM   9401  C CA  . CYS D  1 56  ? 135.412 20.104  24.100  1.00   59.92  ? 56  CYS D CA  1 
ATOM   9402  C C   . CYS D  1 56  ? 135.387 20.940  25.340  1.00   67.77  ? 56  CYS D C   1 
ATOM   9403  O O   . CYS D  1 56  ? 134.770 22.008  25.409  1.00   68.36  ? 56  CYS D O   1 
ATOM   9404  C CB  . CYS D  1 56  ? 135.877 20.861  22.868  1.00   54.47  ? 56  CYS D CB  1 
ATOM   9405  S SG  . CYS D  1 56  ? 135.940 19.725  21.536  1.00   47.25  ? 56  CYS D SG  1 
ATOM   9406  N N   . SER D  1 57  ? 136.048 20.397  26.343  1.00   74.14  ? 57  SER D N   1 
ATOM   9407  C CA  . SER D  1 57  ? 135.994 20.953  27.669  1.00   82.72  ? 57  SER D CA  1 
ATOM   9408  C C   . SER D  1 57  ? 137.222 21.579  28.323  1.00   83.69  ? 57  SER D C   1 
ATOM   9409  O O   . SER D  1 57  ? 138.096 22.234  27.704  1.00   80.47  ? 57  SER D O   1 
ATOM   9410  C CB  . SER D  1 57  ? 135.516 19.849  28.603  1.00   88.28  ? 57  SER D CB  1 
ATOM   9411  O OG  . SER D  1 57  ? 136.598 18.977  28.940  1.00   90.42  ? 57  SER D OG  1 
ATOM   9412  N N   . GLN D  1 58  ? 137.093 21.450  29.646  1.00   88.03  ? 58  GLN D N   1 
ATOM   9413  C CA  . GLN D  1 58  ? 138.054 21.674  30.722  1.00   91.36  ? 58  GLN D CA  1 
ATOM   9414  C C   . GLN D  1 58  ? 139.497 21.557  30.268  1.00   87.97  ? 58  GLN D C   1 
ATOM   9415  O O   . GLN D  1 58  ? 139.991 22.439  29.582  1.00   84.71  ? 58  GLN D O   1 
ATOM   9416  C CB  . GLN D  1 58  ? 137.740 20.678  31.870  1.00   84.55  ? 58  GLN D CB  1 
ATOM   9417  C CG  . GLN D  1 58  ? 138.595 20.822  33.130  1.00   88.60  ? 58  GLN D CG  1 
ATOM   9418  C CD  . GLN D  1 58  ? 138.414 22.148  33.813  1.00   93.09  ? 58  GLN D CD  1 
ATOM   9419  O OE1 . GLN D  1 58  ? 139.213 23.058  33.628  1.00   92.41  ? 58  GLN D OE1 1 
ATOM   9420  N NE2 . GLN D  1 58  ? 137.378 22.259  34.639  1.00   98.38  ? 58  GLN D NE2 1 
ATOM   9421  N N   . HIS D  1 59  ? 140.186 20.510  30.700  1.00   88.36  ? 59  HIS D N   1 
ATOM   9422  C CA  . HIS D  1 59  ? 141.538 20.322  30.283  1.00   86.60  ? 59  HIS D CA  1 
ATOM   9423  C C   . HIS D  1 59  ? 141.533 19.317  29.154  1.00   80.76  ? 59  HIS D C   1 
ATOM   9424  O O   . HIS D  1 59  ? 141.974 18.181  29.328  1.00   80.62  ? 59  HIS D O   1 
ATOM   9425  C CB  . HIS D  1 59  ? 142.452 19.883  31.434  0.0000 89.95  ? 59  HIS D CB  1 
ATOM   9426  C CG  . HIS D  1 59  ? 142.310 20.706  32.677  0.0000 94.65  ? 59  HIS D CG  1 
ATOM   9427  N ND1 . HIS D  1 59  ? 141.463 20.376  33.710  0.0000 97.35  ? 59  HIS D ND1 1 
ATOM   9428  C CD2 . HIS D  1 59  ? 142.851 21.904  33.005  0.0000 97.52  ? 59  HIS D CD2 1 
ATOM   9429  C CE1 . HIS D  1 59  ? 141.530 21.306  34.648  0.0000 101.94 ? 59  HIS D CE1 1 
ATOM   9430  N NE2 . HIS D  1 59  ? 142.378 22.235  34.249  0.0000 102.12 ? 59  HIS D NE2 1 
ATOM   9431  N N   . TYR D  1 60  ? 140.996 19.749  28.014  1.00   75.08  ? 60  TYR D N   1 
ATOM   9432  C CA  . TYR D  1 60  ? 141.135 19.017  26.774  1.00   68.99  ? 60  TYR D CA  1 
ATOM   9433  C C   . TYR D  1 60  ? 142.622 19.073  26.514  1.00   72.32  ? 60  TYR D C   1 
ATOM   9434  O O   . TYR D  1 60  ? 143.186 20.143  26.253  1.00   75.98  ? 60  TYR D O   1 
ATOM   9435  C CB  . TYR D  1 60  ? 140.326 19.659  25.636  1.00   61.38  ? 60  TYR D CB  1 
ATOM   9436  C CG  . TYR D  1 60  ? 140.433 19.009  24.250  1.00   53.04  ? 60  TYR D CG  1 
ATOM   9437  C CD1 . TYR D  1 60  ? 141.639 19.005  23.559  1.00   49.28  ? 60  TYR D CD1 1 
ATOM   9438  C CD2 . TYR D  1 60  ? 139.328 18.466  23.607  1.00   48.86  ? 60  TYR D CD2 1 
ATOM   9439  C CE1 . TYR D  1 60  ? 141.752 18.449  22.289  1.00   44.13  ? 60  TYR D CE1 1 
ATOM   9440  C CE2 . TYR D  1 60  ? 139.442 17.908  22.319  1.00   44.57  ? 60  TYR D CE2 1 
ATOM   9441  C CZ  . TYR D  1 60  ? 140.661 17.907  21.678  1.00   42.20  ? 60  TYR D CZ  1 
ATOM   9442  O OH  . TYR D  1 60  ? 140.800 17.369  20.414  1.00   43.04  ? 60  TYR D OH  1 
ATOM   9443  N N   . SER D  1 61  ? 143.272 17.920  26.592  1.00   69.95  ? 61  SER D N   1 
ATOM   9444  C CA  . SER D  1 61  ? 144.702 17.920  26.428  1.00   68.43  ? 61  SER D CA  1 
ATOM   9445  C C   . SER D  1 61  ? 145.070 17.109  25.208  1.00   60.16  ? 61  SER D C   1 
ATOM   9446  O O   . SER D  1 61  ? 144.796 15.903  25.136  1.00   58.25  ? 61  SER D O   1 
ATOM   9447  C CB  . SER D  1 61  ? 145.380 17.384  27.695  1.00   72.62  ? 61  SER D CB  1 
ATOM   9448  O OG  . SER D  1 61  ? 146.792 17.384  27.562  1.00   73.16  ? 61  SER D OG  1 
ATOM   9449  N N   . SER D  1 62  ? 145.681 17.812  24.257  1.00   54.19  ? 62  SER D N   1 
ATOM   9450  C CA  . SER D  1 62  ? 146.159 17.243  23.013  1.00   49.32  ? 62  SER D CA  1 
ATOM   9451  C C   . SER D  1 62  ? 147.151 18.172  22.390  1.00   53.77  ? 62  SER D C   1 
ATOM   9452  O O   . SER D  1 62  ? 146.892 19.363  22.236  1.00   56.07  ? 62  SER D O   1 
ATOM   9453  C CB  . SER D  1 62  ? 145.049 17.011  22.023  1.00   43.32  ? 62  SER D CB  1 
ATOM   9454  O OG  . SER D  1 62  ? 145.617 16.524  20.823  1.00   43.12  ? 62  SER D OG  1 
ATOM   9455  N N   . SER D  1 63  ? 148.282 17.606  22.005  1.00   54.97  ? 63  SER D N   1 
ATOM   9456  C CA  . SER D  1 63  ? 149.340 18.367  21.375  1.00   55.83  ? 63  SER D CA  1 
ATOM   9457  C C   . SER D  1 63  ? 149.164 18.417  19.876  1.00   53.30  ? 63  SER D C   1 
ATOM   9458  O O   . SER D  1 63  ? 149.963 19.028  19.181  1.00   54.82  ? 63  SER D O   1 
ATOM   9459  C CB  . SER D  1 63  ? 150.707 17.785  21.740  1.00   59.43  ? 63  SER D CB  1 
ATOM   9460  O OG  . SER D  1 63  ? 150.894 16.491  21.203  1.00   58.58  ? 63  SER D OG  1 
ATOM   9461  N N   . THR D  1 64  ? 148.116 17.785  19.369  1.00   50.23  ? 64  THR D N   1 
ATOM   9462  C CA  . THR D  1 64  ? 147.889 17.807  17.930  1.00   47.18  ? 64  THR D CA  1 
ATOM   9463  C C   . THR D  1 64  ? 146.598 18.535  17.613  1.00   45.27  ? 64  THR D C   1 
ATOM   9464  O O   . THR D  1 64  ? 146.153 18.561  16.471  1.00   45.36  ? 64  THR D O   1 
ATOM   9465  C CB  . THR D  1 64  ? 147.847 16.384  17.310  1.00   43.73  ? 64  THR D CB  1 
ATOM   9466  O OG1 . THR D  1 64  ? 147.184 15.481  18.197  1.00   42.37  ? 64  THR D OG1 1 
ATOM   9467  C CG2 . THR D  1 64  ? 149.228 15.871  17.122  1.00   45.62  ? 64  THR D CG2 1 
ATOM   9468  N N   . TYR D  1 65  ? 146.017 19.173  18.615  1.00   43.85  ? 65  TYR D N   1 
ATOM   9469  C CA  . TYR D  1 65  ? 144.763 19.842  18.382  1.00   42.01  ? 65  TYR D CA  1 
ATOM   9470  C C   . TYR D  1 65  ? 145.009 21.144  17.622  1.00   42.05  ? 65  TYR D C   1 
ATOM   9471  O O   . TYR D  1 65  ? 145.987 21.852  17.882  1.00   42.90  ? 65  TYR D O   1 
ATOM   9472  C CB  . TYR D  1 65  ? 144.025 20.110  19.705  1.00   42.16  ? 65  TYR D CB  1 
ATOM   9473  C CG  . TYR D  1 65  ? 142.838 21.038  19.532  1.00   42.32  ? 65  TYR D CG  1 
ATOM   9474  C CD1 . TYR D  1 65  ? 141.599 20.561  19.129  1.00   41.34  ? 65  TYR D CD1 1 
ATOM   9475  C CD2 . TYR D  1 65  ? 142.972 22.398  19.724  1.00   45.22  ? 65  TYR D CD2 1 
ATOM   9476  C CE1 . TYR D  1 65  ? 140.518 21.427  18.945  1.00   41.71  ? 65  TYR D CE1 1 
ATOM   9477  C CE2 . TYR D  1 65  ? 141.908 23.263  19.536  1.00   45.87  ? 65  TYR D CE2 1 
ATOM   9478  C CZ  . TYR D  1 65  ? 140.688 22.783  19.147  1.00   44.15  ? 65  TYR D CZ  1 
ATOM   9479  O OH  . TYR D  1 65  ? 139.658 23.690  18.979  1.00   45.94  ? 65  TYR D OH  1 
ATOM   9480  N N   . GLN D  1 66  ? 144.116 21.409  16.663  1.00   40.50  ? 66  GLN D N   1 
ATOM   9481  C CA  . GLN D  1 66  ? 144.016 22.671  15.926  1.00   41.91  ? 66  GLN D CA  1 
ATOM   9482  C C   . GLN D  1 66  ? 142.574 23.067  15.589  1.00   38.79  ? 66  GLN D C   1 
ATOM   9483  O O   . GLN D  1 66  ? 141.742 22.216  15.269  1.00   37.90  ? 66  GLN D O   1 
ATOM   9484  C CB  . GLN D  1 66  ? 144.771 22.608  14.609  1.00   46.55  ? 66  GLN D CB  1 
ATOM   9485  C CG  . GLN D  1 66  ? 146.251 22.579  14.707  1.00   56.70  ? 66  GLN D CG  1 
ATOM   9486  C CD  . GLN D  1 66  ? 146.849 22.444  13.337  1.00   62.55  ? 66  GLN D CD  1 
ATOM   9487  O OE1 . GLN D  1 66  ? 146.510 23.208  12.434  1.00   62.09  ? 66  GLN D OE1 1 
ATOM   9488  N NE2 . GLN D  1 66  ? 147.709 21.450  13.154  1.00   67.03  ? 66  GLN D NE2 1 
ATOM   9489  N N   . ALA D  1 67  ? 142.303 24.370  15.591  1.00   41.23  ? 67  ALA D N   1 
ATOM   9490  C CA  . ALA D  1 67  ? 141.042 24.905  15.071  1.00   41.70  ? 67  ALA D CA  1 
ATOM   9491  C C   . ALA D  1 67  ? 141.243 25.637  13.729  1.00   41.24  ? 67  ALA D C   1 
ATOM   9492  O O   . ALA D  1 67  ? 141.765 26.762  13.718  1.00   44.34  ? 67  ALA D O   1 
ATOM   9493  C CB  . ALA D  1 67  ? 140.409 25.850  16.100  1.00   43.74  ? 67  ALA D CB  1 
ATOM   9494  N N   . PRO D  1 68  ? 140.803 25.019  12.603  1.00   36.70  ? 68  PRO D N   1 
ATOM   9495  C CA  . PRO D  1 68  ? 140.998 25.608  11.265  1.00   35.95  ? 68  PRO D CA  1 
ATOM   9496  C C   . PRO D  1 68  ? 140.436 27.013  11.170  1.00   36.62  ? 68  PRO D C   1 
ATOM   9497  O O   . PRO D  1 68  ? 139.428 27.307  11.808  1.00   36.89  ? 68  PRO D O   1 
ATOM   9498  C CB  . PRO D  1 68  ? 140.235 24.649  10.339  1.00   33.72  ? 68  PRO D CB  1 
ATOM   9499  C CG  . PRO D  1 68  ? 140.283 23.337  11.026  1.00   31.77  ? 68  PRO D CG  1 
ATOM   9500  C CD  . PRO D  1 68  ? 140.203 23.674  12.521  1.00   33.78  ? 68  PRO D CD  1 
ATOM   9501  N N   . PHE D  1 69  ? 141.084 27.874  10.397  1.00   38.19  ? 69  PHE D N   1 
ATOM   9502  C CA  . PHE D  1 69  ? 140.616 29.246  10.288  1.00   40.08  ? 69  PHE D CA  1 
ATOM   9503  C C   . PHE D  1 69  ? 139.480 29.300  9.287   1.00   40.05  ? 69  PHE D C   1 
ATOM   9504  O O   . PHE D  1 69  ? 139.371 28.416  8.424   1.00   38.53  ? 69  PHE D O   1 
ATOM   9505  C CB  . PHE D  1 69  ? 141.761 30.201  9.908   1.00   41.97  ? 69  PHE D CB  1 
ATOM   9506  C CG  . PHE D  1 69  ? 142.484 29.832  8.636   1.00   43.40  ? 69  PHE D CG  1 
ATOM   9507  C CD1 . PHE D  1 69  ? 141.985 30.198  7.390   1.00   43.59  ? 69  PHE D CD1 1 
ATOM   9508  C CD2 . PHE D  1 69  ? 143.685 29.136  8.684   1.00   44.72  ? 69  PHE D CD2 1 
ATOM   9509  C CE1 . PHE D  1 69  ? 142.666 29.856  6.211   1.00   43.48  ? 69  PHE D CE1 1 
ATOM   9510  C CE2 . PHE D  1 69  ? 144.369 28.800  7.510   1.00   44.68  ? 69  PHE D CE2 1 
ATOM   9511  C CZ  . PHE D  1 69  ? 143.852 29.158  6.275   1.00   43.50  ? 69  PHE D CZ  1 
ATOM   9512  N N   . CYS D  1 70  ? 138.616 30.306  9.416   1.00   39.74  ? 70  CYS D N   1 
ATOM   9513  C CA  . CYS D  1 70  ? 137.484 30.402  8.511   1.00   38.32  ? 70  CYS D CA  1 
ATOM   9514  C C   . CYS D  1 70  ? 138.003 30.587  7.096   1.00   38.68  ? 70  CYS D C   1 
ATOM   9515  O O   . CYS D  1 70  ? 138.993 31.282  6.890   1.00   39.49  ? 70  CYS D O   1 
ATOM   9516  C CB  . CYS D  1 70  ? 136.539 31.535  8.892   1.00   40.57  ? 70  CYS D CB  1 
ATOM   9517  S SG  . CYS D  1 70  ? 134.841 31.324  8.197   1.00   51.12  ? 70  CYS D SG  1 
ATOM   9518  N N   . HIS D  1 71  ? 137.321 29.940  6.154   1.00   38.20  ? 71  HIS D N   1 
ATOM   9519  C CA  . HIS D  1 71  ? 137.651 29.887  4.723   1.00   38.37  ? 71  HIS D CA  1 
ATOM   9520  C C   . HIS D  1 71  ? 138.863 29.014  4.369   1.00   38.48  ? 71  HIS D C   1 
ATOM   9521  O O   . HIS D  1 71  ? 139.350 29.062  3.241   1.00   38.52  ? 71  HIS D O   1 
ATOM   9522  C CB  . HIS D  1 71  ? 137.862 31.274  4.147   1.00   39.15  ? 71  HIS D CB  1 
ATOM   9523  C CG  . HIS D  1 71  ? 136.777 32.237  4.485   1.00   39.62  ? 71  HIS D CG  1 
ATOM   9524  N ND1 . HIS D  1 71  ? 135.475 32.054  4.083   1.00   40.06  ? 71  HIS D ND1 1 
ATOM   9525  C CD2 . HIS D  1 71  ? 136.802 33.402  5.167   1.00   40.59  ? 71  HIS D CD2 1 
ATOM   9526  C CE1 . HIS D  1 71  ? 134.737 33.059  4.518   1.00   40.64  ? 71  HIS D CE1 1 
ATOM   9527  N NE2 . HIS D  1 71  ? 135.520 33.894  5.174   1.00   41.27  ? 71  HIS D NE2 1 
ATOM   9528  N N   . SER D  1 72  ? 139.320 28.194  5.307   1.00   37.75  ? 72  SER D N   1 
ATOM   9529  C CA  . SER D  1 72  ? 140.406 27.260  5.031   1.00   37.42  ? 72  SER D CA  1 
ATOM   9530  C C   . SER D  1 72  ? 139.963 26.082  4.170   1.00   35.40  ? 72  SER D C   1 
ATOM   9531  O O   . SER D  1 72  ? 138.772 25.848  3.977   1.00   35.10  ? 72  SER D O   1 
ATOM   9532  C CB  . SER D  1 72  ? 140.984 26.709  6.326   1.00   37.34  ? 72  SER D CB  1 
ATOM   9533  O OG  . SER D  1 72  ? 139.997 25.974  7.013   1.00   36.27  ? 72  SER D OG  1 
ATOM   9534  N N   . THR D  1 73  ? 140.930 25.319  3.676   1.00   34.28  ? 73  THR D N   1 
ATOM   9535  C CA  . THR D  1 73  ? 140.608 24.102  2.956   1.00   31.85  ? 73  THR D CA  1 
ATOM   9536  C C   . THR D  1 73  ? 139.851 23.103  3.858   1.00   32.36  ? 73  THR D C   1 
ATOM   9537  O O   . THR D  1 73  ? 138.985 22.380  3.380   1.00   34.00  ? 73  THR D O   1 
ATOM   9538  C CB  . THR D  1 73  ? 141.875 23.448  2.416   1.00   29.94  ? 73  THR D CB  1 
ATOM   9539  O OG1 . THR D  1 73  ? 142.825 23.372  3.476   1.00   31.48  ? 73  THR D OG1 1 
ATOM   9540  C CG2 . THR D  1 73  ? 142.474 24.272  1.329   1.00   30.96  ? 73  THR D CG2 1 
ATOM   9541  N N   . GLN D  1 74  ? 140.154 23.080  5.161   1.00   31.63  ? 74  GLN D N   1 
ATOM   9542  C CA  . GLN D  1 74  ? 139.444 22.220  6.102   1.00   27.88  ? 74  GLN D CA  1 
ATOM   9543  C C   . GLN D  1 74  ? 137.990 22.566  6.245   1.00   31.14  ? 74  GLN D C   1 
ATOM   9544  O O   . GLN D  1 74  ? 137.132 21.689  6.309   1.00   31.52  ? 74  GLN D O   1 
ATOM   9545  C CB  . GLN D  1 74  ? 140.093 22.280  7.470   1.00   29.57  ? 74  GLN D CB  1 
ATOM   9546  C CG  . GLN D  1 74  ? 141.468 21.664  7.484   1.00   31.80  ? 74  GLN D CG  1 
ATOM   9547  C CD  . GLN D  1 74  ? 142.576 22.668  7.442   1.00   36.33  ? 74  GLN D CD  1 
ATOM   9548  O OE1 . GLN D  1 74  ? 142.413 23.769  6.938   1.00   39.43  ? 74  GLN D OE1 1 
ATOM   9549  N NE2 . GLN D  1 74  ? 143.734 22.276  7.939   1.00   41.10  ? 74  GLN D NE2 1 
ATOM   9550  N N   . CYS D  1 75  ? 137.711 23.857  6.317   1.00   29.93  ? 75  CYS D N   1 
ATOM   9551  C CA  . CYS D  1 75  ? 136.356 24.316  6.433   1.00   29.62  ? 75  CYS D CA  1 
ATOM   9552  C C   . CYS D  1 75  ? 135.594 24.036  5.140   1.00   31.03  ? 75  CYS D C   1 
ATOM   9553  O O   . CYS D  1 75  ? 134.427 23.670  5.174   1.00   33.62  ? 75  CYS D O   1 
ATOM   9554  C CB  . CYS D  1 75  ? 136.351 25.804  6.786   1.00   30.85  ? 75  CYS D CB  1 
ATOM   9555  S SG  . CYS D  1 75  ? 137.135 26.115  8.383   1.00   44.69  ? 75  CYS D SG  1 
ATOM   9556  N N   . SER D  1 76  ? 136.258 24.179  4.001   1.00   32.58  ? 76  SER D N   1 
ATOM   9557  C CA  . SER D  1 76  ? 135.646 23.863  2.710   1.00   33.46  ? 76  SER D CA  1 
ATOM   9558  C C   . SER D  1 76  ? 135.242 22.387  2.622   1.00   32.86  ? 76  SER D C   1 
ATOM   9559  O O   . SER D  1 76  ? 134.133 22.075  2.176   1.00   34.09  ? 76  SER D O   1 
ATOM   9560  C CB  . SER D  1 76  ? 136.585 24.227  1.560   1.00   33.67  ? 76  SER D CB  1 
ATOM   9561  O OG  . SER D  1 76  ? 135.991 23.958  0.298   1.00   34.45  ? 76  SER D OG  1 
ATOM   9562  N N   . ARG D  1 77  ? 136.140 21.489  3.035   1.00   30.46  ? 77  ARG D N   1 
ATOM   9563  C CA  . ARG D  1 77  ? 135.862 20.052  3.019   1.00   31.39  ? 77  ARG D CA  1 
ATOM   9564  C C   . ARG D  1 77  ? 134.682 19.701  3.923   1.00   32.42  ? 77  ARG D C   1 
ATOM   9565  O O   . ARG D  1 77  ? 133.842 18.865  3.573   1.00   33.56  ? 77  ARG D O   1 
ATOM   9566  C CB  . ARG D  1 77  ? 137.074 19.245  3.457   1.00   31.52  ? 77  ARG D CB  1 
ATOM   9567  C CG  . ARG D  1 77  ? 136.862 17.762  3.192   1.00   35.42  ? 77  ARG D CG  1 
ATOM   9568  C CD  . ARG D  1 77  ? 138.037 16.861  3.622   1.00   37.88  ? 77  ARG D CD  1 
ATOM   9569  N NE  . ARG D  1 77  ? 137.751 15.451  3.324   1.00   38.33  ? 77  ARG D NE  1 
ATOM   9570  C CZ  . ARG D  1 77  ? 138.393 14.414  3.855   1.00   37.78  ? 77  ARG D CZ  1 
ATOM   9571  N NH1 . ARG D  1 77  ? 139.345 14.619  4.752   1.00   37.21  ? 77  ARG D NH1 1 
ATOM   9572  N NH2 . ARG D  1 77  ? 138.064 13.175  3.504   1.00   37.32  ? 77  ARG D NH2 1 
ATOM   9573  N N   . ALA D  1 78  ? 134.617 20.375  5.070   1.00   31.18  ? 78  ALA D N   1 
ATOM   9574  C CA  . ALA D  1 78  ? 133.534 20.197  6.040   1.00   31.16  ? 78  ALA D CA  1 
ATOM   9575  C C   . ALA D  1 78  ? 132.241 20.856  5.577   1.00   33.75  ? 78  ALA D C   1 
ATOM   9576  O O   . ALA D  1 78  ? 131.212 20.715  6.222   1.00   33.71  ? 78  ALA D O   1 
ATOM   9577  C CB  . ALA D  1 78  ? 133.942 20.754  7.402   1.00   29.51  ? 78  ALA D CB  1 
ATOM   9578  N N   . ASN D  1 79  ? 132.322 21.605  4.481   1.00   35.57  ? 79  ASN D N   1 
ATOM   9579  C CA  . ASN D  1 79  ? 131.178 22.250  3.896   1.00   37.36  ? 79  ASN D CA  1 
ATOM   9580  C C   . ASN D  1 79  ? 130.554 23.291  4.807   1.00   41.66  ? 79  ASN D C   1 
ATOM   9581  O O   . ASN D  1 79  ? 129.336 23.433  4.881   1.00   42.30  ? 79  ASN D O   1 
ATOM   9582  C CB  . ASN D  1 79  ? 130.153 21.201  3.523   1.00   39.18  ? 79  ASN D CB  1 
ATOM   9583  C CG  . ASN D  1 79  ? 129.109 21.740  2.636   1.00   48.19  ? 79  ASN D CG  1 
ATOM   9584  O OD1 . ASN D  1 79  ? 129.348 22.693  1.890   1.00   50.08  ? 79  ASN D OD1 1 
ATOM   9585  N ND2 . ASN D  1 79  ? 127.905 21.193  2.749   1.00   53.78  ? 79  ASN D ND2 1 
ATOM   9586  N N   . THR D  1 80  ? 131.399 24.039  5.493   1.00   43.16  ? 80  THR D N   1 
ATOM   9587  C CA  . THR D  1 80  ? 130.931 25.165  6.279   1.00   42.23  ? 80  THR D CA  1 
ATOM   9588  C C   . THR D  1 80  ? 131.704 26.416  5.940   1.00   47.74  ? 80  THR D C   1 
ATOM   9589  O O   . THR D  1 80  ? 132.928 26.434  6.002   1.00   49.23  ? 80  THR D O   1 
ATOM   9590  C CB  . THR D  1 80  ? 131.064 24.928  7.769   1.00   41.28  ? 80  THR D CB  1 
ATOM   9591  O OG1 . THR D  1 80  ? 130.876 26.179  8.435   1.00   51.23  ? 80  THR D OG1 1 
ATOM   9592  C CG2 . THR D  1 80  ? 132.431 24.419  8.128   1.00   34.91  ? 80  THR D CG2 1 
ATOM   9593  N N   . HIS D  1 81  ? 131.005 27.477  5.587   1.00   51.70  ? 81  HIS D N   1 
ATOM   9594  C CA  . HIS D  1 81  ? 131.717 28.696  5.262   1.00   55.63  ? 81  HIS D CA  1 
ATOM   9595  C C   . HIS D  1 81  ? 131.231 29.849  6.148   1.00   56.64  ? 81  HIS D C   1 
ATOM   9596  O O   . HIS D  1 81  ? 131.440 31.025  5.849   1.00   56.21  ? 81  HIS D O   1 
ATOM   9597  C CB  . HIS D  1 81  ? 131.572 28.966  3.760   1.00   60.64  ? 81  HIS D CB  1 
ATOM   9598  C CG  . HIS D  1 81  ? 132.192 27.888  2.910   1.00   62.67  ? 81  HIS D CG  1 
ATOM   9599  N ND1 . HIS D  1 81  ? 133.503 27.926  2.477   1.00   62.19  ? 81  HIS D ND1 1 
ATOM   9600  C CD2 . HIS D  1 81  ? 131.683 26.717  2.450   1.00   61.94  ? 81  HIS D CD2 1 
ATOM   9601  C CE1 . HIS D  1 81  ? 133.766 26.837  1.773   1.00   59.00  ? 81  HIS D CE1 1 
ATOM   9602  N NE2 . HIS D  1 81  ? 132.679 26.087  1.742   1.00   59.16  ? 81  HIS D NE2 1 
ATOM   9603  N N   . GLN D  1 82  ? 130.582 29.472  7.251   1.00   55.85  ? 82  GLN D N   1 
ATOM   9604  C CA  . GLN D  1 82  ? 130.156 30.388  8.301   1.00   52.27  ? 82  GLN D CA  1 
ATOM   9605  C C   . GLN D  1 82  ? 131.205 30.431  9.420   1.00   47.40  ? 82  GLN D C   1 
ATOM   9606  O O   . GLN D  1 82  ? 131.529 29.413  10.004  1.00   45.59  ? 82  GLN D O   1 
ATOM   9607  C CB  . GLN D  1 82  ? 128.816 29.955  8.877   1.00   55.04  ? 82  GLN D CB  1 
ATOM   9608  C CG  . GLN D  1 82  ? 128.609 30.516  10.272  1.00   62.48  ? 82  GLN D CG  1 
ATOM   9609  C CD  . GLN D  1 82  ? 127.319 30.085  10.935  1.00   69.39  ? 82  GLN D CD  1 
ATOM   9610  O OE1 . GLN D  1 82  ? 126.469 29.432  10.325  1.00   73.30  ? 82  GLN D OE1 1 
ATOM   9611  N NE2 . GLN D  1 82  ? 127.182 30.426  12.211  1.00   70.99  ? 82  GLN D NE2 1 
ATOM   9612  N N   . CYS D  1 83  ? 131.727 31.611  9.723   1.00   46.34  ? 83  CYS D N   1 
ATOM   9613  C CA  . CYS D  1 83  ? 132.798 31.768  10.717  1.00   44.55  ? 83  CYS D CA  1 
ATOM   9614  C C   . CYS D  1 83  ? 132.320 31.697  12.166  1.00   46.03  ? 83  CYS D C   1 
ATOM   9615  O O   . CYS D  1 83  ? 131.179 32.039  12.483  1.00   48.28  ? 83  CYS D O   1 
ATOM   9616  C CB  . CYS D  1 83  ? 133.508 33.096  10.499  1.00   44.87  ? 83  CYS D CB  1 
ATOM   9617  S SG  . CYS D  1 83  ? 134.362 33.163  8.915   1.00   64.59  ? 83  CYS D SG  1 
ATOM   9618  N N   . PHE D  1 84  ? 133.211 31.280  13.049  1.00   45.04  ? 84  PHE D N   1 
ATOM   9619  C CA  . PHE D  1 84  ? 132.842 31.047  14.430  1.00   46.98  ? 84  PHE D CA  1 
ATOM   9620  C C   . PHE D  1 84  ? 133.388 32.153  15.282  1.00   50.91  ? 84  PHE D C   1 
ATOM   9621  O O   . PHE D  1 84  ? 134.527 32.571  15.123  1.00   51.83  ? 84  PHE D O   1 
ATOM   9622  C CB  . PHE D  1 84  ? 133.368 29.693  14.897  1.00   46.80  ? 84  PHE D CB  1 
ATOM   9623  C CG  . PHE D  1 84  ? 132.937 29.302  16.290  1.00   48.10  ? 84  PHE D CG  1 
ATOM   9624  C CD1 . PHE D  1 84  ? 131.774 28.591  16.496  1.00   42.39  ? 84  PHE D CD1 1 
ATOM   9625  C CD2 . PHE D  1 84  ? 133.725 29.619  17.386  1.00   48.09  ? 84  PHE D CD2 1 
ATOM   9626  C CE1 . PHE D  1 84  ? 131.406 28.217  17.758  1.00   44.16  ? 84  PHE D CE1 1 
ATOM   9627  C CE2 . PHE D  1 84  ? 133.358 29.248  18.649  1.00   47.89  ? 84  PHE D CE2 1 
ATOM   9628  C CZ  . PHE D  1 84  ? 132.198 28.549  18.838  1.00   48.15  ? 84  PHE D CZ  1 
ATOM   9629  N N   . THR D  1 85  ? 132.563 32.621  16.204  1.00   56.33  ? 85  THR D N   1 
ATOM   9630  C CA  . THR D  1 85  ? 132.974 33.650  17.137  1.00   62.65  ? 85  THR D CA  1 
ATOM   9631  C C   . THR D  1 85  ? 132.747 33.134  18.550  1.00   64.54  ? 85  THR D C   1 
ATOM   9632  O O   . THR D  1 85  ? 131.629 32.785  18.920  1.00   63.30  ? 85  THR D O   1 
ATOM   9633  C CB  . THR D  1 85  ? 132.205 34.963  16.906  1.00   65.62  ? 85  THR D CB  1 
ATOM   9634  O OG1 . THR D  1 85  ? 132.494 35.457  15.591  1.00   65.82  ? 85  THR D OG1 1 
ATOM   9635  C CG2 . THR D  1 85  ? 132.632 35.987  17.902  1.00   68.41  ? 85  THR D CG2 1 
ATOM   9636  N N   . CYS D  1 86  ? 133.798 33.120  19.358  1.00   67.91  ? 86  CYS D N   1 
ATOM   9637  C CA  . CYS D  1 86  ? 133.661 32.518  20.669  1.00   73.35  ? 86  CYS D CA  1 
ATOM   9638  C C   . CYS D  1 86  ? 132.952 33.415  21.646  1.00   82.24  ? 86  CYS D C   1 
ATOM   9639  O O   . CYS D  1 86  ? 133.382 34.535  21.935  1.00   85.15  ? 86  CYS D O   1 
ATOM   9640  C CB  . CYS D  1 86  ? 134.988 32.119  21.269  1.00   72.62  ? 86  CYS D CB  1 
ATOM   9641  S SG  . CYS D  1 86  ? 134.602 31.104  22.706  1.00   80.77  ? 86  CYS D SG  1 
ATOM   9642  N N   . THR D  1 87  ? 131.867 32.863  22.179  1.00   86.93  ? 87  THR D N   1 
ATOM   9643  C CA  . THR D  1 87  ? 130.955 33.595  23.041  1.00   94.58  ? 87  THR D CA  1 
ATOM   9644  C C   . THR D  1 87  ? 130.922 33.246  24.533  1.00   98.98  ? 87  THR D C   1 
ATOM   9645  O O   . THR D  1 87  ? 130.029 33.704  25.249  1.00   105.45 ? 87  THR D O   1 
ATOM   9646  C CB  . THR D  1 87  ? 129.528 33.394  22.525  1.00   95.71  ? 87  THR D CB  1 
ATOM   9647  O OG1 . THR D  1 87  ? 128.613 34.026  23.423  1.00   102.36 ? 87  THR D OG1 1 
ATOM   9648  C CG2 . THR D  1 87  ? 129.192 31.904  22.539  1.00   92.43  ? 87  THR D CG2 1 
ATOM   9649  N N   . ASP D  1 88  ? 131.859 32.450  25.026  1.00   94.62  ? 88  ASP D N   1 
ATOM   9650  C CA  . ASP D  1 88  ? 131.952 32.296  26.472  1.00   95.25  ? 88  ASP D CA  1 
ATOM   9651  C C   . ASP D  1 88  ? 133.166 33.103  26.999  1.00   106.10 ? 88  ASP D C   1 
ATOM   9652  O O   . ASP D  1 88  ? 133.034 34.293  27.306  1.00   110.95 ? 88  ASP D O   1 
ATOM   9653  C CB  . ASP D  1 88  ? 131.924 30.811  26.871  1.00   90.98  ? 88  ASP D CB  1 
ATOM   9654  C CG  . ASP D  1 88  ? 133.026 30.010  26.256  1.00   88.91  ? 88  ASP D CG  1 
ATOM   9655  O OD1 . ASP D  1 88  ? 133.974 30.614  25.724  1.00   91.77  ? 88  ASP D OD1 1 
ATOM   9656  O OD2 . ASP D  1 88  ? 132.919 28.767  26.272  1.00   84.74  ? 88  ASP D OD2 1 
ATOM   9657  N N   . SER D  1 89  ? 134.333 32.477  27.099  1.00   102.15 ? 89  SER D N   1 
ATOM   9658  C CA  . SER D  1 89  ? 135.545 33.137  27.597  1.00   102.79 ? 89  SER D CA  1 
ATOM   9659  C C   . SER D  1 89  ? 136.048 34.321  26.753  1.00   100.18 ? 89  SER D C   1 
ATOM   9660  O O   . SER D  1 89  ? 135.678 34.466  25.582  1.00   97.34  ? 89  SER D O   1 
ATOM   9661  C CB  . SER D  1 89  ? 136.660 32.101  27.707  1.00   101.39 ? 89  SER D CB  1 
ATOM   9662  O OG  . SER D  1 89  ? 137.922 32.732  27.700  1.00   102.86 ? 89  SER D OG  1 
ATOM   9663  N N   . THR D  1 90  ? 136.891 35.163  27.358  1.00   101.01 ? 90  THR D N   1 
ATOM   9664  C CA  . THR D  1 90  ? 137.571 36.229  26.622  1.00   99.45  ? 90  THR D CA  1 
ATOM   9665  C C   . THR D  1 90  ? 139.014 35.805  26.370  1.00   98.70  ? 90  THR D C   1 
ATOM   9666  O O   . THR D  1 90  ? 139.835 36.586  25.876  1.00   98.79  ? 90  THR D O   1 
ATOM   9667  C CB  . THR D  1 90  ? 137.553 37.578  27.378  1.00   102.06 ? 90  THR D CB  1 
ATOM   9668  O OG1 . THR D  1 90  ? 136.317 37.716  28.081  1.00   104.41 ? 90  THR D OG1 1 
ATOM   9669  C CG2 . THR D  1 90  ? 137.696 38.745  26.409  1.00   99.93  ? 90  THR D CG2 1 
ATOM   9670  N N   . THR D  1 91  ? 139.315 34.564  26.741  1.00   98.32  ? 91  THR D N   1 
ATOM   9671  C CA  . THR D  1 91  ? 140.546 33.908  26.319  1.00   96.11  ? 91  THR D CA  1 
ATOM   9672  C C   . THR D  1 91  ? 140.212 32.583  25.600  1.00   90.26  ? 91  THR D C   1 
ATOM   9673  O O   . THR D  1 91  ? 139.147 32.000  25.820  1.00   89.08  ? 91  THR D O   1 
ATOM   9674  C CB  . THR D  1 91  ? 141.497 33.668  27.523  1.00   106.12 ? 91  THR D CB  1 
ATOM   9675  O OG1 . THR D  1 91  ? 142.751 33.150  27.061  1.00   105.25 ? 91  THR D OG1 1 
ATOM   9676  C CG2 . THR D  1 91  ? 140.877 32.736  28.557  1.00   105.84 ? 91  THR D CG2 1 
ATOM   9677  N N   . THR D  1 92  ? 141.133 32.102  24.765  1.00   85.19  ? 92  THR D N   1 
ATOM   9678  C CA  . THR D  1 92  ? 140.889 30.924  23.923  1.00   78.14  ? 92  THR D CA  1 
ATOM   9679  C C   . THR D  1 92  ? 141.152 29.550  24.556  1.00   75.35  ? 92  THR D C   1 
ATOM   9680  O O   . THR D  1 92  ? 141.938 29.418  25.494  1.00   77.24  ? 92  THR D O   1 
ATOM   9681  C CB  . THR D  1 92  ? 141.703 31.010  22.615  1.00   76.15  ? 92  THR D CB  1 
ATOM   9682  O OG1 . THR D  1 92  ? 143.100 30.920  22.910  1.00   76.99  ? 92  THR D OG1 1 
ATOM   9683  C CG2 . THR D  1 92  ? 141.433 32.316  21.913  1.00   77.56  ? 92  THR D CG2 1 
ATOM   9684  N N   . ARG D  1 93  ? 140.450 28.545  24.023  1.00   71.07  ? 93  ARG D N   1 
ATOM   9685  C CA  . ARG D  1 93  ? 140.549 27.138  24.420  1.00   67.50  ? 93  ARG D CA  1 
ATOM   9686  C C   . ARG D  1 93  ? 139.892 26.354  23.285  1.00   62.81  ? 93  ARG D C   1 
ATOM   9687  O O   . ARG D  1 93  ? 139.221 26.955  22.440  1.00   61.28  ? 93  ARG D O   1 
ATOM   9688  C CB  . ARG D  1 93  ? 139.824 26.837  25.728  1.00   69.96  ? 93  ARG D CB  1 
ATOM   9689  C CG  . ARG D  1 93  ? 138.363 27.079  25.572  1.00   72.48  ? 93  ARG D CG  1 
ATOM   9690  C CD  . ARG D  1 93  ? 137.541 26.708  26.771  1.00   78.49  ? 93  ARG D CD  1 
ATOM   9691  N NE  . ARG D  1 93  ? 136.135 26.968  26.465  1.00   82.08  ? 93  ARG D NE  1 
ATOM   9692  C CZ  . ARG D  1 93  ? 135.306 26.080  25.913  1.00   81.14  ? 93  ARG D CZ  1 
ATOM   9693  N NH1 . ARG D  1 93  ? 135.734 24.862  25.602  1.00   78.64  ? 93  ARG D NH1 1 
ATOM   9694  N NH2 . ARG D  1 93  ? 134.045 26.414  25.664  1.00   81.65  ? 93  ARG D NH2 1 
ATOM   9695  N N   . PRO D  1 94  ? 140.067 25.013  23.258  1.00   60.42  ? 94  PRO D N   1 
ATOM   9696  C CA  . PRO D  1 94  ? 139.369 24.195  22.250  1.00   55.07  ? 94  PRO D CA  1 
ATOM   9697  C C   . PRO D  1 94  ? 137.861 24.424  22.232  1.00   52.76  ? 94  PRO D C   1 
ATOM   9698  O O   . PRO D  1 94  ? 137.227 24.395  23.292  1.00   53.52  ? 94  PRO D O   1 
ATOM   9699  C CB  . PRO D  1 94  ? 139.693 22.759  22.683  1.00   53.66  ? 94  PRO D CB  1 
ATOM   9700  C CG  . PRO D  1 94  ? 141.007 22.868  23.368  1.00   56.18  ? 94  PRO D CG  1 
ATOM   9701  C CD  . PRO D  1 94  ? 140.955 24.186  24.104  1.00   60.90  ? 94  PRO D CD  1 
ATOM   9702  N N   . GLY D  1 95  ? 137.305 24.692  21.055  1.00   49.53  ? 95  GLY D N   1 
ATOM   9703  C CA  . GLY D  1 95  ? 135.881 24.925  20.936  1.00   49.79  ? 95  GLY D CA  1 
ATOM   9704  C C   . GLY D  1 95  ? 135.584 26.399  21.030  1.00   53.12  ? 95  GLY D C   1 
ATOM   9705  O O   . GLY D  1 95  ? 134.478 26.849  20.750  1.00   56.58  ? 95  GLY D O   1 
ATOM   9706  N N   . CYS D  1 96  ? 136.598 27.159  21.409  1.00   54.67  ? 96  CYS D N   1 
ATOM   9707  C CA  . CYS D  1 96  ? 136.445 28.586  21.629  1.00   58.27  ? 96  CYS D CA  1 
ATOM   9708  C C   . CYS D  1 96  ? 137.557 29.405  21.011  1.00   59.16  ? 96  CYS D C   1 
ATOM   9709  O O   . CYS D  1 96  ? 138.598 29.631  21.616  1.00   61.37  ? 96  CYS D O   1 
ATOM   9710  C CB  . CYS D  1 96  ? 136.390 28.876  23.128  1.00   62.62  ? 96  CYS D CB  1 
ATOM   9711  S SG  . CYS D  1 96  ? 136.371 30.643  23.553  1.00   119.73 ? 96  CYS D SG  1 
ATOM   9712  N N   . HIS D  1 97  ? 137.330 29.851  19.788  1.00   56.47  ? 97  HIS D N   1 
ATOM   9713  C CA  . HIS D  1 97  ? 138.237 30.782  19.162  1.00   54.43  ? 97  HIS D CA  1 
ATOM   9714  C C   . HIS D  1 97  ? 137.420 31.781  18.362  1.00   58.39  ? 97  HIS D C   1 
ATOM   9715  O O   . HIS D  1 97  ? 136.208 31.620  18.206  1.00   57.44  ? 97  HIS D O   1 
ATOM   9716  C CB  . HIS D  1 97  ? 139.227 30.060  18.264  1.00   48.30  ? 97  HIS D CB  1 
ATOM   9717  C CG  . HIS D  1 97  ? 139.877 28.872  18.900  1.00   46.99  ? 97  HIS D CG  1 
ATOM   9718  N ND1 . HIS D  1 97  ? 139.291 27.625  18.913  1.00   46.59  ? 97  HIS D ND1 1 
ATOM   9719  C CD2 . HIS D  1 97  ? 141.075 28.732  19.520  1.00   47.57  ? 97  HIS D CD2 1 
ATOM   9720  C CE1 . HIS D  1 97  ? 140.096 26.767  19.518  1.00   47.14  ? 97  HIS D CE1 1 
ATOM   9721  N NE2 . HIS D  1 97  ? 141.183 27.415  19.899  1.00   47.86  ? 97  HIS D NE2 1 
ATOM   9722  N N   . ASN D  1 98  ? 138.071 32.814  17.848  1.00   63.77  ? 98  ASN D N   1 
ATOM   9723  C CA  . ASN D  1 98  ? 137.390 33.652  16.891  1.00   69.89  ? 98  ASN D CA  1 
ATOM   9724  C C   . ASN D  1 98  ? 138.020 33.384  15.510  1.00   63.09  ? 98  ASN D C   1 
ATOM   9725  O O   . ASN D  1 98  ? 139.130 32.841  15.428  1.00   58.34  ? 98  ASN D O   1 
ATOM   9726  C CB  . ASN D  1 98  ? 137.444 35.128  17.319  1.00   82.86  ? 98  ASN D CB  1 
ATOM   9727  C CG  . ASN D  1 98  ? 136.422 35.454  18.429  1.00   93.46  ? 98  ASN D CG  1 
ATOM   9728  O OD1 . ASN D  1 98  ? 135.439 34.743  18.593  1.00   88.94  ? 98  ASN D OD1 1 
ATOM   9729  N ND2 . ASN D  1 98  ? 136.642 36.549  19.166  1.00   107.89 ? 98  ASN D ND2 1 
ATOM   9730  N N   . ASN D  1 99  ? 137.276 33.679  14.439  1.00   61.94  ? 99  ASN D N   1 
ATOM   9731  C CA  . ASN D  1 99  ? 137.712 33.432  13.043  1.00   58.66  ? 99  ASN D CA  1 
ATOM   9732  C C   . ASN D  1 99  ? 138.040 31.995  12.720  1.00   47.75  ? 99  ASN D C   1 
ATOM   9733  O O   . ASN D  1 99  ? 138.950 31.696  11.947  1.00   43.58  ? 99  ASN D O   1 
ATOM   9734  C CB  . ASN D  1 99  ? 138.892 34.337  12.678  1.00   65.54  ? 99  ASN D CB  1 
ATOM   9735  C CG  . ASN D  1 99  ? 138.551 35.814  12.868  1.00   73.02  ? 99  ASN D CG  1 
ATOM   9736  O OD1 . ASN D  1 99  ? 137.537 36.304  12.348  1.00   75.40  ? 99  ASN D OD1 1 
ATOM   9737  N ND2 . ASN D  1 99  ? 139.378 36.524  13.637  1.00   75.16  ? 99  ASN D ND2 1 
ATOM   9738  N N   . THR D  1 100 ? 137.280 31.115  13.349  1.00   42.78  ? 100 THR D N   1 
ATOM   9739  C CA  . THR D  1 100 ? 137.303 29.715  13.032  1.00   40.18  ? 100 THR D CA  1 
ATOM   9740  C C   . THR D  1 100 ? 136.023 29.420  12.281  1.00   37.47  ? 100 THR D C   1 
ATOM   9741  O O   . THR D  1 100 ? 135.374 30.347  11.806  1.00   38.72  ? 100 THR D O   1 
ATOM   9742  C CB  . THR D  1 100 ? 137.446 28.894  14.274  1.00   42.59  ? 100 THR D CB  1 
ATOM   9743  O OG1 . THR D  1 100 ? 136.552 29.408  15.272  1.00   45.94  ? 100 THR D OG1 1 
ATOM   9744  C CG2 . THR D  1 100 ? 138.893 29.024  14.775  1.00   41.69  ? 100 THR D CG2 1 
ATOM   9745  N N   . CYS D  1 101 ? 135.647 28.155  12.182  1.00   37.72  ? 101 CYS D N   1 
ATOM   9746  C CA  . CYS D  1 101 ? 134.427 27.805  11.471  1.00   40.36  ? 101 CYS D CA  1 
ATOM   9747  C C   . CYS D  1 101 ? 133.405 27.179  12.356  1.00   41.23  ? 101 CYS D C   1 
ATOM   9748  O O   . CYS D  1 101 ? 133.741 26.392  13.231  1.00   42.84  ? 101 CYS D O   1 
ATOM   9749  C CB  . CYS D  1 101 ? 134.714 26.802  10.355  1.00   41.43  ? 101 CYS D CB  1 
ATOM   9750  S SG  . CYS D  1 101 ? 135.770 27.395  9.108   1.00   70.44  ? 101 CYS D SG  1 
ATOM   9751  N N   . GLY D  1 102 ? 132.148 27.506  12.072  1.00   41.47  ? 102 GLY D N   1 
ATOM   9752  C CA  . GLY D  1 102 ? 131.023 27.040  12.845  1.00   44.07  ? 102 GLY D CA  1 
ATOM   9753  C C   . GLY D  1 102 ? 130.356 25.851  12.166  1.00   44.60  ? 102 GLY D C   1 
ATOM   9754  O O   . GLY D  1 102 ? 130.141 25.853  10.942  1.00   42.09  ? 102 GLY D O   1 
ATOM   9755  N N   . LEU D  1 103 ? 129.947 24.877  12.981  1.00   45.91  ? 103 LEU D N   1 
ATOM   9756  C CA  . LEU D  1 103 ? 129.378 23.626  12.501  1.00   45.87  ? 103 LEU D CA  1 
ATOM   9757  C C   . LEU D  1 103 ? 128.137 23.280  13.325  1.00   45.42  ? 103 LEU D C   1 
ATOM   9758  O O   . LEU D  1 103 ? 128.189 23.235  14.554  1.00   48.91  ? 103 LEU D O   1 
ATOM   9759  C CB  . LEU D  1 103 ? 130.445 22.528  12.603  1.00   46.60  ? 103 LEU D CB  1 
ATOM   9760  C CG  . LEU D  1 103 ? 130.333 21.215  11.853  1.00   47.02  ? 103 LEU D CG  1 
ATOM   9761  C CD1 . LEU D  1 103 ? 130.059 21.484  10.402  1.00   47.94  ? 103 LEU D CD1 1 
ATOM   9762  C CD2 . LEU D  1 103 ? 131.631 20.461  12.015  1.00   46.40  ? 103 LEU D CD2 1 
ATOM   9763  N N   . LEU D  1 104 ? 127.010 23.059  12.667  1.00   41.66  ? 104 LEU D N   1 
ATOM   9764  C CA  . LEU D  1 104 ? 125.819 22.728  13.419  1.00   44.87  ? 104 LEU D CA  1 
ATOM   9765  C C   . LEU D  1 104 ? 125.730 21.224  13.710  1.00   41.82  ? 104 LEU D C   1 
ATOM   9766  O O   . LEU D  1 104 ? 125.691 20.402  12.784  1.00   41.31  ? 104 LEU D O   1 
ATOM   9767  C CB  . LEU D  1 104 ? 124.584 23.207  12.671  1.00   51.85  ? 104 LEU D CB  1 
ATOM   9768  C CG  . LEU D  1 104 ? 123.403 23.426  13.607  1.00   59.70  ? 104 LEU D CG  1 
ATOM   9769  C CD1 . LEU D  1 104 ? 123.704 24.601  14.535  1.00   64.40  ? 104 LEU D CD1 1 
ATOM   9770  C CD2 . LEU D  1 104 ? 122.136 23.662  12.819  1.00   62.91  ? 104 LEU D CD2 1 
ATOM   9771  N N   . SER D  1 105 ? 125.680 20.874  14.999  1.00   41.96  ? 105 SER D N   1 
ATOM   9772  C CA  . SER D  1 105 ? 125.599 19.475  15.464  1.00   38.67  ? 105 SER D CA  1 
ATOM   9773  C C   . SER D  1 105 ? 124.218 19.123  16.022  1.00   41.46  ? 105 SER D C   1 
ATOM   9774  O O   . SER D  1 105 ? 123.572 19.970  16.615  1.00   45.79  ? 105 SER D O   1 
ATOM   9775  C CB  . SER D  1 105 ? 126.631 19.203  16.558  1.00   36.69  ? 105 SER D CB  1 
ATOM   9776  O OG  . SER D  1 105 ? 127.945 19.446  16.130  1.00   36.61  ? 105 SER D OG  1 
ATOM   9777  N N   . SER D  1 106 ? 123.785 17.874  15.876  1.00   37.48  ? 106 SER D N   1 
ATOM   9778  C CA  . SER D  1 106 ? 122.479 17.486  16.363  1.00   39.29  ? 106 SER D CA  1 
ATOM   9779  C C   . SER D  1 106 ? 122.586 16.391  17.389  1.00   39.67  ? 106 SER D C   1 
ATOM   9780  O O   . SER D  1 106 ? 123.291 15.425  17.191  1.00   41.19  ? 106 SER D O   1 
ATOM   9781  C CB  . SER D  1 106 ? 121.613 17.004  15.219  1.00   43.62  ? 106 SER D CB  1 
ATOM   9782  O OG  . SER D  1 106 ? 121.177 18.101  14.458  1.00   48.46  ? 106 SER D OG  1 
ATOM   9783  N N   . ASN D  1 107 ? 121.860 16.542  18.480  1.00   39.27  ? 107 ASN D N   1 
ATOM   9784  C CA  . ASN D  1 107 ? 121.667 15.468  19.429  1.00   39.36  ? 107 ASN D CA  1 
ATOM   9785  C C   . ASN D  1 107 ? 120.556 14.619  18.844  1.00   39.71  ? 107 ASN D C   1 
ATOM   9786  O O   . ASN D  1 107 ? 119.429 15.064  18.772  1.00   42.69  ? 107 ASN D O   1 
ATOM   9787  C CB  . ASN D  1 107 ? 121.311 16.036  20.800  1.00   41.59  ? 107 ASN D CB  1 
ATOM   9788  C CG  . ASN D  1 107 ? 121.144 14.978  21.858  1.00   46.16  ? 107 ASN D CG  1 
ATOM   9789  O OD1 . ASN D  1 107 ? 120.660 13.878  21.601  1.00   45.84  ? 107 ASN D OD1 1 
ATOM   9790  N ND2 . ASN D  1 107 ? 121.548 15.311  23.076  1.00   50.82  ? 107 ASN D ND2 1 
ATOM   9791  N N   . PRO D  1 108 ? 120.867 13.397  18.388  1.00   39.16  ? 108 PRO D N   1 
ATOM   9792  C CA  . PRO D  1 108 ? 119.834 12.684  17.627  1.00   38.02  ? 108 PRO D CA  1 
ATOM   9793  C C   . PRO D  1 108 ? 118.689 12.135  18.475  1.00   44.90  ? 108 PRO D C   1 
ATOM   9794  O O   . PRO D  1 108 ? 117.621 11.832  17.936  1.00   47.14  ? 108 PRO D O   1 
ATOM   9795  C CB  . PRO D  1 108 ? 120.623 11.544  16.979  1.00   34.03  ? 108 PRO D CB  1 
ATOM   9796  C CG  . PRO D  1 108 ? 121.733 11.290  17.917  1.00   34.11  ? 108 PRO D CG  1 
ATOM   9797  C CD  . PRO D  1 108 ? 122.118 12.623  18.486  1.00   35.61  ? 108 PRO D CD  1 
ATOM   9798  N N   . VAL D  1 109 ? 118.912 12.029  19.783  1.00   47.61  ? 109 VAL D N   1 
ATOM   9799  C CA  . VAL D  1 109 ? 117.910 11.527  20.721  1.00   47.68  ? 109 VAL D CA  1 
ATOM   9800  C C   . VAL D  1 109 ? 116.951 12.639  21.145  1.00   50.51  ? 109 VAL D C   1 
ATOM   9801  O O   . VAL D  1 109 ? 115.739 12.492  21.031  1.00   52.95  ? 109 VAL D O   1 
ATOM   9802  C CB  . VAL D  1 109 ? 118.575 10.910  21.974  1.00   47.05  ? 109 VAL D CB  1 
ATOM   9803  C CG1 . VAL D  1 109 ? 117.530 10.588  23.030  1.00   50.60  ? 109 VAL D CG1 1 
ATOM   9804  C CG2 . VAL D  1 109 ? 119.385 9.662   21.603  1.00   43.28  ? 109 VAL D CG2 1 
ATOM   9805  N N   . THR D  1 110 ? 117.506 13.771  21.574  1.00   49.03  ? 110 THR D N   1 
ATOM   9806  C CA  . THR D  1 110 ? 116.723 14.880  22.104  1.00   48.94  ? 110 THR D CA  1 
ATOM   9807  C C   . THR D  1 110 ? 116.259 15.788  20.992  1.00   48.25  ? 110 THR D C   1 
ATOM   9808  O O   . THR D  1 110 ? 115.509 16.716  21.231  1.00   50.25  ? 110 THR D O   1 
ATOM   9809  C CB  . THR D  1 110 ? 117.516 15.751  23.088  1.00   52.17  ? 110 THR D CB  1 
ATOM   9810  O OG1 . THR D  1 110 ? 118.481 16.535  22.381  1.00   51.24  ? 110 THR D OG1 1 
ATOM   9811  C CG2 . THR D  1 110 ? 118.201 14.900  24.124  1.00   54.93  ? 110 THR D CG2 1 
ATOM   9812  N N   . GLN D  1 111 ? 116.794 15.576  19.800  1.00   49.42  ? 111 GLN D N   1 
ATOM   9813  C CA  . GLN D  1 111 ? 116.483 16.389  18.633  1.00   52.12  ? 111 GLN D CA  1 
ATOM   9814  C C   . GLN D  1 111 ? 117.001 17.842  18.786  1.00   68.18  ? 111 GLN D C   1 
ATOM   9815  O O   . GLN D  1 111 ? 116.706 18.698  17.954  1.00   69.50  ? 111 GLN D O   1 
ATOM   9816  C CB  . GLN D  1 111 ? 114.965 16.389  18.384  1.00   57.82  ? 111 GLN D CB  1 
ATOM   9817  C CG  . GLN D  1 111 ? 114.341 15.057  17.947  1.00   63.98  ? 111 GLN D CG  1 
ATOM   9818  C CD  . GLN D  1 111 ? 114.763 14.606  16.560  1.00   71.90  ? 111 GLN D CD  1 
ATOM   9819  O OE1 . GLN D  1 111 ? 115.604 13.713  16.401  1.00   75.99  ? 111 GLN D OE1 1 
ATOM   9820  N NE2 . GLN D  1 111 ? 114.164 15.211  15.542  1.00   73.48  ? 111 GLN D NE2 1 
ATOM   9821  N N   . GLU D  1 112 ? 117.773 18.120  19.837  1.00   65.86  ? 112 GLU D N   1 
ATOM   9822  C CA  . GLU D  1 112 ? 118.482 19.401  19.969  1.00   62.47  ? 112 GLU D CA  1 
ATOM   9823  C C   . GLU D  1 112 ? 119.629 19.579  18.968  1.00   56.95  ? 112 GLU D C   1 
ATOM   9824  O O   . GLU D  1 112 ? 120.259 18.607  18.565  1.00   51.64  ? 112 GLU D O   1 
ATOM   9825  C CB  . GLU D  1 112 ? 119.047 19.572  21.382  1.00   62.95  ? 112 GLU D CB  1 
ATOM   9826  C CG  . GLU D  1 112 ? 118.034 19.928  22.446  1.00   66.62  ? 112 GLU D CG  1 
ATOM   9827  C CD  . GLU D  1 112 ? 118.605 19.806  23.842  1.00   69.11  ? 112 GLU D CD  1 
ATOM   9828  O OE1 . GLU D  1 112 ? 119.491 18.950  24.062  1.00   68.08  ? 112 GLU D OE1 1 
ATOM   9829  O OE2 . GLU D  1 112 ? 118.181 20.589  24.712  1.00   73.87  1 112 GLU D OE2 1 
ATOM   9830  N N   . SER D  1 113 ? 119.908 20.823  18.581  1.00   56.69  ? 113 SER D N   1 
ATOM   9831  C CA  . SER D  1 113 ? 121.118 21.107  17.818  1.00   55.34  ? 113 SER D CA  1 
ATOM   9832  C C   . SER D  1 113 ? 121.863 22.309  18.398  1.00   55.49  ? 113 SER D C   1 
ATOM   9833  O O   . SER D  1 113 ? 121.276 23.159  19.055  1.00   59.06  ? 113 SER D O   1 
ATOM   9834  C CB  . SER D  1 113 ? 120.800 21.343  16.333  1.00   53.95  ? 113 SER D CB  1 
ATOM   9835  O OG  . SER D  1 113 ? 120.029 22.502  16.130  1.00   56.71  ? 113 SER D OG  1 
ATOM   9836  N N   . GLY D  1 114 ? 123.156 22.404  18.123  1.00   51.99  ? 114 GLY D N   1 
ATOM   9837  C CA  . GLY D  1 114 ? 123.922 23.493  18.682  1.00   51.79  ? 114 GLY D CA  1 
ATOM   9838  C C   . GLY D  1 114 ? 125.060 23.843  17.766  1.00   50.73  ? 114 GLY D C   1 
ATOM   9839  O O   . GLY D  1 114 ? 125.520 22.991  17.017  1.00   47.46  ? 114 GLY D O   1 
ATOM   9840  N N   . LEU D  1 115 ? 125.495 25.102  17.799  1.00   52.47  ? 115 LEU D N   1 
ATOM   9841  C CA  . LEU D  1 115 ? 126.582 25.514  16.936  1.00   51.91  ? 115 LEU D CA  1 
ATOM   9842  C C   . LEU D  1 115 ? 127.916 25.285  17.623  1.00   52.40  ? 115 LEU D C   1 
ATOM   9843  O O   . LEU D  1 115 ? 128.203 25.875  18.665  1.00   55.71  ? 115 LEU D O   1 
ATOM   9844  C CB  . LEU D  1 115 ? 126.451 26.972  16.514  1.00   52.55  ? 115 LEU D CB  1 
ATOM   9845  C CG  . LEU D  1 115 ? 127.396 27.234  15.332  1.00   51.66  ? 115 LEU D CG  1 
ATOM   9846  C CD1 . LEU D  1 115 ? 126.792 26.713  14.027  1.00   47.90  ? 115 LEU D CD1 1 
ATOM   9847  C CD2 . LEU D  1 115 ? 127.742 28.707  15.207  1.00   56.27  ? 115 LEU D CD2 1 
ATOM   9848  N N   . GLY D  1 116 ? 128.700 24.389  17.035  1.00   47.37  ? 116 GLY D N   1 
ATOM   9849  C CA  . GLY D  1 116 ? 130.034 24.073  17.494  1.00   43.50  ? 116 GLY D CA  1 
ATOM   9850  C C   . GLY D  1 116 ? 131.087 24.649  16.575  1.00   40.70  ? 116 GLY D C   1 
ATOM   9851  O O   . GLY D  1 116 ? 130.778 25.303  15.591  1.00   41.95  ? 116 GLY D O   1 
ATOM   9852  N N   . GLU D  1 117 ? 132.341 24.400  16.915  1.00   39.24  ? 117 GLU D N   1 
ATOM   9853  C CA  . GLU D  1 117 ? 133.482 24.868  16.142  1.00   38.15  ? 117 GLU D CA  1 
ATOM   9854  C C   . GLU D  1 117 ? 134.212 23.691  15.481  1.00   36.45  ? 117 GLU D C   1 
ATOM   9855  O O   . GLU D  1 117 ? 134.460 22.665  16.121  1.00   36.39  ? 117 GLU D O   1 
ATOM   9856  C CB  . GLU D  1 117 ? 134.430 25.640  17.055  1.00   40.12  ? 117 GLU D CB  1 
ATOM   9857  C CG  . GLU D  1 117 ? 135.535 26.402  16.377  1.00   43.22  ? 117 GLU D CG  1 
ATOM   9858  C CD  . GLU D  1 117 ? 136.489 26.980  17.383  1.00   48.75  ? 117 GLU D CD  1 
ATOM   9859  O OE1 . GLU D  1 117 ? 137.005 26.206  18.220  1.00   51.02  ? 117 GLU D OE1 1 
ATOM   9860  O OE2 . GLU D  1 117 ? 136.681 28.215  17.374  1.00   50.71  1 117 GLU D OE2 1 
ATOM   9861  N N   . LEU D  1 118 ? 134.552 23.828  14.206  1.00   36.17  ? 118 LEU D N   1 
ATOM   9862  C CA  . LEU D  1 118 ? 135.321 22.788  13.536  1.00   34.80  ? 118 LEU D CA  1 
ATOM   9863  C C   . LEU D  1 118 ? 136.673 22.570  14.202  1.00   35.71  ? 118 LEU D C   1 
ATOM   9864  O O   . LEU D  1 118 ? 137.393 23.508  14.526  1.00   36.81  ? 118 LEU D O   1 
ATOM   9865  C CB  . LEU D  1 118 ? 135.510 23.124  12.057  1.00   35.27  ? 118 LEU D CB  1 
ATOM   9866  C CG  . LEU D  1 118 ? 136.184 22.050  11.189  1.00   34.75  ? 118 LEU D CG  1 
ATOM   9867  C CD1 . LEU D  1 118 ? 135.344 20.780  11.136  1.00   33.37  ? 118 LEU D CD1 1 
ATOM   9868  C CD2 . LEU D  1 118 ? 136.417 22.579  9.796   1.00   34.27  ? 118 LEU D CD2 1 
ATOM   9869  N N   . ALA D  1 119 ? 137.026 21.306  14.372  1.00   35.16  ? 119 ALA D N   1 
ATOM   9870  C CA  . ALA D  1 119 ? 138.244 20.938  15.056  1.00   34.70  ? 119 ALA D CA  1 
ATOM   9871  C C   . ALA D  1 119 ? 139.010 19.916  14.247  1.00   33.55  ? 119 ALA D C   1 
ATOM   9872  O O   . ALA D  1 119 ? 138.455 19.272  13.373  1.00   32.71  ? 119 ALA D O   1 
ATOM   9873  C CB  . ALA D  1 119 ? 137.928 20.394  16.410  1.00   35.13  ? 119 ALA D CB  1 
ATOM   9874  N N   . GLN D  1 120 ? 140.291 19.773  14.555  1.00   33.91  ? 120 GLN D N   1 
ATOM   9875  C CA  . GLN D  1 120 ? 141.163 18.823  13.884  1.00   33.50  ? 120 GLN D CA  1 
ATOM   9876  C C   . GLN D  1 120 ? 142.067 18.169  14.939  1.00   34.13  ? 120 GLN D C   1 
ATOM   9877  O O   . GLN D  1 120 ? 142.649 18.861  15.761  1.00   36.67  ? 120 GLN D O   1 
ATOM   9878  C CB  . GLN D  1 120 ? 141.977 19.560  12.814  1.00   36.47  ? 120 GLN D CB  1 
ATOM   9879  C CG  . GLN D  1 120 ? 142.964 18.751  12.027  1.00   38.04  ? 120 GLN D CG  1 
ATOM   9880  C CD  . GLN D  1 120 ? 143.847 19.624  11.135  1.00   41.31  ? 120 GLN D CD  1 
ATOM   9881  O OE1 . GLN D  1 120 ? 143.388 20.164  10.130  1.00   42.35  ? 120 GLN D OE1 1 
ATOM   9882  N NE2 . GLN D  1 120 ? 145.124 19.753  11.498  1.00   42.06  ? 120 GLN D NE2 1 
ATOM   9883  N N   . ASP D  1 121 ? 142.159 16.843  14.949  1.00   34.32  ? 121 ASP D N   1 
ATOM   9884  C CA  . ASP D  1 121 ? 143.035 16.152  15.896  1.00   33.57  ? 121 ASP D CA  1 
ATOM   9885  C C   . ASP D  1 121 ? 143.260 14.729  15.409  1.00   33.04  ? 121 ASP D C   1 
ATOM   9886  O O   . ASP D  1 121 ? 142.767 14.345  14.359  1.00   34.85  ? 121 ASP D O   1 
ATOM   9887  C CB  . ASP D  1 121 ? 142.437 16.160  17.315  1.00   35.35  ? 121 ASP D CB  1 
ATOM   9888  C CG  . ASP D  1 121 ? 143.507 16.143  18.422  1.00   35.45  ? 121 ASP D CG  1 
ATOM   9889  O OD1 . ASP D  1 121 ? 144.636 15.667  18.195  1.00   35.02  ? 121 ASP D OD1 1 
ATOM   9890  O OD2 . ASP D  1 121 ? 143.203 16.578  19.550  1.00   36.04  1 121 ASP D OD2 1 
ATOM   9891  N N   . VAL D  1 122 ? 144.044 13.966  16.155  1.00   36.76  ? 122 VAL D N   1 
ATOM   9892  C CA  . VAL D  1 122 ? 144.297 12.552  15.870  1.00   39.49  ? 122 VAL D CA  1 
ATOM   9893  C C   . VAL D  1 122 ? 143.124 11.650  16.254  1.00   43.10  ? 122 VAL D C   1 
ATOM   9894  O O   . VAL D  1 122 ? 142.603 11.744  17.355  1.00   47.41  ? 122 VAL D O   1 
ATOM   9895  C CB  . VAL D  1 122 ? 145.530 12.041  16.631  1.00   41.58  ? 122 VAL D CB  1 
ATOM   9896  C CG1 . VAL D  1 122 ? 145.701 10.533  16.437  1.00   41.88  ? 122 VAL D CG1 1 
ATOM   9897  C CG2 . VAL D  1 122 ? 146.780 12.769  16.181  1.00   42.97  ? 122 VAL D CG2 1 
ATOM   9898  N N   . LEU D  1 123 ? 142.728 10.767  15.347  1.00   39.53  ? 123 LEU D N   1 
ATOM   9899  C CA  . LEU D  1 123 ? 141.872 9.640   15.668  1.00   36.73  ? 123 LEU D CA  1 
ATOM   9900  C C   . LEU D  1 123 ? 142.622 8.359   15.323  1.00   35.68  ? 123 LEU D C   1 
ATOM   9901  O O   . LEU D  1 123 ? 143.317 8.324   14.310  1.00   35.94  ? 123 LEU D O   1 
ATOM   9902  C CB  . LEU D  1 123 ? 140.552 9.739   14.903  1.00   34.48  ? 123 LEU D CB  1 
ATOM   9903  C CG  . LEU D  1 123 ? 139.539 8.602   15.004  1.00   29.55  ? 123 LEU D CG  1 
ATOM   9904  C CD1 . LEU D  1 123 ? 138.146 9.175   15.000  1.00   27.88  ? 123 LEU D CD1 1 
ATOM   9905  C CD2 . LEU D  1 123 ? 139.701 7.670   13.816  1.00   28.91  ? 123 LEU D CD2 1 
ATOM   9906  N N   . ALA D  1 124 ? 142.498 7.329   16.166  1.00   34.63  ? 124 ALA D N   1 
ATOM   9907  C CA  . ALA D  1 124 ? 143.107 6.022   15.929  1.00   31.78  ? 124 ALA D CA  1 
ATOM   9908  C C   . ALA D  1 124 ? 142.027 4.964   15.919  1.00   32.74  ? 124 ALA D C   1 
ATOM   9909  O O   . ALA D  1 124 ? 140.994 5.123   16.572  1.00   32.88  ? 124 ALA D O   1 
ATOM   9910  C CB  . ALA D  1 124 ? 144.143 5.707   16.998  1.00   31.86  ? 124 ALA D CB  1 
ATOM   9911  N N   . ILE D  1 125 ? 142.260 3.890   15.173  1.00   32.09  ? 125 ILE D N   1 
ATOM   9912  C CA  . ILE D  1 125 ? 141.289 2.799   15.054  1.00   30.58  ? 125 ILE D CA  1 
ATOM   9913  C C   . ILE D  1 125 ? 142.051 1.505   14.770  1.00   32.30  ? 125 ILE D C   1 
ATOM   9914  O O   . ILE D  1 125 ? 143.128 1.530   14.180  1.00   34.75  ? 125 ILE D O   1 
ATOM   9915  C CB  . ILE D  1 125 ? 140.222 3.060   13.939  1.00   27.88  ? 125 ILE D CB  1 
ATOM   9916  C CG1 . ILE D  1 125 ? 139.146 1.972   13.934  1.00   27.58  ? 125 ILE D CG1 1 
ATOM   9917  C CG2 . ILE D  1 125 ? 140.884 3.145   12.578  1.00   29.07  ? 125 ILE D CG2 1 
ATOM   9918  C CD1 . ILE D  1 125 ? 138.027 2.153   12.940  1.00   26.31  ? 125 ILE D CD1 1 
ATOM   9919  N N   . HIS D  1 126 ? 141.514 0.377   15.215  1.00   30.78  ? 126 HIS D N   1 
ATOM   9920  C CA  . HIS D  1 126 ? 142.186 -0.881  14.987  1.00   32.19  ? 126 HIS D CA  1 
ATOM   9921  C C   . HIS D  1 126 ? 142.228 -1.241  13.528  1.00   31.95  ? 126 HIS D C   1 
ATOM   9922  O O   . HIS D  1 126 ? 141.249 -1.051  12.823  1.00   34.32  ? 126 HIS D O   1 
ATOM   9923  C CB  . HIS D  1 126 ? 141.505 -2.022  15.715  1.00   35.88  ? 126 HIS D CB  1 
ATOM   9924  C CG  . HIS D  1 126 ? 141.864 -2.131  17.161  1.00   40.14  ? 126 HIS D CG  1 
ATOM   9925  N ND1 . HIS D  1 126 ? 143.101 -2.567  17.586  1.00   44.82  ? 126 HIS D ND1 1 
ATOM   9926  C CD2 . HIS D  1 126 ? 141.118 -1.971  18.279  1.00   39.02  ? 126 HIS D CD2 1 
ATOM   9927  C CE1 . HIS D  1 126 ? 143.119 -2.613  18.906  1.00   46.01  ? 126 HIS D CE1 1 
ATOM   9928  N NE2 . HIS D  1 126 ? 141.926 -2.264  19.352  1.00   42.52  ? 126 HIS D NE2 1 
ATOM   9929  N N   . SER D  1 127 ? 143.362 -1.758  13.078  1.00   30.21  ? 127 SER D N   1 
ATOM   9930  C CA  . SER D  1 127 ? 143.399 -2.482  11.815  1.00   33.16  ? 127 SER D CA  1 
ATOM   9931  C C   . SER D  1 127 ? 143.171 -3.962  12.143  1.00   34.80  ? 127 SER D C   1 
ATOM   9932  O O   . SER D  1 127 ? 142.740 -4.305  13.253  1.00   34.47  ? 127 SER D O   1 
ATOM   9933  C CB  . SER D  1 127 ? 144.724 -2.268  11.073  1.00   34.83  ? 127 SER D CB  1 
ATOM   9934  O OG  . SER D  1 127 ? 145.840 -2.589  11.886  1.00   36.02  ? 127 SER D OG  1 
ATOM   9935  N N   . THR D  1 128 ? 143.448 -4.844  11.190  1.00   34.96  ? 128 THR D N   1 
ATOM   9936  C CA  . THR D  1 128 ? 143.399 -6.269  11.471  1.00   37.07  ? 128 THR D CA  1 
ATOM   9937  C C   . THR D  1 128 ? 144.756 -6.902  11.228  1.00   42.22  ? 128 THR D C   1 
ATOM   9938  O O   . THR D  1 128 ? 145.580 -6.369  10.486  1.00   45.62  ? 128 THR D O   1 
ATOM   9939  C CB  . THR D  1 128 ? 142.351 -6.987  10.630  1.00   35.97  ? 128 THR D CB  1 
ATOM   9940  O OG1 . THR D  1 128 ? 142.706 -6.895  9.248   1.00   36.80  ? 128 THR D OG1 1 
ATOM   9941  C CG2 . THR D  1 128 ? 141.006 -6.347  10.819  1.00   31.96  ? 128 THR D CG2 1 
ATOM   9942  N N   . HIS D  1 129 ? 144.991 -8.030  11.882  1.00   43.48  ? 129 HIS D N   1 
ATOM   9943  C CA  . HIS D  1 129 ? 146.240 -8.733  11.749  1.00   44.74  ? 129 HIS D CA  1 
ATOM   9944  C C   . HIS D  1 129 ? 145.951 -10.206 11.591  1.00   48.27  ? 129 HIS D C   1 
ATOM   9945  O O   . HIS D  1 129 ? 145.718 -10.901 12.575  1.00   50.29  ? 129 HIS D O   1 
ATOM   9946  C CB  . HIS D  1 129 ? 147.090 -8.481  12.974  1.00   46.96  ? 129 HIS D CB  1 
ATOM   9947  C CG  . HIS D  1 129 ? 148.475 -9.028  12.878  1.00   51.35  ? 129 HIS D CG  1 
ATOM   9948  N ND1 . HIS D  1 129 ? 148.922 -10.061 13.668  1.00   54.69  ? 129 HIS D ND1 1 
ATOM   9949  C CD2 . HIS D  1 129 ? 149.521 -8.668  12.099  1.00   51.66  ? 129 HIS D CD2 1 
ATOM   9950  C CE1 . HIS D  1 129 ? 150.186 -10.316 13.378  1.00   55.21  ? 129 HIS D CE1 1 
ATOM   9951  N NE2 . HIS D  1 129 ? 150.573 -9.485  12.428  1.00   53.64  ? 129 HIS D NE2 1 
ATOM   9952  N N   . GLY D  1 130 ? 145.996 -10.693 10.354  1.00   49.47  ? 130 GLY D N   1 
ATOM   9953  C CA  . GLY D  1 130 ? 145.572 -12.051 10.091  1.00   50.00  ? 130 GLY D CA  1 
ATOM   9954  C C   . GLY D  1 130 ? 144.103 -12.126 10.442  1.00   50.32  ? 130 GLY D C   1 
ATOM   9955  O O   . GLY D  1 130 ? 143.297 -11.340 9.929   1.00   48.02  ? 130 GLY D O   1 
ATOM   9956  N N   . SER D  1 131 ? 143.756 -13.055 11.333  1.00   52.48  ? 131 SER D N   1 
ATOM   9957  C CA  . SER D  1 131 ? 142.368 -13.249 11.792  1.00   52.15  ? 131 SER D CA  1 
ATOM   9958  C C   . SER D  1 131 ? 142.011 -12.470 13.078  1.00   48.07  ? 131 SER D C   1 
ATOM   9959  O O   . SER D  1 131 ? 140.877 -12.556 13.586  1.00   41.78  ? 131 SER D O   1 
ATOM   9960  C CB  . SER D  1 131 ? 142.099 -14.738 12.011  1.00   54.09  ? 131 SER D CB  1 
ATOM   9961  O OG  . SER D  1 131 ? 142.706 -15.193 13.209  1.00   55.63  ? 131 SER D OG  1 
ATOM   9962  N N   . LYS D  1 132 ? 142.987 -11.713 13.586  1.00   48.69  ? 132 LYS D N   1 
ATOM   9963  C CA  . LYS D  1 132 ? 142.849 -10.939 14.815  1.00   46.79  ? 132 LYS D CA  1 
ATOM   9964  C C   . LYS D  1 132 ? 142.769 -9.442  14.526  1.00   41.74  ? 132 LYS D C   1 
ATOM   9965  O O   . LYS D  1 132 ? 143.028 -8.989  13.422  1.00   41.96  ? 132 LYS D O   1 
ATOM   9966  C CB  . LYS D  1 132 ? 144.046 -11.165 15.744  1.00   50.53  ? 132 LYS D CB  1 
ATOM   9967  C CG  . LYS D  1 132 ? 144.314 -12.556 16.238  1.00   57.66  ? 132 LYS D CG  1 
ATOM   9968  C CD  . LYS D  1 132 ? 144.803 -12.438 17.690  1.00   65.06  ? 132 LYS D CD  1 
ATOM   9969  C CE  . LYS D  1 132 ? 145.488 -13.708 18.214  1.00   71.16  ? 132 LYS D CE  1 
ATOM   9970  N NZ  . LYS D  1 132 ? 146.725 -13.469 19.018  1.00   72.23  ? 132 LYS D NZ  1 
ATOM   9971  N N   . LEU D  1 133 ? 142.434 -8.674  15.547  1.00   41.88  ? 133 LEU D N   1 
ATOM   9972  C CA  . LEU D  1 133 ? 142.604 -7.241  15.496  1.00   40.66  ? 133 LEU D CA  1 
ATOM   9973  C C   . LEU D  1 133 ? 144.070 -6.951  15.453  1.00   41.81  ? 133 LEU D C   1 
ATOM   9974  O O   . LEU D  1 133 ? 144.846 -7.577  16.177  1.00   46.01  ? 133 LEU D O   1 
ATOM   9975  C CB  . LEU D  1 133 ? 141.965 -6.557  16.707  1.00   41.69  ? 133 LEU D CB  1 
ATOM   9976  C CG  . LEU D  1 133 ? 140.446 -6.480  16.809  1.00   40.61  ? 133 LEU D CG  1 
ATOM   9977  C CD1 . LEU D  1 133 ? 140.087 -5.814  18.101  1.00   42.36  ? 133 LEU D CD1 1 
ATOM   9978  C CD2 . LEU D  1 133 ? 139.886 -5.687  15.645  1.00   34.47  ? 133 LEU D CD2 1 
ATOM   9979  N N   . GLY D  1 134 ? 144.447 -5.980  14.637  1.00   40.40  ? 134 GLY D N   1 
ATOM   9980  C CA  . GLY D  1 134 ? 145.830 -5.613  14.521  1.00   37.80  ? 134 GLY D CA  1 
ATOM   9981  C C   . GLY D  1 134 ? 146.051 -4.325  15.260  1.00   38.32  ? 134 GLY D C   1 
ATOM   9982  O O   . GLY D  1 134 ? 145.197 -3.858  15.997  1.00   36.41  ? 134 GLY D O   1 
ATOM   9983  N N   . PRO D  1 135 ? 147.216 -3.741  15.070  1.00   40.71  ? 135 PRO D N   1 
ATOM   9984  C CA  . PRO D  1 135 ? 147.604 -2.509  15.753  1.00   42.16  ? 135 PRO D CA  1 
ATOM   9985  C C   . PRO D  1 135 ? 146.719 -1.325  15.347  1.00   41.84  ? 135 PRO D C   1 
ATOM   9986  O O   . PRO D  1 135 ? 146.119 -1.338  14.280  1.00   39.29  ? 135 PRO D O   1 
ATOM   9987  C CB  . PRO D  1 135 ? 149.049 -2.297  15.299  1.00   43.92  ? 135 PRO D CB  1 
ATOM   9988  C CG  . PRO D  1 135 ? 149.173 -3.079  14.027  1.00   43.86  ? 135 PRO D CG  1 
ATOM   9989  C CD  . PRO D  1 135 ? 148.260 -4.249  14.171  1.00   43.49  ? 135 PRO D CD  1 
ATOM   9990  N N   . MET D  1 136 ? 146.624 -0.325  16.215  1.00   43.46  ? 136 MET D N   1 
ATOM   9991  C CA  . MET D  1 136 ? 145.913 0.909   15.906  1.00   42.99  ? 136 MET D CA  1 
ATOM   9992  C C   . MET D  1 136 ? 146.578 1.656   14.774  1.00   38.80  ? 136 MET D C   1 
ATOM   9993  O O   . MET D  1 136 ? 147.794 1.742   14.740  1.00   41.70  ? 136 MET D O   1 
ATOM   9994  C CB  . MET D  1 136 ? 145.863 1.812   17.134  1.00   49.14  ? 136 MET D CB  1 
ATOM   9995  C CG  . MET D  1 136 ? 145.398 1.117   18.393  1.00   54.53  ? 136 MET D CG  1 
ATOM   9996  S SD  . MET D  1 136 ? 143.619 0.980   18.447  1.00   50.22  ? 136 MET D SD  1 
ATOM   9997  C CE  . MET D  1 136 ? 143.186 2.673   18.757  1.00   41.37  ? 136 MET D CE  1 
ATOM   9998  N N   . VAL D  1 137 ? 145.779 2.224   13.874  1.00   32.01  ? 137 VAL D N   1 
ATOM   9999  C CA  . VAL D  1 137 ? 146.270 3.100   12.829  1.00   29.90  ? 137 VAL D CA  1 
ATOM   10000 C C   . VAL D  1 137 ? 145.631 4.483   12.986  1.00   30.96  ? 137 VAL D C   1 
ATOM   10001 O O   . VAL D  1 137 ? 144.549 4.610   13.543  1.00   34.87  ? 137 VAL D O   1 
ATOM   10002 C CB  . VAL D  1 137 ? 145.990 2.535   11.423  1.00   29.89  ? 137 VAL D CB  1 
ATOM   10003 C CG1 . VAL D  1 137 ? 146.899 1.383   11.152  1.00   31.80  ? 137 VAL D CG1 1 
ATOM   10004 C CG2 . VAL D  1 137 ? 144.528 2.120   11.262  1.00   29.70  ? 137 VAL D CG2 1 
ATOM   10005 N N   . LYS D  1 138 ? 146.322 5.523   12.533  1.00   32.78  ? 138 LYS D N   1 
ATOM   10006 C CA  . LYS D  1 138 ? 145.898 6.886   12.792  1.00   31.84  ? 138 LYS D CA  1 
ATOM   10007 C C   . LYS D  1 138 ? 145.476 7.673   11.560  1.00   32.18  ? 138 LYS D C   1 
ATOM   10008 O O   . LYS D  1 138 ? 146.033 7.522   10.463  1.00   31.48  ? 138 LYS D O   1 
ATOM   10009 C CB  . LYS D  1 138 ? 147.029 7.633   13.489  1.00   34.95  ? 138 LYS D CB  1 
ATOM   10010 C CG  . LYS D  1 138 ? 147.443 7.019   14.807  1.00   38.05  ? 138 LYS D CG  1 
ATOM   10011 C CD  . LYS D  1 138 ? 148.618 7.750   15.401  1.00   42.71  ? 138 LYS D CD  1 
ATOM   10012 C CE  . LYS D  1 138 ? 149.081 7.104   16.697  1.00   47.46  ? 138 LYS D CE  1 
ATOM   10013 N NZ  . LYS D  1 138 ? 150.215 7.853   17.292  1.00   50.78  ? 138 LYS D NZ  1 
ATOM   10014 N N   . VAL D  1 139 ? 144.478 8.524   11.776  1.00   34.05  ? 139 VAL D N   1 
ATOM   10015 C CA  . VAL D  1 139 ? 144.195 9.668   10.917  1.00   33.09  ? 139 VAL D CA  1 
ATOM   10016 C C   . VAL D  1 139 ? 144.660 10.923  11.673  1.00   35.20  ? 139 VAL D C   1 
ATOM   10017 O O   . VAL D  1 139 ? 143.965 11.435  12.552  1.00   36.27  ? 139 VAL D O   1 
ATOM   10018 C CB  . VAL D  1 139 ? 142.700 9.790   10.569  1.00   31.10  ? 139 VAL D CB  1 
ATOM   10019 C CG1 . VAL D  1 139 ? 142.474 10.944  9.604   1.00   31.12  ? 139 VAL D CG1 1 
ATOM   10020 C CG2 . VAL D  1 139 ? 142.183 8.481   9.984   1.00   27.17  ? 139 VAL D CG2 1 
ATOM   10021 N N   . PRO D  1 140 ? 145.837 11.436  11.310  1.00   34.29  ? 140 PRO D N   1 
ATOM   10022 C CA  . PRO D  1 140 ? 146.461 12.483  12.116  1.00   34.94  ? 140 PRO D CA  1 
ATOM   10023 C C   . PRO D  1 140 ? 145.721 13.834  12.091  1.00   36.14  ? 140 PRO D C   1 
ATOM   10024 O O   . PRO D  1 140 ? 145.813 14.566  13.070  1.00   37.76  ? 140 PRO D O   1 
ATOM   10025 C CB  . PRO D  1 140 ? 147.858 12.610  11.482  1.00   33.28  ? 140 PRO D CB  1 
ATOM   10026 C CG  . PRO D  1 140 ? 148.034 11.397  10.641  1.00   31.90  ? 140 PRO D CG  1 
ATOM   10027 C CD  . PRO D  1 140 ? 146.684 11.032  10.173  1.00   30.72  ? 140 PRO D CD  1 
ATOM   10028 N N   . GLN D  1 141 ? 144.993 14.151  11.022  1.00   38.91  ? 141 GLN D N   1 
ATOM   10029 C CA  . GLN D  1 141 ? 144.194 15.385  10.978  1.00   41.98  ? 141 GLN D CA  1 
ATOM   10030 C C   . GLN D  1 141 ? 142.696 15.096  10.876  1.00   38.16  ? 141 GLN D C   1 
ATOM   10031 O O   . GLN D  1 141 ? 142.034 15.605  9.972   1.00   36.86  ? 141 GLN D O   1 
ATOM   10032 C CB  . GLN D  1 141 ? 144.536 16.288  9.773   1.00   49.90  ? 141 GLN D CB  1 
ATOM   10033 C CG  . GLN D  1 141 ? 145.893 16.954  9.666   1.00   59.24  ? 141 GLN D CG  1 
ATOM   10034 C CD  . GLN D  1 141 ? 146.900 16.117  8.935   1.00   69.34  ? 141 GLN D CD  1 
ATOM   10035 O OE1 . GLN D  1 141 ? 146.562 15.096  8.329   1.00   72.77  ? 141 GLN D OE1 1 
ATOM   10036 N NE2 . GLN D  1 141 ? 148.147 16.571  8.936   1.00   74.58  ? 141 GLN D NE2 1 
ATOM   10037 N N   . PHE D  1 142 ? 142.142 14.330  11.805  1.00   35.66  ? 142 PHE D N   1 
ATOM   10038 C CA  . PHE D  1 142 ? 140.724 14.021  11.715  1.00   32.68  ? 142 PHE D CA  1 
ATOM   10039 C C   . PHE D  1 142 ? 139.834 15.230  12.025  1.00   29.95  ? 142 PHE D C   1 
ATOM   10040 O O   . PHE D  1 142 ? 139.998 15.879  13.041  1.00   33.48  ? 142 PHE D O   1 
ATOM   10041 C CB  . PHE D  1 142 ? 140.385 12.850  12.642  1.00   35.16  ? 142 PHE D CB  1 
ATOM   10042 C CG  . PHE D  1 142 ? 138.945 12.408  12.558  1.00   37.37  ? 142 PHE D CG  1 
ATOM   10043 C CD1 . PHE D  1 142 ? 138.512 11.582  11.536  1.00   37.31  ? 142 PHE D CD1 1 
ATOM   10044 C CD2 . PHE D  1 142 ? 138.021 12.826  13.506  1.00   38.62  ? 142 PHE D CD2 1 
ATOM   10045 C CE1 . PHE D  1 142 ? 137.172 11.183  11.453  1.00   39.03  ? 142 PHE D CE1 1 
ATOM   10046 C CE2 . PHE D  1 142 ? 136.688 12.438  13.422  1.00   38.54  ? 142 PHE D CE2 1 
ATOM   10047 C CZ  . PHE D  1 142 ? 136.264 11.613  12.400  1.00   37.65  ? 142 PHE D CZ  1 
ATOM   10048 N N   . LEU D  1 143 ? 138.875 15.502  11.146  1.00   29.30  ? 143 LEU D N   1 
ATOM   10049 C CA  . LEU D  1 143 ? 137.947 16.619  11.306  1.00   29.33  ? 143 LEU D CA  1 
ATOM   10050 C C   . LEU D  1 143 ? 136.650 16.256  12.041  1.00   29.48  ? 143 LEU D C   1 
ATOM   10051 O O   . LEU D  1 143 ? 135.999 15.273  11.733  1.00   30.93  ? 143 LEU D O   1 
ATOM   10052 C CB  . LEU D  1 143 ? 137.592 17.187  9.941   1.00   30.10  ? 143 LEU D CB  1 
ATOM   10053 C CG  . LEU D  1 143 ? 138.757 17.747  9.132   1.00   31.83  ? 143 LEU D CG  1 
ATOM   10054 C CD1 . LEU D  1 143 ? 138.313 18.127  7.716   1.00   32.34  ? 143 LEU D CD1 1 
ATOM   10055 C CD2 . LEU D  1 143 ? 139.356 18.922  9.873   1.00   33.30  ? 143 LEU D CD2 1 
ATOM   10056 N N   . PHE D  1 144 ? 136.266 17.093  12.993  1.00   31.43  ? 144 PHE D N   1 
ATOM   10057 C CA  . PHE D  1 144 ? 135.112 16.834  13.833  1.00   29.89  ? 144 PHE D CA  1 
ATOM   10058 C C   . PHE D  1 144 ? 134.666 18.150  14.429  1.00   33.54  ? 144 PHE D C   1 
ATOM   10059 O O   . PHE D  1 144 ? 135.292 19.188  14.191  1.00   38.55  ? 144 PHE D O   1 
ATOM   10060 C CB  . PHE D  1 144 ? 135.460 15.835  14.938  1.00   30.42  ? 144 PHE D CB  1 
ATOM   10061 C CG  . PHE D  1 144 ? 136.460 16.361  15.949  1.00   31.57  ? 144 PHE D CG  1 
ATOM   10062 C CD1 . PHE D  1 144 ? 137.821 16.324  15.693  1.00   30.98  ? 144 PHE D CD1 1 
ATOM   10063 C CD2 . PHE D  1 144 ? 136.041 16.885  17.160  1.00   32.39  ? 144 PHE D CD2 1 
ATOM   10064 C CE1 . PHE D  1 144 ? 138.739 16.824  16.632  1.00   31.19  ? 144 PHE D CE1 1 
ATOM   10065 C CE2 . PHE D  1 144 ? 136.957 17.376  18.097  1.00   32.63  ? 144 PHE D CE2 1 
ATOM   10066 C CZ  . PHE D  1 144 ? 138.300 17.340  17.833  1.00   31.51  ? 144 PHE D CZ  1 
ATOM   10067 N N   . SER D  1 145 ? 133.621 18.123  15.248  1.00   32.81  ? 145 SER D N   1 
ATOM   10068 C CA  . SER D  1 145 ? 133.134 19.358  15.841  1.00   32.70  ? 145 SER D CA  1 
ATOM   10069 C C   . SER D  1 145 ? 133.328 19.400  17.347  1.00   37.10  ? 145 SER D C   1 
ATOM   10070 O O   . SER D  1 145 ? 133.032 18.427  18.034  1.00   40.10  ? 145 SER D O   1 
ATOM   10071 C CB  . SER D  1 145 ? 131.661 19.548  15.514  1.00   31.59  ? 145 SER D CB  1 
ATOM   10072 O OG  . SER D  1 145 ? 131.168 20.698  16.158  1.00   33.55  ? 145 SER D OG  1 
ATOM   10073 N N   . CYS D  1 146 ? 133.835 20.519  17.859  1.00   38.50  ? 146 CYS D N   1 
ATOM   10074 C CA  . CYS D  1 146 ? 133.781 20.778  19.291  1.00   39.49  ? 146 CYS D CA  1 
ATOM   10075 C C   . CYS D  1 146 ? 132.453 21.388  19.597  1.00   42.05  ? 146 CYS D C   1 
ATOM   10076 O O   . CYS D  1 146 ? 132.252 22.569  19.368  1.00   44.89  ? 146 CYS D O   1 
ATOM   10077 C CB  . CYS D  1 146 ? 134.871 21.730  19.745  1.00   39.71  ? 146 CYS D CB  1 
ATOM   10078 S SG  . CYS D  1 146 ? 136.436 20.952  20.016  1.00   47.59  ? 146 CYS D SG  1 
ATOM   10079 N N   . ALA D  1 147 ? 131.545 20.587  20.129  1.00   42.50  ? 147 ALA D N   1 
ATOM   10080 C CA  . ALA D  1 147 ? 130.177 21.027  20.326  1.00   43.48  ? 147 ALA D CA  1 
ATOM   10081 C C   . ALA D  1 147 ? 129.982 21.625  21.713  1.00   51.09  ? 147 ALA D C   1 
ATOM   10082 O O   . ALA D  1 147 ? 130.769 21.332  22.628  1.00   52.69  ? 147 ALA D O   1 
ATOM   10083 C CB  . ALA D  1 147 ? 129.222 19.867  20.095  1.00   42.15  ? 147 ALA D CB  1 
ATOM   10084 N N   . PRO D  1 148 ? 128.940 22.484  21.875  1.00   55.87  ? 148 PRO D N   1 
ATOM   10085 C CA  . PRO D  1 148 ? 128.608 23.032  23.199  1.00   56.92  ? 148 PRO D CA  1 
ATOM   10086 C C   . PRO D  1 148 ? 128.234 21.961  24.228  1.00   58.34  ? 148 PRO D C   1 
ATOM   10087 O O   . PRO D  1 148 ? 127.544 20.984  23.902  1.00   59.21  ? 148 PRO D O   1 
ATOM   10088 C CB  . PRO D  1 148 ? 127.413 23.962  22.914  1.00   56.88  ? 148 PRO D CB  1 
ATOM   10089 C CG  . PRO D  1 148 ? 126.914 23.609  21.561  1.00   54.95  ? 148 PRO D CG  1 
ATOM   10090 C CD  . PRO D  1 148 ? 128.106 23.088  20.813  1.00   55.07  ? 148 PRO D CD  1 
ATOM   10091 N N   . SER D  1 149 ? 128.684 22.173  25.463  1.00   57.83  ? 149 SER D N   1 
ATOM   10092 C CA  . SER D  1 149 ? 128.534 21.212  26.545  1.00   59.49  ? 149 SER D CA  1 
ATOM   10093 C C   . SER D  1 149 ? 127.097 20.763  26.767  1.00   59.83  ? 149 SER D C   1 
ATOM   10094 O O   . SER D  1 149 ? 126.845 19.623  27.154  1.00   61.03  ? 149 SER D O   1 
ATOM   10095 C CB  . SER D  1 149 ? 129.066 21.803  27.834  1.00   63.35  ? 149 SER D CB  1 
ATOM   10096 O OG  . SER D  1 149 ? 128.303 21.339  28.929  1.00   67.98  ? 149 SER D OG  1 
ATOM   10097 N N   . PHE D  1 150 ? 126.158 21.669  26.550  1.00   58.31  ? 150 PHE D N   1 
ATOM   10098 C CA  . PHE D  1 150 ? 124.772 21.362  26.818  1.00   57.68  ? 150 PHE D CA  1 
ATOM   10099 C C   . PHE D  1 150 ? 124.275 20.232  25.918  1.00   53.47  ? 150 PHE D C   1 
ATOM   10100 O O   . PHE D  1 150 ? 123.317 19.563  26.261  1.00   54.69  ? 150 PHE D O   1 
ATOM   10101 C CB  . PHE D  1 150 ? 123.914 22.633  26.673  1.00   61.89  ? 150 PHE D CB  1 
ATOM   10102 C CG  . PHE D  1 150 ? 123.542 22.996  25.244  1.00   62.42  ? 150 PHE D CG  1 
ATOM   10103 C CD1 . PHE D  1 150 ? 122.546 22.306  24.553  1.00   58.88  ? 150 PHE D CD1 1 
ATOM   10104 C CD2 . PHE D  1 150 ? 124.184 24.042  24.599  1.00   62.98  ? 150 PHE D CD2 1 
ATOM   10105 C CE1 . PHE D  1 150 ? 122.207 22.646  23.258  1.00   55.08  ? 150 PHE D CE1 1 
ATOM   10106 C CE2 . PHE D  1 150 ? 123.846 24.382  23.302  1.00   59.89  ? 150 PHE D CE2 1 
ATOM   10107 C CZ  . PHE D  1 150 ? 122.860 23.679  22.633  1.00   56.45  ? 150 PHE D CZ  1 
ATOM   10108 N N   . LEU D  1 151 ? 124.920 20.010  24.774  1.00   49.12  ? 151 LEU D N   1 
ATOM   10109 C CA  . LEU D  1 151 ? 124.341 19.134  23.751  1.00   48.05  ? 151 LEU D CA  1 
ATOM   10110 C C   . LEU D  1 151 ? 124.271 17.653  24.121  1.00   48.81  ? 151 LEU D C   1 
ATOM   10111 O O   . LEU D  1 151 ? 123.326 16.960  23.735  1.00   47.56  ? 151 LEU D O   1 
ATOM   10112 C CB  . LEU D  1 151 ? 125.112 19.258  22.432  1.00   43.79  ? 151 LEU D CB  1 
ATOM   10113 C CG  . LEU D  1 151 ? 124.360 18.680  21.219  1.00   38.86  ? 151 LEU D CG  1 
ATOM   10114 C CD1 . LEU D  1 151 ? 123.012 19.337  21.032  1.00   44.31  ? 151 LEU D CD1 1 
ATOM   10115 C CD2 . LEU D  1 151 ? 125.168 18.709  19.921  1.00   36.81  ? 151 LEU D CD2 1 
ATOM   10116 N N   . ALA D  1 152 ? 125.229 17.182  24.910  1.00   50.82  ? 152 ALA D N   1 
ATOM   10117 C CA  . ALA D  1 152 ? 125.296 15.764  25.261  1.00   50.52  ? 152 ALA D CA  1 
ATOM   10118 C C   . ALA D  1 152 ? 124.669 15.465  26.619  1.00   55.09  ? 152 ALA D C   1 
ATOM   10119 O O   . ALA D  1 152 ? 124.708 14.332  27.094  1.00   56.76  ? 152 ALA D O   1 
ATOM   10120 C CB  . ALA D  1 152 ? 126.740 15.302  25.253  1.00   48.00  ? 152 ALA D CB  1 
ATOM   10121 N N   . GLN D  1 153 ? 124.068 16.480  27.226  1.00   56.93  ? 153 GLN D N   1 
ATOM   10122 C CA  . GLN D  1 153 ? 123.624 16.372  28.606  1.00   60.41  ? 153 GLN D CA  1 
ATOM   10123 C C   . GLN D  1 153 ? 122.325 15.598  28.739  1.00   60.27  ? 153 GLN D C   1 
ATOM   10124 O O   . GLN D  1 153 ? 121.923 15.245  29.845  1.00   63.24  ? 153 GLN D O   1 
ATOM   10125 C CB  . GLN D  1 153 ? 123.448 17.760  29.225  1.00   64.95  ? 153 GLN D CB  1 
ATOM   10126 C CG  . GLN D  1 153 ? 124.731 18.389  29.729  1.00   68.75  ? 153 GLN D CG  1 
ATOM   10127 C CD  . GLN D  1 153 ? 124.512 19.800  30.229  1.00   77.65  ? 153 GLN D CD  1 
ATOM   10128 O OE1 . GLN D  1 153 ? 123.383 20.306  30.227  1.00   78.99  ? 153 GLN D OE1 1 
ATOM   10129 N NE2 . GLN D  1 153 ? 125.599 20.468  30.619  1.00   82.20  ? 153 GLN D NE2 1 
ATOM   10130 N N   . LYS D  1 154 ? 121.665 15.315  27.626  1.00   60.08  ? 154 LYS D N   1 
ATOM   10131 C CA  . LYS D  1 154 ? 120.376 14.652  27.713  1.00   61.87  ? 154 LYS D CA  1 
ATOM   10132 C C   . LYS D  1 154 ? 120.211 13.552  26.689  1.00   57.46  ? 154 LYS D C   1 
ATOM   10133 O O   . LYS D  1 154 ? 120.640 13.712  25.557  1.00   54.88  ? 154 LYS D O   1 
ATOM   10134 C CB  . LYS D  1 154 ? 119.248 15.676  27.535  1.00   67.33  ? 154 LYS D CB  1 
ATOM   10135 C CG  . LYS D  1 154 ? 119.163 16.751  28.614  1.00   73.11  ? 154 LYS D CG  1 
ATOM   10136 C CD  . LYS D  1 154 ? 117.985 17.712  28.401  1.00   77.00  ? 154 LYS D CD  1 
ATOM   10137 C CE  . LYS D  1 154 ? 117.432 17.680  26.982  1.00   77.40  ? 154 LYS D CE  1 
ATOM   10138 N NZ  . LYS D  1 154 ? 116.418 18.759  26.781  1.00   81.34  ? 154 LYS D NZ  1 
ATOM   10139 N N   . GLY D  1 155 ? 119.650 12.418  27.105  1.00   57.86  ? 155 GLY D N   1 
ATOM   10140 C CA  . GLY D  1 155 ? 119.153 11.421  26.165  1.00   55.92  ? 155 GLY D CA  1 
ATOM   10141 C C   . GLY D  1 155 ? 120.155 10.357  25.796  1.00   53.23  ? 155 GLY D C   1 
ATOM   10142 O O   . GLY D  1 155 ? 119.834 9.330   25.207  1.00   53.15  ? 155 GLY D O   1 
ATOM   10143 N N   . LEU D  1 156 ? 121.400 10.634  26.124  1.00   50.36  ? 156 LEU D N   1 
ATOM   10144 C CA  . LEU D  1 156 ? 122.473 9.768   25.735  1.00   47.41  ? 156 LEU D CA  1 
ATOM   10145 C C   . LEU D  1 156 ? 122.778 8.852   26.890  1.00   49.92  ? 156 LEU D C   1 
ATOM   10146 O O   . LEU D  1 156 ? 122.409 9.155   28.018  1.00   54.97  ? 156 LEU D O   1 
ATOM   10147 C CB  . LEU D  1 156 ? 123.711 10.580  25.359  1.00   45.44  ? 156 LEU D CB  1 
ATOM   10148 C CG  . LEU D  1 156 ? 123.531 11.764  24.420  1.00   42.34  ? 156 LEU D CG  1 
ATOM   10149 C CD1 . LEU D  1 156 ? 124.899 12.312  24.069  1.00   40.36  ? 156 LEU D CD1 1 
ATOM   10150 C CD2 . LEU D  1 156 ? 122.743 11.371  23.181  1.00   39.75  ? 156 LEU D CD2 1 
ATOM   10151 N N   . PRO D  1 157 ? 123.454 7.724   26.623  1.00   47.58  ? 157 PRO D N   1 
ATOM   10152 C CA  . PRO D  1 157 ? 123.915 6.889   27.736  1.00   48.75  ? 157 PRO D CA  1 
ATOM   10153 C C   . PRO D  1 157 ? 124.802 7.688   28.685  1.00   51.70  ? 157 PRO D C   1 
ATOM   10154 O O   . PRO D  1 157 ? 125.372 8.669   28.247  1.00   50.28  ? 157 PRO D O   1 
ATOM   10155 C CB  . PRO D  1 157 ? 124.709 5.786   27.033  1.00   46.77  ? 157 PRO D CB  1 
ATOM   10156 C CG  . PRO D  1 157 ? 124.106 5.711   25.662  1.00   43.99  ? 157 PRO D CG  1 
ATOM   10157 C CD  . PRO D  1 157 ? 123.726 7.108   25.309  1.00   44.29  ? 157 PRO D CD  1 
ATOM   10158 N N   . ASN D  1 158 ? 124.914 7.307   29.952  1.00   57.88  ? 158 ASN D N   1 
ATOM   10159 C CA  . ASN D  1 158 ? 125.664 8.150   30.883  1.00   65.75  ? 158 ASN D CA  1 
ATOM   10160 C C   . ASN D  1 158 ? 127.149 8.128   30.544  1.00   64.30  ? 158 ASN D C   1 
ATOM   10161 O O   . ASN D  1 158 ? 127.668 7.125   30.059  1.00   64.02  ? 158 ASN D O   1 
ATOM   10162 C CB  . ASN D  1 158 ? 125.405 7.785   32.361  1.00   75.12  ? 158 ASN D CB  1 
ATOM   10163 C CG  . ASN D  1 158 ? 125.873 6.397   32.738  1.00   81.20  ? 158 ASN D CG  1 
ATOM   10164 O OD1 . ASN D  1 158 ? 126.901 5.910   32.265  1.00   82.94  ? 158 ASN D OD1 1 
ATOM   10165 N ND2 . ASN D  1 158 ? 125.108 5.746   33.612  1.00   84.28  ? 158 ASN D ND2 1 
ATOM   10166 N N   . ASN D  1 159 ? 127.787 9.276   30.725  1.00   64.04  ? 159 ASN D N   1 
ATOM   10167 C CA  . ASN D  1 159 ? 129.201 9.477   30.468  1.00   63.42  ? 159 ASN D CA  1 
ATOM   10168 C C   . ASN D  1 159 ? 129.549 9.522   28.999  1.00   57.53  ? 159 ASN D C   1 
ATOM   10169 O O   . ASN D  1 159 ? 130.695 9.780   28.648  1.00   56.25  ? 159 ASN D O   1 
ATOM   10170 C CB  . ASN D  1 159 ? 130.024 8.395   31.165  1.00   69.86  ? 159 ASN D CB  1 
ATOM   10171 C CG  . ASN D  1 159 ? 130.524 8.836   32.520  1.00   78.32  ? 159 ASN D CG  1 
ATOM   10172 O OD1 . ASN D  1 159 ? 130.033 8.381   33.563  1.00   82.98  ? 159 ASN D OD1 1 
ATOM   10173 N ND2 . ASN D  1 159 ? 131.544 9.698   32.516  1.00   79.81  ? 159 ASN D ND2 1 
ATOM   10174 N N   . VAL D  1 160 ? 128.552 9.334   28.142  1.00   53.67  ? 160 VAL D N   1 
ATOM   10175 C CA  . VAL D  1 160 ? 128.760 9.486   26.707  1.00   51.18  ? 160 VAL D CA  1 
ATOM   10176 C C   . VAL D  1 160 ? 128.794 10.968  26.394  1.00   56.37  ? 160 VAL D C   1 
ATOM   10177 O O   . VAL D  1 160 ? 127.931 11.712  26.840  1.00   60.16  ? 160 VAL D O   1 
ATOM   10178 C CB  . VAL D  1 160 ? 127.681 8.787   25.889  1.00   45.54  ? 160 VAL D CB  1 
ATOM   10179 C CG1 . VAL D  1 160 ? 127.572 9.373   24.522  1.00   36.49  ? 160 VAL D CG1 1 
ATOM   10180 C CG2 . VAL D  1 160 ? 127.970 7.295   25.837  1.00   41.90  ? 160 VAL D CG2 1 
ATOM   10181 N N   . GLN D  1 161 ? 129.777 11.392  25.604  1.00   57.26  ? 161 GLN D N   1 
ATOM   10182 C CA  . GLN D  1 161 ? 130.105 12.809  25.508  1.00   55.71  ? 161 GLN D CA  1 
ATOM   10183 C C   . GLN D  1 161 ? 129.928 13.401  24.095  1.00   47.92  ? 161 GLN D C   1 
ATOM   10184 O O   . GLN D  1 161 ? 130.408 14.498  23.804  1.00   45.93  ? 161 GLN D O   1 
ATOM   10185 C CB  . GLN D  1 161 ? 131.551 12.974  25.984  1.00   58.64  ? 161 GLN D CB  1 
ATOM   10186 C CG  . GLN D  1 161 ? 131.705 12.796  27.496  1.00   64.83  ? 161 GLN D CG  1 
ATOM   10187 C CD  . GLN D  1 161 ? 133.131 12.458  27.888  1.00   69.14  ? 161 GLN D CD  1 
ATOM   10188 O OE1 . GLN D  1 161 ? 134.047 12.627  27.092  1.00   70.54  ? 161 GLN D OE1 1 
ATOM   10189 N NE2 . GLN D  1 161 ? 133.313 11.898  29.084  1.00   70.98  ? 161 GLN D NE2 1 
ATOM   10190 N N   . GLY D  1 162 ? 129.208 12.693  23.232  1.00   41.31  ? 162 GLY D N   1 
ATOM   10191 C CA  . GLY D  1 162 ? 129.005 13.149  21.872  1.00   36.91  ? 162 GLY D CA  1 
ATOM   10192 C C   . GLY D  1 162 ? 128.528 12.015  21.001  1.00   34.34  ? 162 GLY D C   1 
ATOM   10193 O O   . GLY D  1 162 ? 128.017 11.030  21.512  1.00   35.79  ? 162 GLY D O   1 
ATOM   10194 N N   . ALA D  1 163 ? 128.687 12.157  19.688  1.00   31.68  ? 163 ALA D N   1 
ATOM   10195 C CA  . ALA D  1 163 ? 128.255 11.141  18.742  1.00   29.97  ? 163 ALA D CA  1 
ATOM   10196 C C   . ALA D  1 163 ? 129.205 11.014  17.568  1.00   33.59  ? 163 ALA D C   1 
ATOM   10197 O O   . ALA D  1 163 ? 129.865 11.965  17.181  1.00   34.27  ? 163 ALA D O   1 
ATOM   10198 C CB  . ALA D  1 163 ? 126.871 11.442  18.224  1.00   29.52  ? 163 ALA D CB  1 
ATOM   10199 N N   . LEU D  1 164 ? 129.276 9.809   17.024  1.00   34.77  ? 164 LEU D N   1 
ATOM   10200 C CA  . LEU D  1 164 ? 129.949 9.581   15.768  1.00   36.82  ? 164 LEU D CA  1 
ATOM   10201 C C   . LEU D  1 164 ? 128.906 9.282   14.684  1.00   34.58  ? 164 LEU D C   1 
ATOM   10202 O O   . LEU D  1 164 ? 128.029 8.435   14.867  1.00   36.71  ? 164 LEU D O   1 
ATOM   10203 C CB  . LEU D  1 164 ? 130.962 8.446   15.916  1.00   41.22  ? 164 LEU D CB  1 
ATOM   10204 C CG  . LEU D  1 164 ? 130.337 7.120   16.327  1.00   45.69  ? 164 LEU D CG  1 
ATOM   10205 C CD1 . LEU D  1 164 ? 130.385 6.147   15.167  1.00   46.88  ? 164 LEU D CD1 1 
ATOM   10206 C CD2 . LEU D  1 164 ? 130.994 6.563   17.572  1.00   48.10  ? 164 LEU D CD2 1 
ATOM   10207 N N   . GLY D  1 165 ? 128.990 10.006  13.573  1.00   32.70  ? 165 GLY D N   1 
ATOM   10208 C CA  . GLY D  1 165 ? 128.018 9.896   12.505  1.00   30.57  ? 165 GLY D CA  1 
ATOM   10209 C C   . GLY D  1 165 ? 128.565 9.131   11.324  1.00   28.17  ? 165 GLY D C   1 
ATOM   10210 O O   . GLY D  1 165 ? 129.697 9.344   10.919  1.00   27.79  ? 165 GLY D O   1 
ATOM   10211 N N   . LEU D  1 166 ? 127.759 8.241   10.767  1.00   27.68  ? 166 LEU D N   1 
ATOM   10212 C CA  . LEU D  1 166 ? 128.185 7.431   9.653   1.00   25.63  ? 166 LEU D CA  1 
ATOM   10213 C C   . LEU D  1 166 ? 127.324 7.723   8.456   1.00   28.98  ? 166 LEU D C   1 
ATOM   10214 O O   . LEU D  1 166 ? 127.181 6.884   7.561   1.00   29.56  ? 166 LEU D O   1 
ATOM   10215 C CB  . LEU D  1 166 ? 128.109 5.954   9.995   1.00   28.38  ? 166 LEU D CB  1 
ATOM   10216 C CG  . LEU D  1 166 ? 128.967 5.434   11.160  1.00   32.79  ? 166 LEU D CG  1 
ATOM   10217 C CD1 . LEU D  1 166 ? 128.683 3.974   11.407  1.00   32.40  ? 166 LEU D CD1 1 
ATOM   10218 C CD2 . LEU D  1 166 ? 130.422 5.620   10.892  1.00   33.04  ? 166 LEU D CD2 1 
ATOM   10219 N N   . GLY D  1 167 ? 126.746 8.919   8.456   1.00   27.76  ? 167 GLY D N   1 
ATOM   10220 C CA  . GLY D  1 167 ? 125.811 9.320   7.432   1.00   30.53  ? 167 GLY D CA  1 
ATOM   10221 C C   . GLY D  1 167 ? 126.500 9.687   6.146   1.00   32.25  ? 167 GLY D C   1 
ATOM   10222 O O   . GLY D  1 167 ? 127.703 9.825   6.085   1.00   31.06  ? 167 GLY D O   1 
ATOM   10223 N N   . GLN D  1 168 ? 125.705 9.898   5.116   1.00   33.61  ? 168 GLN D N   1 
ATOM   10224 C CA  . GLN D  1 168 ? 126.238 10.283  3.824   1.00   34.29  ? 168 GLN D CA  1 
ATOM   10225 C C   . GLN D  1 168 ? 126.518 11.768  3.829   1.00   35.92  ? 168 GLN D C   1 
ATOM   10226 O O   . GLN D  1 168 ? 125.681 12.559  3.448   1.00   39.81  ? 168 GLN D O   1 
ATOM   10227 C CB  . GLN D  1 168 ? 125.264 9.899   2.710   1.00   29.61  ? 168 GLN D CB  1 
ATOM   10228 C CG  . GLN D  1 168 ? 125.277 8.425   2.454   1.00   25.65  ? 168 GLN D CG  1 
ATOM   10229 C CD  . GLN D  1 168 ? 126.628 8.014   1.957   1.00   27.15  ? 168 GLN D CD  1 
ATOM   10230 O OE1 . GLN D  1 168 ? 127.028 8.425   0.881   1.00   32.92  ? 168 GLN D OE1 1 
ATOM   10231 N NE2 . GLN D  1 168 ? 127.362 7.246   2.748   1.00   25.65  ? 168 GLN D NE2 1 
ATOM   10232 N N   . ALA D  1 169 ? 127.705 12.137  4.281   1.00   34.69  ? 169 ALA D N   1 
ATOM   10233 C CA  . ALA D  1 169 ? 128.059 13.528  4.469   1.00   30.61  ? 169 ALA D CA  1 
ATOM   10234 C C   . ALA D  1 169 ? 129.580 13.613  4.378   1.00   29.45  ? 169 ALA D C   1 
ATOM   10235 O O   . ALA D  1 169 ? 130.252 12.611  4.631   1.00   33.01  ? 169 ALA D O   1 
ATOM   10236 C CB  . ALA D  1 169 ? 127.546 14.021  5.807   1.00   30.61  ? 169 ALA D CB  1 
ATOM   10237 N N   . PRO D  1 170 ? 130.131 14.782  3.970   1.00   29.27  ? 170 PRO D N   1 
ATOM   10238 C CA  . PRO D  1 170 ? 131.560 14.879  3.586   1.00   28.08  ? 170 PRO D CA  1 
ATOM   10239 C C   . PRO D  1 170 ? 132.620 14.582  4.666   1.00   28.85  ? 170 PRO D C   1 
ATOM   10240 O O   . PRO D  1 170 ? 133.660 14.010  4.310   1.00   30.83  ? 170 PRO D O   1 
ATOM   10241 C CB  . PRO D  1 170 ? 131.695 16.336  3.095   1.00   28.95  ? 170 PRO D CB  1 
ATOM   10242 C CG  . PRO D  1 170 ? 130.516 17.044  3.607   1.00   31.43  ? 170 PRO D CG  1 
ATOM   10243 C CD  . PRO D  1 170 ? 129.409 16.013  3.629   1.00   30.38  ? 170 PRO D CD  1 
ATOM   10244 N N   . ILE D  1 171 ? 132.386 14.909  5.937   1.00   30.35  ? 171 ILE D N   1 
ATOM   10245 C CA  . ILE D  1 171 ? 133.330 14.499  6.972   1.00   26.62  ? 171 ILE D CA  1 
ATOM   10246 C C   . ILE D  1 171 ? 132.703 13.524  7.948   1.00   27.38  ? 171 ILE D C   1 
ATOM   10247 O O   . ILE D  1 171 ? 133.034 13.516  9.135   1.00   30.33  ? 171 ILE D O   1 
ATOM   10248 C CB  . ILE D  1 171 ? 133.943 15.690  7.779   1.00   29.57  ? 171 ILE D CB  1 
ATOM   10249 C CG1 . ILE D  1 171 ? 132.895 16.512  8.528   1.00   31.13  ? 171 ILE D CG1 1 
ATOM   10250 C CG2 . ILE D  1 171 ? 134.807 16.574  6.900   1.00   29.44  ? 171 ILE D CG2 1 
ATOM   10251 C CD1 . ILE D  1 171 ? 133.498 17.305  9.679   1.00   30.44  ? 171 ILE D CD1 1 
ATOM   10252 N N   . SER D  1 172 ? 131.822 12.673  7.439   1.00   29.00  ? 172 SER D N   1 
ATOM   10253 C CA  . SER D  1 172 ? 131.315 11.573  8.236   1.00   30.72  ? 172 SER D CA  1 
ATOM   10254 C C   . SER D  1 172 ? 132.493 10.691  8.568   1.00   30.88  ? 172 SER D C   1 
ATOM   10255 O O   . SER D  1 172 ? 133.517 10.745  7.895   1.00   32.23  ? 172 SER D O   1 
ATOM   10256 C CB  . SER D  1 172 ? 130.257 10.780  7.484   1.00   29.38  ? 172 SER D CB  1 
ATOM   10257 O OG  . SER D  1 172 ? 130.824 10.171  6.340   1.00   30.15  ? 172 SER D OG  1 
ATOM   10258 N N   . LEU D  1 173 ? 132.356 9.858   9.584   1.00   30.62  ? 173 LEU D N   1 
ATOM   10259 C CA  . LEU D  1 173 ? 133.461 9.015   9.996   1.00   29.77  ? 173 LEU D CA  1 
ATOM   10260 C C   . LEU D  1 173 ? 133.909 8.080   8.887   1.00   30.90  ? 173 LEU D C   1 
ATOM   10261 O O   . LEU D  1 173 ? 135.100 7.940   8.643   1.00   32.74  ? 173 LEU D O   1 
ATOM   10262 C CB  . LEU D  1 173 ? 133.087 8.193   11.213  1.00   30.73  ? 173 LEU D CB  1 
ATOM   10263 C CG  . LEU D  1 173 ? 134.099 7.112   11.555  1.00   30.14  ? 173 LEU D CG  1 
ATOM   10264 C CD1 . LEU D  1 173 ? 135.403 7.738   11.966  1.00   29.31  ? 173 LEU D CD1 1 
ATOM   10265 C CD2 . LEU D  1 173 ? 133.570 6.217   12.648  1.00   32.06  ? 173 LEU D CD2 1 
ATOM   10266 N N   . GLN D  1 174 ? 132.982 7.405   8.224   1.00   28.55  ? 174 GLN D N   1 
ATOM   10267 C CA  . GLN D  1 174 ? 133.427 6.462   7.209   1.00   28.57  ? 174 GLN D CA  1 
ATOM   10268 C C   . GLN D  1 174 ? 134.059 7.179   5.987   1.00   33.30  ? 174 GLN D C   1 
ATOM   10269 O O   . GLN D  1 174 ? 135.049 6.709   5.448   1.00   33.71  ? 174 GLN D O   1 
ATOM   10270 C CB  . GLN D  1 174 ? 132.273 5.545   6.768   1.00   28.84  ? 174 GLN D CB  1 
ATOM   10271 C CG  . GLN D  1 174 ? 131.312 6.072   5.675   1.00   26.51  ? 174 GLN D CG  1 
ATOM   10272 C CD  . GLN D  1 174 ? 130.299 7.030   6.213   1.00   25.37  ? 174 GLN D CD  1 
ATOM   10273 O OE1 . GLN D  1 174 ? 130.280 7.298   7.401   1.00   30.02  ? 174 GLN D OE1 1 
ATOM   10274 N NE2 . GLN D  1 174 ? 129.457 7.560   5.346   1.00   25.34  ? 174 GLN D NE2 1 
ATOM   10275 N N   . ASN D  1 175 ? 133.512 8.318   5.574   1.00   32.63  ? 175 ASN D N   1 
ATOM   10276 C CA  . ASN D  1 175 ? 134.021 9.003   4.405   1.00   32.72  ? 175 ASN D CA  1 
ATOM   10277 C C   . ASN D  1 175 ? 135.483 9.381   4.676   1.00   31.14  ? 175 ASN D C   1 
ATOM   10278 O O   . ASN D  1 175 ? 136.333 9.294   3.794   1.00   29.32  ? 175 ASN D O   1 
ATOM   10279 C CB  A ASN D  1 175 ? 133.168 10.239  4.041   0.50   36.63  ? 175 ASN D CB  1 
ATOM   10280 C CB  B ASN D  1 175 ? 133.157 10.234  4.081   0.50   36.63  ? 175 ASN D CB  1 
ATOM   10281 C CG  A ASN D  1 175 ? 131.734 9.884   3.581   0.50   41.84  ? 175 ASN D CG  1 
ATOM   10282 C CG  B ASN D  1 175 ? 133.723 11.092  2.942   0.50   38.12  ? 175 ASN D CG  1 
ATOM   10283 O OD1 A ASN D  1 175 ? 131.020 9.140   4.242   0.50   47.00  ? 175 ASN D OD1 1 
ATOM   10284 O OD1 B ASN D  1 175 ? 133.348 10.941  1.780   0.50   38.75  ? 175 ASN D OD1 1 
ATOM   10285 N ND2 A ASN D  1 175 ? 131.319 10.440  2.454   0.50   41.61  ? 175 ASN D ND2 1 
ATOM   10286 N ND2 B ASN D  1 175 ? 134.609 12.014  3.285   0.50   40.98  ? 175 ASN D ND2 1 
ATOM   10287 N N   . GLN D  1 176 ? 135.797 9.740   5.915   1.00   28.98  ? 176 GLN D N   1 
ATOM   10288 C CA  . GLN D  1 176 ? 137.162 10.104  6.231   1.00   26.50  ? 176 GLN D CA  1 
ATOM   10289 C C   . GLN D  1 176 ? 138.138 8.906   6.322   1.00   27.41  ? 176 GLN D C   1 
ATOM   10290 O O   . GLN D  1 176 ? 139.304 9.013   5.930   1.00   26.83  ? 176 GLN D O   1 
ATOM   10291 C CB  . GLN D  1 176 ? 137.198 10.922  7.534   1.00   25.23  ? 176 GLN D CB  1 
ATOM   10292 C CG  . GLN D  1 176 ? 136.676 12.344  7.392   1.00   24.30  ? 176 GLN D CG  1 
ATOM   10293 C CD  . GLN D  1 176 ? 136.987 13.204  8.597   1.00   26.67  ? 176 GLN D CD  1 
ATOM   10294 O OE1 . GLN D  1 176 ? 138.116 13.626  8.800   1.00   27.98  ? 176 GLN D OE1 1 
ATOM   10295 N NE2 . GLN D  1 176 ? 135.982 13.465  9.403   1.00   28.82  ? 176 GLN D NE2 1 
ATOM   10296 N N   . LEU D  1 177 ? 137.675 7.776   6.836   1.00   25.06  ? 177 LEU D N   1 
ATOM   10297 C CA  . LEU D  1 177 ? 138.509 6.601   6.891   1.00   23.14  ? 177 LEU D CA  1 
ATOM   10298 C C   . LEU D  1 177 ? 138.780 6.063   5.510   1.00   26.13  ? 177 LEU D C   1 
ATOM   10299 O O   . LEU D  1 177 ? 139.922 5.751   5.187   1.00   27.25  ? 177 LEU D O   1 
ATOM   10300 C CB  . LEU D  1 177 ? 137.858 5.533   7.748   1.00   23.30  ? 177 LEU D CB  1 
ATOM   10301 C CG  . LEU D  1 177 ? 137.749 5.875   9.233   1.00   25.25  ? 177 LEU D CG  1 
ATOM   10302 C CD1 . LEU D  1 177 ? 136.928 4.825   9.940   1.00   26.31  ? 177 LEU D CD1 1 
ATOM   10303 C CD2 . LEU D  1 177 ? 139.113 5.952   9.883   1.00   24.88  ? 177 LEU D CD2 1 
ATOM   10304 N N   . PHE D  1 178 ? 137.739 5.988   4.684   1.00   26.63  ? 178 PHE D N   1 
ATOM   10305 C CA  . PHE D  1 178 ? 137.878 5.537   3.308   1.00   25.05  ? 178 PHE D CA  1 
ATOM   10306 C C   . PHE D  1 178 ? 138.976 6.304   2.610   1.00   27.18  ? 178 PHE D C   1 
ATOM   10307 O O   . PHE D  1 178 ? 139.872 5.730   2.004   1.00   28.33  ? 178 PHE D O   1 
ATOM   10308 C CB  . PHE D  1 178 ? 136.601 5.771   2.508   1.00   29.90  ? 178 PHE D CB  1 
ATOM   10309 C CG  . PHE D  1 178 ? 135.418 4.970   2.957   1.00   33.41  ? 178 PHE D CG  1 
ATOM   10310 C CD1 . PHE D  1 178 ? 135.566 3.805   3.683   1.00   32.79  ? 178 PHE D CD1 1 
ATOM   10311 C CD2 . PHE D  1 178 ? 134.135 5.403   2.646   1.00   34.66  ? 178 PHE D CD2 1 
ATOM   10312 C CE1 . PHE D  1 178 ? 134.459 3.077   4.089   1.00   30.86  ? 178 PHE D CE1 1 
ATOM   10313 C CE2 . PHE D  1 178 ? 133.021 4.670   3.054   1.00   34.46  ? 178 PHE D CE2 1 
ATOM   10314 C CZ  . PHE D  1 178 ? 133.194 3.497   3.772   1.00   29.62  ? 178 PHE D CZ  1 
ATOM   10315 N N   . SER D  1 179 ? 138.905 7.622   2.684   1.00   26.22  ? 179 SER D N   1 
ATOM   10316 C CA  . SER D  1 179 ? 139.812 8.423   1.887   1.00   26.78  ? 179 SER D CA  1 
ATOM   10317 C C   . SER D  1 179 ? 141.244 8.439   2.502   1.00   29.87  ? 179 SER D C   1 
ATOM   10318 O O   . SER D  1 179 ? 142.219 8.546   1.778   1.00   32.26  ? 179 SER D O   1 
ATOM   10319 C CB  . SER D  1 179 ? 139.252 9.833   1.692   1.00   30.08  ? 179 SER D CB  1 
ATOM   10320 O OG  . SER D  1 179 ? 139.385 10.637  2.832   1.00   38.99  ? 179 SER D OG  1 
ATOM   10321 N N   . HIS D  1 180 ? 141.388 8.342   3.820   1.00   27.12  ? 180 HIS D N   1 
ATOM   10322 C CA  . HIS D  1 180 ? 142.729 8.370   4.372   1.00   25.90  ? 180 HIS D CA  1 
ATOM   10323 C C   . HIS D  1 180 ? 143.475 7.099   4.017   1.00   29.07  ? 180 HIS D C   1 
ATOM   10324 O O   . HIS D  1 180 ? 144.652 7.140   3.703   1.00   31.90  ? 180 HIS D O   1 
ATOM   10325 C CB  . HIS D  1 180 ? 142.725 8.550   5.887   1.00   25.72  ? 180 HIS D CB  1 
ATOM   10326 C CG  . HIS D  1 180 ? 144.085 8.859   6.450   1.00   28.49  ? 180 HIS D CG  1 
ATOM   10327 N ND1 . HIS D  1 180 ? 144.882 7.916   7.063   1.00   30.62  ? 180 HIS D ND1 1 
ATOM   10328 C CD2 . HIS D  1 180 ? 144.807 10.002  6.446   1.00   29.77  ? 180 HIS D CD2 1 
ATOM   10329 C CE1 . HIS D  1 180 ? 146.012 8.471   7.450   1.00   29.37  ? 180 HIS D CE1 1 
ATOM   10330 N NE2 . HIS D  1 180 ? 145.997 9.735   7.079   1.00   31.79  ? 180 HIS D NE2 1 
ATOM   10331 N N   . PHE D  1 181 ? 142.789 5.964   4.048   1.00   27.69  ? 181 PHE D N   1 
ATOM   10332 C CA  . PHE D  1 181 ? 143.459 4.677   3.879   1.00   25.43  ? 181 PHE D CA  1 
ATOM   10333 C C   . PHE D  1 181 ? 143.262 4.032   2.510   1.00   27.62  ? 181 PHE D C   1 
ATOM   10334 O O   . PHE D  1 181 ? 143.788 2.963   2.272   1.00   30.23  ? 181 PHE D O   1 
ATOM   10335 C CB  . PHE D  1 181 ? 143.001 3.700   4.964   1.00   24.53  ? 181 PHE D CB  1 
ATOM   10336 C CG  . PHE D  1 181 ? 143.434 4.084   6.343   1.00   28.27  ? 181 PHE D CG  1 
ATOM   10337 C CD1 . PHE D  1 181 ? 144.739 3.897   6.752   1.00   32.48  ? 181 PHE D CD1 1 
ATOM   10338 C CD2 . PHE D  1 181 ? 142.545 4.653   7.231   1.00   28.01  ? 181 PHE D CD2 1 
ATOM   10339 C CE1 . PHE D  1 181 ? 145.158 4.270   8.049   1.00   34.86  ? 181 PHE D CE1 1 
ATOM   10340 C CE2 . PHE D  1 181 ? 142.947 5.023   8.513   1.00   30.78  ? 181 PHE D CE2 1 
ATOM   10341 C CZ  . PHE D  1 181 ? 144.260 4.820   8.923   1.00   32.61  ? 181 PHE D CZ  1 
ATOM   10342 N N   . GLY D  1 182 ? 142.494 4.651   1.620   1.00   27.21  ? 182 GLY D N   1 
ATOM   10343 C CA  . GLY D  1 182 ? 142.230 4.055   0.314   1.00   27.63  ? 182 GLY D CA  1 
ATOM   10344 C C   . GLY D  1 182 ? 141.369 2.786   0.356   1.00   31.43  ? 182 GLY D C   1 
ATOM   10345 O O   . GLY D  1 182 ? 141.594 1.851   -0.411  1.00   32.81  ? 182 GLY D O   1 
ATOM   10346 N N   . LEU D  1 183 ? 140.369 2.764   1.242   1.00   32.72  ? 183 LEU D N   1 
ATOM   10347 C CA  . LEU D  1 183 ? 139.499 1.605   1.438   1.00   33.24  ? 183 LEU D CA  1 
ATOM   10348 C C   . LEU D  1 183 ? 138.401 1.495   0.365   1.00   32.00  ? 183 LEU D C   1 
ATOM   10349 O O   . LEU D  1 183 ? 138.049 2.477   -0.273  1.00   32.15  ? 183 LEU D O   1 
ATOM   10350 C CB  . LEU D  1 183 ? 138.866 1.684   2.836   1.00   33.23  ? 183 LEU D CB  1 
ATOM   10351 C CG  . LEU D  1 183 ? 139.792 1.828   4.052   1.00   28.78  ? 183 LEU D CG  1 
ATOM   10352 C CD1 . LEU D  1 183 ? 138.984 2.072   5.300   1.00   24.52  ? 183 LEU D CD1 1 
ATOM   10353 C CD2 . LEU D  1 183 ? 140.647 0.588   4.233   1.00   28.65  ? 183 LEU D CD2 1 
ATOM   10354 N N   . LYS D  1 184 ? 137.881 0.292   0.156   1.00   31.47  ? 184 LYS D N   1 
ATOM   10355 C CA  . LYS D  1 184 ? 136.651 0.138   -0.594  1.00   31.66  ? 184 LYS D CA  1 
ATOM   10356 C C   . LYS D  1 184 ? 135.559 0.871   0.201   1.00   31.05  ? 184 LYS D C   1 
ATOM   10357 O O   . LYS D  1 184 ? 135.512 0.806   1.436   1.00   29.10  ? 184 LYS D O   1 
ATOM   10358 C CB  . LYS D  1 184 ? 136.295 -1.342  -0.807  1.00   37.46  ? 184 LYS D CB  1 
ATOM   10359 C CG  . LYS D  1 184 ? 134.875 -1.522  -1.329  1.00   42.63  ? 184 LYS D CG  1 
ATOM   10360 C CD  . LYS D  1 184 ? 134.489 -2.879  -1.889  1.00   46.86  ? 184 LYS D CD  1 
ATOM   10361 C CE  . LYS D  1 184 ? 132.994 -2.801  -2.248  1.00   47.84  ? 184 LYS D CE  1 
ATOM   10362 N NZ  . LYS D  1 184 ? 132.257 -4.093  -2.285  1.00   49.63  ? 184 LYS D NZ  1 
ATOM   10363 N N   . ARG D  1 185 ? 134.676 1.571   -0.504  1.00   29.10  ? 185 ARG D N   1 
ATOM   10364 C CA  . ARG D  1 185 ? 133.655 2.363   0.159   1.00   26.80  ? 185 ARG D CA  1 
ATOM   10365 C C   . ARG D  1 185 ? 132.477 1.485   0.626   1.00   29.56  ? 185 ARG D C   1 
ATOM   10366 O O   . ARG D  1 185 ? 131.420 1.402   -0.014  1.00   29.16  ? 185 ARG D O   1 
ATOM   10367 C CB  . ARG D  1 185 ? 133.193 3.480   -0.779  1.00   26.26  ? 185 ARG D CB  1 
ATOM   10368 C CG  . ARG D  1 185 ? 134.327 4.365   -1.241  1.00   25.86  ? 185 ARG D CG  1 
ATOM   10369 C CD  . ARG D  1 185 ? 133.855 5.542   -2.040  1.00   30.68  ? 185 ARG D CD  1 
ATOM   10370 N NE  . ARG D  1 185 ? 133.185 6.546   -1.218  1.00   37.39  ? 185 ARG D NE  1 
ATOM   10371 C CZ  . ARG D  1 185 ? 133.791 7.532   -0.567  1.00   37.75  ? 185 ARG D CZ  1 
ATOM   10372 N NH1 . ARG D  1 185 ? 135.112 7.686   -0.637  1.00   36.93  ? 185 ARG D NH1 1 
ATOM   10373 N NH2 . ARG D  1 185 ? 133.060 8.372   0.146   1.00   40.21  ? 185 ARG D NH2 1 
ATOM   10374 N N   . GLN D  1 186 ? 132.673 0.860   1.780   1.00   30.24  ? 186 GLN D N   1 
ATOM   10375 C CA  . GLN D  1 186 ? 131.717 -0.087  2.330   1.00   30.82  ? 186 GLN D CA  1 
ATOM   10376 C C   . GLN D  1 186 ? 131.942 -0.220  3.828   1.00   28.06  ? 186 GLN D C   1 
ATOM   10377 O O   . GLN D  1 186 ? 133.080 -0.246  4.278   1.00   27.76  ? 186 GLN D O   1 
ATOM   10378 C CB  . GLN D  1 186 ? 131.844 -1.422  1.590   1.00   31.61  ? 186 GLN D CB  1 
ATOM   10379 C CG  . GLN D  1 186 ? 130.940 -2.532  2.027   1.00   33.23  ? 186 GLN D CG  1 
ATOM   10380 C CD  . GLN D  1 186 ? 131.280 -3.797  1.295   1.00   39.37  ? 186 GLN D CD  1 
ATOM   10381 O OE1 . GLN D  1 186 ? 130.855 -3.967  0.162   1.00   44.71  ? 186 GLN D OE1 1 
ATOM   10382 N NE2 . GLN D  1 186 ? 132.074 -4.674  1.907   1.00   36.96  ? 186 GLN D NE2 1 
ATOM   10383 N N   . PHE D  1 187 ? 130.863 -0.234  4.600   1.00   27.00  ? 187 PHE D N   1 
ATOM   10384 C CA  . PHE D  1 187 ? 130.970 -0.554  6.013   1.00   29.40  ? 187 PHE D CA  1 
ATOM   10385 C C   . PHE D  1 187 ? 129.849 -1.487  6.414   1.00   30.46  ? 187 PHE D C   1 
ATOM   10386 O O   . PHE D  1 187 ? 128.783 -1.501  5.816   1.00   30.93  ? 187 PHE D O   1 
ATOM   10387 C CB  . PHE D  1 187 ? 130.984 0.719   6.901   1.00   26.86  ? 187 PHE D CB  1 
ATOM   10388 C CG  . PHE D  1 187 ? 129.692 1.538   6.864   1.00   29.60  ? 187 PHE D CG  1 
ATOM   10389 C CD1 . PHE D  1 187 ? 129.487 2.499   5.881   1.00   27.30  ? 187 PHE D CD1 1 
ATOM   10390 C CD2 . PHE D  1 187 ? 128.716 1.383   7.833   1.00   30.82  ? 187 PHE D CD2 1 
ATOM   10391 C CE1 . PHE D  1 187 ? 128.330 3.243   5.848   1.00   28.01  ? 187 PHE D CE1 1 
ATOM   10392 C CE2 . PHE D  1 187 ? 127.545 2.142   7.801   1.00   30.70  ? 187 PHE D CE2 1 
ATOM   10393 C CZ  . PHE D  1 187 ? 127.356 3.074   6.815   1.00   29.54  ? 187 PHE D CZ  1 
ATOM   10394 N N   . SER D  1 188 ? 130.143 -2.293  7.420   1.00   30.50  ? 188 SER D N   1 
ATOM   10395 C CA  . SER D  1 188 ? 129.254 -3.334  7.855   1.00   33.44  ? 188 SER D CA  1 
ATOM   10396 C C   . SER D  1 188 ? 129.059 -3.232  9.346   1.00   35.06  ? 188 SER D C   1 
ATOM   10397 O O   . SER D  1 188 ? 130.020 -3.067  10.120  1.00   33.83  ? 188 SER D O   1 
ATOM   10398 C CB  . SER D  1 188 ? 129.801 -4.716  7.475   1.00   35.50  ? 188 SER D CB  1 
ATOM   10399 O OG  . SER D  1 188 ? 129.945 -4.811  6.071   1.00   35.45  ? 188 SER D OG  1 
ATOM   10400 N N   . VAL D  1 189 ? 127.798 -3.365  9.742   1.00   34.66  ? 189 VAL D N   1 
ATOM   10401 C CA  . VAL D  1 189 ? 127.422 -3.230  11.122  1.00   29.24  ? 189 VAL D CA  1 
ATOM   10402 C C   . VAL D  1 189 ? 126.876 -4.542  11.648  1.00   29.71  ? 189 VAL D C   1 
ATOM   10403 O O   . VAL D  1 189 ? 125.999 -5.150  11.042  1.00   29.46  ? 189 VAL D O   1 
ATOM   10404 C CB  . VAL D  1 189 ? 126.405 -2.150  11.279  1.00   29.09  ? 189 VAL D CB  1 
ATOM   10405 C CG1 . VAL D  1 189 ? 126.208 -1.863  12.744  1.00   31.69  ? 189 VAL D CG1 1 
ATOM   10406 C CG2 . VAL D  1 189 ? 126.876 -0.908  10.558  1.00   28.14  ? 189 VAL D CG2 1 
ATOM   10407 N N   . CYS D  1 190 ? 127.464 -5.011  12.743  1.00   31.58  ? 190 CYS D N   1 
ATOM   10408 C CA  . CYS D  1 190 ? 126.964 -6.168  13.451  1.00   32.59  ? 190 CYS D CA  1 
ATOM   10409 C C   . CYS D  1 190 ? 126.796 -5.816  14.919  1.00   36.17  ? 190 CYS D C   1 
ATOM   10410 O O   . CYS D  1 190 ? 127.713 -6.030  15.703  1.00   37.66  ? 190 CYS D O   1 
ATOM   10411 C CB  . CYS D  1 190 ? 127.912 -7.363  13.309  1.00   32.56  ? 190 CYS D CB  1 
ATOM   10412 S SG  . CYS D  1 190 ? 127.061 -8.974  13.386  1.00   41.65  ? 190 CYS D SG  1 
ATOM   10413 N N   . LEU D  1 191 ? 125.625 -5.280  15.281  1.00   36.88  ? 191 LEU D N   1 
ATOM   10414 C CA  . LEU D  1 191 ? 125.333 -4.898  16.659  1.00   33.82  ? 191 LEU D CA  1 
ATOM   10415 C C   . LEU D  1 191 ? 124.992 -6.096  17.482  1.00   33.79  ? 191 LEU D C   1 
ATOM   10416 O O   . LEU D  1 191 ? 124.252 -6.970  17.050  1.00   35.55  ? 191 LEU D O   1 
ATOM   10417 C CB  . LEU D  1 191 ? 124.175 -3.908  16.730  1.00   34.18  ? 191 LEU D CB  1 
ATOM   10418 C CG  . LEU D  1 191 ? 124.337 -2.624  15.926  1.00   33.76  ? 191 LEU D CG  1 
ATOM   10419 C CD1 . LEU D  1 191 ? 123.130 -1.724  16.163  1.00   35.98  ? 191 LEU D CD1 1 
ATOM   10420 C CD2 . LEU D  1 191 ? 125.623 -1.912  16.306  1.00   32.79  ? 191 LEU D CD2 1 
ATOM   10421 N N   . SER D  1 192 ? 125.532 -6.123  18.689  1.00   35.77  ? 192 SER D N   1 
ATOM   10422 C CA  . SER D  1 192 ? 125.262 -7.198  19.605  1.00   40.68  ? 192 SER D CA  1 
ATOM   10423 C C   . SER D  1 192 ? 124.136 -6.787  20.539  1.00   43.79  ? 192 SER D C   1 
ATOM   10424 O O   . SER D  1 192 ? 124.160 -5.688  21.092  1.00   44.90  ? 192 SER D O   1 
ATOM   10425 C CB  . SER D  1 192 ? 126.515 -7.559  20.389  1.00   42.25  ? 192 SER D CB  1 
ATOM   10426 O OG  . SER D  1 192 ? 126.226 -8.559  21.350  1.00   47.90  ? 192 SER D OG  1 
ATOM   10427 N N   . ARG D  1 193 ? 123.153 -7.662  20.715  1.00   41.79  ? 193 ARG D N   1 
ATOM   10428 C CA  . ARG D  1 193 ? 122.056 -7.377  21.622  1.00   43.39  ? 193 ARG D CA  1 
ATOM   10429 C C   . ARG D  1 193 ? 122.417 -7.312  23.112  1.00   44.57  ? 193 ARG D C   1 
ATOM   10430 O O   . ARG D  1 193 ? 121.597 -6.862  23.902  1.00   45.09  ? 193 ARG D O   1 
ATOM   10431 C CB  . ARG D  1 193 ? 120.930 -8.357  21.401  1.00   47.00  ? 193 ARG D CB  1 
ATOM   10432 C CG  . ARG D  1 193 ? 121.088 -9.706  21.981  1.00   54.62  ? 193 ARG D CG  1 
ATOM   10433 C CD  . ARG D  1 193 ? 119.755 -10.414 21.821  1.00   61.57  ? 193 ARG D CD  1 
ATOM   10434 N NE  . ARG D  1 193 ? 119.436 -10.440 20.399  1.00   67.22  ? 193 ARG D NE  1 
ATOM   10435 C CZ  . ARG D  1 193 ? 118.231 -10.650 19.887  1.00   71.26  ? 193 ARG D CZ  1 
ATOM   10436 N NH1 . ARG D  1 193 ? 117.203 -10.895 20.689  1.00   74.37  ? 193 ARG D NH1 1 
ATOM   10437 N NH2 . ARG D  1 193 ? 118.065 -10.620 18.565  1.00   70.25  ? 193 ARG D NH2 1 
ATOM   10438 N N   . TYR D  1 194 ? 123.583 -7.821  23.509  1.00   46.42  ? 194 TYR D N   1 
ATOM   10439 C CA  . TYR D  1 194 ? 123.946 -7.896  24.926  1.00   50.78  ? 194 TYR D CA  1 
ATOM   10440 C C   . TYR D  1 194 ? 124.897 -6.791  25.297  1.00   48.24  ? 194 TYR D C   1 
ATOM   10441 O O   . TYR D  1 194 ? 125.840 -6.537  24.588  1.00   50.28  ? 194 TYR D O   1 
ATOM   10442 C CB  . TYR D  1 194 ? 124.564 -9.264  25.251  1.00   58.61  ? 194 TYR D CB  1 
ATOM   10443 C CG  . TYR D  1 194 ? 123.784 -10.385 24.613  1.00   65.22  ? 194 TYR D CG  1 
ATOM   10444 C CD1 . TYR D  1 194 ? 122.568 -10.799 25.156  1.00   71.93  ? 194 TYR D CD1 1 
ATOM   10445 C CD2 . TYR D  1 194 ? 124.231 -11.007 23.456  1.00   65.52  ? 194 TYR D CD2 1 
ATOM   10446 C CE1 . TYR D  1 194 ? 121.810 -11.814 24.561  1.00   74.39  ? 194 TYR D CE1 1 
ATOM   10447 C CE2 . TYR D  1 194 ? 123.486 -12.030 22.854  1.00   68.76  ? 194 TYR D CE2 1 
ATOM   10448 C CZ  . TYR D  1 194 ? 122.275 -12.429 23.413  1.00   72.48  ? 194 TYR D CZ  1 
ATOM   10449 O OH  . TYR D  1 194 ? 121.526 -13.434 22.827  1.00   72.75  ? 194 TYR D OH  1 
ATOM   10450 N N   . SER D  1 195 ? 124.642 -6.123  26.412  1.00   49.95  ? 195 SER D N   1 
ATOM   10451 C CA  . SER D  1 195 ? 125.528 -5.064  26.874  1.00   51.24  ? 195 SER D CA  1 
ATOM   10452 C C   . SER D  1 195 ? 126.827 -5.664  27.371  1.00   55.94  ? 195 SER D C   1 
ATOM   10453 O O   . SER D  1 195 ? 127.837 -4.981  27.485  1.00   60.36  ? 195 SER D O   1 
ATOM   10454 C CB  . SER D  1 195 ? 124.862 -4.235  27.972  1.00   54.65  ? 195 SER D CB  1 
ATOM   10455 O OG  . SER D  1 195 ? 124.448 -5.041  29.067  1.00   59.10  ? 195 SER D OG  1 
ATOM   10456 N N   . THR D  1 196 ? 126.807 -6.964  27.633  1.00   56.95  ? 196 THR D N   1 
ATOM   10457 C CA  . THR D  1 196 ? 127.946 -7.636  28.244  1.00   58.88  ? 196 THR D CA  1 
ATOM   10458 C C   . THR D  1 196 ? 128.918 -8.128  27.199  1.00   56.78  ? 196 THR D C   1 
ATOM   10459 O O   . THR D  1 196 ? 129.888 -8.785  27.528  1.00   59.48  ? 196 THR D O   1 
ATOM   10460 C CB  . THR D  1 196 ? 127.522 -8.841  29.102  1.00   61.61  ? 196 THR D CB  1 
ATOM   10461 O OG1 . THR D  1 196 ? 127.001 -9.876  28.263  1.00   62.82  ? 196 THR D OG1 1 
ATOM   10462 C CG2 . THR D  1 196 ? 126.491 -8.419  30.146  1.00   62.11  ? 196 THR D CG2 1 
ATOM   10463 N N   . SER D  1 197 ? 128.618 -7.895  25.933  1.00   53.93  ? 197 SER D N   1 
ATOM   10464 C CA  . SER D  1 197 ? 129.566 -8.242  24.890  1.00   54.03  ? 197 SER D CA  1 
ATOM   10465 C C   . SER D  1 197 ? 129.467 -7.260  23.741  1.00   49.80  ? 197 SER D C   1 
ATOM   10466 O O   . SER D  1 197 ? 128.399 -6.730  23.465  1.00   50.84  ? 197 SER D O   1 
ATOM   10467 C CB  . SER D  1 197 ? 129.329 -9.661  24.407  1.00   58.75  ? 197 SER D CB  1 
ATOM   10468 O OG  . SER D  1 197 ? 128.027 -9.779  23.885  1.00   61.36  ? 197 SER D OG  1 
ATOM   10469 N N   . ASN D  1 198 ? 130.589 -7.007  23.084  1.00   46.87  ? 198 ASN D N   1 
ATOM   10470 C CA  . ASN D  1 198 ? 130.644 -5.996  22.043  1.00   44.11  ? 198 ASN D CA  1 
ATOM   10471 C C   . ASN D  1 198 ? 130.184 -6.516  20.678  1.00   41.43  ? 198 ASN D C   1 
ATOM   10472 O O   . ASN D  1 198 ? 130.277 -7.712  20.385  1.00   40.24  ? 198 ASN D O   1 
ATOM   10473 C CB  . ASN D  1 198 ? 132.060 -5.433  21.902  1.00   44.04  ? 198 ASN D CB  1 
ATOM   10474 C CG  . ASN D  1 198 ? 132.478 -4.582  23.077  1.00   47.16  ? 198 ASN D CG  1 
ATOM   10475 O OD1 . ASN D  1 198 ? 131.661 -4.169  23.891  1.00   51.64  ? 198 ASN D OD1 1 
ATOM   10476 N ND2 . ASN D  1 198 ? 133.765 -4.311  23.167  1.00   46.34  ? 198 ASN D ND2 1 
ATOM   10477 N N   . GLY D  1 199 ? 129.678 -5.596  19.861  1.00   37.48  ? 199 GLY D N   1 
ATOM   10478 C CA  . GLY D  1 199 ? 129.482 -5.828  18.446  1.00   37.40  ? 199 GLY D CA  1 
ATOM   10479 C C   . GLY D  1 199 ? 130.526 -4.991  17.730  1.00   39.15  ? 199 GLY D C   1 
ATOM   10480 O O   . GLY D  1 199 ? 131.460 -4.487  18.365  1.00   42.40  ? 199 GLY D O   1 
ATOM   10481 N N   . ALA D  1 200 ? 130.396 -4.828  16.419  1.00   36.07  ? 200 ALA D N   1 
ATOM   10482 C CA  . ALA D  1 200 ? 131.406 -4.066  15.712  1.00   36.15  ? 200 ALA D CA  1 
ATOM   10483 C C   . ALA D  1 200 ? 130.904 -3.406  14.448  1.00   33.16  ? 200 ALA D C   1 
ATOM   10484 O O   . ALA D  1 200 ? 129.890 -3.791  13.891  1.00   36.01  ? 200 ALA D O   1 
ATOM   10485 C CB  . ALA D  1 200 ? 132.588 -4.961  15.397  1.00   37.45  ? 200 ALA D CB  1 
ATOM   10486 N N   . ILE D  1 201 ? 131.640 -2.395  14.018  1.00   32.17  ? 201 ILE D N   1 
ATOM   10487 C CA  . ILE D  1 201 ? 131.532 -1.868  12.678  1.00   27.66  ? 201 ILE D CA  1 
ATOM   10488 C C   . ILE D  1 201 ? 132.846 -2.127  11.966  1.00   29.59  ? 201 ILE D C   1 
ATOM   10489 O O   . ILE D  1 201 ? 133.935 -1.963  12.538  1.00   28.96  ? 201 ILE D O   1 
ATOM   10490 C CB  . ILE D  1 201 ? 131.227 -0.391  12.688  1.00   28.80  ? 201 ILE D CB  1 
ATOM   10491 C CG1 . ILE D  1 201 ? 130.063 -0.156  13.630  1.00   32.73  ? 201 ILE D CG1 1 
ATOM   10492 C CG2 . ILE D  1 201 ? 130.892 0.104   11.288  1.00   25.61  ? 201 ILE D CG2 1 
ATOM   10493 C CD1 . ILE D  1 201 ? 129.649 1.210   13.664  1.00   34.47  ? 201 ILE D CD1 1 
ATOM   10494 N N   . LEU D  1 202 ? 132.743 -2.595  10.730  1.00   29.00  ? 202 LEU D N   1 
ATOM   10495 C CA  . LEU D  1 202 ? 133.925 -2.915  9.957   1.00   29.73  ? 202 LEU D CA  1 
ATOM   10496 C C   . LEU D  1 202 ? 133.959 -1.997  8.748   1.00   30.72  ? 202 LEU D C   1 
ATOM   10497 O O   . LEU D  1 202 ? 132.949 -1.865  8.048   1.00   31.07  ? 202 LEU D O   1 
ATOM   10498 C CB  . LEU D  1 202 ? 133.908 -4.374  9.506   1.00   29.24  ? 202 LEU D CB  1 
ATOM   10499 C CG  . LEU D  1 202 ? 134.371 -5.430  10.490  1.00   30.44  ? 202 LEU D CG  1 
ATOM   10500 C CD1 . LEU D  1 202 ? 133.386 -5.524  11.592  1.00   29.46  ? 202 LEU D CD1 1 
ATOM   10501 C CD2 . LEU D  1 202 ? 134.526 -6.760  9.808   1.00   32.70  ? 202 LEU D CD2 1 
ATOM   10502 N N   . PHE D  1 203 ? 135.117 -1.403  8.472   1.00   30.24  ? 203 PHE D N   1 
ATOM   10503 C CA  . PHE D  1 203 ? 135.246 -0.447  7.372   1.00   31.87  ? 203 PHE D CA  1 
ATOM   10504 C C   . PHE D  1 203 ? 136.155 -1.039  6.301   1.00   32.29  ? 203 PHE D C   1 
ATOM   10505 O O   . PHE D  1 203 ? 137.299 -1.398  6.570   1.00   32.59  ? 203 PHE D O   1 
ATOM   10506 C CB  . PHE D  1 203 ? 135.824 0.894   7.849   1.00   30.46  ? 203 PHE D CB  1 
ATOM   10507 C CG  . PHE D  1 203 ? 135.053 1.530   8.974   1.00   32.73  ? 203 PHE D CG  1 
ATOM   10508 C CD1 . PHE D  1 203 ? 135.318 1.181   10.295  1.00   31.66  ? 203 PHE D CD1 1 
ATOM   10509 C CD2 . PHE D  1 203 ? 134.072 2.480   8.714   1.00   32.00  ? 203 PHE D CD2 1 
ATOM   10510 C CE1 . PHE D  1 203 ? 134.619 1.752   11.332  1.00   31.14  ? 203 PHE D CE1 1 
ATOM   10511 C CE2 . PHE D  1 203 ? 133.365 3.053   9.750   1.00   33.02  ? 203 PHE D CE2 1 
ATOM   10512 C CZ  . PHE D  1 203 ? 133.649 2.685   11.067  1.00   32.34  ? 203 PHE D CZ  1 
ATOM   10513 N N   . GLY D  1 204 ? 135.643 -1.154  5.084   1.00   29.42  ? 204 GLY D N   1 
ATOM   10514 C CA  . GLY D  1 204 ? 136.428 -1.758  4.039   1.00   29.03  ? 204 GLY D CA  1 
ATOM   10515 C C   . GLY D  1 204 ? 135.775 -2.989  3.478   1.00   30.67  ? 204 GLY D C   1 
ATOM   10516 O O   . GLY D  1 204 ? 134.690 -3.392  3.891   1.00   33.33  ? 204 GLY D O   1 
ATOM   10517 N N   . ASP D  1 205 ? 136.481 -3.611  2.549   1.00   32.90  ? 205 ASP D N   1 
ATOM   10518 C CA  . ASP D  1 205 ? 135.982 -4.742  1.784   1.00   35.08  ? 205 ASP D CA  1 
ATOM   10519 C C   . ASP D  1 205 ? 135.904 -6.063  2.567   1.00   37.47  ? 205 ASP D C   1 
ATOM   10520 O O   . ASP D  1 205 ? 136.871 -6.478  3.206   1.00   37.30  ? 205 ASP D O   1 
ATOM   10521 C CB  . ASP D  1 205 ? 136.872 -4.935  0.550   1.00   37.39  ? 205 ASP D CB  1 
ATOM   10522 C CG  . ASP D  1 205 ? 136.323 -5.965  -0.396  1.00   44.39  ? 205 ASP D CG  1 
ATOM   10523 O OD1 . ASP D  1 205 ? 135.163 -6.360  -0.208  1.00   52.83  1 205 ASP D OD1 1 
ATOM   10524 O OD2 . ASP D  1 205 ? 137.024 -6.379  -1.320  1.00   43.17  ? 205 ASP D OD2 1 
ATOM   10525 N N   . ILE D  1 206 ? 134.730 -6.680  2.602   1.00   38.96  ? 206 ILE D N   1 
ATOM   10526 C CA  . ILE D  1 206 ? 134.622 -8.005  3.208   1.00   42.08  ? 206 ILE D CA  1 
ATOM   10527 C C   . ILE D  1 206 ? 134.219 -8.987  2.126   1.00   43.77  ? 206 ILE D C   1 
ATOM   10528 O O   . ILE D  1 206 ? 133.489 -9.932  2.367   1.00   43.76  ? 206 ILE D O   1 
ATOM   10529 C CB  . ILE D  1 206 ? 133.598 -8.076  4.339   1.00   45.04  ? 206 ILE D CB  1 
ATOM   10530 C CG1 . ILE D  1 206 ? 132.207 -7.631  3.891   1.00   40.71  ? 206 ILE D CG1 1 
ATOM   10531 C CG2 . ILE D  1 206 ? 134.067 -7.269  5.526   1.00   48.44  ? 206 ILE D CG2 1 
ATOM   10532 C CD1 . ILE D  1 206 ? 131.225 -7.800  4.982   1.00   39.28  ? 206 ILE D CD1 1 
ATOM   10533 N N   . ASN D  1 207 ? 134.685 -8.754  0.915   1.00   47.35  ? 207 ASN D N   1 
ATOM   10534 C CA  . ASN D  1 207 ? 134.212 -9.547  -0.194  1.00   48.64  ? 207 ASN D CA  1 
ATOM   10535 C C   . ASN D  1 207 ? 135.213 -10.501 -0.751  1.00   51.08  ? 207 ASN D C   1 
ATOM   10536 O O   . ASN D  1 207 ? 134.919 -11.125 -1.759  1.00   52.17  ? 207 ASN D O   1 
ATOM   10537 C CB  . ASN D  1 207 ? 133.768 -8.630  -1.345  1.00   50.28  ? 207 ASN D CB  1 
ATOM   10538 C CG  . ASN D  1 207 ? 132.657 -7.663  -0.949  1.00   48.22  ? 207 ASN D CG  1 
ATOM   10539 O OD1 . ASN D  1 207 ? 132.865 -6.768  -0.123  1.00   45.54  ? 207 ASN D OD1 1 
ATOM   10540 N ND2 . ASN D  1 207 ? 131.474 -7.821  -1.570  1.00   47.05  ? 207 ASN D ND2 1 
ATOM   10541 N N   . ASP D  1 208 ? 136.403 -10.635 -0.171  1.00   54.15  ? 208 ASP D N   1 
ATOM   10542 C CA  . ASP D  1 208 ? 137.304 -11.590 -0.818  1.00   57.54  ? 208 ASP D CA  1 
ATOM   10543 C C   . ASP D  1 208 ? 138.018 -12.467 0.206   1.00   55.45  ? 208 ASP D C   1 
ATOM   10544 O O   . ASP D  1 208 ? 139.112 -12.141 0.662   1.00   51.65  ? 208 ASP D O   1 
ATOM   10545 C CB  . ASP D  1 208 ? 138.315 -10.840 -1.704  1.00   59.40  ? 208 ASP D CB  1 
ATOM   10546 C CG  . ASP D  1 208 ? 139.155 -11.773 -2.579  1.00   61.05  ? 208 ASP D CG  1 
ATOM   10547 O OD1 . ASP D  1 208 ? 138.974 -13.016 -2.549  1.00   59.61  ? 208 ASP D OD1 1 
ATOM   10548 O OD2 . ASP D  1 208 ? 139.976 -11.238 -3.350  1.00   63.42  1 208 ASP D OD2 1 
ATOM   10549 N N   . PRO D  1 209 ? 137.395 -13.610 0.535   1.00   56.43  ? 209 PRO D N   1 
ATOM   10550 C CA  . PRO D  1 209 ? 137.861 -14.629 1.481   1.00   56.23  ? 209 PRO D CA  1 
ATOM   10551 C C   . PRO D  1 209 ? 139.269 -15.176 1.252   1.00   54.62  ? 209 PRO D C   1 
ATOM   10552 O O   . PRO D  1 209 ? 139.979 -15.406 2.234   1.00   55.27  ? 209 PRO D O   1 
ATOM   10553 C CB  . PRO D  1 209 ? 136.848 -15.750 1.294   1.00   58.42  ? 209 PRO D CB  1 
ATOM   10554 C CG  . PRO D  1 209 ? 136.158 -15.455 0.000   1.00   58.45  ? 209 PRO D CG  1 
ATOM   10555 C CD  . PRO D  1 209 ? 136.115 -13.990 -0.081  1.00   55.99  ? 209 PRO D CD  1 
ATOM   10556 N N   . ASN D  1 210 ? 139.678 -15.333 -0.008  1.00   51.65  ? 210 ASN D N   1 
ATOM   10557 C CA  . ASN D  1 210 ? 141.009 -15.852 -0.324  1.00   50.98  ? 210 ASN D CA  1 
ATOM   10558 C C   . ASN D  1 210 ? 142.095 -14.933 0.124   1.00   47.98  ? 210 ASN D C   1 
ATOM   10559 O O   . ASN D  1 210 ? 143.157 -15.352 0.527   1.00   49.91  ? 210 ASN D O   1 
ATOM   10560 C CB  . ASN D  1 210 ? 141.156 -16.043 -1.824  1.00   53.95  ? 210 ASN D CB  1 
ATOM   10561 C CG  . ASN D  1 210 ? 140.320 -17.164 -2.343  1.00   59.15  ? 210 ASN D CG  1 
ATOM   10562 O OD1 . ASN D  1 210 ? 140.095 -18.164 -1.648  1.00   63.13  ? 210 ASN D OD1 1 
ATOM   10563 N ND2 . ASN D  1 210 ? 139.797 -16.993 -3.552  1.00   58.25  ? 210 ASN D ND2 1 
ATOM   10564 N N   . ASN D  1 211 ? 141.802 -13.655 0.047   1.00   47.33  ? 211 ASN D N   1 
ATOM   10565 C CA  . ASN D  1 211 ? 142.737 -12.622 0.421   1.00   48.00  ? 211 ASN D CA  1 
ATOM   10566 C C   . ASN D  1 211 ? 142.364 -11.925 1.733   1.00   43.42  ? 211 ASN D C   1 
ATOM   10567 O O   . ASN D  1 211 ? 142.822 -10.821 2.012   1.00   42.46  ? 211 ASN D O   1 
ATOM   10568 C CB  . ASN D  1 211 ? 142.898 -11.678 -0.768  1.00   51.19  ? 211 ASN D CB  1 
ATOM   10569 C CG  . ASN D  1 211 ? 143.481 -12.407 -1.994  1.00   56.49  ? 211 ASN D CG  1 
ATOM   10570 O OD1 . ASN D  1 211 ? 144.415 -13.202 -1.864  1.00   58.46  ? 211 ASN D OD1 1 
ATOM   10571 N ND2 . ASN D  1 211 ? 142.872 -12.209 -3.159  1.00   57.26  ? 211 ASN D ND2 1 
ATOM   10572 N N   . ASN D  1 212 ? 141.510 -12.563 2.528   1.00   44.02  ? 212 ASN D N   1 
ATOM   10573 C CA  . ASN D  1 212 ? 141.014 -11.954 3.759   1.00   44.15  ? 212 ASN D CA  1 
ATOM   10574 C C   . ASN D  1 212 ? 140.710 -12.975 4.882   1.00   43.93  ? 212 ASN D C   1 
ATOM   10575 O O   . ASN D  1 212 ? 139.624 -13.541 4.930   1.00   44.04  ? 212 ASN D O   1 
ATOM   10576 C CB  . ASN D  1 212 ? 139.755 -11.142 3.429   1.00   46.10  ? 212 ASN D CB  1 
ATOM   10577 C CG  . ASN D  1 212 ? 139.381 -10.110 4.511   1.00   46.52  ? 212 ASN D CG  1 
ATOM   10578 O OD1 . ASN D  1 212 ? 139.724 -10.264 5.683   1.00   47.11  ? 212 ASN D OD1 1 
ATOM   10579 N ND2 . ASN D  1 212 ? 138.646 -9.063  4.108   1.00   43.64  ? 212 ASN D ND2 1 
ATOM   10580 N N   . ASN D  1 213 ? 141.677 -13.212 5.767   1.00   42.75  ? 213 ASN D N   1 
ATOM   10581 C CA  . ASN D  1 213 ? 141.538 -14.168 6.878   1.00   42.22  ? 213 ASN D CA  1 
ATOM   10582 C C   . ASN D  1 213 ? 140.680 -13.677 8.034   1.00   40.06  ? 213 ASN D C   1 
ATOM   10583 O O   . ASN D  1 213 ? 140.193 -14.476 8.828   1.00   40.60  ? 213 ASN D O   1 
ATOM   10584 C CB  . ASN D  1 213 ? 142.898 -14.617 7.423   1.00   39.59  ? 213 ASN D CB  1 
ATOM   10585 C CG  . ASN D  1 213 ? 143.575 -15.631 6.523   1.00   44.55  ? 213 ASN D CG  1 
ATOM   10586 O OD1 . ASN D  1 213 ? 142.914 -16.497 5.951   1.00   45.40  ? 213 ASN D OD1 1 
ATOM   10587 N ND2 . ASN D  1 213 ? 144.898 -15.574 6.446   1.00   44.86  ? 213 ASN D ND2 1 
ATOM   10588 N N   . TYR D  1 214 ? 140.529 -12.366 8.163   1.00   38.03  ? 214 TYR D N   1 
ATOM   10589 C CA  . TYR D  1 214 ? 139.754 -11.820 9.268   1.00   38.88  ? 214 TYR D CA  1 
ATOM   10590 C C   . TYR D  1 214 ? 138.283 -12.223 9.129   1.00   40.25  ? 214 TYR D C   1 
ATOM   10591 O O   . TYR D  1 214 ? 137.595 -12.436 10.129  1.00   38.88  ? 214 TYR D O   1 
ATOM   10592 C CB  . TYR D  1 214 ? 139.891 -10.285 9.349   1.00   36.09  ? 214 TYR D CB  1 
ATOM   10593 C CG  . TYR D  1 214 ? 139.281 -9.737  10.611  1.00   34.71  ? 214 TYR D CG  1 
ATOM   10594 C CD1 . TYR D  1 214 ? 139.948 -9.840  11.820  1.00   34.41  ? 214 TYR D CD1 1 
ATOM   10595 C CD2 . TYR D  1 214 ? 138.020 -9.160  10.608  1.00   34.96  ? 214 TYR D CD2 1 
ATOM   10596 C CE1 . TYR D  1 214 ? 139.380 -9.379  13.003  1.00   33.93  ? 214 TYR D CE1 1 
ATOM   10597 C CE2 . TYR D  1 214 ? 137.446 -8.689  11.780  1.00   34.15  ? 214 TYR D CE2 1 
ATOM   10598 C CZ  . TYR D  1 214 ? 138.136 -8.805  12.970  1.00   33.87  ? 214 TYR D CZ  1 
ATOM   10599 O OH  . TYR D  1 214 ? 137.582 -8.348  14.129  1.00   34.93  ? 214 TYR D OH  1 
ATOM   10600 N N   . ILE D  1 215 ? 137.806 -12.345 7.893   1.00   41.38  ? 215 ILE D N   1 
ATOM   10601 C CA  . ILE D  1 215 ? 136.398 -12.640 7.664   1.00   43.50  ? 215 ILE D CA  1 
ATOM   10602 C C   . ILE D  1 215 ? 136.178 -14.139 7.440   1.00   46.62  ? 215 ILE D C   1 
ATOM   10603 O O   . ILE D  1 215 ? 135.089 -14.566 7.057   1.00   45.57  ? 215 ILE D O   1 
ATOM   10604 C CB  . ILE D  1 215 ? 135.802 -11.852 6.433   1.00   39.24  ? 215 ILE D CB  1 
ATOM   10605 C CG1 . ILE D  1 215 ? 136.408 -12.319 5.096   1.00   41.56  ? 215 ILE D CG1 1 
ATOM   10606 C CG2 . ILE D  1 215 ? 135.865 -10.332 6.650   1.00   34.01  ? 215 ILE D CG2 1 
ATOM   10607 C CD1 . ILE D  1 215 ? 135.971 -11.481 3.895   1.00   42.12  ? 215 ILE D CD1 1 
ATOM   10608 N N   . HIS D  1 216 ? 137.218 -14.936 7.632   1.00   49.39  ? 216 HIS D N   1 
ATOM   10609 C CA  . HIS D  1 216 ? 137.103 -16.365 7.340   1.00   52.76  ? 216 HIS D CA  1 
ATOM   10610 C C   . HIS D  1 216 ? 136.042 -17.099 8.187   1.00   48.80  ? 216 HIS D C   1 
ATOM   10611 O O   . HIS D  1 216 ? 135.338 -17.954 7.682   1.00   43.60  ? 216 HIS D O   1 
ATOM   10612 C CB  . HIS D  1 216 ? 138.457 -17.042 7.477   1.00   58.07  ? 216 HIS D CB  1 
ATOM   10613 C CG  . HIS D  1 216 ? 138.454 -18.449 6.985   1.00   63.02  ? 216 HIS D CG  1 
ATOM   10614 N ND1 . HIS D  1 216 ? 138.611 -18.758 5.651   1.00   64.91  ? 216 HIS D ND1 1 
ATOM   10615 C CD2 . HIS D  1 216 ? 138.305 -19.628 7.634   1.00   65.54  ? 216 HIS D CD2 1 
ATOM   10616 C CE1 . HIS D  1 216 ? 138.554 -20.070 5.498   1.00   67.60  ? 216 HIS D CE1 1 
ATOM   10617 N NE2 . HIS D  1 216 ? 138.373 -20.621 6.686   1.00   67.66  ? 216 HIS D NE2 1 
ATOM   10618 N N   . ASN D  1 217 ? 135.922 -16.764 9.466   1.00   48.45  ? 217 ASN D N   1 
ATOM   10619 C CA  . ASN D  1 217 ? 134.922 -17.393 10.320  1.00   50.08  ? 217 ASN D CA  1 
ATOM   10620 C C   . ASN D  1 217 ? 133.476 -17.006 9.951   1.00   50.15  ? 217 ASN D C   1 
ATOM   10621 O O   . ASN D  1 217 ? 132.514 -17.606 10.423  1.00   52.52  ? 217 ASN D O   1 
ATOM   10622 C CB  . ASN D  1 217 ? 135.209 -17.057 11.783  1.00   54.81  ? 217 ASN D CB  1 
ATOM   10623 C CG  . ASN D  1 217 ? 134.221 -17.714 12.742  1.00   64.17  ? 217 ASN D CG  1 
ATOM   10624 O OD1 . ASN D  1 217 ? 134.153 -18.948 12.856  1.00   67.25  ? 217 ASN D OD1 1 
ATOM   10625 N ND2 . ASN D  1 217 ? 133.464 -16.886 13.461  1.00   66.42  ? 217 ASN D ND2 1 
ATOM   10626 N N   . SER D  1 218 ? 133.317 -16.005 9.101   1.00   46.40  ? 218 SER D N   1 
ATOM   10627 C CA  . SER D  1 218 ? 131.994 -15.546 8.742   1.00   42.72  ? 218 SER D CA  1 
ATOM   10628 C C   . SER D  1 218 ? 131.545 -16.026 7.375   1.00   41.14  ? 218 SER D C   1 
ATOM   10629 O O   . SER D  1 218 ? 130.491 -15.644 6.902   1.00   42.47  ? 218 SER D O   1 
ATOM   10630 C CB  . SER D  1 218 ? 131.946 -14.016 8.809   1.00   41.26  ? 218 SER D CB  1 
ATOM   10631 O OG  . SER D  1 218 ? 132.572 -13.424 7.686   1.00   39.40  ? 218 SER D OG  1 
ATOM   10632 N N   . LEU D  1 219 ? 132.315 -16.897 6.753   1.00   38.03  ? 219 LEU D N   1 
ATOM   10633 C CA  . LEU D  1 219 ? 132.074 -17.212 5.355   1.00   41.12  ? 219 LEU D CA  1 
ATOM   10634 C C   . LEU D  1 219 ? 130.738 -17.854 4.997   1.00   41.83  ? 219 LEU D C   1 
ATOM   10635 O O   . LEU D  1 219 ? 130.191 -17.541 3.953   1.00   42.80  ? 219 LEU D O   1 
ATOM   10636 C CB  . LEU D  1 219 ? 133.170 -18.145 4.852   1.00   44.29  ? 219 LEU D CB  1 
ATOM   10637 C CG  . LEU D  1 219 ? 134.449 -17.406 4.550   1.00   43.62  ? 219 LEU D CG  1 
ATOM   10638 C CD1 . LEU D  1 219 ? 135.527 -18.370 4.127   1.00   46.52  ? 219 LEU D CD1 1 
ATOM   10639 C CD2 . LEU D  1 219 ? 134.119 -16.432 3.476   1.00   44.52  ? 219 LEU D CD2 1 
ATOM   10640 N N   . ASP D  1 220 ? 130.192 -18.719 5.842   1.00   44.37  ? 220 ASP D N   1 
ATOM   10641 C CA  . ASP D  1 220 ? 128.928 -19.362 5.487   1.00   47.78  ? 220 ASP D CA  1 
ATOM   10642 C C   . ASP D  1 220 ? 127.812 -18.332 5.479   1.00   42.71  ? 220 ASP D C   1 
ATOM   10643 O O   . ASP D  1 220 ? 126.887 -18.409 4.677   1.00   43.66  ? 220 ASP D O   1 
ATOM   10644 C CB  . ASP D  1 220 ? 128.605 -20.532 6.422   1.00   55.25  ? 220 ASP D CB  1 
ATOM   10645 C CG  . ASP D  1 220 ? 129.017 -20.281 7.857   1.00   59.10  ? 220 ASP D CG  1 
ATOM   10646 O OD1 . ASP D  1 220 ? 129.452 -19.152 8.177   1.00   58.35  ? 220 ASP D OD1 1 
ATOM   10647 O OD2 . ASP D  1 220 ? 128.914 -21.233 8.666   1.00   61.70  ? 220 ASP D OD2 1 
ATOM   10648 N N   . VAL D  1 221 ? 127.910 -17.373 6.386   1.00   40.34  ? 221 VAL D N   1 
ATOM   10649 C CA  . VAL D  1 221 ? 126.979 -16.254 6.463   1.00   41.34  ? 221 VAL D CA  1 
ATOM   10650 C C   . VAL D  1 221 ? 126.973 -15.350 5.217   1.00   41.70  ? 221 VAL D C   1 
ATOM   10651 O O   . VAL D  1 221 ? 125.914 -15.000 4.674   1.00   42.18  ? 221 VAL D O   1 
ATOM   10652 C CB  . VAL D  1 221 ? 127.332 -15.389 7.666   1.00   35.02  ? 221 VAL D CB  1 
ATOM   10653 C CG1 . VAL D  1 221 ? 126.380 -14.226 7.762   1.00   33.46  ? 221 VAL D CG1 1 
ATOM   10654 C CG2 . VAL D  1 221 ? 127.324 -16.232 8.932   1.00   37.10  ? 221 VAL D CG2 1 
ATOM   10655 N N   . LEU D  1 222 ? 128.182 -14.996 4.782   1.00   39.63  ? 222 LEU D N   1 
ATOM   10656 C CA  . LEU D  1 222 ? 128.437 -14.107 3.654   1.00   37.77  ? 222 LEU D CA  1 
ATOM   10657 C C   . LEU D  1 222 ? 127.947 -14.709 2.366   1.00   39.83  ? 222 LEU D C   1 
ATOM   10658 O O   . LEU D  1 222 ? 127.506 -14.022 1.450   1.00   43.06  ? 222 LEU D O   1 
ATOM   10659 C CB  . LEU D  1 222 ? 129.925 -13.834 3.550   1.00   38.78  ? 222 LEU D CB  1 
ATOM   10660 C CG  . LEU D  1 222 ? 130.567 -13.087 4.707   1.00   39.32  ? 222 LEU D CG  1 
ATOM   10661 C CD1 . LEU D  1 222 ? 132.051 -12.903 4.467   1.00   37.43  ? 222 LEU D CD1 1 
ATOM   10662 C CD2 . LEU D  1 222 ? 129.873 -11.743 4.836   1.00   38.43  ? 222 LEU D CD2 1 
ATOM   10663 N N   . HIS D  1 223 ? 128.070 -16.012 2.295   1.00   39.37  ? 223 HIS D N   1 
ATOM   10664 C CA  . HIS D  1 223 ? 127.642 -16.727 1.133   1.00   46.54  ? 223 HIS D CA  1 
ATOM   10665 C C   . HIS D  1 223 ? 126.150 -16.561 0.903   1.00   45.19  ? 223 HIS D C   1 
ATOM   10666 O O   . HIS D  1 223 ? 125.678 -16.621 -0.225  1.00   45.14  ? 223 HIS D O   1 
ATOM   10667 C CB  . HIS D  1 223 ? 127.970 -18.196 1.279   1.00   55.93  ? 223 HIS D CB  1 
ATOM   10668 C CG  . HIS D  1 223 ? 127.596 -18.987 0.078   1.00   67.35  ? 223 HIS D CG  1 
ATOM   10669 N ND1 . HIS D  1 223 ? 126.533 -19.864 0.067   1.00   73.92  ? 223 HIS D ND1 1 
ATOM   10670 C CD2 . HIS D  1 223 ? 128.135 -19.027 -1.162  1.00   72.30  ? 223 HIS D CD2 1 
ATOM   10671 C CE1 . HIS D  1 223 ? 126.430 -20.408 -1.132  1.00   77.82  ? 223 HIS D CE1 1 
ATOM   10672 N NE2 . HIS D  1 223 ? 127.395 -19.922 -1.894  1.00   77.29  ? 223 HIS D NE2 1 
ATOM   10673 N N   . ASP D  1 224 ? 125.413 -16.378 1.992   1.00   45.06  ? 224 ASP D N   1 
ATOM   10674 C CA  . ASP D  1 224 ? 123.967 -16.341 1.954   1.00   46.91  ? 224 ASP D CA  1 
ATOM   10675 C C   . ASP D  1 224 ? 123.390 -14.932 2.073   1.00   45.08  ? 224 ASP D C   1 
ATOM   10676 O O   . ASP D  1 224 ? 122.193 -14.758 2.292   1.00   42.95  ? 224 ASP D O   1 
ATOM   10677 C CB  . ASP D  1 224 ? 123.423 -17.238 3.059   1.00   51.10  ? 224 ASP D CB  1 
ATOM   10678 C CG  . ASP D  1 224 ? 123.752 -18.709 2.833   1.00   54.28  ? 224 ASP D CG  1 
ATOM   10679 O OD1 . ASP D  1 224 ? 123.926 -19.136 1.669   1.00   54.39  ? 224 ASP D OD1 1 
ATOM   10680 O OD2 . ASP D  1 224 ? 123.874 -19.439 3.830   1.00   55.57  1 224 ASP D OD2 1 
ATOM   10681 N N   . LEU D  1 225 ? 124.241 -13.922 1.949   1.00   42.51  ? 225 LEU D N   1 
ATOM   10682 C CA  . LEU D  1 225 ? 123.773 -12.552 2.009   1.00   38.56  ? 225 LEU D CA  1 
ATOM   10683 C C   . LEU D  1 225 ? 122.785 -12.298 0.905   1.00   36.29  ? 225 LEU D C   1 
ATOM   10684 O O   . LEU D  1 225 ? 122.946 -12.789 -0.208  1.00   36.85  ? 225 LEU D O   1 
ATOM   10685 C CB  . LEU D  1 225 ? 124.910 -11.542 1.875   1.00   36.87  ? 225 LEU D CB  1 
ATOM   10686 C CG  . LEU D  1 225 ? 125.863 -11.277 3.036   1.00   34.03  ? 225 LEU D CG  1 
ATOM   10687 C CD1 . LEU D  1 225 ? 126.648 -10.065 2.712   1.00   34.97  ? 225 LEU D CD1 1 
ATOM   10688 C CD2 . LEU D  1 225 ? 125.173 -11.063 4.334   1.00   30.82  ? 225 LEU D CD2 1 
ATOM   10689 N N   . VAL D  1 226 ? 121.763 -11.522 1.237   1.00   36.30  ? 226 VAL D N   1 
ATOM   10690 C CA  . VAL D  1 226 ? 120.775 -11.054 0.279   1.00   35.95  ? 226 VAL D CA  1 
ATOM   10691 C C   . VAL D  1 226 ? 120.881 -9.518  0.193   1.00   35.32  ? 226 VAL D C   1 
ATOM   10692 O O   . VAL D  1 226 ? 121.104 -8.868  1.203   1.00   35.57  ? 226 VAL D O   1 
ATOM   10693 C CB  . VAL D  1 226 ? 119.357 -11.533 0.703   1.00   44.86  ? 226 VAL D CB  1 
ATOM   10694 C CG1 . VAL D  1 226 ? 118.249 -10.703 0.079   1.00   47.01  ? 226 VAL D CG1 1 
ATOM   10695 C CG2 . VAL D  1 226 ? 119.183 -12.986 0.377   1.00   44.36  ? 226 VAL D CG2 1 
ATOM   10696 N N   . TYR D  1 227 ? 120.759 -8.947  -1.008  1.00   36.33  ? 227 TYR D N   1 
ATOM   10697 C CA  . TYR D  1 227 ? 120.919 -7.498  -1.241  1.00   33.35  ? 227 TYR D CA  1 
ATOM   10698 C C   . TYR D  1 227 ? 119.652 -6.786  -1.726  1.00   33.76  ? 227 TYR D C   1 
ATOM   10699 O O   . TYR D  1 227 ? 118.809 -7.396  -2.372  1.00   37.71  ? 227 TYR D O   1 
ATOM   10700 C CB  . TYR D  1 227 ? 122.049 -7.241  -2.259  1.00   35.43  ? 227 TYR D CB  1 
ATOM   10701 C CG  . TYR D  1 227 ? 123.406 -7.537  -1.694  1.00   39.83  ? 227 TYR D CG  1 
ATOM   10702 C CD1 . TYR D  1 227 ? 124.120 -6.534  -1.047  1.00   42.28  ? 227 TYR D CD1 1 
ATOM   10703 C CD2 . TYR D  1 227 ? 123.952 -8.813  -1.745  1.00   40.36  ? 227 TYR D CD2 1 
ATOM   10704 C CE1 . TYR D  1 227 ? 125.344 -6.778  -0.493  1.00   43.07  ? 227 TYR D CE1 1 
ATOM   10705 C CE2 . TYR D  1 227 ? 125.187 -9.070  -1.184  1.00   41.92  ? 227 TYR D CE2 1 
ATOM   10706 C CZ  . TYR D  1 227 ? 125.872 -8.047  -0.554  1.00   44.21  ? 227 TYR D CZ  1 
ATOM   10707 O OH  . TYR D  1 227 ? 127.106 -8.270  0.009   1.00   48.29  ? 227 TYR D OH  1 
ATOM   10708 N N   . THR D  1 228 ? 119.528 -5.498  -1.409  1.00   31.87  ? 228 THR D N   1 
ATOM   10709 C CA  . THR D  1 228 ? 118.416 -4.657  -1.880  1.00   32.61  ? 228 THR D CA  1 
ATOM   10710 C C   . THR D  1 228 ? 118.912 -3.203  -2.107  1.00   32.49  ? 228 THR D C   1 
ATOM   10711 O O   . THR D  1 228 ? 119.862 -2.784  -1.439  1.00   31.68  ? 228 THR D O   1 
ATOM   10712 C CB  . THR D  1 228 ? 117.209 -4.719  -0.869  1.00   39.69  ? 228 THR D CB  1 
ATOM   10713 O OG1 . THR D  1 228 ? 116.024 -4.138  -1.438  1.00   37.17  ? 228 THR D OG1 1 
ATOM   10714 C CG2 . THR D  1 228 ? 117.537 -4.025  0.433   1.00   40.48  ? 228 THR D CG2 1 
ATOM   10715 N N   . PRO D  1 229 ? 118.295 -2.434  -3.053  1.00   32.55  ? 229 PRO D N   1 
ATOM   10716 C CA  . PRO D  1 229 ? 118.876 -1.115  -3.341  1.00   30.15  ? 229 PRO D CA  1 
ATOM   10717 C C   . PRO D  1 229 ? 118.810 -0.156  -2.188  1.00   29.46  ? 229 PRO D C   1 
ATOM   10718 O O   . PRO D  1 229 ? 117.844 -0.122  -1.431  1.00   32.00  ? 229 PRO D O   1 
ATOM   10719 C CB  . PRO D  1 229 ? 118.044 -0.605  -4.519  1.00   30.95  ? 229 PRO D CB  1 
ATOM   10720 C CG  . PRO D  1 229 ? 117.529 -1.818  -5.171  1.00   32.29  ? 229 PRO D CG  1 
ATOM   10721 C CD  . PRO D  1 229 ? 117.227 -2.755  -4.015  1.00   33.27  ? 229 PRO D CD  1 
ATOM   10722 N N   . LEU D  1 230 ? 119.866 0.624   -2.071  1.00   28.11  ? 230 LEU D N   1 
ATOM   10723 C CA  . LEU D  1 230 ? 119.980 1.628   -1.033  1.00   28.23  ? 230 LEU D CA  1 
ATOM   10724 C C   . LEU D  1 230 ? 119.756 2.992   -1.625  1.00   28.76  ? 230 LEU D C   1 
ATOM   10725 O O   . LEU D  1 230 ? 120.331 3.320   -2.665  1.00   31.64  ? 230 LEU D O   1 
ATOM   10726 C CB  . LEU D  1 230 ? 121.347 1.553   -0.381  1.00   25.53  ? 230 LEU D CB  1 
ATOM   10727 C CG  . LEU D  1 230 ? 121.722 2.575   0.665   1.00   23.92  ? 230 LEU D CG  1 
ATOM   10728 C CD1 . LEU D  1 230 ? 120.790 2.452   1.820   1.00   22.85  ? 230 LEU D CD1 1 
ATOM   10729 C CD2 . LEU D  1 230 ? 123.166 2.251   1.083   1.00   24.63  ? 230 LEU D CD2 1 
ATOM   10730 N N   . THR D  1 231 ? 118.887 3.772   -0.986  1.00   31.72  ? 231 THR D N   1 
ATOM   10731 C CA  . THR D  1 231 ? 118.665 5.160   -1.392  1.00   31.51  ? 231 THR D CA  1 
ATOM   10732 C C   . THR D  1 231 ? 118.962 6.122   -0.229  1.00   30.29  ? 231 THR D C   1 
ATOM   10733 O O   . THR D  1 231 ? 118.870 5.748   0.948   1.00   28.98  ? 231 THR D O   1 
ATOM   10734 C CB  . THR D  1 231 ? 117.210 5.381   -1.918  1.00   29.16  ? 231 THR D CB  1 
ATOM   10735 O OG1 . THR D  1 231 ? 116.260 4.789   -1.016  1.00   31.60  ? 231 THR D OG1 1 
ATOM   10736 C CG2 . THR D  1 231 ? 117.042 4.790   -3.323  1.00   28.10  ? 231 THR D CG2 1 
ATOM   10737 N N   . ILE D  1 232 ? 119.328 7.357   -0.582  1.00   35.04  ? 232 ILE D N   1 
ATOM   10738 C CA  . ILE D  1 232 ? 119.813 8.365   0.379   1.00   36.40  ? 232 ILE D CA  1 
ATOM   10739 C C   . ILE D  1 232 ? 118.955 9.665   0.341   1.00   33.18  ? 232 ILE D C   1 
ATOM   10740 O O   . ILE D  1 232 ? 118.728 10.240  -0.724  1.00   34.40  ? 232 ILE D O   1 
ATOM   10741 C CB  . ILE D  1 232 ? 121.306 8.746   0.098   1.00   28.34  ? 232 ILE D CB  1 
ATOM   10742 C CG1 . ILE D  1 232 ? 122.228 7.514   -0.054  1.00   26.94  ? 232 ILE D CG1 1 
ATOM   10743 C CG2 . ILE D  1 232 ? 121.828 9.697   1.160   1.00   28.06  ? 232 ILE D CG2 1 
ATOM   10744 C CD1 . ILE D  1 232 ? 122.383 6.648   1.190   1.00   24.81  ? 232 ILE D CD1 1 
ATOM   10745 N N   . SER D  1 233 ? 118.487 10.125  1.502   1.00   34.80  ? 233 SER D N   1 
ATOM   10746 C CA  . SER D  1 233 ? 117.680 11.347  1.580   1.00   39.00  ? 233 SER D CA  1 
ATOM   10747 C C   . SER D  1 233 ? 118.548 12.614  1.461   1.00   43.30  ? 233 SER D C   1 
ATOM   10748 O O   . SER D  1 233 ? 119.778 12.535  1.499   1.00   41.91  ? 233 SER D O   1 
ATOM   10749 C CB  . SER D  1 233 ? 116.873 11.368  2.874   1.00   38.35  ? 233 SER D CB  1 
ATOM   10750 O OG  . SER D  1 233 ? 117.709 11.593  3.990   1.00   37.72  ? 233 SER D OG  1 
ATOM   10751 N N   . LYS D  1 234 ? 117.919 13.782  1.336   1.00   45.97  ? 234 LYS D N   1 
ATOM   10752 C CA  . LYS D  1 234 ? 118.693 15.004  1.179   1.00   47.00  ? 234 LYS D CA  1 
ATOM   10753 C C   . LYS D  1 234 ? 119.529 15.285  2.389   1.00   44.13  ? 234 LYS D C   1 
ATOM   10754 O O   . LYS D  1 234 ? 120.518 16.009  2.322   1.00   42.35  ? 234 LYS D O   1 
ATOM   10755 C CB  . LYS D  1 234 ? 117.793 16.220  0.920   1.00   50.29  ? 234 LYS D CB  1 
ATOM   10756 C CG  . LYS D  1 234 ? 117.272 16.337  -0.493  1.00   55.79  ? 234 LYS D CG  1 
ATOM   10757 C CD  . LYS D  1 234 ? 116.339 17.520  -0.647  1.00   61.86  ? 234 LYS D CD  1 
ATOM   10758 C CE  . LYS D  1 234 ? 115.223 17.254  -1.658  1.00   66.19  ? 234 LYS D CE  1 
ATOM   10759 N NZ  . LYS D  1 234 ? 114.068 18.205  -1.524  1.00   68.97  ? 234 LYS D NZ  1 
ATOM   10760 N N   . GLN D  1 235 ? 119.168 14.667  3.497   1.00   43.98  ? 235 GLN D N   1 
ATOM   10761 C CA  . GLN D  1 235 ? 119.906 14.930  4.709   1.00   44.69  ? 235 GLN D CA  1 
ATOM   10762 C C   . GLN D  1 235 ? 120.910 13.832  5.000   1.00   41.55  ? 235 GLN D C   1 
ATOM   10763 O O   . GLN D  1 235 ? 121.509 13.801  6.072   1.00   41.25  ? 235 GLN D O   1 
ATOM   10764 C CB  . GLN D  1 235 ? 118.948 15.159  5.873   1.00   49.06  ? 235 GLN D CB  1 
ATOM   10765 C CG  . GLN D  1 235 ? 118.199 16.490  5.701   1.00   53.71  ? 235 GLN D CG  1 
ATOM   10766 C CD  . GLN D  1 235 ? 119.130 17.725  5.605   1.00   73.48  ? 235 GLN D CD  1 
ATOM   10767 O OE1 . GLN D  1 235 ? 120.138 17.830  6.313   1.00   72.43  ? 235 GLN D OE1 1 
ATOM   10768 N NE2 . GLN D  1 235 ? 118.797 18.648  4.696   1.00   73.18  ? 235 GLN D NE2 1 
ATOM   10769 N N   . GLY D  1 236 ? 121.071 12.919  4.046   1.00   37.74  ? 236 GLY D N   1 
ATOM   10770 C CA  . GLY D  1 236 ? 122.111 11.916  4.147   1.00   35.94  ? 236 GLY D CA  1 
ATOM   10771 C C   . GLY D  1 236 ? 121.749 10.647  4.886   1.00   35.67  ? 236 GLY D C   1 
ATOM   10772 O O   . GLY D  1 236 ? 122.654 9.942   5.360   1.00   34.68  ? 236 GLY D O   1 
ATOM   10773 N N   . GLU D  1 237 ? 120.439 10.374  4.992   1.00   35.37  ? 237 GLU D N   1 
ATOM   10774 C CA  . GLU D  1 237 ? 119.897 9.197   5.689   1.00   31.69  ? 237 GLU D CA  1 
ATOM   10775 C C   . GLU D  1 237 ? 119.769 7.962   4.793   1.00   29.89  ? 237 GLU D C   1 
ATOM   10776 O O   . GLU D  1 237 ? 119.489 8.062   3.603   1.00   30.41  ? 237 GLU D O   1 
ATOM   10777 C CB  . GLU D  1 237 ? 118.522 9.516   6.280   1.00   32.55  ? 237 GLU D CB  1 
ATOM   10778 C CG  . GLU D  1 237 ? 118.495 10.726  7.190   1.00   38.29  ? 237 GLU D CG  1 
ATOM   10779 C CD  . GLU D  1 237 ? 117.120 11.401  7.246   1.00   43.25  ? 237 GLU D CD  1 
ATOM   10780 O OE1 . GLU D  1 237 ? 116.640 11.897  6.196   1.00   42.30  ? 237 GLU D OE1 1 
ATOM   10781 O OE2 . GLU D  1 237 ? 116.522 11.423  8.347   1.00   45.43  1 237 GLU D OE2 1 
ATOM   10782 N N   . TYR D  1 238 ? 119.905 6.791   5.412   1.00   30.41  ? 238 TYR D N   1 
ATOM   10783 C CA  . TYR D  1 238 ? 119.859 5.522   4.712   1.00   27.37  ? 238 TYR D CA  1 
ATOM   10784 C C   . TYR D  1 238 ? 118.456 4.957   4.657   1.00   28.53  ? 238 TYR D C   1 
ATOM   10785 O O   . TYR D  1 238 ? 117.816 4.771   5.685   1.00   30.08  ? 238 TYR D O   1 
ATOM   10786 C CB  . TYR D  1 238 ? 120.809 4.515   5.373   1.00   24.79  ? 238 TYR D CB  1 
ATOM   10787 C CG  . TYR D  1 238 ? 122.258 4.937   5.350   1.00   23.71  ? 238 TYR D CG  1 
ATOM   10788 C CD1 . TYR D  1 238 ? 122.997 4.878   4.178   1.00   24.57  ? 238 TYR D CD1 1 
ATOM   10789 C CD2 . TYR D  1 238 ? 122.896 5.367   6.502   1.00   26.67  ? 238 TYR D CD2 1 
ATOM   10790 C CE1 . TYR D  1 238 ? 124.341 5.268   4.145   1.00   26.27  ? 238 TYR D CE1 1 
ATOM   10791 C CE2 . TYR D  1 238 ? 124.242 5.758   6.489   1.00   27.25  ? 238 TYR D CE2 1 
ATOM   10792 C CZ  . TYR D  1 238 ? 124.954 5.703   5.307   1.00   28.25  ? 238 TYR D CZ  1 
ATOM   10793 O OH  . TYR D  1 238 ? 126.268 6.095   5.284   1.00   29.44  ? 238 TYR D OH  1 
ATOM   10794 N N   . PHE D  1 239 ? 118.019 4.674   3.432   1.00   28.48  ? 239 PHE D N   1 
ATOM   10795 C CA  . PHE D  1 239 ? 116.698 4.144   3.146   1.00   29.99  ? 239 PHE D CA  1 
ATOM   10796 C C   . PHE D  1 239 ? 116.733 2.912   2.282   1.00   28.57  ? 239 PHE D C   1 
ATOM   10797 O O   . PHE D  1 239 ? 117.553 2.790   1.380   1.00   30.34  ? 239 PHE D O   1 
ATOM   10798 C CB  . PHE D  1 239 ? 115.846 5.197   2.436   1.00   32.64  ? 239 PHE D CB  1 
ATOM   10799 C CG  . PHE D  1 239 ? 115.289 6.232   3.358   1.00   35.62  ? 239 PHE D CG  1 
ATOM   10800 C CD1 . PHE D  1 239 ? 116.038 7.332   3.709   1.00   34.57  ? 239 PHE D CD1 1 
ATOM   10801 C CD2 . PHE D  1 239 ? 114.021 6.099   3.885   1.00   39.30  ? 239 PHE D CD2 1 
ATOM   10802 C CE1 . PHE D  1 239 ? 115.546 8.272   4.571   1.00   35.92  ? 239 PHE D CE1 1 
ATOM   10803 C CE2 . PHE D  1 239 ? 113.515 7.055   4.751   1.00   42.23  ? 239 PHE D CE2 1 
ATOM   10804 C CZ  . PHE D  1 239 ? 114.280 8.139   5.091   1.00   39.77  ? 239 PHE D CZ  1 
ATOM   10805 N N   . ILE D  1 240 ? 115.800 2.015   2.544   1.00   30.88  ? 240 ILE D N   1 
ATOM   10806 C CA  . ILE D  1 240 ? 115.490 0.928   1.634   1.00   29.97  ? 240 ILE D CA  1 
ATOM   10807 C C   . ILE D  1 240 ? 113.994 0.930   1.325   1.00   32.86  ? 240 ILE D C   1 
ATOM   10808 O O   . ILE D  1 240 ? 113.210 1.614   1.970   1.00   35.45  ? 240 ILE D O   1 
ATOM   10809 C CB  . ILE D  1 240 ? 115.901 -0.439  2.216   1.00   27.97  ? 240 ILE D CB  1 
ATOM   10810 C CG1 . ILE D  1 240 ? 115.294 -0.614  3.610   1.00   27.32  ? 240 ILE D CG1 1 
ATOM   10811 C CG2 . ILE D  1 240 ? 117.400 -0.546  2.298   1.00   26.52  ? 240 ILE D CG2 1 
ATOM   10812 C CD1 . ILE D  1 240 ? 115.426 -1.964  4.179   1.00   26.33  ? 240 ILE D CD1 1 
ATOM   10813 N N   . GLN D  1 241 ? 113.593 0.159   0.336   1.00   34.11  ? 241 GLN D N   1 
ATOM   10814 C CA  . GLN D  1 241 ? 112.198 0.139   -0.026  1.00   36.02  ? 241 GLN D CA  1 
ATOM   10815 C C   . GLN D  1 241 ? 111.532 -1.114  0.513   1.00   37.27  ? 241 GLN D C   1 
ATOM   10816 O O   . GLN D  1 241 ? 111.992 -2.225  0.269   1.00   38.65  ? 241 GLN D O   1 
ATOM   10817 C CB  . GLN D  1 241 ? 112.032 0.229   -1.535  1.00   40.51  ? 241 GLN D CB  1 
ATOM   10818 C CG  . GLN D  1 241 ? 110.593 0.027   -1.990  1.00   45.40  ? 241 GLN D CG  1 
ATOM   10819 C CD  . GLN D  1 241 ? 109.637 1.049   -1.399  1.00   46.53  ? 241 GLN D CD  1 
ATOM   10820 O OE1 . GLN D  1 241 ? 110.036 2.146   -1.026  1.00   48.46  ? 241 GLN D OE1 1 
ATOM   10821 N NE2 . GLN D  1 241 ? 108.370 0.699   -1.333  1.00   46.03  ? 241 GLN D NE2 1 
ATOM   10822 N N   . VAL D  1 242 ? 110.500 -0.933  1.326   1.00   36.40  ? 242 VAL D N   1 
ATOM   10823 C CA  . VAL D  1 242 ? 109.689 -2.048  1.801   1.00   33.69  ? 242 VAL D CA  1 
ATOM   10824 C C   . VAL D  1 242 ? 108.351 -1.999  1.082   1.00   38.56  ? 242 VAL D C   1 
ATOM   10825 O O   . VAL D  1 242 ? 107.591 -1.041  1.255   1.00   41.05  ? 242 VAL D O   1 
ATOM   10826 C CB  . VAL D  1 242 ? 109.496 -2.004  3.323   1.00   29.39  ? 242 VAL D CB  1 
ATOM   10827 C CG1 . VAL D  1 242 ? 108.521 -3.084  3.786   1.00   29.34  ? 242 VAL D CG1 1 
ATOM   10828 C CG2 . VAL D  1 242 ? 110.841 -2.177  3.989   1.00   31.08  ? 242 VAL D CG2 1 
ATOM   10829 N N   . ASN D  1 243 ? 108.082 -2.987  0.230   1.00   35.67  ? 243 ASN D N   1 
ATOM   10830 C CA  . ASN D  1 243 ? 106.826 -2.984  -0.491  1.00   35.19  ? 243 ASN D CA  1 
ATOM   10831 C C   . ASN D  1 243 ? 105.657 -3.423  0.367   1.00   37.18  ? 243 ASN D C   1 
ATOM   10832 O O   . ASN D  1 243 ? 104.529 -2.959  0.168   1.00   38.23  ? 243 ASN D O   1 
ATOM   10833 C CB  . ASN D  1 243 ? 106.907 -3.879  -1.713  1.00   36.89  ? 243 ASN D CB  1 
ATOM   10834 C CG  . ASN D  1 243 ? 107.502 -3.182  -2.904  1.00   41.56  ? 243 ASN D CG  1 
ATOM   10835 O OD1 . ASN D  1 243 ? 107.917 -2.023  -2.829  1.00   41.53  ? 243 ASN D OD1 1 
ATOM   10836 N ND2 . ASN D  1 243 ? 107.513 -3.873  -4.038  1.00   44.83  ? 243 ASN D ND2 1 
ATOM   10837 N N   . ALA D  1 244 ? 105.932 -4.314  1.319   1.00   36.17  ? 244 ALA D N   1 
ATOM   10838 C CA  . ALA D  1 244 ? 104.899 -4.864  2.181   1.00   33.68  ? 244 ALA D CA  1 
ATOM   10839 C C   . ALA D  1 244 ? 105.460 -5.535  3.417   1.00   32.73  ? 244 ALA D C   1 
ATOM   10840 O O   . ALA D  1 244 ? 106.607 -5.936  3.446   1.00   34.03  ? 244 ALA D O   1 
ATOM   10841 C CB  . ALA D  1 244 ? 104.044 -5.854  1.415   1.00   33.81  ? 244 ALA D CB  1 
ATOM   10842 N N   . ILE D  1 245 ? 104.627 -5.635  4.440   1.00   34.36  ? 245 ILE D N   1 
ATOM   10843 C CA  . ILE D  1 245 ? 104.882 -6.485  5.587   1.00   35.32  ? 245 ILE D CA  1 
ATOM   10844 C C   . ILE D  1 245 ? 103.984 -7.702  5.529   1.00   34.53  ? 245 ILE D C   1 
ATOM   10845 O O   . ILE D  1 245 ? 102.782 -7.564  5.387   1.00   36.74  ? 245 ILE D O   1 
ATOM   10846 C CB  . ILE D  1 245 ? 104.627 -5.763  6.907   1.00   33.71  ? 245 ILE D CB  1 
ATOM   10847 C CG1 . ILE D  1 245 ? 105.415 -4.463  6.955   1.00   32.73  ? 245 ILE D CG1 1 
ATOM   10848 C CG2 . ILE D  1 245 ? 105.013 -6.650  8.083   1.00   34.26  ? 245 ILE D CG2 1 
ATOM   10849 C CD1 . ILE D  1 245 ? 104.938 -3.551  8.058   1.00   33.88  ? 245 ILE D CD1 1 
ATOM   10850 N N   . ARG D  1 246 ? 104.584 -8.884  5.558   1.00   34.72  ? 246 ARG D N   1 
ATOM   10851 C CA  . ARG D  1 246 ? 103.867 -10.167 5.561   1.00   39.80  ? 246 ARG D CA  1 
ATOM   10852 C C   . ARG D  1 246 ? 103.774 -10.750 6.979   1.00   38.47  ? 246 ARG D C   1 
ATOM   10853 O O   . ARG D  1 246 ? 104.767 -10.841 7.675   1.00   42.03  ? 246 ARG D O   1 
ATOM   10854 C CB  . ARG D  1 246 ? 104.593 -11.181 4.671   1.00   42.38  ? 246 ARG D CB  1 
ATOM   10855 C CG  . ARG D  1 246 ? 103.970 -12.580 4.575   1.00   44.39  ? 246 ARG D CG  1 
ATOM   10856 C CD  . ARG D  1 246 ? 105.078 -13.625 4.291   1.00   47.67  ? 246 ARG D CD  1 
ATOM   10857 N NE  . ARG D  1 246 ? 105.604 -13.625 2.930   1.00   48.20  ? 246 ARG D NE  1 
ATOM   10858 C CZ  . ARG D  1 246 ? 106.861 -13.931 2.614   1.00   51.58  ? 246 ARG D CZ  1 
ATOM   10859 N NH1 . ARG D  1 246 ? 107.735 -14.234 3.564   1.00   52.33  ? 246 ARG D NH1 1 
ATOM   10860 N NH2 . ARG D  1 246 ? 107.261 -13.914 1.348   1.00   53.70  ? 246 ARG D NH2 1 
ATOM   10861 N N   . VAL D  1 247 ? 102.598 -11.133 7.430   1.00   38.46  ? 247 VAL D N   1 
ATOM   10862 C CA  . VAL D  1 247 ? 102.513 -11.950 8.638   1.00   39.32  ? 247 VAL D CA  1 
ATOM   10863 C C   . VAL D  1 247 ? 101.737 -13.193 8.281   1.00   41.53  ? 247 VAL D C   1 
ATOM   10864 O O   . VAL D  1 247 ? 100.556 -13.115 8.013   1.00   42.54  ? 247 VAL D O   1 
ATOM   10865 C CB  . VAL D  1 247 ? 101.844 -11.232 9.795   1.00   40.96  ? 247 VAL D CB  1 
ATOM   10866 C CG1 . VAL D  1 247 ? 101.814 -12.131 11.019  1.00   41.34  ? 247 VAL D CG1 1 
ATOM   10867 C CG2 . VAL D  1 247 ? 102.562 -9.953  10.080  1.00   40.01  ? 247 VAL D CG2 1 
ATOM   10868 N N   . ASN D  1 248 ? 102.408 -14.331 8.234   1.00   44.28  ? 248 ASN D N   1 
ATOM   10869 C CA  . ASN D  1 248 ? 101.821 -15.545 7.685   1.00   47.82  ? 248 ASN D CA  1 
ATOM   10870 C C   . ASN D  1 248 ? 101.299 -15.281 6.299   1.00   46.47  ? 248 ASN D C   1 
ATOM   10871 O O   . ASN D  1 248 ? 102.088 -14.982 5.408   1.00   45.39  ? 248 ASN D O   1 
ATOM   10872 C CB  . ASN D  1 248 ? 100.724 -16.083 8.582   1.00   52.72  ? 248 ASN D CB  1 
ATOM   10873 C CG  . ASN D  1 248 ? 101.269 -16.662 9.870   1.00   56.90  ? 248 ASN D CG  1 
ATOM   10874 O OD1 . ASN D  1 248 ? 102.446 -16.998 9.958   1.00   60.38  ? 248 ASN D OD1 1 
ATOM   10875 N ND2 . ASN D  1 248 ? 100.414 -16.779 10.881  1.00   56.21  ? 248 ASN D ND2 1 
ATOM   10876 N N   . LYS D  1 249 ? 99.988  -15.328 6.105   1.00   50.58  ? 249 LYS D N   1 
ATOM   10877 C CA  . LYS D  1 249 ? 99.487  -15.053 4.761   1.00   53.36  ? 249 LYS D CA  1 
ATOM   10878 C C   . LYS D  1 249 ? 98.750  -13.719 4.610   1.00   47.99  ? 249 LYS D C   1 
ATOM   10879 O O   . LYS D  1 249 ? 98.047  -13.518 3.623   1.00   44.97  ? 249 LYS D O   1 
ATOM   10880 C CB  . LYS D  1 249 ? 98.594  -16.211 4.280   1.00   60.40  ? 249 LYS D CB  1 
ATOM   10881 C CG  . LYS D  1 249 ? 99.243  -17.569 4.562   1.00   67.00  ? 249 LYS D CG  1 
ATOM   10882 C CD  . LYS D  1 249 ? 99.877  -18.195 3.328   1.00   69.44  ? 249 LYS D CD  1 
ATOM   10883 C CE  . LYS D  1 249 ? 100.463 -19.569 3.616   1.00   71.61  ? 249 LYS D CE  1 
ATOM   10884 N NZ  . LYS D  1 249 ? 101.360 -19.983 2.515   1.00   70.93  ? 249 LYS D NZ  1 
ATOM   10885 N N   . HIS D  1 250 ? 98.982  -12.806 5.556   1.00   46.86  ? 250 HIS D N   1 
ATOM   10886 C CA  . HIS D  1 250 ? 98.487  -11.428 5.520   1.00   44.22  ? 250 HIS D CA  1 
ATOM   10887 C C   . HIS D  1 250 ? 99.582  -10.473 5.087   1.00   43.31  ? 250 HIS D C   1 
ATOM   10888 O O   . HIS D  1 250 ? 100.703 -10.564 5.556   1.00   43.86  ? 250 HIS D O   1 
ATOM   10889 C CB  . HIS D  1 250 ? 97.975  -10.929 6.881   1.00   42.89  ? 250 HIS D CB  1 
ATOM   10890 C CG  . HIS D  1 250 ? 96.610  -11.406 7.285   1.00   45.09  ? 250 HIS D CG  1 
ATOM   10891 N ND1 . HIS D  1 250 ? 96.390  -12.586 7.962   1.00   45.78  ? 250 HIS D ND1 1 
ATOM   10892 C CD2 . HIS D  1 250 ? 95.396  -10.810 7.170   1.00   45.74  ? 250 HIS D CD2 1 
ATOM   10893 C CE1 . HIS D  1 250 ? 95.099  -12.713 8.211   1.00   48.40  ? 250 HIS D CE1 1 
ATOM   10894 N NE2 . HIS D  1 250 ? 94.474  -11.647 7.743   1.00   47.02  ? 250 HIS D NE2 1 
ATOM   10895 N N   . LEU D  1 251 ? 99.226  -9.576  4.174   1.00   42.73  ? 251 LEU D N   1 
ATOM   10896 C CA  . LEU D  1 251 ? 100.093 -8.542  3.651   1.00   38.84  ? 251 LEU D CA  1 
ATOM   10897 C C   . LEU D  1 251 ? 99.610  -7.175  4.079   1.00   39.36  ? 251 LEU D C   1 
ATOM   10898 O O   . LEU D  1 251 ? 98.412  -6.888  3.966   1.00   38.38  ? 251 LEU D O   1 
ATOM   10899 C CB  . LEU D  1 251 ? 100.121 -8.579  2.134   1.00   37.30  ? 251 LEU D CB  1 
ATOM   10900 C CG  . LEU D  1 251 ? 100.797 -9.774  1.499   1.00   38.79  ? 251 LEU D CG  1 
ATOM   10901 C CD1 . LEU D  1 251 ? 100.780 -9.587  0.007   1.00   39.08  ? 251 LEU D CD1 1 
ATOM   10902 C CD2 . LEU D  1 251 ? 102.201 -9.808  2.000   1.00   39.16  ? 251 LEU D CD2 1 
ATOM   10903 N N   . VAL D  1 252 ? 100.493 -6.384  4.686   1.00   39.76  ? 252 VAL D N   1 
ATOM   10904 C CA  . VAL D  1 252 ? 100.191 -4.973  4.921   1.00   38.91  ? 252 VAL D CA  1 
ATOM   10905 C C   . VAL D  1 252 ? 100.935 -4.171  3.852   1.00   35.98  ? 252 VAL D C   1 
ATOM   10906 O O   . VAL D  1 252 ? 102.146 -4.092  3.884   1.00   36.63  ? 252 VAL D O   1 
ATOM   10907 C CB  . VAL D  1 252 ? 100.585 -4.544  6.340   1.00   39.08  ? 252 VAL D CB  1 
ATOM   10908 C CG1 . VAL D  1 252 ? 100.200 -3.093  6.595   1.00   37.44  ? 252 VAL D CG1 1 
ATOM   10909 C CG2 . VAL D  1 252 ? 99.886  -5.467  7.339   1.00   37.72  ? 252 VAL D CG2 1 
ATOM   10910 N N   . ILE D  1 253 ? 100.192 -3.598  2.907   1.00   38.28  ? 253 ILE D N   1 
ATOM   10911 C CA  . ILE D  1 253 ? 100.746 -2.918  1.740   1.00   38.01  ? 253 ILE D CA  1 
ATOM   10912 C C   . ILE D  1 253 ? 100.554 -1.403  1.709   1.00   38.29  ? 253 ILE D C   1 
ATOM   10913 O O   . ILE D  1 253 ? 99.497  -0.926  1.308   1.00   37.11  ? 253 ILE D O   1 
ATOM   10914 C CB  . ILE D  1 253 ? 100.112 -3.493  0.459   1.00   38.33  ? 253 ILE D CB  1 
ATOM   10915 C CG1 . ILE D  1 253 ? 100.244 -5.025  0.470   1.00   37.85  ? 253 ILE D CG1 1 
ATOM   10916 C CG2 . ILE D  1 253 ? 100.746 -2.872  -0.786  1.00   35.11  ? 253 ILE D CG2 1 
ATOM   10917 C CD1 . ILE D  1 253 ? 99.218  -5.753  -0.398  1.00   37.00  ? 253 ILE D CD1 1 
ATOM   10918 N N   . PRO D  1 254 ? 101.601 -0.650  2.078   1.00   42.37  ? 254 PRO D N   1 
ATOM   10919 C CA  . PRO D  1 254 ? 101.639 0.812   2.098   1.00   42.99  ? 254 PRO D CA  1 
ATOM   10920 C C   . PRO D  1 254 ? 101.632 1.343   0.679   1.00   45.21  ? 254 PRO D C   1 
ATOM   10921 O O   . PRO D  1 254 ? 102.261 0.704   -0.159  1.00   44.62  ? 254 PRO D O   1 
ATOM   10922 C CB  . PRO D  1 254 ? 102.959 1.121   2.793   1.00   42.84  ? 254 PRO D CB  1 
ATOM   10923 C CG  . PRO D  1 254 ? 103.380 -0.147  3.451   1.00   42.93  ? 254 PRO D CG  1 
ATOM   10924 C CD  . PRO D  1 254 ? 102.871 -1.218  2.563   1.00   43.81  ? 254 PRO D CD  1 
ATOM   10925 N N   . THR D  1 255 ? 100.941 2.444   0.400   1.00   50.24  ? 255 THR D N   1 
ATOM   10926 C CA  . THR D  1 255 ? 101.014 3.058   -0.924  1.00   54.07  ? 255 THR D CA  1 
ATOM   10927 C C   . THR D  1 255 ? 101.813 4.374   -0.909  1.00   55.63  ? 255 THR D C   1 
ATOM   10928 O O   . THR D  1 255 ? 102.201 4.908   -1.962  1.00   56.83  ? 255 THR D O   1 
ATOM   10929 C CB  . THR D  1 255 ? 99.593  3.318   -1.504  1.00   40.65  ? 255 THR D CB  1 
ATOM   10930 O OG1 . THR D  1 255 ? 98.894  4.262   -0.692  1.00   45.59  ? 255 THR D OG1 1 
ATOM   10931 C CG2 . THR D  1 255 ? 98.770  2.040   -1.584  1.00   38.20  ? 255 THR D CG2 1 
ATOM   10932 N N   . GLU D  1 272 ? 111.644 9.121   -5.414  1.00   75.09  ? 272 GLU D N   1 
ATOM   10933 C CA  . GLU D  1 272 ? 111.711 7.670   -5.313  1.00   73.52  ? 272 GLU D CA  1 
ATOM   10934 C C   . GLU D  1 272 ? 112.726 7.138   -4.292  1.00   63.99  ? 272 GLU D C   1 
ATOM   10935 O O   . GLU D  1 272 ? 113.457 6.177   -4.562  1.00   55.17  ? 272 GLU D O   1 
ATOM   10936 C CB  . GLU D  1 272 ? 112.002 7.055   -6.686  1.00   80.08  ? 272 GLU D CB  1 
ATOM   10937 C CG  . GLU D  1 272 ? 110.803 6.324   -7.304  1.00   87.27  ? 272 GLU D CG  1 
ATOM   10938 C CD  . GLU D  1 272 ? 110.234 5.215   -6.401  1.00   92.65  ? 272 GLU D CD  1 
ATOM   10939 O OE1 . GLU D  1 272 ? 110.956 4.736   -5.496  1.00   95.09  ? 272 GLU D OE1 1 
ATOM   10940 O OE2 . GLU D  1 272 ? 109.064 4.808   -6.604  1.00   94.10  ? 272 GLU D OE2 1 
ATOM   10941 N N   . ILE D  1 273 ? 112.789 7.809   -3.146  1.00   64.35  ? 273 ILE D N   1 
ATOM   10942 C CA  . ILE D  1 273 ? 113.598 7.378   -2.013  1.00   64.50  ? 273 ILE D CA  1 
ATOM   10943 C C   . ILE D  1 273 ? 112.838 6.180   -1.447  1.00   65.02  ? 273 ILE D C   1 
ATOM   10944 O O   . ILE D  1 273 ? 111.608 6.132   -1.573  1.00   69.26  ? 273 ILE D O   1 
ATOM   10945 C CB  . ILE D  1 273 ? 113.760 8.477   -0.938  1.00   63.38  ? 273 ILE D CB  1 
ATOM   10946 C CG1 . ILE D  1 273 ? 114.170 9.794   -1.572  1.00   64.58  ? 273 ILE D CG1 1 
ATOM   10947 C CG2 . ILE D  1 273 ? 114.760 8.062   0.133   1.00   61.79  ? 273 ILE D CG2 1 
ATOM   10948 C CD1 . ILE D  1 273 ? 114.466 10.851  -0.562  1.00   65.70  ? 273 ILE D CD1 1 
ATOM   10949 N N   . GLY D  1 274 ? 113.528 5.195   -0.880  1.00   58.14  ? 274 GLY D N   1 
ATOM   10950 C CA  . GLY D  1 274 ? 112.826 4.090   -0.251  1.00   54.68  ? 274 GLY D CA  1 
ATOM   10951 C C   . GLY D  1 274 ? 111.908 4.594   0.864   1.00   52.61  ? 274 GLY D C   1 
ATOM   10952 O O   . GLY D  1 274 ? 112.033 5.734   1.317   1.00   55.28  ? 274 GLY D O   1 
ATOM   10953 N N   . GLY D  1 275 ? 110.972 3.764   1.307   1.00   45.12  ? 275 GLY D N   1 
ATOM   10954 C CA  . GLY D  1 275 ? 110.045 4.203   2.316   1.00   41.72  ? 275 GLY D CA  1 
ATOM   10955 C C   . GLY D  1 275 ? 110.492 3.814   3.703   1.00   41.26  ? 275 GLY D C   1 
ATOM   10956 O O   . GLY D  1 275 ? 109.912 4.237   4.681   1.00   45.67  ? 275 GLY D O   1 
ATOM   10957 N N   . ALA D  1 276 ? 111.525 3.001   3.818   1.00   36.95  ? 276 ALA D N   1 
ATOM   10958 C CA  . ALA D  1 276 ? 111.938 2.573   5.141   1.00   33.36  ? 276 ALA D CA  1 
ATOM   10959 C C   . ALA D  1 276 ? 113.300 3.136   5.562   1.00   33.15  ? 276 ALA D C   1 
ATOM   10960 O O   . ALA D  1 276 ? 114.321 2.852   4.955   1.00   32.81  ? 276 ALA D O   1 
ATOM   10961 C CB  . ALA D  1 276 ? 111.946 1.060   5.206   1.00   32.36  ? 276 ALA D CB  1 
ATOM   10962 N N   . LEU D  1 277 ? 113.302 3.945   6.608   1.00   34.23  ? 277 LEU D N   1 
ATOM   10963 C CA  . LEU D  1 277 ? 114.535 4.467   7.166   1.00   33.50  ? 277 LEU D CA  1 
ATOM   10964 C C   . LEU D  1 277 ? 115.209 3.417   7.983   1.00   31.15  ? 277 LEU D C   1 
ATOM   10965 O O   . LEU D  1 277 ? 114.545 2.627   8.646   1.00   31.14  ? 277 LEU D O   1 
ATOM   10966 C CB  . LEU D  1 277 ? 114.279 5.700   8.042   1.00   35.17  ? 277 LEU D CB  1 
ATOM   10967 C CG  . LEU D  1 277 ? 115.456 6.241   8.870   1.00   37.36  ? 277 LEU D CG  1 
ATOM   10968 C CD1 . LEU D  1 277 ? 116.522 6.933   8.022   1.00   37.25  ? 277 LEU D CD1 1 
ATOM   10969 C CD2 . LEU D  1 277 ? 114.978 7.163   9.948   1.00   39.66  ? 277 LEU D CD2 1 
ATOM   10970 N N   . ILE D  1 278 ? 116.534 3.413   7.906   1.00   32.59  ? 278 ILE D N   1 
ATOM   10971 C CA  . ILE D  1 278 ? 117.379 2.658   8.818   1.00   34.09  ? 278 ILE D CA  1 
ATOM   10972 C C   . ILE D  1 278 ? 118.130 3.629   9.719   1.00   34.10  ? 278 ILE D C   1 
ATOM   10973 O O   . ILE D  1 278 ? 118.753 4.563   9.220   1.00   34.29  ? 278 ILE D O   1 
ATOM   10974 C CB  . ILE D  1 278 ? 118.388 1.796   8.080   1.00   34.06  ? 278 ILE D CB  1 
ATOM   10975 C CG1 . ILE D  1 278 ? 117.710 0.941   7.011   1.00   33.59  ? 278 ILE D CG1 1 
ATOM   10976 C CG2 . ILE D  1 278 ? 119.140 0.941   9.075   1.00   32.97  ? 278 ILE D CG2 1 
ATOM   10977 C CD1 . ILE D  1 278 ? 118.708 0.270   6.085   1.00   32.80  ? 278 ILE D CD1 1 
ATOM   10978 N N   . THR D  1 279 ? 118.053 3.411   11.035  1.00   33.20  ? 279 THR D N   1 
ATOM   10979 C CA  . THR D  1 279 ? 118.607 4.341   12.019  1.00   35.09  ? 279 THR D CA  1 
ATOM   10980 C C   . THR D  1 279 ? 119.094 3.634   13.290  1.00   38.86  ? 279 THR D C   1 
ATOM   10981 O O   . THR D  1 279 ? 118.622 2.558   13.594  1.00   40.75  ? 279 THR D O   1 
ATOM   10982 C CB  . THR D  1 279 ? 117.552 5.396   12.400  1.00   35.08  ? 279 THR D CB  1 
ATOM   10983 O OG1 . THR D  1 279 ? 118.112 6.302   13.355  1.00   40.18  ? 279 THR D OG1 1 
ATOM   10984 C CG2 . THR D  1 279 ? 116.308 4.738   13.008  1.00   31.81  ? 279 THR D CG2 1 
ATOM   10985 N N   . THR D  1 280 ? 120.020 4.218   14.050  1.00   40.78  ? 280 THR D N   1 
ATOM   10986 C CA  . THR D  1 280 ? 120.452 3.583   15.316  1.00   37.90  ? 280 THR D CA  1 
ATOM   10987 C C   . THR D  1 280 ? 120.113 4.396   16.551  1.00   38.53  ? 280 THR D C   1 
ATOM   10988 O O   . THR D  1 280 ? 120.491 4.036   17.664  1.00   40.86  ? 280 THR D O   1 
ATOM   10989 C CB  . THR D  1 280 ? 121.975 3.317   15.381  1.00   35.76  ? 280 THR D CB  1 
ATOM   10990 O OG1 . THR D  1 280 ? 122.693 4.537   15.160  1.00   34.88  ? 280 THR D OG1 1 
ATOM   10991 C CG2 . THR D  1 280 ? 122.401 2.271   14.361  1.00   35.62  ? 280 THR D CG2 1 
ATOM   10992 N N   . THR D  1 281 ? 119.378 5.475   16.370  1.00   38.45  ? 281 THR D N   1 
ATOM   10993 C CA  . THR D  1 281 ? 119.225 6.419   17.456  1.00   41.73  ? 281 THR D CA  1 
ATOM   10994 C C   . THR D  1 281 ? 117.899 6.278   18.224  1.00   43.43  ? 281 THR D C   1 
ATOM   10995 O O   . THR D  1 281 ? 117.595 7.079   19.100  1.00   43.36  ? 281 THR D O   1 
ATOM   10996 C CB  . THR D  1 281 ? 119.388 7.817   16.905  1.00   41.03  ? 281 THR D CB  1 
ATOM   10997 O OG1 . THR D  1 281 ? 118.509 7.991   15.790  1.00   40.67  ? 281 THR D OG1 1 
ATOM   10998 C CG2 . THR D  1 281 ? 120.812 7.959   16.418  1.00   40.72  ? 281 THR D CG2 1 
ATOM   10999 N N   . HIS D  1 282 ? 117.143 5.224   17.914  1.00   45.03  ? 282 HIS D N   1 
ATOM   11000 C CA  . HIS D  1 282 ? 116.099 4.717   18.801  1.00   45.61  ? 282 HIS D CA  1 
ATOM   11001 C C   . HIS D  1 282 ? 116.071 3.192   18.677  1.00   41.51  ? 282 HIS D C   1 
ATOM   11002 O O   . HIS D  1 282 ? 116.389 2.660   17.623  1.00   43.32  ? 282 HIS D O   1 
ATOM   11003 C CB  . HIS D  1 282 ? 114.735 5.338   18.482  1.00   49.94  ? 282 HIS D CB  1 
ATOM   11004 C CG  . HIS D  1 282 ? 114.287 5.160   17.063  1.00   53.28  ? 282 HIS D CG  1 
ATOM   11005 N ND1 . HIS D  1 282 ? 113.916 3.938   16.542  1.00   52.18  ? 282 HIS D ND1 1 
ATOM   11006 C CD2 . HIS D  1 282 ? 114.146 6.052   16.053  1.00   55.67  ? 282 HIS D CD2 1 
ATOM   11007 C CE1 . HIS D  1 282 ? 113.557 4.087   15.279  1.00   51.46  ? 282 HIS D CE1 1 
ATOM   11008 N NE2 . HIS D  1 282 ? 113.692 5.360   14.956  1.00   53.92  ? 282 HIS D NE2 1 
ATOM   11009 N N   . PRO D  1 283 ? 115.740 2.481   19.768  1.00   38.95  ? 283 PRO D N   1 
ATOM   11010 C CA  . PRO D  1 283 ? 115.782 1.009   19.808  1.00   37.66  ? 283 PRO D CA  1 
ATOM   11011 C C   . PRO D  1 283 ? 114.700 0.266   19.001  1.00   38.99  ? 283 PRO D C   1 
ATOM   11012 O O   . PRO D  1 283 ? 115.033 -0.661  18.280  1.00   40.41  ? 283 PRO D O   1 
ATOM   11013 C CB  . PRO D  1 283 ? 115.637 0.693   21.302  1.00   38.32  ? 283 PRO D CB  1 
ATOM   11014 C CG  . PRO D  1 283 ? 115.018 1.892   21.888  1.00   40.00  ? 283 PRO D CG  1 
ATOM   11015 C CD  . PRO D  1 283 ? 115.502 3.058   21.101  1.00   39.75  ? 283 PRO D CD  1 
ATOM   11016 N N   . TYR D  1 284 ? 113.431 0.630   19.117  1.00   40.52  ? 284 TYR D N   1 
ATOM   11017 C CA  . TYR D  1 284 ? 112.381 -0.157  18.479  1.00   41.01  ? 284 TYR D CA  1 
ATOM   11018 C C   . TYR D  1 284 ? 111.994 0.364   17.103  1.00   39.34  ? 284 TYR D C   1 
ATOM   11019 O O   . TYR D  1 284 ? 112.215 1.528   16.783  1.00   39.97  ? 284 TYR D O   1 
ATOM   11020 C CB  . TYR D  1 284 ? 111.163 -0.189  19.400  1.00   47.88  ? 284 TYR D CB  1 
ATOM   11021 C CG  . TYR D  1 284 ? 111.549 -0.629  20.784  1.00   53.52  ? 284 TYR D CG  1 
ATOM   11022 C CD1 . TYR D  1 284 ? 112.117 -1.875  21.000  1.00   56.07  ? 284 TYR D CD1 1 
ATOM   11023 C CD2 . TYR D  1 284 ? 111.425 0.228   21.863  1.00   56.78  ? 284 TYR D CD2 1 
ATOM   11024 C CE1 . TYR D  1 284 ? 112.502 -2.269  22.258  1.00   59.25  ? 284 TYR D CE1 1 
ATOM   11025 C CE2 . TYR D  1 284 ? 111.809 -0.161  23.126  1.00   59.63  ? 284 TYR D CE2 1 
ATOM   11026 C CZ  . TYR D  1 284 ? 112.345 -1.407  23.315  1.00   61.40  ? 284 TYR D CZ  1 
ATOM   11027 O OH  . TYR D  1 284 ? 112.735 -1.791  24.569  1.00   65.42  ? 284 TYR D OH  1 
ATOM   11028 N N   . THR D  1 285 ? 111.393 -0.488  16.289  1.00   38.39  ? 285 THR D N   1 
ATOM   11029 C CA  . THR D  1 285 ? 110.940 -0.040  14.981  1.00   40.29  ? 285 THR D CA  1 
ATOM   11030 C C   . THR D  1 285 ? 109.650 0.784   15.053  1.00   39.63  ? 285 THR D C   1 
ATOM   11031 O O   . THR D  1 285 ? 108.674 0.419   15.716  1.00   42.82  ? 285 THR D O   1 
ATOM   11032 C CB  . THR D  1 285 ? 110.745 -1.221  14.029  1.00   41.05  ? 285 THR D CB  1 
ATOM   11033 O OG1 . THR D  1 285 ? 112.003 -1.881  13.832  1.00   39.50  ? 285 THR D OG1 1 
ATOM   11034 C CG2 . THR D  1 285 ? 110.194 -0.730  12.678  1.00   39.50  ? 285 THR D CG2 1 
ATOM   11035 N N   . VAL D  1 286 ? 109.651 1.900   14.346  1.00   37.59  ? 286 VAL D N   1 
ATOM   11036 C CA  . VAL D  1 286 ? 108.569 2.843   14.445  1.00   36.77  ? 286 VAL D CA  1 
ATOM   11037 C C   . VAL D  1 286 ? 107.704 2.844   13.196  1.00   38.13  ? 286 VAL D C   1 
ATOM   11038 O O   . VAL D  1 286 ? 108.220 2.924   12.088  1.00   39.48  ? 286 VAL D O   1 
ATOM   11039 C CB  . VAL D  1 286 ? 109.132 4.226   14.664  1.00   37.62  ? 286 VAL D CB  1 
ATOM   11040 C CG1 . VAL D  1 286 ? 108.010 5.275   14.679  1.00   35.67  ? 286 VAL D CG1 1 
ATOM   11041 C CG2 . VAL D  1 286 ? 109.955 4.231   15.951  1.00   37.76  ? 286 VAL D CG2 1 
ATOM   11042 N N   . LEU D  1 287 ? 106.393 2.749   13.371  1.00   38.90  ? 287 LEU D N   1 
ATOM   11043 C CA  . LEU D  1 287 ? 105.483 2.760   12.241  1.00   38.38  ? 287 LEU D CA  1 
ATOM   11044 C C   . LEU D  1 287 ? 104.584 3.965   12.266  1.00   38.53  ? 287 LEU D C   1 
ATOM   11045 O O   . LEU D  1 287 ? 104.096 4.367   13.311  1.00   40.67  ? 287 LEU D O   1 
ATOM   11046 C CB  . LEU D  1 287 ? 104.621 1.505   12.218  1.00   42.22  ? 287 LEU D CB  1 
ATOM   11047 C CG  . LEU D  1 287 ? 105.393 0.189   12.335  1.00   43.41  ? 287 LEU D CG  1 
ATOM   11048 C CD1 . LEU D  1 287 ? 104.430 -0.974  12.425  1.00   36.07  ? 287 LEU D CD1 1 
ATOM   11049 C CD2 . LEU D  1 287 ? 106.377 0.015   11.182  1.00   42.45  ? 287 LEU D CD2 1 
ATOM   11050 N N   . SER D  1 288 ? 104.344 4.519   11.092  1.00   38.16  ? 288 SER D N   1 
ATOM   11051 C CA  . SER D  1 288 ? 103.433 5.619   10.998  1.00   42.76  ? 288 SER D CA  1 
ATOM   11052 C C   . SER D  1 288 ? 102.092 5.078   11.446  1.00   44.15  ? 288 SER D C   1 
ATOM   11053 O O   . SER D  1 288 ? 101.839 3.883   11.338  1.00   43.22  ? 288 SER D O   1 
ATOM   11054 C CB  . SER D  1 288 ? 103.405 6.163   9.584   1.00   44.85  ? 288 SER D CB  1 
ATOM   11055 O OG  . SER D  1 288 ? 102.943 5.163   8.706   1.00   46.33  ? 288 SER D OG  1 
ATOM   11056 N N   . HIS D  1 289 ? 101.245 5.959   11.957  1.00   40.20  ? 289 HIS D N   1 
ATOM   11057 C CA  . HIS D  1 289 ? 100.058 5.543   12.660  1.00   41.87  ? 289 HIS D CA  1 
ATOM   11058 C C   . HIS D  1 289 ? 99.175  4.598   11.868  1.00   47.76  ? 289 HIS D C   1 
ATOM   11059 O O   . HIS D  1 289 ? 98.689  3.596   12.391  1.00   44.85  ? 289 HIS D O   1 
ATOM   11060 C CB  . HIS D  1 289 ? 99.247  6.749   13.061  1.00   43.70  ? 289 HIS D CB  1 
ATOM   11061 C CG  . HIS D  1 289 ? 98.006  6.400   13.825  1.00   48.24  ? 289 HIS D CG  1 
ATOM   11062 N ND1 . HIS D  1 289 ? 98.037  5.933   15.121  1.00   49.79  ? 289 HIS D ND1 1 
ATOM   11063 C CD2 . HIS D  1 289 ? 96.707  6.389   13.454  1.00   46.88  ? 289 HIS D CD2 1 
ATOM   11064 C CE1 . HIS D  1 289 ? 96.807  5.691   15.527  1.00   53.26  ? 289 HIS D CE1 1 
ATOM   11065 N NE2 . HIS D  1 289 ? 95.981  5.954   14.533  1.00   55.15  ? 289 HIS D NE2 1 
ATOM   11066 N N   . SER D  1 290 ? 98.957  4.912   10.605  1.00   50.10  ? 290 SER D N   1 
ATOM   11067 C CA  . SER D  1 290 ? 98.074  4.080   9.805   1.00   51.91  ? 290 SER D CA  1 
ATOM   11068 C C   . SER D  1 290 ? 98.606  2.674   9.619   1.00   46.43  ? 290 SER D C   1 
ATOM   11069 O O   . SER D  1 290 ? 97.865  1.711   9.696   1.00   47.58  ? 290 SER D O   1 
ATOM   11070 C CB  . SER D  1 290 ? 97.852  4.710   8.444   1.00   56.37  ? 290 SER D CB  1 
ATOM   11071 O OG  . SER D  1 290 ? 96.633  4.235   7.921   1.00   59.64  ? 290 SER D OG  1 
ATOM   11072 N N   . ILE D  1 291 ? 99.903  2.566   9.386   1.00   44.58  ? 291 ILE D N   1 
ATOM   11073 C CA  . ILE D  1 291 ? 100.541 1.273   9.242   1.00   42.65  ? 291 ILE D CA  1 
ATOM   11074 C C   . ILE D  1 291 ? 100.563 0.579   10.568  1.00   40.86  ? 291 ILE D C   1 
ATOM   11075 O O   . ILE D  1 291 ? 100.275 -0.605  10.661  1.00   38.66  ? 291 ILE D O   1 
ATOM   11076 C CB  . ILE D  1 291 ? 101.960 1.403   8.735   1.00   40.61  ? 291 ILE D CB  1 
ATOM   11077 C CG1 . ILE D  1 291 ? 101.931 2.097   7.375   1.00   40.57  ? 291 ILE D CG1 1 
ATOM   11078 C CG2 . ILE D  1 291 ? 102.643 0.030   8.701   1.00   38.95  ? 291 ILE D CG2 1 
ATOM   11079 C CD1 . ILE D  1 291 ? 103.254 2.328   6.778   1.00   37.65  ? 291 ILE D CD1 1 
ATOM   11080 N N   . PHE D  1 292 ? 100.887 1.339   11.600  1.00   41.67  ? 292 PHE D N   1 
ATOM   11081 C CA  . PHE D  1 292 ? 100.923 0.803   12.940  1.00   44.77  ? 292 PHE D CA  1 
ATOM   11082 C C   . PHE D  1 292 ? 99.597  0.157   13.352  1.00   49.04  ? 292 PHE D C   1 
ATOM   11083 O O   . PHE D  1 292 ? 99.577  -0.938  13.906  1.00   49.63  ? 292 PHE D O   1 
ATOM   11084 C CB  . PHE D  1 292 ? 101.297 1.894   13.934  1.00   47.77  ? 292 PHE D CB  1 
ATOM   11085 C CG  . PHE D  1 292 ? 101.190 1.453   15.357  1.00   51.73  ? 292 PHE D CG  1 
ATOM   11086 C CD1 . PHE D  1 292 ? 102.202 0.705   15.939  1.00   51.99  ? 292 PHE D CD1 1 
ATOM   11087 C CD2 . PHE D  1 292 ? 100.077 1.769   16.114  1.00   53.91  ? 292 PHE D CD2 1 
ATOM   11088 C CE1 . PHE D  1 292 ? 102.102 0.286   17.258  1.00   53.31  ? 292 PHE D CE1 1 
ATOM   11089 C CE2 . PHE D  1 292 ? 99.977  1.354   17.434  1.00   55.37  ? 292 PHE D CE2 1 
ATOM   11090 C CZ  . PHE D  1 292 ? 100.993 0.612   18.002  1.00   54.68  ? 292 PHE D CZ  1 
ATOM   11091 N N   . GLU D  1 293 ? 98.487  0.841   13.107  1.00   49.01  ? 293 GLU D N   1 
ATOM   11092 C CA  . GLU D  1 293 ? 97.198  0.319   13.514  1.00   49.09  ? 293 GLU D CA  1 
ATOM   11093 C C   . GLU D  1 293 ? 96.787  -0.940  12.761  1.00   43.87  ? 293 GLU D C   1 
ATOM   11094 O O   . GLU D  1 293 ? 96.312  -1.902  13.346  1.00   44.83  ? 293 GLU D O   1 
ATOM   11095 C CB  . GLU D  1 293 ? 96.137  1.393   13.332  1.00   54.24  ? 293 GLU D CB  1 
ATOM   11096 C CG  . GLU D  1 293 ? 96.182  2.463   14.392  1.00   59.76  ? 293 GLU D CG  1 
ATOM   11097 C CD  . GLU D  1 293 ? 95.641  1.962   15.713  1.00   67.21  ? 293 GLU D CD  1 
ATOM   11098 O OE1 . GLU D  1 293 ? 94.408  1.777   15.823  1.00   72.63  ? 293 GLU D OE1 1 
ATOM   11099 O OE2 . GLU D  1 293 ? 96.450  1.749   16.644  1.00   68.04  1 293 GLU D OE2 1 
ATOM   11100 N N   . VAL D  1 294 ? 96.997  -0.933  11.460  1.00   42.62  ? 294 VAL D N   1 
ATOM   11101 C CA  . VAL D  1 294 ? 96.611  -2.036  10.600  1.00   42.38  ? 294 VAL D CA  1 
ATOM   11102 C C   . VAL D  1 294 ? 97.485  -3.247  10.842  1.00   41.65  ? 294 VAL D C   1 
ATOM   11103 O O   . VAL D  1 294 ? 97.023  -4.381  10.904  1.00   46.81  ? 294 VAL D O   1 
ATOM   11104 C CB  . VAL D  1 294 ? 96.715  -1.633  9.128   1.00   48.18  ? 294 VAL D CB  1 
ATOM   11105 C CG1 . VAL D  1 294 ? 96.482  -2.823  8.255   1.00   46.24  ? 294 VAL D CG1 1 
ATOM   11106 C CG2 . VAL D  1 294 ? 95.715  -0.544  8.815   1.00   47.78  ? 294 VAL D CG2 1 
ATOM   11107 N N   . PHE D  1 295 ? 98.770  -2.990  10.951  1.00   40.40  ? 295 PHE D N   1 
ATOM   11108 C CA  . PHE D  1 295 ? 99.737  -4.039  11.181  1.00   39.74  ? 295 PHE D CA  1 
ATOM   11109 C C   . PHE D  1 295 ? 99.497  -4.760  12.506  1.00   41.44  ? 295 PHE D C   1 
ATOM   11110 O O   . PHE D  1 295 ? 99.564  -5.982  12.569  1.00   41.35  ? 295 PHE D O   1 
ATOM   11111 C CB  . PHE D  1 295 ? 101.143 -3.464  11.124  1.00   42.04  ? 295 PHE D CB  1 
ATOM   11112 C CG  . PHE D  1 295 ? 102.161 -4.389  11.645  1.00   42.51  ? 295 PHE D CG  1 
ATOM   11113 C CD1 . PHE D  1 295 ? 102.567 -5.477  10.893  1.00   42.07  ? 295 PHE D CD1 1 
ATOM   11114 C CD2 . PHE D  1 295 ? 102.704 -4.198  12.903  1.00   41.91  ? 295 PHE D CD2 1 
ATOM   11115 C CE1 . PHE D  1 295 ? 103.492 -6.376  11.391  1.00   42.56  ? 295 PHE D CE1 1 
ATOM   11116 C CE2 . PHE D  1 295 ? 103.634 -5.087  13.404  1.00   42.81  ? 295 PHE D CE2 1 
ATOM   11117 C CZ  . PHE D  1 295 ? 104.033 -6.179  12.643  1.00   42.55  ? 295 PHE D CZ  1 
ATOM   11118 N N   . THR D  1 296 ? 99.237  -4.015  13.572  1.00   42.19  ? 296 THR D N   1 
ATOM   11119 C CA  . THR D  1 296 ? 99.034  -4.646  14.865  1.00   45.93  ? 296 THR D CA  1 
ATOM   11120 C C   . THR D  1 296 ? 97.761  -5.498  14.879  1.00   48.14  ? 296 THR D C   1 
ATOM   11121 O O   . THR D  1 296 ? 97.719  -6.543  15.549  1.00   48.37  ? 296 THR D O   1 
ATOM   11122 C CB  . THR D  1 296 ? 98.990  -3.617  16.020  1.00   49.96  ? 296 THR D CB  1 
ATOM   11123 O OG1 . THR D  1 296 ? 97.983  -2.648  15.746  1.00   57.44  ? 296 THR D OG1 1 
ATOM   11124 C CG2 . THR D  1 296 ? 100.304 -2.897  16.146  1.00   48.22  ? 296 THR D CG2 1 
ATOM   11125 N N   . GLN D  1 297 ? 96.725  -5.087  14.149  1.00   47.66  ? 297 GLN D N   1 
ATOM   11126 C CA  . GLN D  1 297 ? 95.529  -5.912  14.133  1.00   50.86  ? 297 GLN D CA  1 
ATOM   11127 C C   . GLN D  1 297 ? 95.747  -7.194  13.343  1.00   46.11  ? 297 GLN D C   1 
ATOM   11128 O O   . GLN D  1 297 ? 95.374  -8.260  13.787  1.00   61.78  ? 297 GLN D O   1 
ATOM   11129 C CB  . GLN D  1 297 ? 94.327  -5.149  13.604  1.00   55.19  ? 297 GLN D CB  1 
ATOM   11130 C CG  . GLN D  1 297 ? 93.051  -5.983  13.719  1.00   62.28  ? 297 GLN D CG  1 
ATOM   11131 C CD  . GLN D  1 297 ? 92.737  -6.413  15.170  1.00   68.72  ? 297 GLN D CD  1 
ATOM   11132 O OE1 . GLN D  1 297 ? 92.608  -5.576  16.065  1.00   74.23  ? 297 GLN D OE1 1 
ATOM   11133 N NE2 . GLN D  1 297 ? 92.599  -7.727  15.392  1.00   67.15  ? 297 GLN D NE2 1 
ATOM   11134 N N   . VAL D  1 298 ? 96.372  -7.096  12.187  1.00   45.67  ? 298 VAL D N   1 
ATOM   11135 C CA  . VAL D  1 298 ? 96.735  -8.281  11.413  1.00   47.38  ? 298 VAL D CA  1 
ATOM   11136 C C   . VAL D  1 298 ? 97.560  -9.291  12.237  1.00   49.96  ? 298 VAL D C   1 
ATOM   11137 O O   . VAL D  1 298 ? 97.355  -10.512 12.171  1.00   51.92  ? 298 VAL D O   1 
ATOM   11138 C CB  . VAL D  1 298 ? 97.551  -7.859  10.179  1.00   46.04  ? 298 VAL D CB  1 
ATOM   11139 C CG1 . VAL D  1 298 ? 98.393  -8.997  9.646   1.00   41.52  ? 298 VAL D CG1 1 
ATOM   11140 C CG2 . VAL D  1 298 ? 96.640  -7.236  9.125   1.00   47.02  ? 298 VAL D CG2 1 
ATOM   11141 N N   . PHE D  1 299 ? 98.485  -8.768  13.031  1.00   51.47  ? 299 PHE D N   1 
ATOM   11142 C CA  . PHE D  1 299 ? 99.318  -9.612  13.859  1.00   50.48  ? 299 PHE D CA  1 
ATOM   11143 C C   . PHE D  1 299 ? 98.453  -10.302 14.887  1.00   49.73  ? 299 PHE D C   1 
ATOM   11144 O O   . PHE D  1 299 ? 98.544  -11.511 15.037  1.00   50.70  ? 299 PHE D O   1 
ATOM   11145 C CB  . PHE D  1 299 ? 100.420 -8.808  14.537  1.00   52.25  ? 299 PHE D CB  1 
ATOM   11146 C CG  . PHE D  1 299 ? 101.482 -9.663  15.156  1.00   57.98  ? 299 PHE D CG  1 
ATOM   11147 C CD1 . PHE D  1 299 ? 102.435 -10.286 14.352  1.00   59.45  ? 299 PHE D CD1 1 
ATOM   11148 C CD2 . PHE D  1 299 ? 101.533 -9.860  16.525  1.00   62.06  ? 299 PHE D CD2 1 
ATOM   11149 C CE1 . PHE D  1 299 ? 103.435 -11.091 14.905  1.00   60.92  ? 299 PHE D CE1 1 
ATOM   11150 C CE2 . PHE D  1 299 ? 102.526 -10.659 17.087  1.00   64.76  ? 299 PHE D CE2 1 
ATOM   11151 C CZ  . PHE D  1 299 ? 103.483 -11.278 16.271  1.00   63.24  ? 299 PHE D CZ  1 
ATOM   11152 N N   . ALA D  1 300 ? 97.601  -9.531  15.565  1.00   50.41  ? 300 ALA D N   1 
ATOM   11153 C CA  . ALA D  1 300 ? 96.688  -10.067 16.582  1.00   54.02  ? 300 ALA D CA  1 
ATOM   11154 C C   . ALA D  1 300 ? 95.715  -11.117 16.027  1.00   55.71  ? 300 ALA D C   1 
ATOM   11155 O O   . ALA D  1 300 ? 95.292  -12.019 16.741  1.00   56.39  ? 300 ALA D O   1 
ATOM   11156 C CB  . ALA D  1 300 ? 95.920  -8.944  17.235  1.00   57.32  ? 300 ALA D CB  1 
ATOM   11157 N N   . ASN D  1 301 ? 95.328  -10.969 14.765  1.00   57.35  ? 301 ASN D N   1 
ATOM   11158 C CA  . ASN D  1 301 ? 94.490  -11.959 14.088  1.00   61.01  ? 301 ASN D CA  1 
ATOM   11159 C C   . ASN D  1 301 ? 95.245  -13.223 13.783  1.00   63.93  ? 301 ASN D C   1 
ATOM   11160 O O   . ASN D  1 301 ? 94.647  -14.239 13.436  1.00   67.82  ? 301 ASN D O   1 
ATOM   11161 C CB  . ASN D  1 301 ? 93.918  -11.412 12.795  1.00   62.39  ? 301 ASN D CB  1 
ATOM   11162 C CG  . ASN D  1 301 ? 92.879  -10.368 13.035  1.00   67.66  ? 301 ASN D CG  1 
ATOM   11163 O OD1 . ASN D  1 301 ? 92.376  -10.224 14.152  1.00   69.61  ? 301 ASN D OD1 1 
ATOM   11164 N ND2 . ASN D  1 301 ? 92.545  -9.621  11.992  1.00   69.00  ? 301 ASN D ND2 1 
ATOM   11165 N N   . ASN D  1 302 ? 96.568  -13.139 13.842  1.00   62.26  ? 302 ASN D N   1 
ATOM   11166 C CA  . ASN D  1 302 ? 97.408  -14.306 13.637  1.00   60.28  ? 302 ASN D CA  1 
ATOM   11167 C C   . ASN D  1 302 ? 97.922  -14.825 14.973  1.00   62.54  ? 302 ASN D C   1 
ATOM   11168 O O   . ASN D  1 302 ? 98.939  -15.493 15.045  1.00   65.81  ? 302 ASN D O   1 
ATOM   11169 C CB  . ASN D  1 302 ? 98.558  -13.972 12.699  1.00   55.55  ? 302 ASN D CB  1 
ATOM   11170 C CG  . ASN D  1 302 ? 98.112  -13.883 11.263  1.00   54.46  ? 302 ASN D CG  1 
ATOM   11171 O OD1 . ASN D  1 302 ? 98.181  -14.864 10.518  1.00   53.03  ? 302 ASN D OD1 1 
ATOM   11172 N ND2 . ASN D  1 302 ? 97.627  -12.708 10.865  1.00   53.81  ? 302 ASN D ND2 1 
ATOM   11173 N N   . MET D  1 303 ? 97.189  -14.520 16.032  1.00   62.25  ? 303 MET D N   1 
ATOM   11174 C CA  . MET D  1 303 ? 97.559  -14.922 17.375  1.00   60.21  ? 303 MET D CA  1 
ATOM   11175 C C   . MET D  1 303 ? 96.322  -15.385 18.129  1.00   61.73  ? 303 MET D C   1 
ATOM   11176 O O   . MET D  1 303 ? 95.197  -15.113 17.718  1.00   62.54  ? 303 MET D O   1 
ATOM   11177 C CB  . MET D  1 303 ? 98.246  -13.760 18.104  1.00   57.22  ? 303 MET D CB  1 
ATOM   11178 C CG  . MET D  1 303 ? 99.637  -13.408 17.566  1.00   55.03  ? 303 MET D CG  1 
ATOM   11179 S SD  . MET D  1 303 ? 100.925 -14.596 18.000  1.00   75.02  ? 303 MET D SD  1 
ATOM   11180 C CE  . MET D  1 303 ? 101.304 -14.122 19.683  1.00   58.69  ? 303 MET D CE  1 
ATOM   11181 N N   . PRO D  1 304 ? 96.527  -16.118 19.225  1.00   65.33  ? 304 PRO D N   1 
ATOM   11182 C CA  . PRO D  1 304 ? 95.406  -16.452 20.102  1.00   68.65  ? 304 PRO D CA  1 
ATOM   11183 C C   . PRO D  1 304 ? 94.873  -15.183 20.760  1.00   69.46  ? 304 PRO D C   1 
ATOM   11184 O O   . PRO D  1 304 ? 95.611  -14.574 21.536  1.00   68.04  ? 304 PRO D O   1 
ATOM   11185 C CB  . PRO D  1 304 ? 96.034  -17.386 21.136  1.00   71.17  ? 304 PRO D CB  1 
ATOM   11186 C CG  . PRO D  1 304 ? 97.492  -17.067 21.120  1.00   70.11  ? 304 PRO D CG  1 
ATOM   11187 C CD  . PRO D  1 304 ? 97.790  -16.724 19.688  1.00   66.81  ? 304 PRO D CD  1 
ATOM   11188 N N   . LYS D  1 305 ? 93.644  -14.777 20.444  1.00   70.24  ? 305 LYS D N   1 
ATOM   11189 C CA  . LYS D  1 305 ? 93.130  -13.503 20.938  1.00   70.17  ? 305 LYS D CA  1 
ATOM   11190 C C   . LYS D  1 305 ? 92.991  -13.463 22.459  1.00   72.83  ? 305 LYS D C   1 
ATOM   11191 O O   . LYS D  1 305 ? 92.937  -12.381 23.045  1.00   76.08  ? 305 LYS D O   1 
ATOM   11192 C CB  . LYS D  1 305 ? 91.795  -13.156 20.274  0.0000 68.95  ? 305 LYS D CB  1 
ATOM   11193 C CG  . LYS D  1 305 ? 91.933  -12.115 19.162  0.0000 65.49  ? 305 LYS D CG  1 
ATOM   11194 C CD  . LYS D  1 305 ? 92.403  -10.776 19.741  0.0000 64.21  ? 305 LYS D CD  1 
ATOM   11195 C CE  . LYS D  1 305 ? 92.590  -9.685  18.682  0.0000 61.73  ? 305 LYS D CE  1 
ATOM   11196 N NZ  . LYS D  1 305 ? 92.478  -8.324  19.293  0.0000 61.92  ? 305 LYS D NZ  1 
ATOM   11197 N N   . GLN D  1 306 ? 92.921  -14.614 23.114  1.00   71.97  ? 306 GLN D N   1 
ATOM   11198 C CA  . GLN D  1 306 ? 92.740  -14.592 24.558  1.00   73.59  ? 306 GLN D CA  1 
ATOM   11199 C C   . GLN D  1 306 ? 94.042  -14.726 25.309  1.00   74.89  ? 306 GLN D C   1 
ATOM   11200 O O   . GLN D  1 306 ? 94.025  -15.059 26.490  1.00   77.55  ? 306 GLN D O   1 
ATOM   11201 C CB  . GLN D  1 306 ? 91.788  -15.710 24.996  0.0000 74.76  ? 306 GLN D CB  1 
ATOM   11202 C CG  . GLN D  1 306 ? 90.381  -15.612 24.425  0.0000 74.10  ? 306 GLN D CG  1 
ATOM   11203 C CD  . GLN D  1 306 ? 89.600  -14.479 25.043  0.0000 74.38  ? 306 GLN D CD  1 
ATOM   11204 O OE1 . GLN D  1 306 ? 89.455  -13.412 24.447  0.0000 72.66  ? 306 GLN D OE1 1 
ATOM   11205 N NE2 . GLN D  1 306 ? 89.099  -14.700 26.248  0.0000 76.88  ? 306 GLN D NE2 1 
ATOM   11206 N N   . ALA D  1 307 ? 95.155  -14.390 24.649  1.00   71.94  ? 307 ALA D N   1 
ATOM   11207 C CA  . ALA D  1 307 ? 96.481  -14.412 25.284  1.00   69.01  ? 307 ALA D CA  1 
ATOM   11208 C C   . ALA D  1 307 ? 96.983  -13.003 25.575  1.00   66.98  ? 307 ALA D C   1 
ATOM   11209 O O   . ALA D  1 307 ? 98.045  -12.821 26.174  1.00   62.83  ? 307 ALA D O   1 
ATOM   11210 C CB  . ALA D  1 307 ? 97.486  -15.158 24.417  1.00   62.18  ? 307 ALA D CB  1 
ATOM   11211 N N   . GLN D  1 308 ? 96.208  -12.010 25.144  1.00   66.91  ? 308 GLN D N   1 
ATOM   11212 C CA  . GLN D  1 308 ? 96.583  -10.602 25.288  1.00   66.33  ? 308 GLN D CA  1 
ATOM   11213 C C   . GLN D  1 308 ? 96.518  -10.048 26.703  1.00   66.00  ? 308 GLN D C   1 
ATOM   11214 O O   . GLN D  1 308 ? 95.718  -10.475 27.522  1.00   67.34  ? 308 GLN D O   1 
ATOM   11215 C CB  . GLN D  1 308 ? 95.725  -9.722  24.382  1.00   67.11  ? 308 GLN D CB  1 
ATOM   11216 C CG  . GLN D  1 308 ? 95.725  -10.137 22.932  1.00   64.97  ? 308 GLN D CG  1 
ATOM   11217 C CD  . GLN D  1 308 ? 94.967  -9.161  22.076  1.00   64.38  ? 308 GLN D CD  1 
ATOM   11218 O OE1 . GLN D  1 308 ? 94.499  -8.134  22.553  1.00   66.17  ? 308 GLN D OE1 1 
ATOM   11219 N NE2 . GLN D  1 308 ? 94.875  -9.453  20.799  1.00   63.05  ? 308 GLN D NE2 1 
ATOM   11220 N N   . VAL D  1 309 ? 97.376  -9.063  26.941  1.00   66.44  ? 309 VAL D N   1 
ATOM   11221 C CA  . VAL D  1 309 ? 97.493  -8.352  28.200  1.00   67.78  ? 309 VAL D CA  1 
ATOM   11222 C C   . VAL D  1 309 ? 97.421  -6.852  27.883  1.00   66.07  ? 309 VAL D C   1 
ATOM   11223 O O   . VAL D  1 309 ? 97.773  -6.442  26.769  1.00   61.25  ? 309 VAL D O   1 
ATOM   11224 C CB  . VAL D  1 309 ? 98.847  -8.735  28.885  1.00   75.29  ? 309 VAL D CB  1 
ATOM   11225 C CG1 . VAL D  1 309 ? 99.209  -7.822  30.033  1.00   77.65  ? 309 VAL D CG1 1 
ATOM   11226 C CG2 . VAL D  1 309 ? 98.818  -10.177 29.313  1.00   75.67  ? 309 VAL D CG2 1 
ATOM   11227 N N   . LYS D  1 310 ? 97.016  -6.036  28.861  1.00   67.17  ? 310 LYS D N   1 
ATOM   11228 C CA  . LYS D  1 310 ? 97.013  -4.585  28.687  1.00   69.47  ? 310 LYS D CA  1 
ATOM   11229 C C   . LYS D  1 310 ? 98.370  -4.126  28.240  1.00   71.02  ? 310 LYS D C   1 
ATOM   11230 O O   . LYS D  1 310 ? 99.335  -4.217  28.994  1.00   73.25  ? 310 LYS D O   1 
ATOM   11231 C CB  . LYS D  1 310 ? 96.648  -3.865  29.995  1.00   71.89  ? 310 LYS D CB  1 
ATOM   11232 C CG  . LYS D  1 310 ? 96.520  -2.331  29.883  1.00   72.56  ? 310 LYS D CG  1 
ATOM   11233 C CD  . LYS D  1 310 ? 96.051  -1.692  31.205  1.00   77.45  ? 310 LYS D CD  1 
ATOM   11234 C CE  . LYS D  1 310 ? 95.960  -0.152  31.158  1.00   78.77  ? 310 LYS D CE  1 
ATOM   11235 N NZ  . LYS D  1 310 ? 97.284  0.543   31.178  1.00   77.50  ? 310 LYS D NZ  1 
ATOM   11236 N N   . ALA D  1 311 ? 98.455  -3.625  27.019  1.00   71.43  ? 311 ALA D N   1 
ATOM   11237 C CA  . ALA D  1 311 ? 99.729  -3.111  26.562  1.00   72.92  ? 311 ALA D CA  1 
ATOM   11238 C C   . ALA D  1 311 ? 100.114 -1.933  27.443  1.00   76.45  ? 311 ALA D C   1 
ATOM   11239 O O   . ALA D  1 311 ? 99.279  -1.084  27.763  1.00   78.74  ? 311 ALA D O   1 
ATOM   11240 C CB  . ALA D  1 311 ? 99.654  -2.702  25.117  1.00   71.52  ? 311 ALA D CB  1 
ATOM   11241 N N   . VAL D  1 312 ? 101.371 -1.888  27.855  1.00   76.86  ? 312 VAL D N   1 
ATOM   11242 C CA  . VAL D  1 312 ? 101.832 -0.812  28.716  1.00   78.71  ? 312 VAL D CA  1 
ATOM   11243 C C   . VAL D  1 312 ? 103.214 -0.472  28.175  1.00   76.06  ? 312 VAL D C   1 
ATOM   11244 O O   . VAL D  1 312 ? 103.873 -1.297  27.550  1.00   72.58  ? 312 VAL D O   1 
ATOM   11245 C CB  . VAL D  1 312 ? 101.809 -1.174  30.233  1.00   79.81  ? 312 VAL D CB  1 
ATOM   11246 C CG1 . VAL D  1 312 ? 102.499 -0.091  31.066  1.00   82.47  ? 312 VAL D CG1 1 
ATOM   11247 C CG2 . VAL D  1 312 ? 100.358 -1.283  30.733  1.00   78.96  ? 312 VAL D CG2 1 
ATOM   11248 N N   . GLY D  1 313 ? 103.630 0.759   28.396  1.00   78.42  ? 313 GLY D N   1 
ATOM   11249 C CA  . GLY D  1 313 ? 104.887 1.264   27.900  1.00   77.22  ? 313 GLY D CA  1 
ATOM   11250 C C   . GLY D  1 313 ? 104.638 1.842   26.529  1.00   75.61  ? 313 GLY D C   1 
ATOM   11251 O O   . GLY D  1 313 ? 103.550 2.385   26.281  1.00   80.53  ? 313 GLY D O   1 
ATOM   11252 N N   . PRO D  1 314 ? 105.620 1.734   25.629  1.00   66.86  ? 314 PRO D N   1 
ATOM   11253 C CA  . PRO D  1 314 ? 105.451 2.293   24.289  1.00   61.07  ? 314 PRO D CA  1 
ATOM   11254 C C   . PRO D  1 314 ? 104.699 1.373   23.332  1.00   58.75  ? 314 PRO D C   1 
ATOM   11255 O O   . PRO D  1 314 ? 104.424 1.786   22.204  1.00   57.44  ? 314 PRO D O   1 
ATOM   11256 C CB  . PRO D  1 314 ? 106.887 2.520   23.834  1.00   60.13  ? 314 PRO D CB  1 
ATOM   11257 C CG  . PRO D  1 314 ? 107.643 1.453   24.512  1.00   61.31  ? 314 PRO D CG  1 
ATOM   11258 C CD  . PRO D  1 314 ? 106.985 1.245   25.852  1.00   64.35  ? 314 PRO D CD  1 
ATOM   11259 N N   . PHE D  1 315 ? 104.361 0.164   23.778  1.00   57.46  ? 315 PHE D N   1 
ATOM   11260 C CA  . PHE D  1 315 ? 103.755 -0.834  22.903  1.00   54.81  ? 315 PHE D CA  1 
ATOM   11261 C C   . PHE D  1 315 ? 102.252 -0.808  22.853  1.00   57.94  ? 315 PHE D C   1 
ATOM   11262 O O   . PHE D  1 315 ? 101.582 -0.351  23.780  1.00   60.76  ? 315 PHE D O   1 
ATOM   11263 C CB  . PHE D  1 315 ? 104.172 -2.231  23.309  1.00   54.16  ? 315 PHE D CB  1 
ATOM   11264 C CG  . PHE D  1 315 ? 105.631 -2.436  23.284  1.00   55.35  ? 315 PHE D CG  1 
ATOM   11265 C CD1 . PHE D  1 315 ? 106.317 -2.363  22.087  1.00   51.87  ? 315 PHE D CD1 1 
ATOM   11266 C CD2 . PHE D  1 315 ? 106.328 -2.710  24.440  1.00   60.15  ? 315 PHE D CD2 1 
ATOM   11267 C CE1 . PHE D  1 315 ? 107.676 -2.543  22.033  1.00   52.13  ? 315 PHE D CE1 1 
ATOM   11268 C CE2 . PHE D  1 315 ? 107.695 -2.906  24.393  1.00   59.56  ? 315 PHE D CE2 1 
ATOM   11269 C CZ  . PHE D  1 315 ? 108.369 -2.818  23.186  1.00   55.44  ? 315 PHE D CZ  1 
ATOM   11270 N N   . GLY D  1 316 ? 101.732 -1.330  21.751  1.00   57.46  ? 316 GLY D N   1 
ATOM   11271 C CA  . GLY D  1 316 ? 100.306 -1.372  21.526  1.00   58.31  ? 316 GLY D CA  1 
ATOM   11272 C C   . GLY D  1 316 ? 99.714  -2.761  21.642  1.00   57.33  ? 316 GLY D C   1 
ATOM   11273 O O   . GLY D  1 316 ? 98.514  -2.900  21.804  1.00   59.41  ? 316 GLY D O   1 
ATOM   11274 N N   . LEU D  1 317 ? 100.537 -3.793  21.514  1.00   55.04  ? 317 LEU D N   1 
ATOM   11275 C CA  . LEU D  1 317 ? 100.031 -5.160  21.576  1.00   53.29  ? 317 LEU D CA  1 
ATOM   11276 C C   . LEU D  1 317 ? 100.977 -6.015  22.401  1.00   53.71  ? 317 LEU D C   1 
ATOM   11277 O O   . LEU D  1 317 ? 102.080 -6.308  21.966  1.00   49.41  ? 317 LEU D O   1 
ATOM   11278 C CB  . LEU D  1 317 ? 99.856  -5.734  20.177  1.00   48.93  ? 317 LEU D CB  1 
ATOM   11279 C CG  . LEU D  1 317 ? 99.308  -7.156  20.118  1.00   49.80  ? 317 LEU D CG  1 
ATOM   11280 C CD1 . LEU D  1 317 ? 97.965  -7.250  20.796  1.00   52.05  ? 317 LEU D CD1 1 
ATOM   11281 C CD2 . LEU D  1 317 ? 99.213  -7.625  18.672  1.00   53.43  ? 317 LEU D CD2 1 
ATOM   11282 N N   . CYS D  1 318 ? 100.553 -6.393  23.601  1.00   58.25  ? 318 CYS D N   1 
ATOM   11283 C CA  . CYS D  1 318 ? 101.401 -7.149  24.504  1.00   59.18  ? 318 CYS D CA  1 
ATOM   11284 C C   . CYS D  1 318 ? 100.741 -8.461  24.906  1.00   64.76  ? 318 CYS D C   1 
ATOM   11285 O O   . CYS D  1 318 ? 99.515  -8.514  24.968  1.00   69.34  ? 318 CYS D O   1 
ATOM   11286 C CB  . CYS D  1 318 ? 101.690 -6.307  25.741  1.00   60.06  ? 318 CYS D CB  1 
ATOM   11287 S SG  . CYS D  1 318 ? 102.625 -4.820  25.374  1.00   61.49  ? 318 CYS D SG  1 
ATOM   11288 N N   . TYR D  1 319 ? 101.531 -9.500  25.204  1.00   65.45  ? 319 TYR D N   1 
ATOM   11289 C CA  . TYR D  1 319 ? 100.979 -10.809 25.593  1.00   68.48  ? 319 TYR D CA  1 
ATOM   11290 C C   . TYR D  1 319 ? 101.555 -11.356 26.903  1.00   70.86  ? 319 TYR D C   1 
ATOM   11291 O O   . TYR D  1 319 ? 102.608 -10.902 27.351  1.00   68.25  ? 319 TYR D O   1 
ATOM   11292 C CB  . TYR D  1 319 ? 101.240 -11.854 24.501  1.00   66.24  ? 319 TYR D CB  1 
ATOM   11293 C CG  . TYR D  1 319 ? 100.510 -11.628 23.205  1.00   66.37  ? 319 TYR D CG  1 
ATOM   11294 C CD1 . TYR D  1 319 ? 99.251  -12.160 23.000  1.00   68.73  ? 319 TYR D CD1 1 
ATOM   11295 C CD2 . TYR D  1 319 ? 101.104 -10.921 22.162  1.00   66.23  ? 319 TYR D CD2 1 
ATOM   11296 C CE1 . TYR D  1 319 ? 98.578  -11.970 21.806  1.00   69.74  ? 319 TYR D CE1 1 
ATOM   11297 C CE2 . TYR D  1 319 ? 100.443 -10.730 20.962  1.00   66.81  ? 319 TYR D CE2 1 
ATOM   11298 C CZ  . TYR D  1 319 ? 99.178  -11.255 20.792  1.00   69.11  ? 319 TYR D CZ  1 
ATOM   11299 O OH  . TYR D  1 319 ? 98.514  -11.060 19.604  1.00   69.01  ? 319 TYR D OH  1 
ATOM   11300 N N   . ASP D  1 320 ? 100.848 -12.301 27.535  1.00   75.72  ? 320 ASP D N   1 
ATOM   11301 C CA  . ASP D  1 320 ? 101.430 -13.082 28.634  1.00   77.56  ? 320 ASP D CA  1 
ATOM   11302 C C   . ASP D  1 320 ? 102.299 -14.178 27.991  1.00   74.02  ? 320 ASP D C   1 
ATOM   11303 O O   . ASP D  1 320 ? 101.877 -14.816 27.026  1.00   71.88  ? 320 ASP D O   1 
ATOM   11304 C CB  . ASP D  1 320 ? 100.364 -13.668 29.555  0.0000 81.30  ? 320 ASP D CB  1 
ATOM   11305 C CG  . ASP D  1 320 ? 100.954 -14.600 30.597  0.0000 83.65  ? 320 ASP D CG  1 
ATOM   11306 O OD1 . ASP D  1 320 ? 101.389 -14.101 31.660  0.0000 84.72  ? 320 ASP D OD1 1 
ATOM   11307 O OD2 . ASP D  1 320 ? 101.004 -15.821 30.357  0.0000 84.59  ? 320 ASP D OD2 1 
ATOM   11308 N N   . SER D  1 321 ? 103.505 -14.394 28.504  1.00   73.26  ? 321 SER D N   1 
ATOM   11309 C CA  . SER D  1 321 ? 104.456 -15.275 27.811  1.00   73.00  ? 321 SER D CA  1 
ATOM   11310 C C   . SER D  1 321 ? 104.313 -16.808 27.797  1.00   78.84  ? 321 SER D C   1 
ATOM   11311 O O   . SER D  1 321 ? 104.591 -17.412 26.761  1.00   80.61  ? 321 SER D O   1 
ATOM   11312 C CB  . SER D  1 321 ? 105.862 -14.955 28.316  1.00   70.57  ? 321 SER D CB  1 
ATOM   11313 O OG  . SER D  1 321 ? 106.106 -13.558 28.285  1.00   68.07  ? 321 SER D OG  1 
ATOM   11314 N N   . ARG D  1 322 ? 103.919 -17.463 28.889  1.00   81.13  ? 322 ARG D N   1 
ATOM   11315 C CA  . ARG D  1 322 ? 103.835 -18.927 28.815  1.00   82.88  ? 322 ARG D CA  1 
ATOM   11316 C C   . ARG D  1 322 ? 102.574 -19.354 28.090  1.00   84.68  ? 322 ARG D C   1 
ATOM   11317 O O   . ARG D  1 322 ? 102.339 -20.539 27.845  1.00   85.52  ? 322 ARG D O   1 
ATOM   11318 C CB  . ARG D  1 322 ? 103.911 -19.569 30.193  0.0000 86.09  ? 322 ARG D CB  1 
ATOM   11319 C CG  . ARG D  1 322 ? 105.176 -20.384 30.372  0.0000 86.07  ? 322 ARG D CG  1 
ATOM   11320 C CD  . ARG D  1 322 ? 105.116 -21.211 31.636  0.0000 90.55  ? 322 ARG D CD  1 
ATOM   11321 N NE  . ARG D  1 322 ? 103.868 -21.966 31.708  0.0000 93.42  ? 322 ARG D NE  1 
ATOM   11322 C CZ  . ARG D  1 322 ? 103.575 -22.840 32.666  0.0000 97.91  ? 322 ARG D CZ  1 
ATOM   11323 N NH1 . ARG D  1 322 ? 102.413 -23.484 32.654  0.0000 100.70 ? 322 ARG D NH1 1 
ATOM   11324 N NH2 . ARG D  1 322 ? 104.445 -23.071 33.639  0.0000 99.95  ? 322 ARG D NH2 1 
ATOM   11325 N N   . LYS D  1 323 ? 101.777 -18.353 27.745  1.00   86.58  ? 323 LYS D N   1 
ATOM   11326 C CA  . LYS D  1 323 ? 100.566 -18.514 26.962  1.00   90.92  ? 323 LYS D CA  1 
ATOM   11327 C C   . LYS D  1 323 ? 100.872 -18.606 25.471  1.00   91.60  ? 323 LYS D C   1 
ATOM   11328 O O   . LYS D  1 323 ? 100.212 -19.350 24.741  1.00   96.19  ? 323 LYS D O   1 
ATOM   11329 C CB  . LYS D  1 323 ? 99.606  -17.339 27.169  1.00   90.01  ? 323 LYS D CB  1 
ATOM   11330 C CG  . LYS D  1 323 ? 98.966  -17.159 28.528  1.00   92.74  ? 323 LYS D CG  1 
ATOM   11331 C CD  . LYS D  1 323 ? 97.586  -17.775 28.459  1.00   95.04  ? 323 LYS D CD  1 
ATOM   11332 C CE  . LYS D  1 323 ? 96.708  -17.369 29.625  1.00   98.03  ? 323 LYS D CE  1 
ATOM   11333 N NZ  . LYS D  1 323 ? 97.488  -16.882 30.778  1.00   99.00  ? 323 LYS D NZ  1 
ATOM   11334 N N   . ILE D  1 324 ? 101.823 -17.791 25.017  1.00   86.79  ? 324 ILE D N   1 
ATOM   11335 C CA  . ILE D  1 324 ? 102.207 -17.725 23.611  1.00   82.42  ? 324 ILE D CA  1 
ATOM   11336 C C   . ILE D  1 324 ? 103.456 -18.501 23.133  1.00   88.09  ? 324 ILE D C   1 
ATOM   11337 O O   . ILE D  1 324 ? 103.757 -18.463 21.943  1.00   86.38  ? 324 ILE D O   1 
ATOM   11338 C CB  . ILE D  1 324 ? 102.416 -16.248 23.208  1.00   71.73  ? 324 ILE D CB  1 
ATOM   11339 C CG1 . ILE D  1 324 ? 103.823 -15.792 23.619  0.0000 68.79  ? 324 ILE D CG1 1 
ATOM   11340 C CG2 . ILE D  1 324 ? 101.309 -15.349 23.792  0.0000 71.98  ? 324 ILE D CG2 1 
ATOM   11341 C CD1 . ILE D  1 324 ? 104.148 -14.368 23.180  0.0000 65.09  ? 324 ILE D CD1 1 
ATOM   11342 N N   . SER D  1 325 ? 104.207 -19.183 24.004  1.00   94.95  ? 325 SER D N   1 
ATOM   11343 C CA  . SER D  1 325 ? 105.354 -19.957 23.491  1.00   95.71  ? 325 SER D CA  1 
ATOM   11344 C C   . SER D  1 325 ? 104.886 -21.241 22.779  1.00   100.56 ? 325 SER D C   1 
ATOM   11345 O O   . SER D  1 325 ? 105.630 -22.214 22.668  1.00   102.92 ? 325 SER D O   1 
ATOM   11346 C CB  . SER D  1 325 ? 106.354 -20.280 24.602  1.00   94.24  ? 325 SER D CB  1 
ATOM   11347 O OG  . SER D  1 325 ? 107.080 -21.459 24.326  1.00   93.32  ? 325 SER D OG  1 
ATOM   11348 N N   . GLY D  1 326 ? 103.643 -21.208 22.299  1.00   101.82 ? 326 GLY D N   1 
ATOM   11349 C CA  . GLY D  1 326 ? 103.089 -22.188 21.387  1.00   101.94 ? 326 GLY D CA  1 
ATOM   11350 C C   . GLY D  1 326 ? 103.382 -21.774 19.943  1.00   96.75  ? 326 GLY D C   1 
ATOM   11351 O O   . GLY D  1 326 ? 102.807 -22.353 19.019  1.00   98.19  ? 326 GLY D O   1 
ATOM   11352 N N   . GLY D  1 327 ? 104.222 -20.747 19.742  1.00   89.26  ? 327 GLY D N   1 
ATOM   11353 C CA  . GLY D  1 327 ? 104.637 -20.352 18.397  1.00   81.27  ? 327 GLY D CA  1 
ATOM   11354 C C   . GLY D  1 327 ? 104.158 -19.011 17.844  1.00   75.11  ? 327 GLY D C   1 
ATOM   11355 O O   . GLY D  1 327 ? 102.957 -18.791 17.741  1.00   75.32  ? 327 GLY D O   1 
ATOM   11356 N N   . ALA D  1 328 ? 105.090 -18.109 17.520  1.00   71.32  ? 328 ALA D N   1 
ATOM   11357 C CA  . ALA D  1 328 ? 104.793 -16.808 16.871  1.00   69.37  ? 328 ALA D CA  1 
ATOM   11358 C C   . ALA D  1 328 ? 104.917 -16.851 15.337  1.00   69.41  ? 328 ALA D C   1 
ATOM   11359 O O   . ALA D  1 328 ? 105.673 -17.654 14.803  1.00   70.66  ? 328 ALA D O   1 
ATOM   11360 C CB  . ALA D  1 328 ? 105.694 -15.718 17.436  1.00   65.92  ? 328 ALA D CB  1 
ATOM   11361 N N   . PRO D  1 329 ? 104.181 -15.978 14.624  1.00   68.19  ? 329 PRO D N   1 
ATOM   11362 C CA  . PRO D  1 329 ? 104.122 -16.081 13.158  1.00   67.19  ? 329 PRO D CA  1 
ATOM   11363 C C   . PRO D  1 329 ? 105.333 -15.544 12.399  1.00   64.47  ? 329 PRO D C   1 
ATOM   11364 O O   . PRO D  1 329 ? 106.200 -14.854 12.950  1.00   60.35  ? 329 PRO D O   1 
ATOM   11365 C CB  . PRO D  1 329 ? 102.883 -15.243 12.799  1.00   66.27  ? 329 PRO D CB  1 
ATOM   11366 C CG  . PRO D  1 329 ? 102.750 -14.274 13.897  1.00   64.74  ? 329 PRO D CG  1 
ATOM   11367 C CD  . PRO D  1 329 ? 103.284 -14.926 15.136  1.00   66.90  ? 329 PRO D CD  1 
ATOM   11368 N N   . SER D  1 330 ? 105.386 -15.913 11.120  1.00   68.09  ? 330 SER D N   1 
ATOM   11369 C CA  . SER D  1 330 ? 106.314 -15.332 10.155  1.00   71.00  ? 330 SER D CA  1 
ATOM   11370 C C   . SER D  1 330 ? 106.094 -13.820 10.011  1.00   67.28  ? 330 SER D C   1 
ATOM   11371 O O   . SER D  1 330 ? 105.002 -13.371 9.674   1.00   71.03  ? 330 SER D O   1 
ATOM   11372 C CB  . SER D  1 330 ? 106.156 -16.013 8.785   1.00   76.34  ? 330 SER D CB  1 
ATOM   11373 O OG  . SER D  1 330 ? 105.295 -15.281 7.915   1.00   78.26  ? 330 SER D OG  1 
ATOM   11374 N N   . VAL D  1 331 ? 107.109 -13.022 10.302  1.00   59.45  ? 331 VAL D N   1 
ATOM   11375 C CA  . VAL D  1 331 ? 107.009 -11.601 9.984   1.00   52.71  ? 331 VAL D CA  1 
ATOM   11376 C C   . VAL D  1 331 ? 108.102 -11.175 9.008   1.00   48.25  ? 331 VAL D C   1 
ATOM   11377 O O   . VAL D  1 331 ? 109.278 -11.108 9.351   1.00   48.33  ? 331 VAL D O   1 
ATOM   11378 C CB  . VAL D  1 331 ? 107.058 -10.767 11.252  1.00   47.08  ? 331 VAL D CB  1 
ATOM   11379 C CG1 . VAL D  1 331 ? 107.080 -9.297  10.927  1.00   43.87  ? 331 VAL D CG1 1 
ATOM   11380 C CG2 . VAL D  1 331 ? 105.869 -11.147 12.129  1.00   45.71  ? 331 VAL D CG2 1 
ATOM   11381 N N   . ASP D  1 332 ? 107.713 -10.866 7.781   1.00   42.72  ? 332 ASP D N   1 
ATOM   11382 C CA  . ASP D  1 332 ? 108.707 -10.626 6.757   1.00   39.33  ? 332 ASP D CA  1 
ATOM   11383 C C   . ASP D  1 332 ? 108.517 -9.301  6.053   1.00   38.07  ? 332 ASP D C   1 
ATOM   11384 O O   . ASP D  1 332 ? 107.390 -8.927  5.725   1.00   38.47  ? 332 ASP D O   1 
ATOM   11385 C CB  . ASP D  1 332 ? 108.665 -11.764 5.744   1.00   45.65  ? 332 ASP D CB  1 
ATOM   11386 C CG  . ASP D  1 332 ? 108.810 -13.129 6.402   1.00   52.26  ? 332 ASP D CG  1 
ATOM   11387 O OD1 . ASP D  1 332 ? 109.433 -13.210 7.480   1.00   52.24  ? 332 ASP D OD1 1 
ATOM   11388 O OD2 . ASP D  1 332 ? 108.276 -14.120 5.860   1.00   56.06  ? 332 ASP D OD2 1 
ATOM   11389 N N   . LEU D  1 333 ? 109.632 -8.609  5.790   1.00   35.84  ? 333 LEU D N   1 
ATOM   11390 C CA  . LEU D  1 333 ? 109.627 -7.408  4.954   1.00   32.89  ? 333 LEU D CA  1 
ATOM   11391 C C   . LEU D  1 333 ? 109.771 -7.756  3.496   1.00   32.54  ? 333 LEU D C   1 
ATOM   11392 O O   . LEU D  1 333 ? 110.765 -8.339  3.123   1.00   32.65  ? 333 LEU D O   1 
ATOM   11393 C CB  . LEU D  1 333 ? 110.763 -6.486  5.338   1.00   29.76  ? 333 LEU D CB  1 
ATOM   11394 C CG  . LEU D  1 333 ? 110.753 -6.213  6.819   1.00   29.11  ? 333 LEU D CG  1 
ATOM   11395 C CD1 . LEU D  1 333 ? 111.876 -5.288  7.135   1.00   28.66  ? 333 LEU D CD1 1 
ATOM   11396 C CD2 . LEU D  1 333 ? 109.439 -5.571  7.148   1.00   30.15  ? 333 LEU D CD2 1 
ATOM   11397 N N   . ILE D  1 334 ? 108.772 -7.417  2.683   1.00   34.05  ? 334 ILE D N   1 
ATOM   11398 C CA  . ILE D  1 334 ? 108.883 -7.623  1.252   1.00   35.26  ? 334 ILE D CA  1 
ATOM   11399 C C   . ILE D  1 334 ? 109.482 -6.359  0.676   1.00   36.66  ? 334 ILE D C   1 
ATOM   11400 O O   . ILE D  1 334 ? 108.911 -5.268  0.765   1.00   36.37  ? 334 ILE D O   1 
ATOM   11401 C CB  . ILE D  1 334 ? 107.554 -7.943  0.585   1.00   37.26  ? 334 ILE D CB  1 
ATOM   11402 C CG1 . ILE D  1 334 ? 106.803 -9.009  1.386   1.00   40.43  ? 334 ILE D CG1 1 
ATOM   11403 C CG2 . ILE D  1 334 ? 107.793 -8.425  -0.834  1.00   38.66  ? 334 ILE D CG2 1 
ATOM   11404 C CD1 . ILE D  1 334 ? 107.553 -10.304 1.531   1.00   41.38  ? 334 ILE D CD1 1 
ATOM   11405 N N   . LEU D  1 335 ? 110.640 -6.539  0.059   1.00   38.56  ? 335 LEU D N   1 
ATOM   11406 C CA  . LEU D  1 335 ? 111.500 -5.430  -0.301  1.00   39.88  ? 335 LEU D CA  1 
ATOM   11407 C C   . LEU D  1 335 ? 111.345 -5.014  -1.750  1.00   45.35  ? 335 LEU D C   1 
ATOM   11408 O O   . LEU D  1 335 ? 110.565 -5.598  -2.490  1.00   49.14  ? 335 LEU D O   1 
ATOM   11409 C CB  . LEU D  1 335 ? 112.946 -5.793  0.023   1.00   37.54  ? 335 LEU D CB  1 
ATOM   11410 C CG  . LEU D  1 335 ? 113.092 -6.183  1.492   1.00   34.56  ? 335 LEU D CG  1 
ATOM   11411 C CD1 . LEU D  1 335 ? 114.506 -6.570  1.751   1.00   34.53  ? 335 LEU D CD1 1 
ATOM   11412 C CD2 . LEU D  1 335 ? 112.703 -5.010  2.376   1.00   31.32  ? 335 LEU D CD2 1 
ATOM   11413 N N   . ASP D  1 336 ? 112.097 -3.984  -2.115  1.00   49.36  ? 336 ASP D N   1 
ATOM   11414 C CA  . ASP D  1 336 ? 112.021 -3.280  -3.383  1.00   60.51  ? 336 ASP D CA  1 
ATOM   11415 C C   . ASP D  1 336 ? 111.821 -4.259  -4.540  1.00   69.13  ? 336 ASP D C   1 
ATOM   11416 O O   . ASP D  1 336 ? 112.598 -5.203  -4.674  1.00   72.05  ? 336 ASP D O   1 
ATOM   11417 C CB  . ASP D  1 336 ? 113.334 -2.477  -3.549  1.00   64.44  ? 336 ASP D CB  1 
ATOM   11418 C CG  . ASP D  1 336 ? 113.322 -1.509  -4.730  1.00   70.45  ? 336 ASP D CG  1 
ATOM   11419 O OD1 . ASP D  1 336 ? 112.320 -0.786  -4.930  1.00   73.93  ? 336 ASP D OD1 1 
ATOM   11420 O OD2 . ASP D  1 336 ? 114.344 -1.445  -5.440  1.00   72.07  ? 336 ASP D OD2 1 
ATOM   11421 N N   . LYS D  1 337 ? 110.755 -4.058  -5.330  1.00   74.30  ? 337 LYS D N   1 
ATOM   11422 C CA  . LYS D  1 337 ? 110.488 -4.842  -6.557  1.00   77.25  ? 337 LYS D CA  1 
ATOM   11423 C C   . LYS D  1 337 ? 110.255 -6.338  -6.247  1.00   78.26  ? 337 LYS D C   1 
ATOM   11424 O O   . LYS D  1 337 ? 110.474 -7.201  -7.098  1.00   81.06  ? 337 LYS D O   1 
ATOM   11425 C CB  . LYS D  1 337 ? 111.623 -4.657  -7.584  1.00   76.21  ? 337 LYS D CB  1 
ATOM   11426 C CG  . LYS D  1 337 ? 111.154 -4.284  -9.004  1.00   76.70  ? 337 LYS D CG  1 
ATOM   11427 C CD  . LYS D  1 337 ? 110.992 -2.767  -9.189  1.00   75.08  ? 337 LYS D CD  1 
ATOM   11428 C CE  . LYS D  1 337 ? 110.034 -2.424  -10.338 1.00   76.54  ? 337 LYS D CE  1 
ATOM   11429 N NZ  . LYS D  1 337 ? 108.607 -2.750  -10.039 1.00   76.82  ? 337 LYS D NZ  1 
ATOM   11430 N N   . ASN D  1 338 ? 109.791 -6.607  -5.026  1.00   76.35  ? 338 ASN D N   1 
ATOM   11431 C CA  . ASN D  1 338 ? 109.689 -7.937  -4.394  1.00   76.20  ? 338 ASN D CA  1 
ATOM   11432 C C   . ASN D  1 338 ? 110.673 -9.013  -4.887  1.00   77.41  ? 338 ASN D C   1 
ATOM   11433 O O   . ASN D  1 338 ? 110.292 -10.179 -5.057  1.00   80.95  ? 338 ASN D O   1 
ATOM   11434 C CB  . ASN D  1 338 ? 108.266 -8.482  -4.595  1.00   78.95  ? 338 ASN D CB  1 
ATOM   11435 C CG  . ASN D  1 338 ? 107.183 -7.456  -4.269  1.00   80.59  ? 338 ASN D CG  1 
ATOM   11436 O OD1 . ASN D  1 338 ? 107.296 -6.691  -3.315  1.00   82.66  ? 338 ASN D OD1 1 
ATOM   11437 N ND2 . ASN D  1 338 ? 106.115 -7.452  -5.064  1.00   80.10  ? 338 ASN D ND2 1 
ATOM   11438 N N   . ASP D  1 339 ? 111.940 -8.625  -5.064  1.00   74.41  ? 339 ASP D N   1 
ATOM   11439 C CA  . ASP D  1 339 ? 113.008 -9.550  -5.451  1.00   72.92  ? 339 ASP D CA  1 
ATOM   11440 C C   . ASP D  1 339 ? 113.547 -10.274 -4.218  1.00   67.33  ? 339 ASP D C   1 
ATOM   11441 O O   . ASP D  1 339 ? 114.163 -11.339 -4.318  1.00   71.04  ? 339 ASP D O   1 
ATOM   11442 C CB  . ASP D  1 339 ? 114.158 -8.815  -6.170  1.00   74.68  ? 339 ASP D CB  1 
ATOM   11443 C CG  . ASP D  1 339 ? 113.766 -8.282  -7.550  1.00   79.76  ? 339 ASP D CG  1 
ATOM   11444 O OD1 . ASP D  1 339 ? 113.402 -9.088  -8.433  1.00   81.72  ? 339 ASP D OD1 1 
ATOM   11445 O OD2 . ASP D  1 339 ? 113.864 -7.056  -7.769  1.00   81.75  1 339 ASP D OD2 1 
ATOM   11446 N N   . ALA D  1 340 ? 113.320 -9.669  -3.059  1.00   56.09  ? 340 ALA D N   1 
ATOM   11447 C CA  . ALA D  1 340 ? 113.952 -10.116 -1.838  1.00   48.44  ? 340 ALA D CA  1 
ATOM   11448 C C   . ALA D  1 340 ? 113.015 -9.991  -0.667  1.00   43.99  ? 340 ALA D C   1 
ATOM   11449 O O   . ALA D  1 340 ? 111.988 -9.332  -0.754  1.00   44.47  ? 340 ALA D O   1 
ATOM   11450 C CB  . ALA D  1 340 ? 115.227 -9.320  -1.580  1.00   47.43  ? 340 ALA D CB  1 
ATOM   11451 N N   . VAL D  1 341 ? 113.371 -10.653 0.424   1.00   41.72  ? 341 VAL D N   1 
ATOM   11452 C CA  . VAL D  1 341 ? 112.548 -10.691 1.619   1.00   38.80  ? 341 VAL D CA  1 
ATOM   11453 C C   . VAL D  1 341 ? 113.504 -10.534 2.787   1.00   36.38  ? 341 VAL D C   1 
ATOM   11454 O O   . VAL D  1 341 ? 114.531 -11.192 2.817   1.00   37.81  ? 341 VAL D O   1 
ATOM   11455 C CB  . VAL D  1 341 ? 111.759 -12.026 1.748   1.00   36.34  ? 341 VAL D CB  1 
ATOM   11456 C CG1 . VAL D  1 341 ? 111.100 -12.131 3.111   1.00   35.74  ? 341 VAL D CG1 1 
ATOM   11457 C CG2 . VAL D  1 341 ? 110.683 -12.113 0.696   1.00   37.98  ? 341 VAL D CG2 1 
ATOM   11458 N N   . TRP D  1 342 ? 113.197 -9.666  3.738   1.00   35.07  ? 342 TRP D N   1 
ATOM   11459 C CA  . TRP D  1 342 ? 113.960 -9.635  4.990   1.00   33.59  ? 342 TRP D CA  1 
ATOM   11460 C C   . TRP D  1 342 ? 113.144 -10.265 6.097   1.00   38.33  ? 342 TRP D C   1 
ATOM   11461 O O   . TRP D  1 342 ? 112.288 -9.605  6.708   1.00   37.95  ? 342 TRP D O   1 
ATOM   11462 C CB  . TRP D  1 342 ? 114.352 -8.204  5.392   1.00   32.05  ? 342 TRP D CB  1 
ATOM   11463 C CG  . TRP D  1 342 ? 115.499 -8.145  6.399   1.00   33.75  ? 342 TRP D CG  1 
ATOM   11464 C CD1 . TRP D  1 342 ? 115.954 -9.168  7.197   1.00   37.20  ? 342 TRP D CD1 1 
ATOM   11465 C CD2 . TRP D  1 342 ? 116.361 -7.032  6.662   1.00   33.80  ? 342 TRP D CD2 1 
ATOM   11466 N NE1 . TRP D  1 342 ? 117.020 -8.752  7.957   1.00   36.23  ? 342 TRP D NE1 1 
ATOM   11467 C CE2 . TRP D  1 342 ? 117.297 -7.447  7.647   1.00   35.15  ? 342 TRP D CE2 1 
ATOM   11468 C CE3 . TRP D  1 342 ? 116.429 -5.719  6.173   1.00   31.90  ? 342 TRP D CE3 1 
ATOM   11469 C CZ2 . TRP D  1 342 ? 118.282 -6.596  8.151   1.00   33.12  ? 342 TRP D CZ2 1 
ATOM   11470 C CZ3 . TRP D  1 342 ? 117.408 -4.879  6.672   1.00   32.27  ? 342 TRP D CZ3 1 
ATOM   11471 C CH2 . TRP D  1 342 ? 118.323 -5.320  7.653   1.00   31.66  ? 342 TRP D CH2 1 
ATOM   11472 N N   . ARG D  1 343 ? 113.404 -11.542 6.357   1.00   41.42  ? 343 ARG D N   1 
ATOM   11473 C CA  . ARG D  1 343 ? 112.672 -12.261 7.380   1.00   44.49  ? 343 ARG D CA  1 
ATOM   11474 C C   . ARG D  1 343 ? 113.121 -11.876 8.777   1.00   42.05  ? 343 ARG D C   1 
ATOM   11475 O O   . ARG D  1 343 ? 114.298 -11.769 9.057   1.00   41.34  ? 343 ARG D O   1 
ATOM   11476 C CB  . ARG D  1 343 ? 112.777 -13.758 7.139   1.00   52.40  ? 343 ARG D CB  1 
ATOM   11477 C CG  . ARG D  1 343 ? 111.983 -14.126 5.898   1.00   62.01  ? 343 ARG D CG  1 
ATOM   11478 C CD  . ARG D  1 343 ? 111.739 -15.605 5.748   1.00   72.40  ? 343 ARG D CD  1 
ATOM   11479 N NE  . ARG D  1 343 ? 112.981 -16.335 5.548   1.00   78.15  ? 343 ARG D NE  1 
ATOM   11480 C CZ  . ARG D  1 343 ? 113.536 -16.523 4.358   1.00   80.54  ? 343 ARG D CZ  1 
ATOM   11481 N NH1 . ARG D  1 343 ? 112.953 -16.028 3.268   1.00   81.39  ? 343 ARG D NH1 1 
ATOM   11482 N NH2 . ARG D  1 343 ? 114.671 -17.206 4.259   1.00   80.38  ? 343 ARG D NH2 1 
ATOM   11483 N N   . ILE D  1 344 ? 112.149 -11.649 9.646   1.00   44.96  ? 344 ILE D N   1 
ATOM   11484 C CA  . ILE D  1 344 ? 112.410 -11.264 11.017  1.00   45.44  ? 344 ILE D CA  1 
ATOM   11485 C C   . ILE D  1 344 ? 112.039 -12.372 11.983  1.00   51.36  ? 344 ILE D C   1 
ATOM   11486 O O   . ILE D  1 344 ? 110.899 -12.848 12.013  1.00   54.93  ? 344 ILE D O   1 
ATOM   11487 C CB  . ILE D  1 344 ? 111.636 -9.988  11.376  1.00   41.43  ? 344 ILE D CB  1 
ATOM   11488 C CG1 . ILE D  1 344 ? 111.967 -8.892  10.376  1.00   41.00  ? 344 ILE D CG1 1 
ATOM   11489 C CG2 . ILE D  1 344 ? 111.975 -9.515  12.752  1.00   40.30  ? 344 ILE D CG2 1 
ATOM   11490 C CD1 . ILE D  1 344 ? 111.184 -7.635  10.584  1.00   42.10  ? 344 ILE D CD1 1 
ATOM   11491 N N   . SER D  1 345 ? 113.025 -12.790 12.760  1.00   54.82  ? 345 SER D N   1 
ATOM   11492 C CA  . SER D  1 345 ? 112.835 -13.861 13.717  1.00   61.49  ? 345 SER D CA  1 
ATOM   11493 C C   . SER D  1 345 ? 111.971 -13.358 14.874  1.00   59.05  ? 345 SER D C   1 
ATOM   11494 O O   . SER D  1 345 ? 112.057 -12.193 15.267  1.00   56.58  ? 345 SER D O   1 
ATOM   11495 C CB  . SER D  1 345 ? 114.195 -14.388 14.208  1.00   67.37  ? 345 SER D CB  1 
ATOM   11496 O OG  . SER D  1 345 ? 114.114 -15.027 15.478  1.00   73.29  ? 345 SER D OG  1 
ATOM   11497 N N   . SER D  1 346 ? 111.124 -14.233 15.402  1.00   59.12  ? 346 SER D N   1 
ATOM   11498 C CA  . SER D  1 346 ? 110.274 -13.866 16.518  1.00   60.72  ? 346 SER D CA  1 
ATOM   11499 C C   . SER D  1 346 ? 111.096 -13.704 17.776  1.00   58.88  ? 346 SER D C   1 
ATOM   11500 O O   . SER D  1 346 ? 110.606 -13.167 18.753  1.00   58.00  ? 346 SER D O   1 
ATOM   11501 C CB  . SER D  1 346 ? 109.155 -14.895 16.736  1.00   67.18  ? 346 SER D CB  1 
ATOM   11502 O OG  . SER D  1 346 ? 109.621 -16.082 17.344  1.00   70.93  ? 346 SER D OG  1 
ATOM   11503 N N   . GLU D  1 347 ? 112.362 -14.102 17.742  1.00   58.65  ? 347 GLU D N   1 
ATOM   11504 C CA  . GLU D  1 347 ? 113.207 -13.920 18.906  1.00   61.20  ? 347 GLU D CA  1 
ATOM   11505 C C   . GLU D  1 347 ? 113.754 -12.505 18.818  1.00   59.72  ? 347 GLU D C   1 
ATOM   11506 O O   . GLU D  1 347 ? 114.241 -11.940 19.795  1.00   61.53  ? 347 GLU D O   1 
ATOM   11507 C CB  . GLU D  1 347 ? 114.342 -14.965 18.925  1.00   64.64  ? 347 GLU D CB  1 
ATOM   11508 C CG  . GLU D  1 347 ? 113.852 -16.412 18.753  1.00   72.77  ? 347 GLU D CG  1 
ATOM   11509 C CD  . GLU D  1 347 ? 114.899 -17.483 19.103  1.00   79.78  ? 347 GLU D CD  1 
ATOM   11510 O OE1 . GLU D  1 347 ? 116.062 -17.117 19.386  1.00   82.07  ? 347 GLU D OE1 1 
ATOM   11511 O OE2 . GLU D  1 347 ? 114.554 -18.694 19.080  1.00   81.22  ? 347 GLU D OE2 1 
ATOM   11512 N N   . ASN D  1 348 ? 113.607 -11.915 17.638  1.00   57.02  ? 348 ASN D N   1 
ATOM   11513 C CA  . ASN D  1 348 ? 113.969 -10.525 17.426  1.00   58.53  ? 348 ASN D CA  1 
ATOM   11514 C C   . ASN D  1 348 ? 112.788 -9.547  17.652  1.00   61.49  ? 348 ASN D C   1 
ATOM   11515 O O   . ASN D  1 348 ? 112.971 -8.537  18.343  1.00   66.22  ? 348 ASN D O   1 
ATOM   11516 C CB  . ASN D  1 348 ? 114.598 -10.381 16.025  1.00   59.84  ? 348 ASN D CB  1 
ATOM   11517 C CG  . ASN D  1 348 ? 115.181 -8.987  15.752  1.00   58.80  ? 348 ASN D CG  1 
ATOM   11518 O OD1 . ASN D  1 348 ? 114.492 -7.974  15.841  1.00   57.66  ? 348 ASN D OD1 1 
ATOM   11519 N ND2 . ASN D  1 348 ? 116.478 -8.946  15.437  1.00   57.61  ? 348 ASN D ND2 1 
ATOM   11520 N N   . PHE D  1 349 ? 111.588 -9.832  17.117  1.00   55.33  ? 349 PHE D N   1 
ATOM   11521 C CA  . PHE D  1 349 ? 110.495 -8.832  17.169  1.00   49.41  ? 349 PHE D CA  1 
ATOM   11522 C C   . PHE D  1 349 ? 109.593 -8.913  18.393  1.00   49.08  ? 349 PHE D C   1 
ATOM   11523 O O   . PHE D  1 349 ? 108.720 -8.064  18.563  1.00   49.55  ? 349 PHE D O   1 
ATOM   11524 C CB  . PHE D  1 349 ? 109.603 -8.870  15.912  1.00   42.86  ? 349 PHE D CB  1 
ATOM   11525 C CG  . PHE D  1 349 ? 108.798 -10.135 15.721  1.00   42.20  ? 349 PHE D CG  1 
ATOM   11526 C CD1 . PHE D  1 349 ? 107.701 -10.421 16.519  1.00   45.15  ? 349 PHE D CD1 1 
ATOM   11527 C CD2 . PHE D  1 349 ? 109.075 -10.983 14.659  1.00   42.95  ? 349 PHE D CD2 1 
ATOM   11528 C CE1 . PHE D  1 349 ? 106.940 -11.567 16.304  1.00   49.63  ? 349 PHE D CE1 1 
ATOM   11529 C CE2 . PHE D  1 349 ? 108.314 -12.135 14.428  1.00   45.82  ? 349 PHE D CE2 1 
ATOM   11530 C CZ  . PHE D  1 349 ? 107.246 -12.426 15.252  1.00   49.91  ? 349 PHE D CZ  1 
ATOM   11531 N N   . MET D  1 350 ? 109.781 -9.944  19.212  1.00   50.70  ? 350 MET D N   1 
ATOM   11532 C CA  . MET D  1 350 ? 109.129 -10.039 20.521  1.00   52.47  ? 350 MET D CA  1 
ATOM   11533 C C   . MET D  1 350 ? 110.040 -9.514  21.613  1.00   55.19  ? 350 MET D C   1 
ATOM   11534 O O   . MET D  1 350 ? 111.198 -9.914  21.722  1.00   55.18  ? 350 MET D O   1 
ATOM   11535 C CB  . MET D  1 350 ? 108.735 -11.465 20.862  1.00   52.79  ? 350 MET D CB  1 
ATOM   11536 C CG  . MET D  1 350 ? 107.673 -12.033 19.989  1.00   55.45  ? 350 MET D CG  1 
ATOM   11537 S SD  . MET D  1 350 ? 106.249 -10.945 19.942  1.00   67.72  ? 350 MET D SD  1 
ATOM   11538 C CE  . MET D  1 350 ? 105.859 -10.854 21.677  1.00   52.47  ? 350 MET D CE  1 
ATOM   11539 N N   . VAL D  1 351 ? 109.512 -8.603  22.414  1.00   59.07  ? 351 VAL D N   1 
ATOM   11540 C CA  . VAL D  1 351 ? 110.281 -7.983  23.471  1.00   62.19  ? 351 VAL D CA  1 
ATOM   11541 C C   . VAL D  1 351 ? 109.791 -8.448  24.836  1.00   64.41  ? 351 VAL D C   1 
ATOM   11542 O O   . VAL D  1 351 ? 108.608 -8.583  25.074  1.00   66.02  ? 351 VAL D O   1 
ATOM   11543 C CB  . VAL D  1 351 ? 110.189 -6.443  23.367  1.00   64.13  ? 351 VAL D CB  1 
ATOM   11544 C CG1 . VAL D  1 351 ? 111.061 -5.762  24.395  1.00   66.02  ? 351 VAL D CG1 1 
ATOM   11545 C CG2 . VAL D  1 351 ? 110.570 -5.984  21.959  1.00   63.59  ? 351 VAL D CG2 1 
ATOM   11546 N N   . GLN D  1 352 ? 110.722 -8.630  25.747  1.00   66.25  ? 352 GLN D N   1 
ATOM   11547 C CA  . GLN D  1 352 ? 110.437 -9.098  27.086  1.00   72.58  ? 352 GLN D CA  1 
ATOM   11548 C C   . GLN D  1 352 ? 110.312 -7.903  28.013  1.00   75.15  ? 352 GLN D C   1 
ATOM   11549 O O   . GLN D  1 352 ? 111.291 -7.208  28.262  1.00   76.79  ? 352 GLN D O   1 
ATOM   11550 C CB  . GLN D  1 352 ? 111.578 -10.014 27.517  1.00   76.33  ? 352 GLN D CB  1 
ATOM   11551 C CG  . GLN D  1 352 ? 111.579 -10.617 28.905  1.00   82.12  ? 352 GLN D CG  1 
ATOM   11552 C CD  . GLN D  1 352 ? 112.862 -11.455 29.096  1.00   84.76  ? 352 GLN D CD  1 
ATOM   11553 O OE1 . GLN D  1 352 ? 113.865 -11.280 28.364  1.00   83.18  ? 352 GLN D OE1 1 
ATOM   11554 N NE2 . GLN D  1 352 ? 112.840 -12.353 30.077  1.00   88.16  ? 352 GLN D NE2 1 
ATOM   11555 N N   . ALA D  1 353 ? 109.115 -7.637  28.512  1.00   76.69  ? 353 ALA D N   1 
ATOM   11556 C CA  . ALA D  1 353 ? 108.951 -6.563  29.481  1.00   76.27  ? 353 ALA D CA  1 
ATOM   11557 C C   . ALA D  1 353 ? 109.324 -7.074  30.853  1.00   80.21  ? 353 ALA D C   1 
ATOM   11558 O O   . ALA D  1 353 ? 110.494 -7.201  31.209  1.00   83.56  ? 353 ALA D O   1 
ATOM   11559 C CB  . ALA D  1 353 ? 107.529 -6.045  29.473  1.00   74.38  ? 353 ALA D CB  1 
ATOM   11560 N N   . GLN D  1 354 ? 108.304 -7.406  31.609  1.00   79.22  ? 354 GLN D N   1 
ATOM   11561 C CA  . GLN D  1 354 ? 108.490 -7.878  32.953  1.00   80.65  ? 354 GLN D CA  1 
ATOM   11562 C C   . GLN D  1 354 ? 107.524 -8.975  33.063  1.00   79.92  ? 354 GLN D C   1 
ATOM   11563 O O   . GLN D  1 354 ? 106.704 -9.145  32.168  1.00   81.31  ? 354 GLN D O   1 
ATOM   11564 C CB  . GLN D  1 354 ? 108.153 -6.833  33.996  1.00   84.97  ? 354 GLN D CB  1 
ATOM   11565 C CG  . GLN D  1 354 ? 109.235 -5.878  34.354  1.00   87.31  ? 354 GLN D CG  1 
ATOM   11566 C CD  . GLN D  1 354 ? 108.688 -4.806  35.261  1.00   91.49  ? 354 GLN D CD  1 
ATOM   11567 O OE1 . GLN D  1 354 ? 108.233 -5.088  36.375  1.00   93.30  ? 354 GLN D OE1 1 
ATOM   11568 N NE2 . GLN D  1 354 ? 108.654 -3.580  34.763  1.00   92.61  ? 354 GLN D NE2 1 
ATOM   11569 N N   . ASP D  1 355 ? 107.641 -9.750  34.122  1.00   79.62  ? 355 ASP D N   1 
ATOM   11570 C CA  . ASP D  1 355 ? 106.535 -10.595 34.486  1.00   85.52  ? 355 ASP D CA  1 
ATOM   11571 C C   . ASP D  1 355 ? 106.107 -11.552 33.397  1.00   82.91  ? 355 ASP D C   1 
ATOM   11572 O O   . ASP D  1 355 ? 104.913 -11.815 33.258  1.00   83.16  ? 355 ASP D O   1 
ATOM   11573 C CB  . ASP D  1 355 ? 105.325 -9.727  34.844  1.00   90.23  ? 355 ASP D CB  1 
ATOM   11574 C CG  . ASP D  1 355 ? 105.569 -8.853  36.046  1.00   96.13  ? 355 ASP D CG  1 
ATOM   11575 O OD1 . ASP D  1 355 ? 106.717 -8.392  36.220  1.00   97.28  ? 355 ASP D OD1 1 
ATOM   11576 O OD2 . ASP D  1 355 ? 104.603 -8.594  36.796  1.00   99.40  ? 355 ASP D OD2 1 
ATOM   11577 N N   . GLY D  1 356 ? 107.029 -12.030 32.577  1.00   81.68  ? 356 GLY D N   1 
ATOM   11578 C CA  . GLY D  1 356 ? 106.577 -12.947 31.555  1.00   82.63  ? 356 GLY D CA  1 
ATOM   11579 C C   . GLY D  1 356 ? 105.596 -12.267 30.624  1.00   81.20  ? 356 GLY D C   1 
ATOM   11580 O O   . GLY D  1 356 ? 104.626 -12.873 30.177  1.00   82.16  ? 356 GLY D O   1 
ATOM   11581 N N   . VAL D  1 357 ? 105.809 -10.985 30.376  1.00   78.30  ? 357 VAL D N   1 
ATOM   11582 C CA  . VAL D  1 357 ? 104.968 -10.293 29.428  1.00   72.80  ? 357 VAL D CA  1 
ATOM   11583 C C   . VAL D  1 357 ? 105.856 -9.894  28.280  1.00   71.06  ? 357 VAL D C   1 
ATOM   11584 O O   . VAL D  1 357 ? 106.864 -9.221  28.454  1.00   71.32  ? 357 VAL D O   1 
ATOM   11585 C CB  . VAL D  1 357 ? 104.296 -9.071  30.039  1.00   69.23  ? 357 VAL D CB  1 
ATOM   11586 C CG1 . VAL D  1 357 ? 103.485 -8.349  28.998  1.00   66.33  ? 357 VAL D CG1 1 
ATOM   11587 C CG2 . VAL D  1 357 ? 103.426 -9.501  31.182  1.00   69.48  ? 357 VAL D CG2 1 
ATOM   11588 N N   . SER D  1 358 ? 105.483 -10.366 27.103  1.00   69.26  ? 358 SER D N   1 
ATOM   11589 C CA  . SER D  1 358 ? 106.245 -10.134 25.895  1.00   67.10  ? 358 SER D CA  1 
ATOM   11590 C C   . SER D  1 358 ? 105.435 -9.356  24.868  1.00   62.77  ? 358 SER D C   1 
ATOM   11591 O O   . SER D  1 358 ? 104.303 -9.721  24.547  1.00   59.54  ? 358 SER D O   1 
ATOM   11592 C CB  . SER D  1 358 ? 106.723 -11.453 25.310  1.00   70.56  ? 358 SER D CB  1 
ATOM   11593 O OG  . SER D  1 358 ? 105.624 -12.329 25.208  1.00   74.69  ? 358 SER D OG  1 
ATOM   11594 N N   . CYS D  1 359 ? 106.012 -8.258  24.390  1.00   62.14  ? 359 CYS D N   1 
ATOM   11595 C CA  . CYS D  1 359 ? 105.304 -7.341  23.520  1.00   49.80  ? 359 CYS D CA  1 
ATOM   11596 C C   . CYS D  1 359 ? 105.808 -7.339  22.094  1.00   46.91  ? 359 CYS D C   1 
ATOM   11597 O O   . CYS D  1 359 ? 106.988 -7.563  21.830  1.00   45.37  ? 359 CYS D O   1 
ATOM   11598 C CB  . CYS D  1 359 ? 105.377 -5.935  24.084  1.00   49.95  ? 359 CYS D CB  1 
ATOM   11599 S SG  . CYS D  1 359 ? 104.439 -5.729  25.597  1.00   76.48  ? 359 CYS D SG  1 
ATOM   11600 N N   . LEU D  1 360 ? 104.893 -7.063  21.177  1.00   46.40  ? 360 LEU D N   1 
ATOM   11601 C CA  . LEU D  1 360 ? 105.222 -6.929  19.773  1.00   43.99  ? 360 LEU D CA  1 
ATOM   11602 C C   . LEU D  1 360 ? 106.072 -5.678  19.623  1.00   50.60  ? 360 LEU D C   1 
ATOM   11603 O O   . LEU D  1 360 ? 105.609 -4.579  19.904  1.00   50.36  ? 360 LEU D O   1 
ATOM   11604 C CB  . LEU D  1 360 ? 103.950 -6.839  18.942  1.00   44.41  ? 360 LEU D CB  1 
ATOM   11605 C CG  . LEU D  1 360 ? 104.103 -6.675  17.439  1.00   45.15  ? 360 LEU D CG  1 
ATOM   11606 C CD1 . LEU D  1 360 ? 104.816 -7.883  16.897  1.00   43.86  ? 360 LEU D CD1 1 
ATOM   11607 C CD2 . LEU D  1 360 ? 102.751 -6.471  16.754  1.00   47.14  ? 360 LEU D CD2 1 
ATOM   11608 N N   . GLY D  1 361 ? 107.316 -5.836  19.180  1.00   50.01  ? 361 GLY D N   1 
ATOM   11609 C CA  . GLY D  1 361 ? 108.269 -4.746  19.259  1.00   47.96  ? 361 GLY D CA  1 
ATOM   11610 C C   . GLY D  1 361 ? 108.165 -3.649  18.217  1.00   46.43  ? 361 GLY D C   1 
ATOM   11611 O O   . GLY D  1 361 ? 109.162 -3.263  17.634  1.00   46.06  ? 361 GLY D O   1 
ATOM   11612 N N   . PHE D  1 362 ? 106.968 -3.120  17.992  1.00   47.71  ? 362 PHE D N   1 
ATOM   11613 C CA  . PHE D  1 362 ? 106.792 -1.977  17.086  1.00   46.45  ? 362 PHE D CA  1 
ATOM   11614 C C   . PHE D  1 362 ? 106.078 -0.798  17.764  1.00   47.81  ? 362 PHE D C   1 
ATOM   11615 O O   . PHE D  1 362 ? 105.191 -1.021  18.576  1.00   51.99  ? 362 PHE D O   1 
ATOM   11616 C CB  . PHE D  1 362 ? 106.012 -2.406  15.850  1.00   44.60  ? 362 PHE D CB  1 
ATOM   11617 C CG  . PHE D  1 362 ? 106.703 -3.449  15.033  1.00   44.15  ? 362 PHE D CG  1 
ATOM   11618 C CD1 . PHE D  1 362 ? 106.737 -4.772  15.453  1.00   45.73  ? 362 PHE D CD1 1 
ATOM   11619 C CD2 . PHE D  1 362 ? 107.316 -3.118  13.844  1.00   43.45  ? 362 PHE D CD2 1 
ATOM   11620 C CE1 . PHE D  1 362 ? 107.366 -5.743  14.709  1.00   43.40  ? 362 PHE D CE1 1 
ATOM   11621 C CE2 . PHE D  1 362 ? 107.946 -4.084  13.096  1.00   43.09  ? 362 PHE D CE2 1 
ATOM   11622 C CZ  . PHE D  1 362 ? 107.967 -5.404  13.534  1.00   43.59  ? 362 PHE D CZ  1 
ATOM   11623 N N   . VAL D  1 363 ? 106.474 0.440   17.457  1.00   44.44  ? 363 VAL D N   1 
ATOM   11624 C CA  . VAL D  1 363 ? 105.878 1.606   18.104  1.00   44.08  ? 363 VAL D CA  1 
ATOM   11625 C C   . VAL D  1 363 ? 105.228 2.597   17.117  1.00   40.46  ? 363 VAL D C   1 
ATOM   11626 O O   . VAL D  1 363 ? 105.670 2.771   15.992  1.00   44.29  ? 363 VAL D O   1 
ATOM   11627 C CB  . VAL D  1 363 ? 106.932 2.311   18.955  1.00   44.32  ? 363 VAL D CB  1 
ATOM   11628 C CG1 . VAL D  1 363 ? 106.361 3.539   19.614  1.00   50.26  ? 363 VAL D CG1 1 
ATOM   11629 C CG2 . VAL D  1 363 ? 107.435 1.354   20.005  1.00   41.03  ? 363 VAL D CG2 1 
ATOM   11630 N N   . ASP D  1 364 ? 104.169 3.249   17.561  1.00   42.53  ? 364 ASP D N   1 
ATOM   11631 C CA  . ASP D  1 364 ? 103.418 4.160   16.721  1.00   43.90  ? 364 ASP D CA  1 
ATOM   11632 C C   . ASP D  1 364 ? 104.165 5.451   16.586  1.00   44.11  ? 364 ASP D C   1 
ATOM   11633 O O   . ASP D  1 364 ? 104.419 6.124   17.573  1.00   46.65  ? 364 ASP D O   1 
ATOM   11634 C CB  . ASP D  1 364 ? 102.032 4.411   17.318  1.00   46.19  ? 364 ASP D CB  1 
ATOM   11635 C CG  . ASP D  1 364 ? 101.095 5.098   16.355  1.00   46.56  ? 364 ASP D CG  1 
ATOM   11636 O OD1 . ASP D  1 364 ? 101.572 5.636   15.339  1.00   50.34  ? 364 ASP D OD1 1 
ATOM   11637 O OD2 . ASP D  1 364 ? 99.884  5.093   16.620  1.00   48.55  1 364 ASP D OD2 1 
ATOM   11638 N N   . GLY D  1 365 ? 104.520 5.793   15.358  1.00   42.92  ? 365 GLY D N   1 
ATOM   11639 C CA  . GLY D  1 365 ? 105.194 7.046   15.100  1.00   43.86  ? 365 GLY D CA  1 
ATOM   11640 C C   . GLY D  1 365 ? 104.208 8.187   14.988  1.00   49.10  ? 365 GLY D C   1 
ATOM   11641 O O   . GLY D  1 365 ? 104.589 9.326   14.759  1.00   52.47  ? 365 GLY D O   1 
ATOM   11642 N N   . GLY D  1 366 ? 102.925 7.879   15.105  1.00   49.49  ? 366 GLY D N   1 
ATOM   11643 C CA  . GLY D  1 366 ? 101.929 8.919   15.056  1.00   47.95  ? 366 GLY D CA  1 
ATOM   11644 C C   . GLY D  1 366 ? 101.720 9.288   13.614  1.00   51.30  ? 366 GLY D C   1 
ATOM   11645 O O   . GLY D  1 366 ? 102.220 8.617   12.719  1.00   45.61  ? 366 GLY D O   1 
ATOM   11646 N N   . VAL D  1 367 ? 101.012 10.390  13.403  1.00   56.99  ? 367 VAL D N   1 
ATOM   11647 C CA  . VAL D  1 367 ? 100.600 10.845  12.075  1.00   59.54  ? 367 VAL D CA  1 
ATOM   11648 C C   . VAL D  1 367 ? 101.566 11.814  11.395  1.00   61.82  ? 367 VAL D C   1 
ATOM   11649 O O   . VAL D  1 367 ? 101.390 12.122  10.219  1.00   63.82  ? 367 VAL D O   1 
ATOM   11650 C CB  . VAL D  1 367 ? 99.238  11.523  12.129  1.00   61.33  ? 367 VAL D CB  1 
ATOM   11651 C CG1 . VAL D  1 367 ? 98.172  10.519  12.523  1.00   58.07  ? 367 VAL D CG1 1 
ATOM   11652 C CG2 . VAL D  1 367 ? 99.297  12.683  13.099  1.00   65.08  ? 367 VAL D CG2 1 
ATOM   11653 N N   . HIS D  1 368 ? 102.543 12.340  12.128  1.00   62.95  ? 368 HIS D N   1 
ATOM   11654 C CA  . HIS D  1 368 ? 103.585 13.132  11.482  1.00   65.28  ? 368 HIS D CA  1 
ATOM   11655 C C   . HIS D  1 368 ? 104.928 12.447  11.602  1.00   66.09  ? 368 HIS D C   1 
ATOM   11656 O O   . HIS D  1 368 ? 105.954 13.095  11.805  1.00   66.63  ? 368 HIS D O   1 
ATOM   11657 C CB  . HIS D  1 368 ? 103.686 14.540  12.061  1.00   71.31  ? 368 HIS D CB  1 
ATOM   11658 C CG  . HIS D  1 368 ? 102.466 15.373  11.843  1.00   77.13  ? 368 HIS D CG  1 
ATOM   11659 N ND1 . HIS D  1 368 ? 102.150 16.450  12.639  1.00   81.07  ? 368 HIS D ND1 1 
ATOM   11660 C CD2 . HIS D  1 368 ? 101.487 15.288  10.909  1.00   80.49  ? 368 HIS D CD2 1 
ATOM   11661 C CE1 . HIS D  1 368 ? 101.026 16.995  12.205  1.00   86.13  ? 368 HIS D CE1 1 
ATOM   11662 N NE2 . HIS D  1 368 ? 100.603 16.307  11.159  1.00   85.52  ? 368 HIS D NE2 1 
ATOM   11663 N N   . ALA D  1 369 ? 104.917 11.127  11.455  1.00   64.47  ? 369 ALA D N   1 
ATOM   11664 C CA  . ALA D  1 369 ? 106.139 10.361  11.490  1.00   58.16  ? 369 ALA D CA  1 
ATOM   11665 C C   . ALA D  1 369 ? 106.960 10.730  10.272  1.00   60.76  ? 369 ALA D C   1 
ATOM   11666 O O   . ALA D  1 369 ? 106.412 10.958  9.191   1.00   61.57  ? 369 ALA D O   1 
ATOM   11667 C CB  . ALA D  1 369 ? 105.825 8.873   11.518  1.00   52.18  ? 369 ALA D CB  1 
ATOM   11668 N N   . ARG D  1 370 ? 108.277 10.763  10.453  1.00   63.65  ? 370 ARG D N   1 
ATOM   11669 C CA  . ARG D  1 370 ? 109.223 11.158  9.406   1.00   66.30  ? 370 ARG D CA  1 
ATOM   11670 C C   . ARG D  1 370 ? 109.264 10.121  8.254   1.00   64.51  ? 370 ARG D C   1 
ATOM   11671 O O   . ARG D  1 370 ? 109.483 10.483  7.095   1.00   68.45  ? 370 ARG D O   1 
ATOM   11672 C CB  . ARG D  1 370 ? 110.592 11.424  10.025  1.00   67.54  ? 370 ARG D CB  1 
ATOM   11673 C CG  . ARG D  1 370 ? 111.788 11.350  9.112   1.00   70.39  ? 370 ARG D CG  1 
ATOM   11674 C CD  . ARG D  1 370 ? 113.007 11.310  10.017  1.00   75.52  ? 370 ARG D CD  1 
ATOM   11675 N NE  . ARG D  1 370 ? 113.019 10.065  10.788  1.00   81.13  ? 370 ARG D NE  1 
ATOM   11676 C CZ  . ARG D  1 370 ? 113.410 9.955   12.062  1.00   86.35  ? 370 ARG D CZ  1 
ATOM   11677 N NH1 . ARG D  1 370 ? 113.830 11.018  12.732  1.00   88.67  ? 370 ARG D NH1 1 
ATOM   11678 N NH2 . ARG D  1 370 ? 113.364 8.778   12.679  1.00   87.23  ? 370 ARG D NH2 1 
ATOM   11679 N N   . ALA D  1 371 ? 109.104 8.836   8.580   1.00   56.82  ? 371 ALA D N   1 
ATOM   11680 C CA  . ALA D  1 371 ? 109.005 7.790   7.560   1.00   48.86  ? 371 ALA D CA  1 
ATOM   11681 C C   . ALA D  1 371 ? 107.875 6.825   7.916   1.00   49.26  ? 371 ALA D C   1 
ATOM   11682 O O   . ALA D  1 371 ? 107.460 6.758   9.075   1.00   52.30  ? 371 ALA D O   1 
ATOM   11683 C CB  . ALA D  1 371 ? 110.312 7.044   7.444   1.00   41.97  ? 371 ALA D CB  1 
ATOM   11684 N N   . GLY D  1 372 ? 107.393 6.063   6.933   1.00   45.91  ? 372 GLY D N   1 
ATOM   11685 C CA  . GLY D  1 372 ? 106.324 5.098   7.166   1.00   42.57  ? 372 GLY D CA  1 
ATOM   11686 C C   . GLY D  1 372 ? 106.770 3.959   8.070   1.00   37.72  ? 372 GLY D C   1 
ATOM   11687 O O   . GLY D  1 372 ? 106.043 3.521   8.951   1.00   37.53  ? 372 GLY D O   1 
ATOM   11688 N N   . ILE D  1 373 ? 107.994 3.507   7.829   1.00   35.07  ? 373 ILE D N   1 
ATOM   11689 C CA  . ILE D  1 373 ? 108.679 2.503   8.607   1.00   34.52  ? 373 ILE D CA  1 
ATOM   11690 C C   . ILE D  1 373 ? 110.039 3.063   8.943   1.00   34.38  ? 373 ILE D C   1 
ATOM   11691 O O   . ILE D  1 373 ? 110.727 3.575   8.066   1.00   32.75  ? 373 ILE D O   1 
ATOM   11692 C CB  . ILE D  1 373 ? 108.869 1.212   7.834   1.00   35.06  ? 373 ILE D CB  1 
ATOM   11693 C CG1 . ILE D  1 373 ? 107.533 0.666   7.340   1.00   36.21  ? 373 ILE D CG1 1 
ATOM   11694 C CG2 . ILE D  1 373 ? 109.578 0.197   8.694   1.00   35.89  ? 373 ILE D CG2 1 
ATOM   11695 C CD1 . ILE D  1 373 ? 107.704 -0.475  6.359   1.00   34.59  ? 373 ILE D CD1 1 
ATOM   11696 N N   . ALA D  1 374 ? 110.419 3.008   10.211  1.00   36.57  ? 374 ALA D N   1 
ATOM   11697 C CA  . ALA D  1 374 ? 111.773 3.382   10.599  1.00   35.34  ? 374 ALA D CA  1 
ATOM   11698 C C   . ALA D  1 374 ? 112.415 2.258   11.390  1.00   35.80  ? 374 ALA D C   1 
ATOM   11699 O O   . ALA D  1 374 ? 112.070 2.053   12.555  1.00   36.10  ? 374 ALA D O   1 
ATOM   11700 C CB  . ALA D  1 374 ? 111.776 4.675   11.407  1.00   35.35  ? 374 ALA D CB  1 
ATOM   11701 N N   . LEU D  1 375 ? 113.345 1.546   10.752  1.00   35.42  ? 375 LEU D N   1 
ATOM   11702 C CA  . LEU D  1 375 ? 114.025 0.403   11.364  1.00   35.82  ? 375 LEU D CA  1 
ATOM   11703 C C   . LEU D  1 375 ? 115.103 0.826   12.354  1.00   36.17  ? 375 LEU D C   1 
ATOM   11704 O O   . LEU D  1 375 ? 115.987 1.588   12.005  1.00   37.42  ? 375 LEU D O   1 
ATOM   11705 C CB  . LEU D  1 375 ? 114.629 -0.483  10.273  1.00   33.65  ? 375 LEU D CB  1 
ATOM   11706 C CG  . LEU D  1 375 ? 113.634 -0.890  9.176   1.00   33.37  ? 375 LEU D CG  1 
ATOM   11707 C CD1 . LEU D  1 375 ? 114.319 -1.516  7.985   1.00   34.64  ? 375 LEU D CD1 1 
ATOM   11708 C CD2 . LEU D  1 375 ? 112.605 -1.844  9.731   1.00   33.51  ? 375 LEU D CD2 1 
ATOM   11709 N N   . GLY D  1 376 ? 115.023 0.336   13.588  1.00   34.28  ? 376 GLY D N   1 
ATOM   11710 C CA  . GLY D  1 376 ? 115.904 0.795   14.652  1.00   31.69  ? 376 GLY D CA  1 
ATOM   11711 C C   . GLY D  1 376 ? 116.960 -0.197  15.120  1.00   32.40  ? 376 GLY D C   1 
ATOM   11712 O O   . GLY D  1 376 ? 117.235 -1.211  14.464  1.00   32.19  ? 376 GLY D O   1 
ATOM   11713 N N   . ALA D  1 377 ? 117.540 0.077   16.287  1.00   33.62  ? 377 ALA D N   1 
ATOM   11714 C CA  . ALA D  1 377 ? 118.670 -0.714  16.788  1.00   33.23  ? 377 ALA D CA  1 
ATOM   11715 C C   . ALA D  1 377 ? 118.314 -2.176  17.056  1.00   30.60  ? 377 ALA D C   1 
ATOM   11716 O O   . ALA D  1 377 ? 119.117 -3.053  16.808  1.00   34.19  ? 377 ALA D O   1 
ATOM   11717 C CB  . ALA D  1 377 ? 119.258 -0.068  18.046  1.00   34.95  ? 377 ALA D CB  1 
ATOM   11718 N N   A HIS D  1 378 ? 117.109 -2.410  17.566  0.50   33.40  ? 378 HIS D N   1 
ATOM   11719 N N   B HIS D  1 378 ? 117.119 -2.438  17.568  0.50   33.40  ? 378 HIS D N   1 
ATOM   11720 C CA  A HIS D  1 378 ? 116.642 -3.749  17.902  0.50   30.94  ? 378 HIS D CA  1 
ATOM   11721 C CA  B HIS D  1 378 ? 116.750 -3.805  17.913  0.50   31.57  ? 378 HIS D CA  1 
ATOM   11722 C C   A HIS D  1 378 ? 116.546 -4.604  16.653  0.50   34.03  ? 378 HIS D C   1 
ATOM   11723 C C   B HIS D  1 378 ? 116.514 -4.635  16.652  0.50   34.05  ? 378 HIS D C   1 
ATOM   11724 O O   A HIS D  1 378 ? 116.865 -5.794  16.669  0.50   34.37  ? 378 HIS D O   1 
ATOM   11725 O O   B HIS D  1 378 ? 116.710 -5.851  16.659  0.50   34.59  ? 378 HIS D O   1 
ATOM   11726 C CB  A HIS D  1 378 ? 115.279 -3.684  18.587  0.50   32.53  ? 378 HIS D CB  1 
ATOM   11727 C CB  B HIS D  1 378 ? 115.522 -3.827  18.824  0.50   33.25  ? 378 HIS D CB  1 
ATOM   11728 C CG  A HIS D  1 378 ? 114.908 -4.933  19.320  0.50   34.03  ? 378 HIS D CG  1 
ATOM   11729 C CG  B HIS D  1 378 ? 115.830 -3.528  20.265  0.50   34.53  ? 378 HIS D CG  1 
ATOM   11730 N ND1 A HIS D  1 378 ? 115.306 -5.185  20.615  0.50   35.75  ? 378 HIS D ND1 1 
ATOM   11731 N ND1 B HIS D  1 378 ? 115.194 -4.162  21.308  0.50   36.59  ? 378 HIS D ND1 1 
ATOM   11732 C CD2 A HIS D  1 378 ? 114.172 -6.004  18.938  0.50   34.37  ? 378 HIS D CD2 1 
ATOM   11733 C CD2 B HIS D  1 378 ? 116.706 -2.664  20.833  0.50   39.41  ? 378 HIS D CD2 1 
ATOM   11734 C CE1 A HIS D  1 378 ? 114.833 -6.358  20.996  0.50   37.08  ? 378 HIS D CE1 1 
ATOM   11735 C CE1 B HIS D  1 378 ? 115.654 -3.696  22.456  0.50   38.12  ? 378 HIS D CE1 1 
ATOM   11736 N NE2 A HIS D  1 378 ? 114.144 -6.877  19.996  0.50   36.27  ? 378 HIS D NE2 1 
ATOM   11737 N NE2 B HIS D  1 378 ? 116.570 -2.786  22.196  0.50   37.13  ? 378 HIS D NE2 1 
ATOM   11738 N N   . HIS D  1 379 ? 116.126 -3.985  15.560  1.00   30.84  ? 379 HIS D N   1 
ATOM   11739 C CA  . HIS D  1 379 ? 116.065 -4.680  14.286  1.00   31.92  ? 379 HIS D CA  1 
ATOM   11740 C C   . HIS D  1 379 ? 117.465 -5.136  13.820  1.00   34.23  ? 379 HIS D C   1 
ATOM   11741 O O   . HIS D  1 379 ? 117.658 -6.263  13.358  1.00   35.90  ? 379 HIS D O   1 
ATOM   11742 C CB  . HIS D  1 379 ? 115.443 -3.790  13.226  1.00   30.53  ? 379 HIS D CB  1 
ATOM   11743 C CG  . HIS D  1 379 ? 115.367 -4.433  11.880  1.00   31.31  ? 379 HIS D CG  1 
ATOM   11744 N ND1 . HIS D  1 379 ? 114.299 -5.206  11.484  1.00   32.69  ? 379 HIS D ND1 1 
ATOM   11745 C CD2 . HIS D  1 379 ? 116.236 -4.436  10.844  1.00   33.20  ? 379 HIS D CD2 1 
ATOM   11746 C CE1 . HIS D  1 379 ? 114.504 -5.641  10.256  1.00   31.96  ? 379 HIS D CE1 1 
ATOM   11747 N NE2 . HIS D  1 379 ? 115.672 -5.188  9.843   1.00   32.90  ? 379 HIS D NE2 1 
ATOM   11748 N N   . LEU D  1 380 ? 118.449 -4.259  13.970  1.00   34.51  ? 380 LEU D N   1 
ATOM   11749 C CA  . LEU D  1 380 ? 119.792 -4.542  13.482  1.00   33.10  ? 380 LEU D CA  1 
ATOM   11750 C C   . LEU D  1 380 ? 120.571 -5.537  14.320  1.00   31.92  ? 380 LEU D C   1 
ATOM   11751 O O   . LEU D  1 380 ? 121.416 -6.253  13.786  1.00   35.38  ? 380 LEU D O   1 
ATOM   11752 C CB  . LEU D  1 380 ? 120.606 -3.245  13.401  1.00   30.92  ? 380 LEU D CB  1 
ATOM   11753 C CG  . LEU D  1 380 ? 120.024 -2.208  12.456  1.00   30.19  ? 380 LEU D CG  1 
ATOM   11754 C CD1 . LEU D  1 380 ? 120.747 -0.916  12.614  1.00   29.32  ? 380 LEU D CD1 1 
ATOM   11755 C CD2 . LEU D  1 380 ? 120.105 -2.707  11.020  1.00   28.37  ? 380 LEU D CD2 1 
ATOM   11756 N N   . GLU D  1 381 ? 120.290 -5.581  15.618  1.00   30.72  ? 381 GLU D N   1 
ATOM   11757 C CA  . GLU D  1 381 ? 121.056 -6.406  16.535  1.00   30.99  ? 381 GLU D CA  1 
ATOM   11758 C C   . GLU D  1 381 ? 121.021 -7.858  16.115  1.00   34.10  ? 381 GLU D C   1 
ATOM   11759 O O   . GLU D  1 381 ? 119.993 -8.341  15.650  1.00   37.75  ? 381 GLU D O   1 
ATOM   11760 C CB  . GLU D  1 381 ? 120.537 -6.256  17.949  1.00   32.40  ? 381 GLU D CB  1 
ATOM   11761 C CG  . GLU D  1 381 ? 120.940 -4.971  18.594  1.00   34.56  ? 381 GLU D CG  1 
ATOM   11762 C CD  . GLU D  1 381 ? 120.126 -4.654  19.845  1.00   39.38  ? 381 GLU D CD  1 
ATOM   11763 O OE1 . GLU D  1 381 ? 119.266 -5.475  20.236  1.00   38.78  ? 381 GLU D OE1 1 
ATOM   11764 O OE2 . GLU D  1 381 ? 120.324 -3.556  20.421  1.00   44.39  1 381 GLU D OE2 1 
ATOM   11765 N N   . GLU D  1 382 ? 122.187 -8.502  16.228  1.00   34.30  ? 382 GLU D N   1 
ATOM   11766 C CA  . GLU D  1 382 ? 122.446 -9.901  15.874  1.00   35.59  ? 382 GLU D CA  1 
ATOM   11767 C C   . GLU D  1 382 ? 122.220 -10.194 14.403  1.00   33.97  ? 382 GLU D C   1 
ATOM   11768 O O   . GLU D  1 382 ? 121.986 -11.345 14.011  1.00   32.81  ? 382 GLU D O   1 
ATOM   11769 C CB  . GLU D  1 382 ? 121.605 -10.848 16.731  1.00   37.46  ? 382 GLU D CB  1 
ATOM   11770 C CG  . GLU D  1 382 ? 121.923 -10.778 18.216  1.00   37.65  ? 382 GLU D CG  1 
ATOM   11771 C CD  . GLU D  1 382 ? 123.395 -10.956 18.520  1.00   39.17  ? 382 GLU D CD  1 
ATOM   11772 O OE1 . GLU D  1 382 ? 124.066 -11.809 17.907  1.00   40.16  ? 382 GLU D OE1 1 
ATOM   11773 O OE2 . GLU D  1 382 ? 123.898 -10.200 19.365  1.00   42.46  1 382 GLU D OE2 1 
ATOM   11774 N N   . ASN D  1 383 ? 122.320 -9.144  13.597  1.00   34.42  ? 383 ASN D N   1 
ATOM   11775 C CA  . ASN D  1 383 ? 122.354 -9.262  12.138  1.00   34.96  ? 383 ASN D CA  1 
ATOM   11776 C C   . ASN D  1 383 ? 123.568 -8.587  11.577  1.00   32.66  ? 383 ASN D C   1 
ATOM   11777 O O   . ASN D  1 383 ? 124.009 -7.579  12.112  1.00   32.23  ? 383 ASN D O   1 
ATOM   11778 C CB  . ASN D  1 383 ? 121.112 -8.653  11.493  1.00   33.23  ? 383 ASN D CB  1 
ATOM   11779 C CG  . ASN D  1 383 ? 119.871 -9.447  11.778  1.00   35.27  ? 383 ASN D CG  1 
ATOM   11780 O OD1 . ASN D  1 383 ? 119.716 -10.564 11.287  1.00   37.92  ? 383 ASN D OD1 1 
ATOM   11781 N ND2 . ASN D  1 383 ? 118.981 -8.885  12.585  1.00   34.03  ? 383 ASN D ND2 1 
ATOM   11782 N N   . LEU D  1 384 ? 124.107 -9.144  10.500  1.00   34.32  ? 384 LEU D N   1 
ATOM   11783 C CA  . LEU D  1 384 ? 125.163 -8.462  9.762   1.00   31.09  ? 384 LEU D CA  1 
ATOM   11784 C C   . LEU D  1 384 ? 124.565 -7.698  8.588   1.00   29.79  ? 384 LEU D C   1 
ATOM   11785 O O   . LEU D  1 384 ? 123.965 -8.289  7.691   1.00   28.84  ? 384 LEU D O   1 
ATOM   11786 C CB  . LEU D  1 384 ? 126.206 -9.449  9.275   1.00   31.11  ? 384 LEU D CB  1 
ATOM   11787 C CG  . LEU D  1 384 ? 127.310 -8.822  8.434   1.00   28.95  ? 384 LEU D CG  1 
ATOM   11788 C CD1 . LEU D  1 384 ? 128.231 -7.955  9.289   1.00   28.45  ? 384 LEU D CD1 1 
ATOM   11789 C CD2 . LEU D  1 384 ? 128.059 -9.938  7.732   1.00   30.51  ? 384 LEU D CD2 1 
ATOM   11790 N N   . VAL D  1 385 ? 124.714 -6.379  8.606   1.00   29.70  ? 385 VAL D N   1 
ATOM   11791 C CA  . VAL D  1 385 ? 124.087 -5.552  7.599   1.00   29.30  ? 385 VAL D CA  1 
ATOM   11792 C C   . VAL D  1 385 ? 125.145 -4.779  6.850   1.00   30.80  ? 385 VAL D C   1 
ATOM   11793 O O   . VAL D  1 385 ? 125.841 -3.957  7.434   1.00   28.34  ? 385 VAL D O   1 
ATOM   11794 C CB  . VAL D  1 385 ? 123.080 -4.592  8.219   1.00   26.91  ? 385 VAL D CB  1 
ATOM   11795 C CG1 . VAL D  1 385 ? 122.346 -3.848  7.124   1.00   27.20  ? 385 VAL D CG1 1 
ATOM   11796 C CG2 . VAL D  1 385 ? 122.084 -5.362  9.113   1.00   22.28  ? 385 VAL D CG2 1 
ATOM   11797 N N   . VAL D  1 386 ? 125.249 -5.035  5.553   1.00   32.28  ? 386 VAL D N   1 
ATOM   11798 C CA  . VAL D  1 386 ? 126.320 -4.478  4.749   1.00   31.35  ? 386 VAL D CA  1 
ATOM   11799 C C   . VAL D  1 386 ? 125.846 -3.258  3.957   1.00   32.17  ? 386 VAL D C   1 
ATOM   11800 O O   . VAL D  1 386 ? 124.882 -3.334  3.194   1.00   30.91  ? 386 VAL D O   1 
ATOM   11801 C CB  . VAL D  1 386 ? 126.899 -5.569  3.826   1.00   28.52  ? 386 VAL D CB  1 
ATOM   11802 C CG1 . VAL D  1 386 ? 128.037 -5.044  2.944   1.00   29.65  ? 386 VAL D CG1 1 
ATOM   11803 C CG2 . VAL D  1 386 ? 127.405 -6.675  4.664   1.00   25.35  ? 386 VAL D CG2 1 
ATOM   11804 N N   . PHE D  1 387 ? 126.506 -2.122  4.222   1.00   30.41  ? 387 PHE D N   1 
ATOM   11805 C CA  . PHE D  1 387 ? 126.272 -0.872  3.510   1.00   28.72  ? 387 PHE D CA  1 
ATOM   11806 C C   . PHE D  1 387 ? 127.298 -0.725  2.420   1.00   28.45  ? 387 PHE D C   1 
ATOM   11807 O O   . PHE D  1 387 ? 128.395 -0.245  2.657   1.00   28.16  ? 387 PHE D O   1 
ATOM   11808 C CB  . PHE D  1 387 ? 126.328 0.332   4.445   1.00   29.28  ? 387 PHE D CB  1 
ATOM   11809 C CG  . PHE D  1 387 ? 125.201 0.372   5.451   1.00   30.57  ? 387 PHE D CG  1 
ATOM   11810 C CD1 . PHE D  1 387 ? 125.262 -0.375  6.613   1.00   29.12  ? 387 PHE D CD1 1 
ATOM   11811 C CD2 . PHE D  1 387 ? 124.060 1.119   5.201   1.00   33.11  ? 387 PHE D CD2 1 
ATOM   11812 C CE1 . PHE D  1 387 ? 124.246 -0.349  7.520   1.00   29.32  ? 387 PHE D CE1 1 
ATOM   11813 C CE2 . PHE D  1 387 ? 123.018 1.145   6.110   1.00   31.85  ? 387 PHE D CE2 1 
ATOM   11814 C CZ  . PHE D  1 387 ? 123.119 0.410   7.277   1.00   31.98  ? 387 PHE D CZ  1 
ATOM   11815 N N   . ASP D  1 388 ? 126.902 -1.151  1.227   1.00   28.87  ? 388 ASP D N   1 
ATOM   11816 C CA  . ASP D  1 388 ? 127.730 -1.167  0.045   1.00   26.32  ? 388 ASP D CA  1 
ATOM   11817 C C   . ASP D  1 388 ? 127.518 0.129   -0.695  1.00   27.64  ? 388 ASP D C   1 
ATOM   11818 O O   . ASP D  1 388 ? 126.597 0.275   -1.478  1.00   29.72  ? 388 ASP D O   1 
ATOM   11819 C CB  . ASP D  1 388 ? 127.380 -2.387  -0.821  1.00   27.09  ? 388 ASP D CB  1 
ATOM   11820 C CG  . ASP D  1 388 ? 128.323 -2.574  -1.996  1.00   31.85  ? 388 ASP D CG  1 
ATOM   11821 O OD1 . ASP D  1 388 ? 129.145 -1.683  -2.245  1.00   36.05  ? 388 ASP D OD1 1 
ATOM   11822 O OD2 . ASP D  1 388 ? 128.210 -3.583  -2.721  1.00   35.07  1 388 ASP D OD2 1 
ATOM   11823 N N   . LEU D  1 389 ? 128.363 1.105   -0.413  1.00   31.76  ? 389 LEU D N   1 
ATOM   11824 C CA  . LEU D  1 389 ? 128.198 2.424   -0.987  1.00   32.08  ? 389 LEU D CA  1 
ATOM   11825 C C   . LEU D  1 389 ? 128.644 2.429   -2.452  1.00   33.59  ? 389 LEU D C   1 
ATOM   11826 O O   . LEU D  1 389 ? 128.200 3.280   -3.219  1.00   37.96  ? 389 LEU D O   1 
ATOM   11827 C CB  . LEU D  1 389 ? 128.949 3.458   -0.150  1.00   33.14  ? 389 LEU D CB  1 
ATOM   11828 C CG  . LEU D  1 389 ? 128.627 3.274   1.331   1.00   34.39  ? 389 LEU D CG  1 
ATOM   11829 C CD1 . LEU D  1 389 ? 129.579 4.017   2.204   1.00   35.56  ? 389 LEU D CD1 1 
ATOM   11830 C CD2 . LEU D  1 389 ? 127.178 3.687   1.643   1.00   35.30  ? 389 LEU D CD2 1 
ATOM   11831 N N   . GLU D  1 390 ? 129.508 1.488   -2.847  1.00   31.71  ? 390 GLU D N   1 
ATOM   11832 C CA  . GLU D  1 390 ? 129.986 1.429   -4.237  1.00   31.98  ? 390 GLU D CA  1 
ATOM   11833 C C   . GLU D  1 390 ? 128.938 0.947   -5.246  1.00   32.45  ? 390 GLU D C   1 
ATOM   11834 O O   . GLU D  1 390 ? 128.928 1.411   -6.385  1.00   35.81  ? 390 GLU D O   1 
ATOM   11835 C CB  . GLU D  1 390 ? 131.240 0.543   -4.356  1.00   33.74  ? 390 GLU D CB  1 
ATOM   11836 C CG  . GLU D  1 390 ? 132.419 1.085   -3.590  1.00   38.57  ? 390 GLU D CG  1 
ATOM   11837 C CD  . GLU D  1 390 ? 133.784 0.525   -4.019  1.00   41.63  ? 390 GLU D CD  1 
ATOM   11838 O OE1 . GLU D  1 390 ? 133.835 -0.551  -4.692  1.00   41.59  ? 390 GLU D OE1 1 
ATOM   11839 O OE2 . GLU D  1 390 ? 134.796 1.186   -3.646  1.00   40.47  ? 390 GLU D OE2 1 
ATOM   11840 N N   . ARG D  1 391 ? 128.041 0.053   -4.822  1.00   31.32  ? 391 ARG D N   1 
ATOM   11841 C CA  . ARG D  1 391 ? 126.987 -0.501  -5.686  1.00   30.92  ? 391 ARG D CA  1 
ATOM   11842 C C   . ARG D  1 391 ? 125.625 0.014   -5.272  1.00   32.08  ? 391 ARG D C   1 
ATOM   11843 O O   . ARG D  1 391 ? 124.617 -0.378  -5.860  1.00   34.36  ? 391 ARG D O   1 
ATOM   11844 C CB  . ARG D  1 391 ? 126.992 -2.038  -5.652  1.00   29.90  ? 391 ARG D CB  1 
ATOM   11845 C CG  . ARG D  1 391 ? 128.290 -2.640  -6.147  1.00   34.94  ? 391 ARG D CG  1 
ATOM   11846 C CD  . ARG D  1 391 ? 128.247 -4.151  -6.336  1.00   40.58  ? 391 ARG D CD  1 
ATOM   11847 N NE  . ARG D  1 391 ? 127.108 -4.612  -7.127  1.00   46.45  ? 391 ARG D NE  1 
ATOM   11848 C CZ  . ARG D  1 391 ? 126.951 -5.864  -7.558  1.00   49.74  ? 391 ARG D CZ  1 
ATOM   11849 N NH1 . ARG D  1 391 ? 127.866 -6.781  -7.282  1.00   49.61  ? 391 ARG D NH1 1 
ATOM   11850 N NH2 . ARG D  1 391 ? 125.875 -6.199  -8.262  1.00   51.33  ? 391 ARG D NH2 1 
ATOM   11851 N N   . SER D  1 392 ? 125.624 0.901   -4.269  1.00   30.36  ? 392 SER D N   1 
ATOM   11852 C CA  . SER D  1 392 ? 124.429 1.536   -3.696  1.00   30.23  ? 392 SER D CA  1 
ATOM   11853 C C   . SER D  1 392 ? 123.364 0.508   -3.273  1.00   29.77  ? 392 SER D C   1 
ATOM   11854 O O   . SER D  1 392 ? 122.220 0.543   -3.732  1.00   31.41  ? 392 SER D O   1 
ATOM   11855 C CB  . SER D  1 392 ? 123.843 2.551   -4.684  1.00   31.16  ? 392 SER D CB  1 
ATOM   11856 O OG  . SER D  1 392 ? 122.995 3.456   -4.011  1.00   30.61  ? 392 SER D OG  1 
ATOM   11857 N N   . ARG D  1 393 ? 123.753 -0.401  -2.385  1.00   28.66  ? 393 ARG D N   1 
ATOM   11858 C CA  . ARG D  1 393 ? 122.886 -1.493  -1.946  1.00   27.79  ? 393 ARG D CA  1 
ATOM   11859 C C   . ARG D  1 393 ? 123.161 -1.879  -0.495  1.00   28.33  ? 393 ARG D C   1 
ATOM   11860 O O   . ARG D  1 393 ? 124.225 -1.589  0.036   1.00   29.95  ? 393 ARG D O   1 
ATOM   11861 C CB  . ARG D  1 393 ? 123.075 -2.723  -2.842  1.00   28.33  ? 393 ARG D CB  1 
ATOM   11862 C CG  . ARG D  1 393 ? 124.478 -3.291  -2.746  1.00   27.84  ? 393 ARG D CG  1 
ATOM   11863 C CD  . ARG D  1 393 ? 124.733 -4.415  -3.705  1.00   29.85  ? 393 ARG D CD  1 
ATOM   11864 N NE  . ARG D  1 393 ? 126.052 -4.993  -3.443  1.00   33.08  ? 393 ARG D NE  1 
ATOM   11865 C CZ  . ARG D  1 393 ? 126.434 -6.197  -3.847  1.00   34.38  ? 393 ARG D CZ  1 
ATOM   11866 N NH1 . ARG D  1 393 ? 125.587 -6.965  -4.522  1.00   35.95  ? 393 ARG D NH1 1 
ATOM   11867 N NH2 . ARG D  1 393 ? 127.654 -6.635  -3.568  1.00   33.32  ? 393 ARG D NH2 1 
ATOM   11868 N N   . VAL D  1 394 ? 122.183 -2.520  0.135   1.00   26.89  ? 394 VAL D N   1 
ATOM   11869 C CA  . VAL D  1 394 ? 122.316 -3.050  1.482   1.00   28.22  ? 394 VAL D CA  1 
ATOM   11870 C C   . VAL D  1 394 ? 122.250 -4.572  1.451   1.00   29.30  ? 394 VAL D C   1 
ATOM   11871 O O   . VAL D  1 394 ? 121.342 -5.132  0.839   1.00   30.98  ? 394 VAL D O   1 
ATOM   11872 C CB  . VAL D  1 394 ? 121.167 -2.543  2.431   1.00   31.57  ? 394 VAL D CB  1 
ATOM   11873 C CG1 . VAL D  1 394 ? 121.257 -3.211  3.793   1.00   29.21  ? 394 VAL D CG1 1 
ATOM   11874 C CG2 . VAL D  1 394 ? 121.185 -1.048  2.578   1.00   27.78  ? 394 VAL D CG2 1 
ATOM   11875 N N   . GLY D  1 395 ? 123.164 -5.245  2.144   1.00   29.96  ? 395 GLY D N   1 
ATOM   11876 C CA  . GLY D  1 395 ? 123.108 -6.692  2.238   1.00   29.33  ? 395 GLY D CA  1 
ATOM   11877 C C   . GLY D  1 395 ? 122.848 -7.127  3.668   1.00   30.94  ? 395 GLY D C   1 
ATOM   11878 O O   . GLY D  1 395 ? 123.199 -6.411  4.598   1.00   30.61  ? 395 GLY D O   1 
ATOM   11879 N N   . PHE D  1 396 ? 122.203 -8.276  3.854   1.00   31.42  ? 396 PHE D N   1 
ATOM   11880 C CA  . PHE D  1 396 ? 121.962 -8.785  5.199   1.00   29.57  ? 396 PHE D CA  1 
ATOM   11881 C C   . PHE D  1 396 ? 121.943 -10.303 5.194   1.00   32.26  ? 396 PHE D C   1 
ATOM   11882 O O   . PHE D  1 396 ? 121.738 -10.931 4.145   1.00   32.70  ? 396 PHE D O   1 
ATOM   11883 C CB  . PHE D  1 396 ? 120.648 -8.238  5.760   1.00   30.80  ? 396 PHE D CB  1 
ATOM   11884 C CG  . PHE D  1 396 ? 119.473 -8.435  4.828   1.00   32.94  ? 396 PHE D CG  1 
ATOM   11885 C CD1 . PHE D  1 396 ? 118.785 -9.646  4.791   1.00   33.93  ? 396 PHE D CD1 1 
ATOM   11886 C CD2 . PHE D  1 396 ? 119.058 -7.411  3.991   1.00   30.06  ? 396 PHE D CD2 1 
ATOM   11887 C CE1 . PHE D  1 396 ? 117.748 -9.845  3.928   1.00   31.69  ? 396 PHE D CE1 1 
ATOM   11888 C CE2 . PHE D  1 396 ? 118.013 -7.608  3.122   1.00   28.15  ? 396 PHE D CE2 1 
ATOM   11889 C CZ  . PHE D  1 396 ? 117.353 -8.825  3.099   1.00   30.84  ? 396 PHE D CZ  1 
ATOM   11890 N N   . ASN D  1 397 ? 122.168 -10.900 6.365   1.00   33.11  ? 397 ASN D N   1 
ATOM   11891 C CA  . ASN D  1 397 ? 122.155 -12.358 6.476   1.00   33.89  ? 397 ASN D CA  1 
ATOM   11892 C C   . ASN D  1 397 ? 120.757 -12.874 6.247   1.00   33.58  ? 397 ASN D C   1 
ATOM   11893 O O   . ASN D  1 397 ? 119.819 -12.380 6.865   1.00   34.66  ? 397 ASN D O   1 
ATOM   11894 C CB  . ASN D  1 397 ? 122.674 -12.833 7.839   1.00   32.40  ? 397 ASN D CB  1 
ATOM   11895 C CG  . ASN D  1 397 ? 122.060 -12.084 8.997   1.00   32.14  ? 397 ASN D CG  1 
ATOM   11896 O OD1 . ASN D  1 397 ? 122.282 -10.889 9.163   1.00   29.66  ? 397 ASN D OD1 1 
ATOM   11897 N ND2 . ASN D  1 397 ? 121.299 -12.796 9.824   1.00   34.11  ? 397 ASN D ND2 1 
ATOM   11898 N N   . SER D  1 398 ? 120.615 -13.869 5.374   1.00   35.73  ? 398 SER D N   1 
ATOM   11899 C CA  . SER D  1 398 ? 119.297 -14.370 5.027   1.00   40.01  ? 398 SER D CA  1 
ATOM   11900 C C   . SER D  1 398 ? 118.809 -15.457 5.982   1.00   44.74  ? 398 SER D C   1 
ATOM   11901 O O   . SER D  1 398 ? 117.645 -15.850 5.917   1.00   49.71  ? 398 SER D O   1 
ATOM   11902 C CB  . SER D  1 398 ? 119.279 -14.881 3.597   1.00   43.71  ? 398 SER D CB  1 
ATOM   11903 O OG  . SER D  1 398 ? 120.248 -15.889 3.427   1.00   50.02  ? 398 SER D OG  1 
ATOM   11904 N N   . ASN D  1 399 ? 119.694 -15.954 6.845   1.00   43.48  ? 399 ASN D N   1 
ATOM   11905 C CA  . ASN D  1 399 ? 119.282 -16.806 7.962   1.00   45.39  ? 399 ASN D CA  1 
ATOM   11906 C C   . ASN D  1 399 ? 119.831 -16.203 9.244   1.00   43.64  ? 399 ASN D C   1 
ATOM   11907 O O   . ASN D  1 399 ? 120.747 -15.389 9.192   1.00   43.58  ? 399 ASN D O   1 
ATOM   11908 C CB  . ASN D  1 399 ? 119.771 -18.253 7.819   1.00   50.40  ? 399 ASN D CB  1 
ATOM   11909 C CG  . ASN D  1 399 ? 119.279 -18.925 6.548   1.00   55.94  ? 399 ASN D CG  1 
ATOM   11910 O OD1 . ASN D  1 399 ? 118.096 -19.251 6.422   1.00   58.00  ? 399 ASN D OD1 1 
ATOM   11911 N ND2 . ASN D  1 399 ? 120.204 -19.204 5.628   1.00   55.99  ? 399 ASN D ND2 1 
ATOM   11912 N N   . SER D  1 400 ? 119.276 -16.583 10.390  1.00   43.59  ? 400 SER D N   1 
ATOM   11913 C CA  . SER D  1 400 ? 119.752 -16.044 11.657  1.00   43.15  ? 400 SER D CA  1 
ATOM   11914 C C   . SER D  1 400 ? 121.196 -16.455 11.907  1.00   46.98  ? 400 SER D C   1 
ATOM   11915 O O   . SER D  1 400 ? 121.617 -17.538 11.519  1.00   50.43  ? 400 SER D O   1 
ATOM   11916 C CB  . SER D  1 400 ? 118.874 -16.514 12.819  1.00   39.91  ? 400 SER D CB  1 
ATOM   11917 O OG  . SER D  1 400 ? 119.088 -17.881 13.096  1.00   41.04  ? 400 SER D OG  1 
ATOM   11918 N N   . LEU D  1 401 ? 121.947 -15.583 12.568  1.00   46.08  ? 401 LEU D N   1 
ATOM   11919 C CA  . LEU D  1 401 ? 123.315 -15.889 12.944  1.00   44.60  ? 401 LEU D CA  1 
ATOM   11920 C C   . LEU D  1 401 ? 123.326 -17.107 13.830  1.00   45.93  ? 401 LEU D C   1 
ATOM   11921 O O   . LEU D  1 401 ? 124.199 -17.977 13.725  1.00   45.48  ? 401 LEU D O   1 
ATOM   11922 C CB  . LEU D  1 401 ? 123.956 -14.709 13.672  1.00   42.51  ? 401 LEU D CB  1 
ATOM   11923 C CG  . LEU D  1 401 ? 124.129 -13.484 12.781  1.00   41.40  ? 401 LEU D CG  1 
ATOM   11924 C CD1 . LEU D  1 401 ? 125.025 -12.433 13.428  1.00   40.31  ? 401 LEU D CD1 1 
ATOM   11925 C CD2 . LEU D  1 401 ? 124.648 -13.878 11.398  1.00   41.22  ? 401 LEU D CD2 1 
ATOM   11926 N N   . LYS D  1 402 ? 122.311 -17.177 14.680  1.00   45.06  ? 402 LYS D N   1 
ATOM   11927 C CA  . LYS D  1 402 ? 122.243 -18.215 15.685  1.00   47.55  ? 402 LYS D CA  1 
ATOM   11928 C C   . LYS D  1 402 ? 122.152 -19.550 14.967  1.00   47.56  ? 402 LYS D C   1 
ATOM   11929 O O   . LYS D  1 402 ? 122.670 -20.547 15.451  1.00   48.24  ? 402 LYS D O   1 
ATOM   11930 C CB  . LYS D  1 402 ? 121.049 -17.968 16.605  1.00   51.09  ? 402 LYS D CB  1 
ATOM   11931 C CG  . LYS D  1 402 ? 120.667 -19.103 17.536  1.00   60.93  ? 402 LYS D CG  1 
ATOM   11932 C CD  . LYS D  1 402 ? 119.551 -18.637 18.478  1.00   65.36  ? 402 LYS D CD  1 
ATOM   11933 C CE  . LYS D  1 402 ? 118.912 -19.765 19.295  1.00   70.49  ? 402 LYS D CE  1 
ATOM   11934 N NZ  . LYS D  1 402 ? 118.360 -19.259 20.607  1.00   71.71  ? 402 LYS D NZ  1 
ATOM   11935 N N   . SER D  1 403 ? 121.548 -19.552 13.778  1.00   47.51  ? 403 SER D N   1 
ATOM   11936 C CA  . SER D  1 403 ? 121.462 -20.766 12.957  1.00   50.09  ? 403 SER D CA  1 
ATOM   11937 C C   . SER D  1 403 ? 122.792 -21.177 12.336  1.00   52.84  ? 403 SER D C   1 
ATOM   11938 O O   . SER D  1 403 ? 122.934 -22.316 11.885  1.00   57.52  ? 403 SER D O   1 
ATOM   11939 C CB  . SER D  1 403 ? 120.434 -20.606 11.834  1.00   50.22  ? 403 SER D CB  1 
ATOM   11940 O OG  . SER D  1 403 ? 121.007 -19.999 10.695  1.00   48.61  ? 403 SER D OG  1 
ATOM   11941 N N   . TYR D  1 404 ? 123.761 -20.267 12.283  1.00   50.17  ? 404 TYR D N   1 
ATOM   11942 C CA  . TYR D  1 404 ? 125.106 -20.654 11.841  1.00   49.61  ? 404 TYR D CA  1 
ATOM   11943 C C   . TYR D  1 404 ? 125.975 -20.955 13.062  1.00   51.28  ? 404 TYR D C   1 
ATOM   11944 O O   . TYR D  1 404 ? 127.131 -21.317 12.925  1.00   50.83  ? 404 TYR D O   1 
ATOM   11945 C CB  . TYR D  1 404 ? 125.767 -19.576 10.996  1.00   44.36  ? 404 TYR D CB  1 
ATOM   11946 C CG  . TYR D  1 404 ? 125.060 -19.247 9.706   1.00   41.30  ? 404 TYR D CG  1 
ATOM   11947 C CD1 . TYR D  1 404 ? 125.284 -19.983 8.555   1.00   42.01  ? 404 TYR D CD1 1 
ATOM   11948 C CD2 . TYR D  1 404 ? 124.179 -18.192 9.642   1.00   39.70  ? 404 TYR D CD2 1 
ATOM   11949 C CE1 . TYR D  1 404 ? 124.641 -19.668 7.366   1.00   41.88  ? 404 TYR D CE1 1 
ATOM   11950 C CE2 . TYR D  1 404 ? 123.534 -17.860 8.464   1.00   40.99  ? 404 TYR D CE2 1 
ATOM   11951 C CZ  . TYR D  1 404 ? 123.762 -18.599 7.327   1.00   42.26  ? 404 TYR D CZ  1 
ATOM   11952 O OH  . TYR D  1 404 ? 123.106 -18.244 6.159   1.00   41.49  ? 404 TYR D OH  1 
ATOM   11953 N N   . GLY D  1 405 ? 125.402 -20.812 14.255  1.00   53.39  ? 405 GLY D N   1 
ATOM   11954 C CA  . GLY D  1 405 ? 126.136 -20.946 15.504  1.00   53.50  ? 405 GLY D CA  1 
ATOM   11955 C C   . GLY D  1 405 ? 126.951 -19.729 15.891  1.00   51.57  ? 405 GLY D C   1 
ATOM   11956 O O   . GLY D  1 405 ? 127.869 -19.814 16.706  1.00   50.13  ? 405 GLY D O   1 
ATOM   11957 N N   . LYS D  1 406 ? 126.575 -18.581 15.330  1.00   49.91  ? 406 LYS D N   1 
ATOM   11958 C CA  . LYS D  1 406 ? 127.335 -17.353 15.483  1.00   46.52  ? 406 LYS D CA  1 
ATOM   11959 C C   . LYS D  1 406 ? 126.539 -16.295 16.234  1.00   44.96  ? 406 LYS D C   1 
ATOM   11960 O O   . LYS D  1 406 ? 125.319 -16.382 16.382  1.00   45.75  ? 406 LYS D O   1 
ATOM   11961 C CB  . LYS D  1 406 ? 127.749 -16.807 14.110  1.00   42.43  ? 406 LYS D CB  1 
ATOM   11962 C CG  . LYS D  1 406 ? 128.448 -17.796 13.189  1.00   45.54  ? 406 LYS D CG  1 
ATOM   11963 C CD  . LYS D  1 406 ? 129.867 -18.071 13.646  1.00   53.10  ? 406 LYS D CD  1 
ATOM   11964 C CE  . LYS D  1 406 ? 130.504 -19.276 12.935  1.00   61.23  ? 406 LYS D CE  1 
ATOM   11965 N NZ  . LYS D  1 406 ? 130.254 -19.323 11.466  1.00   64.45  ? 406 LYS D NZ  1 
ATOM   11966 N N   . THR D  1 407 ? 127.262 -15.303 16.731  1.00   41.91  ? 407 THR D N   1 
ATOM   11967 C CA  . THR D  1 407 ? 126.665 -14.103 17.275  1.00   38.77  ? 407 THR D CA  1 
ATOM   11968 C C   . THR D  1 407 ? 127.430 -12.916 16.709  1.00   36.94  ? 407 THR D C   1 
ATOM   11969 O O   . THR D  1 407 ? 128.488 -13.088 16.127  1.00   37.92  ? 407 THR D O   1 
ATOM   11970 C CB  . THR D  1 407 ? 126.735 -14.059 18.785  1.00   41.09  ? 407 THR D CB  1 
ATOM   11971 O OG1 . THR D  1 407 ? 128.102 -13.878 19.163  1.00   42.15  ? 407 THR D OG1 1 
ATOM   11972 C CG2 . THR D  1 407 ? 126.205 -15.360 19.394  1.00   45.30  ? 407 THR D CG2 1 
ATOM   11973 N N   . CYS D  1 408 ? 126.911 -11.711 16.904  1.00   34.27  ? 408 CYS D N   1 
ATOM   11974 C CA  . CYS D  1 408 ? 127.601 -10.522 16.442  1.00   34.20  ? 408 CYS D CA  1 
ATOM   11975 C C   . CYS D  1 408 ? 128.885 -10.291 17.250  1.00   37.47  ? 408 CYS D C   1 
ATOM   11976 O O   . CYS D  1 408 ? 129.751 -9.535  16.818  1.00   39.61  ? 408 CYS D O   1 
ATOM   11977 C CB  . CYS D  1 408 ? 126.679 -9.282  16.487  1.00   33.55  ? 408 CYS D CB  1 
ATOM   11978 S SG  . CYS D  1 408 ? 125.741 -8.982  14.935  1.00   36.83  ? 408 CYS D SG  1 
ATOM   11979 N N   . SER D  1 409 ? 129.024 -10.911 18.420  1.00   39.08  ? 409 SER D N   1 
ATOM   11980 C CA  . SER D  1 409 ? 130.281 -10.775 19.139  1.00   39.86  ? 409 SER D CA  1 
ATOM   11981 C C   . SER D  1 409 ? 131.338 -11.724 18.649  1.00   42.25  ? 409 SER D C   1 
ATOM   11982 O O   . SER D  1 409 ? 132.516 -11.401 18.714  1.00   44.36  ? 409 SER D O   1 
ATOM   11983 C CB  . SER D  1 409 ? 130.100 -10.974 20.633  1.00   46.14  ? 409 SER D CB  1 
ATOM   11984 O OG  . SER D  1 409 ? 129.266 -9.967  21.150  1.00   49.67  ? 409 SER D OG  1 
ATOM   11985 N N   . ASN D  1 410 ? 130.937 -12.891 18.155  1.00   43.17  ? 410 ASN D N   1 
ATOM   11986 C CA  . ASN D  1 410 ? 131.931 -13.874 17.768  1.00   43.31  ? 410 ASN D CA  1 
ATOM   11987 C C   . ASN D  1 410 ? 131.977 -14.125 16.265  1.00   43.25  ? 410 ASN D C   1 
ATOM   11988 O O   . ASN D  1 410 ? 132.711 -15.000 15.810  1.00   46.20  ? 410 ASN D O   1 
ATOM   11989 C CB  . ASN D  1 410 ? 131.704 -15.211 18.509  1.00   44.39  ? 410 ASN D CB  1 
ATOM   11990 C CG  . ASN D  1 410 ? 130.421 -15.928 18.101  1.00   45.49  ? 410 ASN D CG  1 
ATOM   11991 O OD1 . ASN D  1 410 ? 129.992 -15.881 16.950  1.00   46.59  ? 410 ASN D OD1 1 
ATOM   11992 N ND2 . ASN D  1 410 ? 129.818 -16.629 19.052  1.00   46.81  ? 410 ASN D ND2 1 
ATOM   11993 N N   . LEU D  1 411 ? 131.215 -13.362 15.491  1.00   39.77  ? 411 LEU D N   1 
ATOM   11994 C CA  . LEU D  1 411 ? 131.286 -13.525 14.053  1.00   37.78  ? 411 LEU D CA  1 
ATOM   11995 C C   . LEU D  1 411 ? 132.714 -13.180 13.602  1.00   41.23  ? 411 LEU D C   1 
ATOM   11996 O O   . LEU D  1 411 ? 133.286 -13.837 12.719  1.00   38.79  ? 411 LEU D O   1 
ATOM   11997 C CB  . LEU D  1 411 ? 130.239 -12.668 13.365  1.00   33.72  ? 411 LEU D CB  1 
ATOM   11998 C CG  . LEU D  1 411 ? 130.026 -12.964 11.879  1.00   35.43  ? 411 LEU D CG  1 
ATOM   11999 C CD1 . LEU D  1 411 ? 129.590 -14.403 11.597  1.00   34.89  ? 411 LEU D CD1 1 
ATOM   12000 C CD2 . LEU D  1 411 ? 129.012 -11.997 11.338  1.00   37.17  ? 411 LEU D CD2 1 
ATOM   12001 N N   . PHE D  1 412 ? 133.286 -12.160 14.245  1.00   41.56  ? 412 PHE D N   1 
ATOM   12002 C CA  . PHE D  1 412 ? 134.669 -11.743 14.029  1.00   36.66  ? 412 PHE D CA  1 
ATOM   12003 C C   . PHE D  1 412 ? 135.401 -11.704 15.352  1.00   39.75  ? 412 PHE D C   1 
ATOM   12004 O O   . PHE D  1 412 ? 134.779 -11.580 16.399  1.00   43.00  ? 412 PHE D O   1 
ATOM   12005 C CB  . PHE D  1 412 ? 134.732 -10.367 13.379  1.00   34.37  ? 412 PHE D CB  1 
ATOM   12006 C CG  . PHE D  1 412 ? 133.891 -10.242 12.148  1.00   32.72  ? 412 PHE D CG  1 
ATOM   12007 C CD1 . PHE D  1 412 ? 134.332 -10.754 10.935  1.00   33.15  ? 412 PHE D CD1 1 
ATOM   12008 C CD2 . PHE D  1 412 ? 132.642 -9.634  12.205  1.00   31.66  ? 412 PHE D CD2 1 
ATOM   12009 C CE1 . PHE D  1 412 ? 133.558 -10.637 9.797   1.00   31.21  ? 412 PHE D CE1 1 
ATOM   12010 C CE2 . PHE D  1 412 ? 131.855 -9.516  11.072  1.00   29.39  ? 412 PHE D CE2 1 
ATOM   12011 C CZ  . PHE D  1 412 ? 132.304 -10.017 9.867   1.00   29.96  ? 412 PHE D CZ  1 
ATOM   12012 N N   . ASP D  1 413 ? 136.724 -11.805 15.305  1.00   42.40  ? 413 ASP D N   1 
ATOM   12013 C CA  . ASP D  1 413 ? 137.555 -11.738 16.510  1.00   44.66  ? 413 ASP D CA  1 
ATOM   12014 C C   . ASP D  1 413 ? 137.700 -10.306 16.967  1.00   43.05  ? 413 ASP D C   1 
ATOM   12015 O O   . ASP D  1 413 ? 138.370 -9.520  16.304  1.00   41.33  ? 413 ASP D O   1 
ATOM   12016 C CB  . ASP D  1 413 ? 138.943 -12.321 16.254  1.00   46.05  ? 413 ASP D CB  1 
ATOM   12017 C CG  . ASP D  1 413 ? 139.714 -12.565 17.536  1.00   50.67  ? 413 ASP D CG  1 
ATOM   12018 O OD1 . ASP D  1 413 ? 139.490 -11.829 18.518  1.00   53.71  ? 413 ASP D OD1 1 
ATOM   12019 O OD2 . ASP D  1 413 ? 140.568 -13.474 17.561  1.00   52.63  1 413 ASP D OD2 1 
ATOM   12020 N N   . LEU D  1 414 ? 137.089 -9.982  18.104  1.00   44.58  ? 414 LEU D N   1 
ATOM   12021 C CA  . LEU D  1 414 ? 137.106 -8.621  18.631  1.00   42.70  ? 414 LEU D CA  1 
ATOM   12022 C C   . LEU D  1 414 ? 137.902 -8.504  19.909  1.00   48.93  ? 414 LEU D C   1 
ATOM   12023 O O   . LEU D  1 414 ? 137.751 -7.535  20.653  1.00   51.09  ? 414 LEU D O   1 
ATOM   12024 C CB  . LEU D  1 414 ? 135.689 -8.124  18.887  1.00   39.20  ? 414 LEU D CB  1 
ATOM   12025 C CG  . LEU D  1 414 ? 134.707 -8.104  17.729  1.00   36.09  ? 414 LEU D CG  1 
ATOM   12026 C CD1 . LEU D  1 414 ? 133.378 -7.612  18.243  1.00   36.80  ? 414 LEU D CD1 1 
ATOM   12027 C CD2 . LEU D  1 414 ? 135.204 -7.247  16.582  1.00   34.25  ? 414 LEU D CD2 1 
ATOM   12028 N N   . ASN D  1 415 ? 138.735 -9.498  20.178  1.00   53.74  ? 415 ASN D N   1 
ATOM   12029 C CA  . ASN D  1 415 ? 139.596 -9.483  21.366  1.00   60.41  ? 415 ASN D CA  1 
ATOM   12030 C C   . ASN D  1 415 ? 140.856 -8.643  21.137  1.00   61.81  ? 415 ASN D C   1 
ATOM   12031 O O   . ASN D  1 415 ? 141.433 -8.683  20.048  1.00   58.54  ? 415 ASN D O   1 
ATOM   12032 C CB  . ASN D  1 415 ? 139.965 -10.907 21.729  1.00   65.36  ? 415 ASN D CB  1 
ATOM   12033 C CG  . ASN D  1 415 ? 138.747 -11.785 21.886  1.00   67.52  ? 415 ASN D CG  1 
ATOM   12034 O OD1 . ASN D  1 415 ? 137.758 -11.395 22.502  1.00   70.27  ? 415 ASN D OD1 1 
ATOM   12035 N ND2 . ASN D  1 415 ? 138.800 -12.969 21.301  1.00   66.14  ? 415 ASN D ND2 1 
ATOM   12036 N N   . ASN D  1 416 ? 141.287 -7.889  22.146  1.00   67.16  ? 416 ASN D N   1 
ATOM   12037 C CA  . ASN D  1 416 ? 142.272 -6.840  21.906  1.00   73.88  ? 416 ASN D CA  1 
ATOM   12038 C C   . ASN D  1 416 ? 143.733 -7.287  22.140  1.00   75.80  ? 416 ASN D C   1 
ATOM   12039 O O   . ASN D  1 416 ? 144.025 -7.928  23.161  1.00   79.19  ? 416 ASN D O   1 
ATOM   12040 C CB  . ASN D  1 416 ? 141.928 -5.638  22.801  1.00   81.40  ? 416 ASN D CB  1 
ATOM   12041 C CG  . ASN D  1 416 ? 143.039 -4.614  22.861  1.00   89.74  ? 416 ASN D CG  1 
ATOM   12042 O OD1 . ASN D  1 416 ? 143.513 -4.286  23.946  1.00   93.79  ? 416 ASN D OD1 1 
ATOM   12043 N ND2 . ASN D  1 416 ? 143.429 -4.066  21.713  1.00   92.27  ? 416 ASN D ND2 1 
ATOM   12044 N N   . PRO D  1 417 ? 144.655 -6.940  21.198  1.00   71.79  ? 417 PRO D N   1 
ATOM   12045 C CA  . PRO D  1 417 ? 146.085 -7.164  21.453  1.00   73.67  ? 417 PRO D CA  1 
ATOM   12046 C C   . PRO D  1 417 ? 146.704 -6.145  22.392  1.00   77.17  ? 417 PRO D C   1 
ATOM   12047 O O   . PRO D  1 417 ? 147.144 -6.493  23.475  1.00   80.01  ? 417 PRO D O   1 
ATOM   12048 C CB  . PRO D  1 417 ? 146.713 -7.090  20.065  1.00   69.53  ? 417 PRO D CB  1 
ATOM   12049 C CG  . PRO D  1 417 ? 145.776 -6.303  19.208  1.00   64.98  ? 417 PRO D CG  1 
ATOM   12050 C CD  . PRO D  1 417 ? 144.418 -6.308  19.885  1.00   65.41  ? 417 PRO D CD  1 
ATOM   12051 N N   . LYS E  1 11  ? 149.692 0.301   -3.643  1.00   79.64  ? 11  LYS E N   1 
ATOM   12052 C CA  . LYS E  1 11  ? 149.096 1.633   -3.732  1.00   74.53  ? 11  LYS E CA  1 
ATOM   12053 C C   . LYS E  1 11  ? 150.176 2.726   -3.806  1.00   73.45  ? 11  LYS E C   1 
ATOM   12054 O O   . LYS E  1 11  ? 150.993 2.870   -2.884  1.00   74.90  ? 11  LYS E O   1 
ATOM   12055 C CB  . LYS E  1 11  ? 148.125 1.861   -2.568  1.00   71.59  ? 11  LYS E CB  1 
ATOM   12056 C CG  . LYS E  1 11  ? 146.661 1.525   -2.936  1.00   65.77  ? 11  LYS E CG  1 
ATOM   12057 C CD  . LYS E  1 11  ? 145.717 1.397   -1.714  1.00   63.60  ? 11  LYS E CD  1 
ATOM   12058 C CE  . LYS E  1 11  ? 144.327 0.789   -2.093  1.00   76.96  ? 11  LYS E CE  1 
ATOM   12059 N NZ  . LYS E  1 11  ? 143.819 1.067   -3.492  1.00   73.37  ? 11  LYS E NZ  1 
ATOM   12060 N N   . PRO E  1 12  ? 150.205 3.458   -4.942  1.00   68.74  ? 12  PRO E N   1 
ATOM   12061 C CA  . PRO E  1 12  ? 151.211 4.454   -5.323  1.00   67.27  ? 12  PRO E CA  1 
ATOM   12062 C C   . PRO E  1 12  ? 151.173 5.683   -4.428  1.00   65.07  ? 12  PRO E C   1 
ATOM   12063 O O   . PRO E  1 12  ? 150.118 6.003   -3.872  1.00   64.80  ? 12  PRO E O   1 
ATOM   12064 C CB  . PRO E  1 12  ? 150.818 4.820   -6.753  1.00   63.84  ? 12  PRO E CB  1 
ATOM   12065 C CG  . PRO E  1 12  ? 149.373 4.587   -6.812  1.00   61.07  ? 12  PRO E CG  1 
ATOM   12066 C CD  . PRO E  1 12  ? 149.096 3.419   -5.916  1.00   64.08  ? 12  PRO E CD  1 
ATOM   12067 N N   . ASN E  1 13  ? 152.315 6.359   -4.310  1.00   62.34  ? 13  ASN E N   1 
ATOM   12068 C CA  . ASN E  1 13  ? 152.423 7.528   -3.463  1.00   58.44  ? 13  ASN E CA  1 
ATOM   12069 C C   . ASN E  1 13  ? 152.411 8.793   -4.277  1.00   58.33  ? 13  ASN E C   1 
ATOM   12070 O O   . ASN E  1 13  ? 152.426 9.894   -3.721  1.00   62.65  ? 13  ASN E O   1 
ATOM   12071 C CB  . ASN E  1 13  ? 153.715 7.486   -2.664  1.00   57.77  ? 13  ASN E CB  1 
ATOM   12072 C CG  . ASN E  1 13  ? 153.646 6.541   -1.522  1.00   61.79  ? 13  ASN E CG  1 
ATOM   12073 O OD1 . ASN E  1 13  ? 152.653 6.486   -0.800  1.00   61.69  ? 13  ASN E OD1 1 
ATOM   12074 N ND2 . ASN E  1 13  ? 154.698 5.756   -1.353  1.00   66.51  ? 13  ASN E ND2 1 
ATOM   12075 N N   . LEU E  1 14  ? 152.398 8.650   -5.595  1.00   51.51  ? 14  LEU E N   1 
ATOM   12076 C CA  . LEU E  1 14  ? 152.432 9.831   -6.431  1.00   43.62  ? 14  LEU E CA  1 
ATOM   12077 C C   . LEU E  1 14  ? 151.858 9.511   -7.795  1.00   38.71  ? 14  LEU E C   1 
ATOM   12078 O O   . LEU E  1 14  ? 152.121 8.444   -8.337  1.00   40.99  ? 14  LEU E O   1 
ATOM   12079 C CB  . LEU E  1 14  ? 153.862 10.363  -6.533  1.00   42.17  ? 14  LEU E CB  1 
ATOM   12080 C CG  . LEU E  1 14  ? 154.089 11.787  -7.053  1.00   38.91  ? 14  LEU E CG  1 
ATOM   12081 C CD1 . LEU E  1 14  ? 153.673 12.832  -6.035  1.00   35.56  ? 14  LEU E CD1 1 
ATOM   12082 C CD2 . LEU E  1 14  ? 155.545 11.964  -7.424  1.00   39.65  ? 14  LEU E CD2 1 
ATOM   12083 N N   . LEU E  1 15  ? 151.019 10.410  -8.298  1.00   33.84  ? 15  LEU E N   1 
ATOM   12084 C CA  . LEU E  1 15  ? 150.430 10.297  -9.619  1.00   32.08  ? 15  LEU E CA  1 
ATOM   12085 C C   . LEU E  1 15  ? 150.793 11.513  -10.428 1.00   32.90  ? 15  LEU E C   1 
ATOM   12086 O O   . LEU E  1 15  ? 150.995 12.599  -9.890  1.00   35.08  ? 15  LEU E O   1 
ATOM   12087 C CB  . LEU E  1 15  ? 148.920 10.163  -9.556  1.00   30.94  ? 15  LEU E CB  1 
ATOM   12088 C CG  . LEU E  1 15  ? 148.418 9.099   -8.589  1.00   34.70  ? 15  LEU E CG  1 
ATOM   12089 C CD1 . LEU E  1 15  ? 146.930 9.192   -8.471  1.00   28.35  ? 15  LEU E CD1 1 
ATOM   12090 C CD2 . LEU E  1 15  ? 148.858 7.727   -9.052  1.00   39.89  ? 15  LEU E CD2 1 
ATOM   12091 N N   . VAL E  1 16  ? 150.885 11.321  -11.735 1.00   33.01  ? 16  VAL E N   1 
ATOM   12092 C CA  . VAL E  1 16  ? 151.366 12.362  -12.606 1.00   31.72  ? 16  VAL E CA  1 
ATOM   12093 C C   . VAL E  1 16  ? 150.485 12.483  -13.820 1.00   30.89  ? 16  VAL E C   1 
ATOM   12094 O O   . VAL E  1 16  ? 150.194 11.492  -14.490 1.00   31.63  ? 16  VAL E O   1 
ATOM   12095 C CB  . VAL E  1 16  ? 152.795 12.081  -13.080 1.00   34.51  ? 16  VAL E CB  1 
ATOM   12096 C CG1 . VAL E  1 16  ? 153.289 13.239  -13.939 1.00   32.70  ? 16  VAL E CG1 1 
ATOM   12097 C CG2 . VAL E  1 16  ? 153.721 11.832  -11.902 1.00   35.21  ? 16  VAL E CG2 1 
ATOM   12098 N N   . LEU E  1 17  ? 150.065 13.705  -14.101 1.00   29.03  ? 17  LEU E N   1 
ATOM   12099 C CA  . LEU E  1 17  ? 149.274 13.976  -15.276 1.00   28.82  ? 17  LEU E CA  1 
ATOM   12100 C C   . LEU E  1 17  ? 149.919 15.029  -16.159 1.00   30.57  ? 17  LEU E C   1 
ATOM   12101 O O   . LEU E  1 17  ? 150.023 16.186  -15.789 1.00   33.20  ? 17  LEU E O   1 
ATOM   12102 C CB  . LEU E  1 17  ? 147.873 14.409  -14.882 1.00   32.47  ? 17  LEU E CB  1 
ATOM   12103 C CG  . LEU E  1 17  ? 146.996 14.733  -16.084 1.00   34.63  ? 17  LEU E CG  1 
ATOM   12104 C CD1 . LEU E  1 17  ? 146.672 13.482  -16.876 1.00   34.88  ? 17  LEU E CD1 1 
ATOM   12105 C CD2 . LEU E  1 17  ? 145.748 15.393  -15.590 1.00   33.95  ? 17  LEU E CD2 1 
ATOM   12106 N N   . PRO E  1 18  ? 150.379 14.625  -17.337 1.00   31.79  ? 18  PRO E N   1 
ATOM   12107 C CA  . PRO E  1 18  ? 150.952 15.607  -18.261 1.00   32.52  ? 18  PRO E CA  1 
ATOM   12108 C C   . PRO E  1 18  ? 149.913 16.564  -18.818 1.00   33.11  ? 18  PRO E C   1 
ATOM   12109 O O   . PRO E  1 18  ? 148.811 16.145  -19.128 1.00   32.87  ? 18  PRO E O   1 
ATOM   12110 C CB  . PRO E  1 18  ? 151.548 14.739  -19.364 1.00   34.53  ? 18  PRO E CB  1 
ATOM   12111 C CG  . PRO E  1 18  ? 151.721 13.377  -18.728 1.00   35.14  ? 18  PRO E CG  1 
ATOM   12112 C CD  . PRO E  1 18  ? 150.551 13.246  -17.806 1.00   31.45  ? 18  PRO E CD  1 
ATOM   12113 N N   . VAL E  1 19  ? 150.273 17.841  -18.918 1.00   33.25  ? 19  VAL E N   1 
ATOM   12114 C CA  . VAL E  1 19  ? 149.370 18.862  -19.407 1.00   31.12  ? 19  VAL E CA  1 
ATOM   12115 C C   . VAL E  1 19  ? 150.083 19.616  -20.517 1.00   34.17  ? 19  VAL E C   1 
ATOM   12116 O O   . VAL E  1 19  ? 151.296 19.765  -20.504 1.00   34.07  ? 19  VAL E O   1 
ATOM   12117 C CB  A VAL E  1 19  ? 148.963 19.823  -18.269 0.50   28.46  ? 19  VAL E CB  1 
ATOM   12118 C CB  B VAL E  1 19  ? 148.901 19.834  -18.296 0.50   28.43  ? 19  VAL E CB  1 
ATOM   12119 C CG1 A VAL E  1 19  ? 148.066 20.927  -18.771 0.50   26.91  ? 19  VAL E CG1 1 
ATOM   12120 C CG1 B VAL E  1 19  ? 148.252 19.063  -17.173 0.50   27.48  ? 19  VAL E CG1 1 
ATOM   12121 C CG2 A VAL E  1 19  ? 148.292 19.056  -17.155 0.50   27.53  ? 19  VAL E CG2 1 
ATOM   12122 C CG2 B VAL E  1 19  ? 150.049 20.679  -17.769 0.50   28.58  ? 19  VAL E CG2 1 
ATOM   12123 N N   . GLN E  1 20  ? 149.324 20.113  -21.476 1.00   38.33  ? 20  GLN E N   1 
ATOM   12124 C CA  . GLN E  1 20  ? 149.918 20.771  -22.625 1.00   38.96  ? 20  GLN E CA  1 
ATOM   12125 C C   . GLN E  1 20  ? 149.304 22.145  -22.865 1.00   36.74  ? 20  GLN E C   1 
ATOM   12126 O O   . GLN E  1 20  ? 148.102 22.341  -22.706 1.00   35.84  ? 20  GLN E O   1 
ATOM   12127 C CB  . GLN E  1 20  ? 149.745 19.923  -23.887 1.00   43.90  ? 20  GLN E CB  1 
ATOM   12128 C CG  . GLN E  1 20  ? 150.581 20.462  -25.068 1.00   55.07  ? 20  GLN E CG  1 
ATOM   12129 C CD  . GLN E  1 20  ? 150.663 19.509  -26.236 1.00   63.40  ? 20  GLN E CD  1 
ATOM   12130 O OE1 . GLN E  1 20  ? 150.570 18.293  -26.072 1.00   64.77  ? 20  GLN E OE1 1 
ATOM   12131 N NE2 . GLN E  1 20  ? 150.821 20.062  -27.433 1.00   68.38  ? 20  GLN E NE2 1 
ATOM   12132 N N   . GLU E  1 21  ? 150.143 23.087  -23.266 1.00   37.43  ? 21  GLU E N   1 
ATOM   12133 C CA  . GLU E  1 21  ? 149.703 24.417  -23.614 1.00   37.79  ? 21  GLU E CA  1 
ATOM   12134 C C   . GLU E  1 21  ? 149.172 24.455  -25.052 1.00   40.36  ? 21  GLU E C   1 
ATOM   12135 O O   . GLU E  1 21  ? 149.754 23.854  -25.960 1.00   42.08  ? 21  GLU E O   1 
ATOM   12136 C CB  . GLU E  1 21  ? 150.858 25.396  -23.425 1.00   39.41  ? 21  GLU E CB  1 
ATOM   12137 C CG  . GLU E  1 21  ? 150.402 26.809  -23.254 1.00   41.72  ? 21  GLU E CG  1 
ATOM   12138 C CD  . GLU E  1 21  ? 150.519 27.615  -24.510 1.00   48.76  ? 21  GLU E CD  1 
ATOM   12139 O OE1 . GLU E  1 21  ? 150.958 27.065  -25.539 1.00   52.14  ? 21  GLU E OE1 1 
ATOM   12140 O OE2 . GLU E  1 21  ? 150.162 28.806  -24.475 1.00   51.16  ? 21  GLU E OE2 1 
ATOM   12141 N N   . ASP E  1 22  ? 148.041 25.127  -25.237 1.00   41.57  ? 22  ASP E N   1 
ATOM   12142 C CA  . ASP E  1 22  ? 147.460 25.351  -26.551 1.00   42.07  ? 22  ASP E CA  1 
ATOM   12143 C C   . ASP E  1 22  ? 147.817 26.745  -26.985 1.00   47.20  ? 22  ASP E C   1 
ATOM   12144 O O   . ASP E  1 22  ? 147.483 27.701  -26.309 1.00   46.97  ? 22  ASP E O   1 
ATOM   12145 C CB  . ASP E  1 22  ? 145.948 25.173  -26.534 1.00   42.00  ? 22  ASP E CB  1 
ATOM   12146 C CG  . ASP E  1 22  ? 145.316 25.435  -27.884 1.00   46.96  ? 22  ASP E CG  1 
ATOM   12147 O OD1 . ASP E  1 22  ? 145.609 24.686  -28.842 1.00   48.98  ? 22  ASP E OD1 1 
ATOM   12148 O OD2 . ASP E  1 22  ? 144.531 26.397  -27.990 1.00   48.00  1 22  ASP E OD2 1 
ATOM   12149 N N   . ALA E  1 23  ? 148.556 26.854  -28.080 1.00   52.76  ? 23  ALA E N   1 
ATOM   12150 C CA  . ALA E  1 23  ? 149.101 28.128  -28.521 1.00   55.14  ? 23  ALA E CA  1 
ATOM   12151 C C   . ALA E  1 23  ? 148.017 29.123  -28.905 1.00   58.25  ? 23  ALA E C   1 
ATOM   12152 O O   . ALA E  1 23  ? 148.056 30.295  -28.531 1.00   58.64  ? 23  ALA E O   1 
ATOM   12153 C CB  . ALA E  1 23  ? 150.037 27.899  -29.679 1.00   55.95  ? 23  ALA E CB  1 
ATOM   12154 N N   . SER E  1 24  ? 147.036 28.628  -29.641 1.00   59.74  ? 24  SER E N   1 
ATOM   12155 C CA  . SER E  1 24  ? 145.973 29.458  -30.150 1.00   61.21  ? 24  SER E CA  1 
ATOM   12156 C C   . SER E  1 24  ? 145.207 30.154  -29.035 1.00   57.83  ? 24  SER E C   1 
ATOM   12157 O O   . SER E  1 24  ? 145.002 31.358  -29.070 1.00   59.36  ? 24  SER E O   1 
ATOM   12158 C CB  . SER E  1 24  ? 145.028 28.615  -30.981 1.00   64.59  ? 24  SER E CB  1 
ATOM   12159 O OG  . SER E  1 24  ? 143.926 29.396  -31.372 1.00   69.25  ? 24  SER E OG  1 
ATOM   12160 N N   . THR E  1 25  ? 144.802 29.390  -28.031 1.00   55.66  ? 25  THR E N   1 
ATOM   12161 C CA  . THR E  1 25  ? 143.945 29.911  -26.970 1.00   52.77  ? 25  THR E CA  1 
ATOM   12162 C C   . THR E  1 25  ? 144.702 30.338  -25.729 1.00   48.57  ? 25  THR E C   1 
ATOM   12163 O O   . THR E  1 25  ? 144.175 31.056  -24.902 1.00   47.79  ? 25  THR E O   1 
ATOM   12164 C CB  . THR E  1 25  ? 142.919 28.873  -26.509 1.00   50.21  ? 25  THR E CB  1 
ATOM   12165 O OG1 . THR E  1 25  ? 143.606 27.775  -25.908 1.00   48.59  ? 25  THR E OG1 1 
ATOM   12166 C CG2 . THR E  1 25  ? 142.100 28.374  -27.671 1.00   53.14  ? 25  THR E CG2 1 
ATOM   12167 N N   . GLY E  1 26  ? 145.916 29.845  -25.562 1.00   47.13  ? 26  GLY E N   1 
ATOM   12168 C CA  . GLY E  1 26  ? 146.685 30.158  -24.375 1.00   45.07  ? 26  GLY E CA  1 
ATOM   12169 C C   . GLY E  1 26  ? 146.239 29.345  -23.170 1.00   42.38  ? 26  GLY E C   1 
ATOM   12170 O O   . GLY E  1 26  ? 146.730 29.546  -22.059 1.00   41.09  ? 26  GLY E O   1 
ATOM   12171 N N   . LEU E  1 27  ? 145.327 28.403  -23.398 1.00   40.68  ? 27  LEU E N   1 
ATOM   12172 C CA  . LEU E  1 27  ? 144.819 27.553  -22.334 1.00   34.96  ? 27  LEU E CA  1 
ATOM   12173 C C   . LEU E  1 27  ? 145.557 26.242  -22.331 1.00   33.27  ? 27  LEU E C   1 
ATOM   12174 O O   . LEU E  1 27  ? 146.284 25.964  -23.255 1.00   36.35  ? 27  LEU E O   1 
ATOM   12175 C CB  . LEU E  1 27  ? 143.316 27.310  -22.486 1.00   36.88  ? 27  LEU E CB  1 
ATOM   12176 C CG  . LEU E  1 27  ? 142.399 28.537  -22.496 1.00   40.70  ? 27  LEU E CG  1 
ATOM   12177 C CD1 . LEU E  1 27  ? 140.970 28.132  -22.749 1.00   41.76  ? 27  LEU E CD1 1 
ATOM   12178 C CD2 . LEU E  1 27  ? 142.500 29.310  -21.198 1.00   41.14  ? 27  LEU E CD2 1 
ATOM   12179 N N   . HIS E  1 28  ? 145.369 25.454  -21.278 1.00   35.71  ? 28  HIS E N   1 
ATOM   12180 C CA  . HIS E  1 28  ? 146.037 24.161  -21.102 1.00   34.57  ? 28  HIS E CA  1 
ATOM   12181 C C   . HIS E  1 28  ? 145.028 23.021  -21.087 1.00   34.22  ? 28  HIS E C   1 
ATOM   12182 O O   . HIS E  1 28  ? 143.907 23.200  -20.633 1.00   33.98  ? 28  HIS E O   1 
ATOM   12183 C CB  . HIS E  1 28  ? 146.843 24.148  -19.800 1.00   31.72  ? 28  HIS E CB  1 
ATOM   12184 C CG  . HIS E  1 28  ? 147.996 25.095  -19.810 1.00   30.20  ? 28  HIS E CG  1 
ATOM   12185 N ND1 . HIS E  1 28  ? 149.305 24.672  -19.860 1.00   30.37  ? 28  HIS E ND1 1 
ATOM   12186 C CD2 . HIS E  1 28  ? 148.036 26.446  -19.797 1.00   31.56  ? 28  HIS E CD2 1 
ATOM   12187 C CE1 . HIS E  1 28  ? 150.102 25.724  -19.889 1.00   33.10  ? 28  HIS E CE1 1 
ATOM   12188 N NE2 . HIS E  1 28  ? 149.356 26.814  -19.849 1.00   33.04  ? 28  HIS E NE2 1 
ATOM   12189 N N   . TRP E  1 29  ? 145.430 21.856  -21.584 1.00   34.72  ? 29  TRP E N   1 
ATOM   12190 C CA  . TRP E  1 29  ? 144.542 20.695  -21.663 1.00   36.28  ? 29  TRP E CA  1 
ATOM   12191 C C   . TRP E  1 29  ? 145.331 19.414  -21.396 1.00   37.33  ? 29  TRP E C   1 
ATOM   12192 O O   . TRP E  1 29  ? 146.556 19.428  -21.422 1.00   37.59  ? 29  TRP E O   1 
ATOM   12193 C CB  . TRP E  1 29  ? 143.849 20.644  -23.025 1.00   38.33  ? 29  TRP E CB  1 
ATOM   12194 C CG  . TRP E  1 29  ? 144.814 20.512  -24.117 1.00   40.71  ? 29  TRP E CG  1 
ATOM   12195 C CD1 . TRP E  1 29  ? 145.528 21.514  -24.704 1.00   43.22  ? 29  TRP E CD1 1 
ATOM   12196 C CD2 . TRP E  1 29  ? 145.218 19.303  -24.750 1.00   44.29  ? 29  TRP E CD2 1 
ATOM   12197 N NE1 . TRP E  1 29  ? 146.355 21.000  -25.675 1.00   45.21  ? 29  TRP E NE1 1 
ATOM   12198 C CE2 . TRP E  1 29  ? 146.182 19.643  -25.722 1.00   47.05  ? 29  TRP E CE2 1 
ATOM   12199 C CE3 . TRP E  1 29  ? 144.858 17.958  -24.592 1.00   45.12  ? 29  TRP E CE3 1 
ATOM   12200 C CZ2 . TRP E  1 29  ? 146.786 18.689  -26.533 1.00   51.54  ? 29  TRP E CZ2 1 
ATOM   12201 C CZ3 . TRP E  1 29  ? 145.462 17.013  -25.391 1.00   48.07  ? 29  TRP E CZ3 1 
ATOM   12202 C CH2 . TRP E  1 29  ? 146.416 17.381  -26.352 1.00   51.15  ? 29  TRP E CH2 1 
ATOM   12203 N N   . ALA E  1 30  ? 144.631 18.317  -21.124 1.00   37.61  ? 30  ALA E N   1 
ATOM   12204 C CA  . ALA E  1 30  ? 145.281 17.034  -20.856 1.00   35.36  ? 30  ALA E CA  1 
ATOM   12205 C C   . ALA E  1 30  ? 144.570 15.864  -21.540 1.00   38.84  ? 30  ALA E C   1 
ATOM   12206 O O   . ALA E  1 30  ? 143.349 15.880  -21.695 1.00   39.83  ? 30  ALA E O   1 
ATOM   12207 C CB  . ALA E  1 30  ? 145.331 16.797  -19.365 1.00   29.83  ? 30  ALA E CB  1 
ATOM   12208 N N   . ASN E  1 31  ? 145.331 14.860  -21.964 1.00   40.37  ? 31  ASN E N   1 
ATOM   12209 C CA  . ASN E  1 31  ? 144.735 13.586  -22.341 1.00   43.95  ? 31  ASN E CA  1 
ATOM   12210 C C   . ASN E  1 31  ? 144.481 12.720  -21.127 1.00   44.75  ? 31  ASN E C   1 
ATOM   12211 O O   . ASN E  1 31  ? 145.398 12.255  -20.463 1.00   46.65  ? 31  ASN E O   1 
ATOM   12212 C CB  . ASN E  1 31  ? 145.613 12.827  -23.322 1.00   47.90  ? 31  ASN E CB  1 
ATOM   12213 C CG  . ASN E  1 31  ? 145.340 13.196  -24.753 1.00   52.94  ? 31  ASN E CG  1 
ATOM   12214 O OD1 . ASN E  1 31  ? 144.189 13.301  -25.183 1.00   52.48  ? 31  ASN E OD1 1 
ATOM   12215 N ND2 . ASN E  1 31  ? 146.402 13.367  -25.515 1.00   58.29  ? 31  ASN E ND2 1 
ATOM   12216 N N   . ILE E  1 32  ? 143.212 12.486  -20.863 1.00   43.47  ? 32  ILE E N   1 
ATOM   12217 C CA  . ILE E  1 32  ? 142.809 11.665  -19.758 1.00   39.85  ? 32  ILE E CA  1 
ATOM   12218 C C   . ILE E  1 32  ? 142.410 10.304  -20.269 1.00   39.43  ? 32  ILE E C   1 
ATOM   12219 O O   . ILE E  1 32  ? 141.694 10.196  -21.261 1.00   37.16  ? 32  ILE E O   1 
ATOM   12220 C CB  . ILE E  1 32  ? 141.639 12.323  -19.009 1.00   39.36  ? 32  ILE E CB  1 
ATOM   12221 C CG1 . ILE E  1 32  ? 142.023 13.737  -18.606 1.00   38.05  ? 32  ILE E CG1 1 
ATOM   12222 C CG2 . ILE E  1 32  ? 141.264 11.544  -17.765 1.00   37.60  ? 32  ILE E CG2 1 
ATOM   12223 C CD1 . ILE E  1 32  ? 143.049 13.760  -17.526 1.00   36.79  ? 32  ILE E CD1 1 
ATOM   12224 N N   . HIS E  1 33  ? 142.873 9.264   -19.587 1.00   43.29  ? 33  HIS E N   1 
ATOM   12225 C CA  . HIS E  1 33  ? 142.518 7.891   -19.937 1.00   45.19  ? 33  HIS E CA  1 
ATOM   12226 C C   . HIS E  1 33  ? 141.272 7.409   -19.208 1.00   42.31  ? 33  HIS E C   1 
ATOM   12227 O O   . HIS E  1 33  ? 141.230 7.384   -17.978 1.00   38.86  ? 33  HIS E O   1 
ATOM   12228 C CB  . HIS E  1 33  ? 143.659 6.961   -19.612 1.00   47.88  ? 33  HIS E CB  1 
ATOM   12229 C CG  . HIS E  1 33  ? 144.884 7.239   -20.404 1.00   52.11  ? 33  HIS E CG  1 
ATOM   12230 N ND1 . HIS E  1 33  ? 145.648 8.366   -20.202 1.00   51.03  ? 33  HIS E ND1 1 
ATOM   12231 C CD2 . HIS E  1 33  ? 145.485 6.537   -21.389 1.00   55.54  ? 33  HIS E CD2 1 
ATOM   12232 C CE1 . HIS E  1 33  ? 146.668 8.349   -21.038 1.00   54.23  ? 33  HIS E CE1 1 
ATOM   12233 N NE2 . HIS E  1 33  ? 146.595 7.250   -21.766 1.00   57.08  ? 33  HIS E NE2 1 
ATOM   12234 N N   . LYS E  1 34  ? 140.270 7.007   -19.984 1.00   42.61  ? 34  LYS E N   1 
ATOM   12235 C CA  . LYS E  1 34  ? 138.985 6.582   -19.457 1.00   43.01  ? 34  LYS E CA  1 
ATOM   12236 C C   . LYS E  1 34  ? 138.398 5.395   -20.200 1.00   46.08  ? 34  LYS E C   1 
ATOM   12237 O O   . LYS E  1 34  ? 138.824 5.078   -21.312 1.00   49.76  ? 34  LYS E O   1 
ATOM   12238 C CB  . LYS E  1 34  ? 138.008 7.745   -19.495 1.00   43.69  ? 34  LYS E CB  1 
ATOM   12239 C CG  . LYS E  1 34  ? 138.536 8.964   -18.787 1.00   44.58  ? 34  LYS E CG  1 
ATOM   12240 C CD  . LYS E  1 34  ? 137.429 9.883   -18.424 1.00   46.28  ? 34  LYS E CD  1 
ATOM   12241 C CE  . LYS E  1 34  ? 136.431 9.229   -17.515 1.00   46.28  ? 34  LYS E CE  1 
ATOM   12242 N NZ  . LYS E  1 34  ? 135.147 9.933   -17.704 1.00   46.30  ? 34  LYS E NZ  1 
ATOM   12243 N N   . ARG E  1 35  ? 137.418 4.754   -19.563 1.00   44.71  ? 35  ARG E N   1 
ATOM   12244 C CA  . ARG E  1 35  ? 136.591 3.703   -20.161 1.00   44.39  ? 35  ARG E CA  1 
ATOM   12245 C C   . ARG E  1 35  ? 137.254 2.325   -20.228 1.00   46.18  ? 35  ARG E C   1 
ATOM   12246 O O   . ARG E  1 35  ? 138.441 2.163   -19.937 1.00   47.90  ? 35  ARG E O   1 
ATOM   12247 C CB  . ARG E  1 35  ? 136.129 4.134   -21.560 1.00   43.81  ? 35  ARG E CB  1 
ATOM   12248 C CG  . ARG E  1 35  ? 135.350 5.438   -21.520 1.00   42.11  ? 35  ARG E CG  1 
ATOM   12249 C CD  . ARG E  1 35  ? 135.060 6.078   -22.877 1.00   45.69  ? 35  ARG E CD  1 
ATOM   12250 N NE  . ARG E  1 35  ? 134.696 7.493   -22.712 1.00   47.04  ? 35  ARG E NE  1 
ATOM   12251 C CZ  . ARG E  1 35  ? 134.254 8.291   -23.684 1.00   49.34  ? 35  ARG E CZ  1 
ATOM   12252 N NH1 . ARG E  1 35  ? 134.090 7.831   -24.920 1.00   52.73  ? 35  ARG E NH1 1 
ATOM   12253 N NH2 . ARG E  1 35  ? 133.948 9.552   -23.410 1.00   46.83  ? 35  ARG E NH2 1 
ATOM   12254 N N   . THR E  1 36  ? 136.453 1.320   -20.569 1.00   46.30  ? 36  THR E N   1 
ATOM   12255 C CA  . THR E  1 36  ? 136.975 -0.011  -20.838 1.00   46.71  ? 36  THR E CA  1 
ATOM   12256 C C   . THR E  1 36  ? 136.480 -0.465  -22.206 1.00   52.04  ? 36  THR E C   1 
ATOM   12257 O O   . THR E  1 36  ? 135.281 -0.682  -22.386 1.00   54.28  ? 36  THR E O   1 
ATOM   12258 C CB  . THR E  1 36  ? 136.554 -1.032  -19.770 1.00   45.49  ? 36  THR E CB  1 
ATOM   12259 O OG1 . THR E  1 36  ? 136.870 -0.537  -18.462 1.00   44.71  ? 36  THR E OG1 1 
ATOM   12260 C CG2 . THR E  1 36  ? 137.276 -2.330  -19.992 1.00   45.30  ? 36  THR E CG2 1 
ATOM   12261 N N   . PRO E  1 37  ? 137.399 -0.630  -23.177 1.00   54.84  ? 37  PRO E N   1 
ATOM   12262 C CA  . PRO E  1 37  ? 138.861 -0.485  -23.107 1.00   54.10  ? 37  PRO E CA  1 
ATOM   12263 C C   . PRO E  1 37  ? 139.324 0.954   -22.905 1.00   53.40  ? 37  PRO E C   1 
ATOM   12264 O O   . PRO E  1 37  ? 138.614 1.899   -23.252 1.00   54.77  ? 37  PRO E O   1 
ATOM   12265 C CB  . PRO E  1 37  ? 139.327 -1.015  -24.463 1.00   58.59  ? 37  PRO E CB  1 
ATOM   12266 C CG  . PRO E  1 37  ? 138.187 -0.804  -25.363 1.00   59.92  ? 37  PRO E CG  1 
ATOM   12267 C CD  . PRO E  1 37  ? 136.962 -1.017  -24.530 1.00   58.49  ? 37  PRO E CD  1 
ATOM   12268 N N   . LEU E  1 38  ? 140.506 1.110   -22.328 1.00   49.96  ? 38  LEU E N   1 
ATOM   12269 C CA  . LEU E  1 38  ? 141.011 2.424   -21.966 1.00   48.78  ? 38  LEU E CA  1 
ATOM   12270 C C   . LEU E  1 38  ? 141.247 3.279   -23.214 1.00   49.84  ? 38  LEU E C   1 
ATOM   12271 O O   . LEU E  1 38  ? 141.729 2.774   -24.215 1.00   52.36  ? 38  LEU E O   1 
ATOM   12272 C CB  . LEU E  1 38  ? 142.305 2.261   -21.177 1.00   49.60  ? 38  LEU E CB  1 
ATOM   12273 C CG  . LEU E  1 38  ? 142.694 3.267   -20.108 1.00   47.31  ? 38  LEU E CG  1 
ATOM   12274 C CD1 . LEU E  1 38  ? 141.674 3.273   -18.992 1.00   42.88  ? 38  LEU E CD1 1 
ATOM   12275 C CD2 . LEU E  1 38  ? 144.089 2.935   -19.597 1.00   50.28  ? 38  LEU E CD2 1 
ATOM   12276 N N   . MET E  1 39  ? 140.890 4.561   -23.173 1.00   48.27  ? 39  MET E N   1 
ATOM   12277 C CA  . MET E  1 39  ? 141.193 5.452   -24.295 1.00   49.23  ? 39  MET E CA  1 
ATOM   12278 C C   . MET E  1 39  ? 141.440 6.899   -23.831 1.00   46.04  ? 39  MET E C   1 
ATOM   12279 O O   . MET E  1 39  ? 141.236 7.221   -22.680 1.00   45.93  ? 39  MET E O   1 
ATOM   12280 C CB  A MET E  1 39  ? 140.071 5.391   -25.333 0.50   51.48  ? 39  MET E CB  1 
ATOM   12281 C CB  B MET E  1 39  ? 140.065 5.406   -25.325 0.50   51.45  ? 39  MET E CB  1 
ATOM   12282 C CG  A MET E  1 39  ? 138.684 5.452   -24.741 0.50   49.66  ? 39  MET E CG  1 
ATOM   12283 C CG  B MET E  1 39  ? 138.831 6.191   -24.932 0.50   49.48  ? 39  MET E CG  1 
ATOM   12284 S SD  A MET E  1 39  ? 138.250 7.087   -24.124 0.50   47.01  ? 39  MET E SD  1 
ATOM   12285 S SD  B MET E  1 39  ? 137.653 6.297   -26.292 0.50   71.87  ? 39  MET E SD  1 
ATOM   12286 C CE  A MET E  1 39  ? 137.861 7.923   -25.660 0.50   41.99  ? 39  MET E CE  1 
ATOM   12287 C CE  B MET E  1 39  ? 137.422 8.069   -26.418 0.50   43.77  ? 39  MET E CE  1 
ATOM   12288 N N   . GLN E  1 40  ? 141.863 7.778   -24.731 1.00   48.38  ? 40  GLN E N   1 
ATOM   12289 C CA  . GLN E  1 40  ? 142.255 9.137   -24.343 1.00   46.65  ? 40  GLN E CA  1 
ATOM   12290 C C   . GLN E  1 40  ? 141.192 10.157  -24.616 1.00   47.61  ? 40  GLN E C   1 
ATOM   12291 O O   . GLN E  1 40  ? 140.637 10.198  -25.714 1.00   51.51  ? 40  GLN E O   1 
ATOM   12292 C CB  . GLN E  1 40  ? 143.515 9.572   -25.083 1.00   47.10  ? 40  GLN E CB  1 
ATOM   12293 C CG  . GLN E  1 40  ? 144.741 8.828   -24.683 1.00   51.17  ? 40  GLN E CG  1 
ATOM   12294 C CD  . GLN E  1 40  ? 145.941 9.251   -25.473 1.00   58.24  ? 40  GLN E CD  1 
ATOM   12295 O OE1 . GLN E  1 40  ? 145.961 9.144   -26.701 1.00   63.06  ? 40  GLN E OE1 1 
ATOM   12296 N NE2 . GLN E  1 40  ? 146.953 9.744   -24.782 1.00   59.85  ? 40  GLN E NE2 1 
ATOM   12297 N N   . VAL E  1 41  ? 140.939 10.997  -23.620 1.00   45.53  ? 41  VAL E N   1 
ATOM   12298 C CA  . VAL E  1 41  ? 139.995 12.103  -23.735 1.00   45.07  ? 41  VAL E CA  1 
ATOM   12299 C C   . VAL E  1 41  ? 140.683 13.454  -23.532 1.00   42.81  ? 41  VAL E C   1 
ATOM   12300 O O   . VAL E  1 41  ? 141.206 13.709  -22.454 1.00   42.41  ? 41  VAL E O   1 
ATOM   12301 C CB  . VAL E  1 41  ? 138.863 11.968  -22.697 1.00   44.13  ? 41  VAL E CB  1 
ATOM   12302 C CG1 . VAL E  1 41  ? 137.763 12.957  -22.978 1.00   45.71  ? 41  VAL E CG1 1 
ATOM   12303 C CG2 . VAL E  1 41  ? 138.319 10.553  -22.676 1.00   42.54  ? 41  VAL E CG2 1 
ATOM   12304 N N   . PRO E  1 42  ? 140.692 14.321  -24.565 1.00   43.71  ? 42  PRO E N   1 
ATOM   12305 C CA  . PRO E  1 42  ? 141.267 15.655  -24.393 1.00   40.59  ? 42  PRO E CA  1 
ATOM   12306 C C   . PRO E  1 42  ? 140.303 16.537  -23.633 1.00   39.50  ? 42  PRO E C   1 
ATOM   12307 O O   . PRO E  1 42  ? 139.157 16.694  -24.072 1.00   38.02  ? 42  PRO E O   1 
ATOM   12308 C CB  . PRO E  1 42  ? 141.437 16.160  -25.820 1.00   44.87  ? 42  PRO E CB  1 
ATOM   12309 C CG  . PRO E  1 42  ? 140.380 15.439  -26.588 1.00   47.96  ? 42  PRO E CG  1 
ATOM   12310 C CD  . PRO E  1 42  ? 140.216 14.100  -25.942 1.00   46.12  ? 42  PRO E CD  1 
ATOM   12311 N N   . LEU E  1 43  ? 140.752 17.071  -22.500 1.00   39.50  ? 43  LEU E N   1 
ATOM   12312 C CA  . LEU E  1 43  ? 139.921 17.905  -21.643 1.00   36.40  ? 43  LEU E CA  1 
ATOM   12313 C C   . LEU E  1 43  ? 140.670 19.147  -21.192 1.00   36.01  ? 43  LEU E C   1 
ATOM   12314 O O   . LEU E  1 43  ? 141.871 19.115  -20.957 1.00   35.38  ? 43  LEU E O   1 
ATOM   12315 C CB  . LEU E  1 43  ? 139.432 17.132  -20.422 1.00   33.25  ? 43  LEU E CB  1 
ATOM   12316 C CG  . LEU E  1 43  ? 138.594 15.871  -20.652 1.00   33.88  ? 43  LEU E CG  1 
ATOM   12317 C CD1 . LEU E  1 43  ? 138.353 15.205  -19.333 1.00   34.82  ? 43  LEU E CD1 1 
ATOM   12318 C CD2 . LEU E  1 43  ? 137.285 16.194  -21.331 1.00   34.46  ? 43  LEU E CD2 1 
ATOM   12319 N N   . LEU E  1 44  ? 139.927 20.236  -21.067 1.00   36.11  ? 44  LEU E N   1 
ATOM   12320 C CA  . LEU E  1 44  ? 140.452 21.495  -20.597 1.00   34.91  ? 44  LEU E CA  1 
ATOM   12321 C C   . LEU E  1 44  ? 140.809 21.390  -19.131 1.00   31.94  ? 44  LEU E C   1 
ATOM   12322 O O   . LEU E  1 44  ? 140.049 20.867  -18.337 1.00   34.28  ? 44  LEU E O   1 
ATOM   12323 C CB  . LEU E  1 44  ? 139.427 22.607  -20.806 1.00   36.16  ? 44  LEU E CB  1 
ATOM   12324 C CG  . LEU E  1 44  ? 139.893 23.990  -20.376 1.00   36.21  ? 44  LEU E CG  1 
ATOM   12325 C CD1 . LEU E  1 44  ? 140.730 24.549  -21.481 1.00   38.47  ? 44  LEU E CD1 1 
ATOM   12326 C CD2 . LEU E  1 44  ? 138.749 24.920  -20.058 1.00   36.97  ? 44  LEU E CD2 1 
ATOM   12327 N N   . LEU E  1 45  ? 141.966 21.922  -18.783 1.00   31.16  ? 45  LEU E N   1 
ATOM   12328 C CA  . LEU E  1 45  ? 142.398 22.000  -17.408 1.00   30.52  ? 45  LEU E CA  1 
ATOM   12329 C C   . LEU E  1 45  ? 141.678 23.159  -16.721 1.00   33.02  ? 45  LEU E C   1 
ATOM   12330 O O   . LEU E  1 45  ? 141.932 24.328  -17.029 1.00   32.92  ? 45  LEU E O   1 
ATOM   12331 C CB  . LEU E  1 45  ? 143.916 22.190  -17.357 1.00   31.10  ? 45  LEU E CB  1 
ATOM   12332 C CG  . LEU E  1 45  ? 144.468 22.452  -15.956 1.00   33.79  ? 45  LEU E CG  1 
ATOM   12333 C CD1 . LEU E  1 45  ? 144.244 21.220  -15.086 1.00   35.28  ? 45  LEU E CD1 1 
ATOM   12334 C CD2 . LEU E  1 45  ? 145.941 22.858  -15.977 1.00   30.99  ? 45  LEU E CD2 1 
ATOM   12335 N N   . ASP E  1 46  ? 140.776 22.845  -15.794 1.00   34.54  ? 46  ASP E N   1 
ATOM   12336 C CA  . ASP E  1 46  ? 140.015 23.881  -15.114 1.00   32.83  ? 46  ASP E CA  1 
ATOM   12337 C C   . ASP E  1 46  ? 140.247 23.784  -13.621 1.00   32.67  ? 46  ASP E C   1 
ATOM   12338 O O   . ASP E  1 46  ? 139.551 23.071  -12.931 1.00   32.14  ? 46  ASP E O   1 
ATOM   12339 C CB  . ASP E  1 46  ? 138.534 23.768  -15.435 1.00   32.90  ? 46  ASP E CB  1 
ATOM   12340 C CG  . ASP E  1 46  ? 137.703 24.882  -14.792 1.00   37.78  ? 46  ASP E CG  1 
ATOM   12341 O OD1 . ASP E  1 46  ? 138.277 25.823  -14.203 1.00   41.05  ? 46  ASP E OD1 1 
ATOM   12342 O OD2 . ASP E  1 46  ? 136.456 24.819  -14.868 1.00   39.34  1 46  ASP E OD2 1 
ATOM   12343 N N   . LEU E  1 47  ? 141.200 24.570  -13.136 1.00   33.11  ? 47  LEU E N   1 
ATOM   12344 C CA  . LEU E  1 47  ? 141.646 24.512  -11.753 1.00   31.00  ? 47  LEU E CA  1 
ATOM   12345 C C   . LEU E  1 47  ? 140.506 24.615  -10.733 1.00   30.96  ? 47  LEU E C   1 
ATOM   12346 O O   . LEU E  1 47  ? 140.477 23.868  -9.757  1.00   30.15  ? 47  LEU E O   1 
ATOM   12347 C CB  . LEU E  1 47  ? 142.667 25.636  -11.504 1.00   30.77  ? 47  LEU E CB  1 
ATOM   12348 C CG  . LEU E  1 47  ? 143.168 25.777  -10.070 1.00   30.01  ? 47  LEU E CG  1 
ATOM   12349 C CD1 . LEU E  1 47  ? 143.941 24.546  -9.709  1.00   27.35  ? 47  LEU E CD1 1 
ATOM   12350 C CD2 . LEU E  1 47  ? 144.011 27.040  -9.830  1.00   31.51  ? 47  LEU E CD2 1 
ATOM   12351 N N   . ASN E  1 48  ? 139.553 25.513  -10.960 1.00   30.25  ? 48  ASN E N   1 
ATOM   12352 C CA  . ASN E  1 48  ? 138.500 25.737  -9.974  1.00   30.26  ? 48  ASN E CA  1 
ATOM   12353 C C   . ASN E  1 48  ? 137.224 24.937  -10.248 1.00   32.25  ? 48  ASN E C   1 
ATOM   12354 O O   . ASN E  1 48  ? 136.221 25.088  -9.545  1.00   35.92  ? 48  ASN E O   1 
ATOM   12355 C CB  . ASN E  1 48  ? 138.184 27.229  -9.901  1.00   32.92  ? 48  ASN E CB  1 
ATOM   12356 C CG  . ASN E  1 48  ? 139.324 28.025  -9.353  1.00   33.02  ? 48  ASN E CG  1 
ATOM   12357 O OD1 . ASN E  1 48  ? 139.843 27.725  -8.286  1.00   34.99  ? 48  ASN E OD1 1 
ATOM   12358 N ND2 . ASN E  1 48  ? 139.749 29.027  -10.093 1.00   34.11  ? 48  ASN E ND2 1 
ATOM   12359 N N   . GLY E  1 49  ? 137.254 24.100  -11.283 1.00   29.83  ? 49  GLY E N   1 
ATOM   12360 C CA  . GLY E  1 49  ? 136.092 23.315  -11.669 1.00   26.69  ? 49  GLY E CA  1 
ATOM   12361 C C   . GLY E  1 49  ? 135.687 22.297  -10.628 1.00   25.59  ? 49  GLY E C   1 
ATOM   12362 O O   . GLY E  1 49  ? 136.516 21.629  -10.030 1.00   29.04  ? 49  GLY E O   1 
ATOM   12363 N N   . LYS E  1 50  ? 134.390 22.150  -10.416 1.00   29.05  ? 50  LYS E N   1 
ATOM   12364 C CA  . LYS E  1 50  ? 133.914 21.283  -9.345  1.00   28.25  ? 50  LYS E CA  1 
ATOM   12365 C C   . LYS E  1 50  ? 133.975 19.796  -9.689  1.00   30.34  ? 50  LYS E C   1 
ATOM   12366 O O   . LYS E  1 50  ? 133.960 18.937  -8.804  1.00   31.83  ? 50  LYS E O   1 
ATOM   12367 C CB  . LYS E  1 50  ? 132.483 21.649  -8.981  1.00   28.17  ? 50  LYS E CB  1 
ATOM   12368 C CG  . LYS E  1 50  ? 132.366 22.961  -8.300  1.00   31.67  ? 50  LYS E CG  1 
ATOM   12369 C CD  . LYS E  1 50  ? 130.951 23.179  -7.874  1.00   35.36  ? 50  LYS E CD  1 
ATOM   12370 C CE  . LYS E  1 50  ? 130.774 24.576  -7.364  1.00   40.90  ? 50  LYS E CE  1 
ATOM   12371 N NZ  . LYS E  1 50  ? 129.356 24.816  -7.033  1.00   47.88  ? 50  LYS E NZ  1 
ATOM   12372 N N   . HIS E  1 51  ? 134.005 19.485  -10.976 1.00   29.85  ? 51  HIS E N   1 
ATOM   12373 C CA  . HIS E  1 51  ? 134.047 18.096  -11.397 1.00   29.35  ? 51  HIS E CA  1 
ATOM   12374 C C   . HIS E  1 51  ? 134.550 17.981  -12.830 1.00   33.19  ? 51  HIS E C   1 
ATOM   12375 O O   . HIS E  1 51  ? 134.717 18.999  -13.525 1.00   36.78  ? 51  HIS E O   1 
ATOM   12376 C CB  . HIS E  1 51  ? 132.664 17.441  -11.263 1.00   26.97  ? 51  HIS E CB  1 
ATOM   12377 C CG  . HIS E  1 51  ? 131.601 18.068  -12.107 1.00   29.77  ? 51  HIS E CG  1 
ATOM   12378 N ND1 . HIS E  1 51  ? 130.613 18.868  -11.579 1.00   32.34  ? 51  HIS E ND1 1 
ATOM   12379 C CD2 . HIS E  1 51  ? 131.382 18.035  -13.442 1.00   31.43  ? 51  HIS E CD2 1 
ATOM   12380 C CE1 . HIS E  1 51  ? 129.825 19.290  -12.550 1.00   33.44  ? 51  HIS E CE1 1 
ATOM   12381 N NE2 . HIS E  1 51  ? 130.276 18.810  -13.693 1.00   32.57  ? 51  HIS E NE2 1 
ATOM   12382 N N   . LEU E  1 52  ? 134.787 16.742  -13.265 1.00   32.39  ? 52  LEU E N   1 
ATOM   12383 C CA  . LEU E  1 52  ? 135.117 16.459  -14.657 1.00   29.69  ? 52  LEU E CA  1 
ATOM   12384 C C   . LEU E  1 52  ? 133.818 16.328  -15.460 1.00   31.36  ? 52  LEU E C   1 
ATOM   12385 O O   . LEU E  1 52  ? 132.899 15.635  -15.042 1.00   30.99  ? 52  LEU E O   1 
ATOM   12386 C CB  . LEU E  1 52  ? 135.942 15.174  -14.741 1.00   29.76  ? 52  LEU E CB  1 
ATOM   12387 C CG  . LEU E  1 52  ? 136.563 14.752  -16.072 1.00   31.14  ? 52  LEU E CG  1 
ATOM   12388 C CD1 . LEU E  1 52  ? 137.778 13.891  -15.798 1.00   30.25  ? 52  LEU E CD1 1 
ATOM   12389 C CD2 . LEU E  1 52  ? 135.589 14.022  -16.957 1.00   33.12  ? 52  LEU E CD2 1 
ATOM   12390 N N   . TRP E  1 53  ? 133.719 16.988  -16.608 1.00   32.55  ? 53  TRP E N   1 
ATOM   12391 C CA  . TRP E  1 53  ? 132.551 16.760  -17.446 1.00   35.33  ? 53  TRP E CA  1 
ATOM   12392 C C   . TRP E  1 53  ? 132.953 16.578  -18.879 1.00   40.05  ? 53  TRP E C   1 
ATOM   12393 O O   . TRP E  1 53  ? 133.970 17.089  -19.337 1.00   42.15  ? 53  TRP E O   1 
ATOM   12394 C CB  . TRP E  1 53  ? 131.524 17.892  -17.344 1.00   34.04  ? 53  TRP E CB  1 
ATOM   12395 C CG  . TRP E  1 53  ? 131.997 19.216  -17.748 1.00   34.17  ? 53  TRP E CG  1 
ATOM   12396 C CD1 . TRP E  1 53  ? 132.529 20.158  -16.938 1.00   33.62  ? 53  TRP E CD1 1 
ATOM   12397 C CD2 . TRP E  1 53  ? 131.974 19.781  -19.073 1.00   35.33  ? 53  TRP E CD2 1 
ATOM   12398 N NE1 . TRP E  1 53  ? 132.843 21.277  -17.666 1.00   37.05  ? 53  TRP E NE1 1 
ATOM   12399 C CE2 . TRP E  1 53  ? 132.517 21.071  -18.980 1.00   36.39  ? 53  TRP E CE2 1 
ATOM   12400 C CE3 . TRP E  1 53  ? 131.569 19.312  -20.324 1.00   38.05  ? 53  TRP E CE3 1 
ATOM   12401 C CZ2 . TRP E  1 53  ? 132.663 21.907  -20.086 1.00   38.21  ? 53  TRP E CZ2 1 
ATOM   12402 C CZ3 . TRP E  1 53  ? 131.702 20.141  -21.417 1.00   41.24  ? 53  TRP E CZ3 1 
ATOM   12403 C CH2 . TRP E  1 53  ? 132.246 21.425  -21.295 1.00   41.01  ? 53  TRP E CH2 1 
ATOM   12404 N N   . VAL E  1 54  ? 132.163 15.786  -19.574 1.00   40.98  ? 54  VAL E N   1 
ATOM   12405 C CA  . VAL E  1 54  ? 132.438 15.511  -20.948 1.00   41.57  ? 54  VAL E CA  1 
ATOM   12406 C C   . VAL E  1 54  ? 131.112 15.403  -21.660 1.00   46.18  ? 54  VAL E C   1 
ATOM   12407 O O   . VAL E  1 54  ? 130.093 15.082  -21.061 1.00   45.90  ? 54  VAL E O   1 
ATOM   12408 C CB  . VAL E  1 54  ? 133.284 14.223  -21.114 1.00   38.72  ? 54  VAL E CB  1 
ATOM   12409 C CG1 . VAL E  1 54  ? 132.500 12.974  -20.687 1.00   37.08  ? 54  VAL E CG1 1 
ATOM   12410 C CG2 . VAL E  1 54  ? 133.784 14.096  -22.552 1.00   43.28  ? 54  VAL E CG2 1 
ATOM   12411 N N   . THR E  1 55  ? 131.124 15.722  -22.940 1.00   51.79  ? 55  THR E N   1 
ATOM   12412 C CA  . THR E  1 55  ? 129.993 15.444  -23.781 1.00   58.67  ? 55  THR E CA  1 
ATOM   12413 C C   . THR E  1 55  ? 130.045 13.931  -24.029 1.00   59.81  ? 55  THR E C   1 
ATOM   12414 O O   . THR E  1 55  ? 131.113 13.392  -24.336 1.00   59.90  ? 55  THR E O   1 
ATOM   12415 C CB  . THR E  1 55  ? 130.045 16.264  -25.087 1.00   63.94  ? 55  THR E CB  1 
ATOM   12416 O OG1 . THR E  1 55  ? 131.291 16.034  -25.753 1.00   66.63  ? 55  THR E OG1 1 
ATOM   12417 C CG2 . THR E  1 55  ? 129.919 17.761  -24.776 1.00   62.18  ? 55  THR E CG2 1 
ATOM   12418 N N   . CYS E  1 56  ? 128.919 13.243  -23.824 1.00   59.28  ? 56  CYS E N   1 
ATOM   12419 C CA  . CYS E  1 56  ? 128.831 11.792  -24.016 1.00   55.44  ? 56  CYS E CA  1 
ATOM   12420 C C   . CYS E  1 56  ? 128.022 11.508  -25.269 1.00   62.04  ? 56  CYS E C   1 
ATOM   12421 O O   . CYS E  1 56  ? 127.019 12.162  -25.504 1.00   65.95  ? 56  CYS E O   1 
ATOM   12422 C CB  . CYS E  1 56  ? 128.196 11.125  -22.814 1.00   47.85  ? 56  CYS E CB  1 
ATOM   12423 S SG  . CYS E  1 56  ? 129.218 11.235  -21.407 1.00   47.18  ? 56  CYS E SG  1 
ATOM   12424 N N   . SER E  1 57  ? 128.424 10.512  -26.052 1.00   65.31  ? 57  SER E N   1 
ATOM   12425 C CA  . SER E  1 57  ? 127.803 10.286  -27.360 1.00   71.02  ? 57  SER E CA  1 
ATOM   12426 C C   . SER E  1 57  ? 126.911 9.042   -27.466 1.00   75.99  ? 57  SER E C   1 
ATOM   12427 O O   . SER E  1 57  ? 126.684 8.319   -26.496 1.00   72.07  ? 57  SER E O   1 
ATOM   12428 C CB  . SER E  1 57  ? 128.918 10.203  -28.423 1.00   71.03  ? 57  SER E CB  1 
ATOM   12429 O OG  . SER E  1 57  ? 128.432 10.196  -29.755 1.00   75.60  ? 57  SER E OG  1 
ATOM   12430 N N   . GLN E  1 58  ? 126.317 8.872   -28.642 1.00   84.81  ? 58  GLN E N   1 
ATOM   12431 C CA  . GLN E  1 58  ? 125.708 7.604   -29.018 1.00   88.23  ? 58  GLN E CA  1 
ATOM   12432 C C   . GLN E  1 58  ? 126.810 6.564   -29.162 1.00   84.77  ? 58  GLN E C   1 
ATOM   12433 O O   . GLN E  1 58  ? 126.590 5.370   -28.944 1.00   84.06  ? 58  GLN E O   1 
ATOM   12434 C CB  . GLN E  1 58  ? 124.953 7.724   -30.341 1.00   96.12  ? 58  GLN E CB  1 
ATOM   12435 C CG  . GLN E  1 58  ? 125.520 8.809   -31.258 1.00   99.23  ? 58  GLN E CG  1 
ATOM   12436 C CD  . GLN E  1 58  ? 124.594 9.140   -32.411 1.00   104.97 ? 58  GLN E CD  1 
ATOM   12437 O OE1 . GLN E  1 58  ? 123.536 8.532   -32.560 1.00   107.18 ? 58  GLN E OE1 1 
ATOM   12438 N NE2 . GLN E  1 58  ? 124.979 10.121  -33.221 1.00   107.05 ? 58  GLN E NE2 1 
ATOM   12439 N N   . HIS E  1 59  ? 127.998 7.043   -29.543 1.00   81.69  ? 59  HIS E N   1 
ATOM   12440 C CA  . HIS E  1 59  ? 129.141 6.176   -29.788 1.00   78.84  ? 59  HIS E CA  1 
ATOM   12441 C C   . HIS E  1 59  ? 130.068 6.101   -28.586 1.00   73.05  ? 59  HIS E C   1 
ATOM   12442 O O   . HIS E  1 59  ? 131.213 5.675   -28.701 1.00   74.49  ? 59  HIS E O   1 
ATOM   12443 C CB  . HIS E  1 59  ? 129.929 6.677   -31.002 1.00   80.71  ? 59  HIS E CB  1 
ATOM   12444 C CG  . HIS E  1 59  ? 129.093 6.877   -32.229 1.00   85.49  ? 59  HIS E CG  1 
ATOM   12445 N ND1 . HIS E  1 59  ? 128.390 5.851   -32.829 1.00   88.76  ? 59  HIS E ND1 1 
ATOM   12446 C CD2 . HIS E  1 59  ? 128.862 7.980   -32.980 1.00   86.83  ? 59  HIS E CD2 1 
ATOM   12447 C CE1 . HIS E  1 59  ? 127.756 6.316   -33.889 1.00   93.00  ? 59  HIS E CE1 1 
ATOM   12448 N NE2 . HIS E  1 59  ? 128.027 7.605   -34.003 1.00   92.30  ? 59  HIS E NE2 1 
ATOM   12449 N N   . TYR E  1 60  ? 129.547 6.454   -27.419 1.00   67.36  ? 60  TYR E N   1 
ATOM   12450 C CA  . TYR E  1 60  ? 130.270 6.257   -26.182 1.00   62.68  ? 60  TYR E CA  1 
ATOM   12451 C C   . TYR E  1 60  ? 130.275 4.758   -25.982 1.00   67.22  ? 60  TYR E C   1 
ATOM   12452 O O   . TYR E  1 60  ? 129.219 4.148   -25.777 1.00   71.22  ? 60  TYR E O   1 
ATOM   12453 C CB  . TYR E  1 60  ? 129.588 6.987   -25.024 1.00   56.03  ? 60  TYR E CB  1 
ATOM   12454 C CG  . TYR E  1 60  ? 130.310 6.993   -23.683 1.00   50.14  ? 60  TYR E CG  1 
ATOM   12455 C CD1 . TYR E  1 60  ? 130.565 5.813   -22.992 1.00   48.36  ? 60  TYR E CD1 1 
ATOM   12456 C CD2 . TYR E  1 60  ? 130.658 8.191   -23.067 1.00   44.99  ? 60  TYR E CD2 1 
ATOM   12457 C CE1 . TYR E  1 60  ? 131.198 5.826   -21.757 1.00   44.07  ? 60  TYR E CE1 1 
ATOM   12458 C CE2 . TYR E  1 60  ? 131.277 8.210   -21.830 1.00   42.48  ? 60  TYR E CE2 1 
ATOM   12459 C CZ  . TYR E  1 60  ? 131.548 7.028   -21.180 1.00   40.64  ? 60  TYR E CZ  1 
ATOM   12460 O OH  . TYR E  1 60  ? 132.161 7.051   -19.948 1.00   37.54  ? 60  TYR E OH  1 
ATOM   12461 N N   . SER E  1 61  ? 131.458 4.161   -26.066 1.00   65.44  ? 61  SER E N   1 
ATOM   12462 C CA  . SER E  1 61  ? 131.597 2.716   -25.924 1.00   64.54  ? 61  SER E CA  1 
ATOM   12463 C C   . SER E  1 61  ? 132.465 2.317   -24.712 1.00   63.81  ? 61  SER E C   1 
ATOM   12464 O O   . SER E  1 61  ? 133.656 2.650   -24.654 1.00   63.38  ? 61  SER E O   1 
ATOM   12465 C CB  . SER E  1 61  ? 132.179 2.138   -27.206 1.00   64.35  ? 61  SER E CB  1 
ATOM   12466 O OG  . SER E  1 61  ? 132.373 0.750   -27.076 1.00   65.31  ? 61  SER E OG  1 
ATOM   12467 N N   . SER E  1 62  ? 131.865 1.599   -23.754 1.00   61.72  ? 62  SER E N   1 
ATOM   12468 C CA  . SER E  1 62  ? 132.571 1.164   -22.543 1.00   55.50  ? 62  SER E CA  1 
ATOM   12469 C C   . SER E  1 62  ? 131.800 0.040   -21.828 1.00   53.29  ? 62  SER E C   1 
ATOM   12470 O O   . SER E  1 62  ? 130.585 0.134   -21.623 1.00   52.25  ? 62  SER E O   1 
ATOM   12471 C CB  . SER E  1 62  ? 132.796 2.358   -21.602 1.00   49.08  ? 62  SER E CB  1 
ATOM   12472 O OG  . SER E  1 62  ? 133.484 1.987   -20.422 1.00   44.92  ? 62  SER E OG  1 
ATOM   12473 N N   . SER E  1 63  ? 132.517 -1.013  -21.442 1.00   51.55  ? 63  SER E N   1 
ATOM   12474 C CA  . SER E  1 63  ? 131.903 -2.127  -20.744 1.00   50.03  ? 63  SER E CA  1 
ATOM   12475 C C   . SER E  1 63  ? 131.846 -1.869  -19.262 1.00   49.81  ? 63  SER E C   1 
ATOM   12476 O O   . SER E  1 63  ? 131.338 -2.694  -18.505 1.00   53.96  ? 63  SER E O   1 
ATOM   12477 C CB  . SER E  1 63  ? 132.672 -3.406  -20.986 1.00   50.46  ? 63  SER E CB  1 
ATOM   12478 O OG  . SER E  1 63  ? 133.937 -3.339  -20.374 1.00   50.36  ? 63  SER E OG  1 
ATOM   12479 N N   . THR E  1 64  ? 132.367 -0.722  -18.842 1.00   45.93  ? 64  THR E N   1 
ATOM   12480 C CA  . THR E  1 64  ? 132.369 -0.389  -17.433 1.00   39.21  ? 64  THR E CA  1 
ATOM   12481 C C   . THR E  1 64  ? 131.581 0.864   -17.103 1.00   36.77  ? 64  THR E C   1 
ATOM   12482 O O   . THR E  1 64  ? 131.640 1.334   -15.980 1.00   37.95  ? 64  THR E O   1 
ATOM   12483 C CB  . THR E  1 64  ? 133.773 -0.216  -16.935 1.00   39.68  ? 64  THR E CB  1 
ATOM   12484 O OG1 . THR E  1 64  ? 134.517 0.484   -17.927 1.00   43.57  ? 64  THR E OG1 1 
ATOM   12485 C CG2 . THR E  1 64  ? 134.413 -1.560  -16.739 1.00   37.88  ? 64  THR E CG2 1 
ATOM   12486 N N   . TYR E  1 65  ? 130.844 1.402   -18.066 1.00   36.90  ? 65  TYR E N   1 
ATOM   12487 C CA  . TYR E  1 65  ? 130.057 2.626   -17.851 1.00   39.31  ? 65  TYR E CA  1 
ATOM   12488 C C   . TYR E  1 65  ? 128.746 2.375   -17.098 1.00   42.07  ? 65  TYR E C   1 
ATOM   12489 O O   . TYR E  1 65  ? 128.107 1.348   -17.295 1.00   46.15  ? 65  TYR E O   1 
ATOM   12490 C CB  . TYR E  1 65  ? 129.767 3.325   -19.190 1.00   41.54  ? 65  TYR E CB  1 
ATOM   12491 C CG  . TYR E  1 65  ? 128.689 4.401   -19.127 1.00   44.19  ? 65  TYR E CG  1 
ATOM   12492 C CD1 . TYR E  1 65  ? 128.970 5.695   -18.681 1.00   44.86  ? 65  TYR E CD1 1 
ATOM   12493 C CD2 . TYR E  1 65  ? 127.389 4.129   -19.538 1.00   45.81  ? 65  TYR E CD2 1 
ATOM   12494 C CE1 . TYR E  1 65  ? 127.959 6.684   -18.628 1.00   46.06  ? 65  TYR E CE1 1 
ATOM   12495 C CE2 . TYR E  1 65  ? 126.384 5.107   -19.492 1.00   46.74  ? 65  TYR E CE2 1 
ATOM   12496 C CZ  . TYR E  1 65  ? 126.668 6.376   -19.043 1.00   46.43  ? 65  TYR E CZ  1 
ATOM   12497 O OH  . TYR E  1 65  ? 125.651 7.317   -19.008 1.00   46.19  ? 65  TYR E OH  1 
ATOM   12498 N N   . GLN E  1 66  ? 128.368 3.304   -16.215 1.00   39.07  ? 66  GLN E N   1 
ATOM   12499 C CA  . GLN E  1 66  ? 127.063 3.276   -15.535 1.00   40.56  ? 66  GLN E CA  1 
ATOM   12500 C C   . GLN E  1 66  ? 126.482 4.661   -15.299 1.00   36.76  ? 66  GLN E C   1 
ATOM   12501 O O   . GLN E  1 66  ? 127.210 5.619   -15.117 1.00   36.65  ? 66  GLN E O   1 
ATOM   12502 C CB  . GLN E  1 66  ? 127.188 2.569   -14.195 1.00   46.98  ? 66  GLN E CB  1 
ATOM   12503 C CG  . GLN E  1 66  ? 127.401 1.099   -14.319 1.00   58.85  ? 66  GLN E CG  1 
ATOM   12504 C CD  . GLN E  1 66  ? 127.719 0.460   -13.000 1.00   67.53  ? 66  GLN E CD  1 
ATOM   12505 O OE1 . GLN E  1 66  ? 127.084 0.759   -11.981 1.00   70.40  ? 66  GLN E OE1 1 
ATOM   12506 N NE2 . GLN E  1 66  ? 128.701 -0.445  -13.004 1.00   70.18  ? 66  GLN E NE2 1 
ATOM   12507 N N   . ALA E  1 67  ? 125.165 4.775   -15.318 1.00   37.21  ? 67  ALA E N   1 
ATOM   12508 C CA  . ALA E  1 67  ? 124.521 6.003   -14.861 1.00   37.28  ? 67  ALA E CA  1 
ATOM   12509 C C   . ALA E  1 67  ? 123.862 5.723   -13.516 1.00   38.10  ? 67  ALA E C   1 
ATOM   12510 O O   . ALA E  1 67  ? 122.866 5.000   -13.482 1.00   41.30  ? 67  ALA E O   1 
ATOM   12511 C CB  . ALA E  1 67  ? 123.487 6.489   -15.871 1.00   38.97  ? 67  ALA E CB  1 
ATOM   12512 N N   . PRO E  1 68  ? 124.423 6.261   -12.405 1.00   35.13  ? 68  PRO E N   1 
ATOM   12513 C CA  . PRO E  1 68  ? 123.833 5.992   -11.085 1.00   33.58  ? 68  PRO E CA  1 
ATOM   12514 C C   . PRO E  1 68  ? 122.351 6.374   -11.048 1.00   34.60  ? 68  PRO E C   1 
ATOM   12515 O O   . PRO E  1 68  ? 121.951 7.318   -11.739 1.00   35.66  ? 68  PRO E O   1 
ATOM   12516 C CB  . PRO E  1 68  ? 124.662 6.875   -10.146 1.00   31.82  ? 68  PRO E CB  1 
ATOM   12517 C CG  . PRO E  1 68  ? 125.995 6.999   -10.835 1.00   31.14  ? 68  PRO E CG  1 
ATOM   12518 C CD  . PRO E  1 68  ? 125.675 7.042   -12.300 1.00   32.30  ? 68  PRO E CD  1 
ATOM   12519 N N   . PHE E  1 69  ? 121.538 5.641   -10.289 1.00   34.95  ? 69  PHE E N   1 
ATOM   12520 C CA  . PHE E  1 69  ? 120.113 5.955   -10.230 1.00   36.70  ? 69  PHE E CA  1 
ATOM   12521 C C   . PHE E  1 69  ? 119.858 7.091   -9.266  1.00   40.24  ? 69  PHE E C   1 
ATOM   12522 O O   . PHE E  1 69  ? 120.683 7.373   -8.398  1.00   41.98  ? 69  PHE E O   1 
ATOM   12523 C CB  . PHE E  1 69  ? 119.254 4.725   -9.880  1.00   36.39  ? 69  PHE E CB  1 
ATOM   12524 C CG  . PHE E  1 69  ? 119.634 4.011   -8.594  1.00   37.07  ? 69  PHE E CG  1 
ATOM   12525 C CD1 . PHE E  1 69  ? 119.218 4.482   -7.355  1.00   37.05  ? 69  PHE E CD1 1 
ATOM   12526 C CD2 . PHE E  1 69  ? 120.316 2.798   -8.641  1.00   37.05  ? 69  PHE E CD2 1 
ATOM   12527 C CE1 . PHE E  1 69  ? 119.530 3.784   -6.187  1.00   37.33  ? 69  PHE E CE1 1 
ATOM   12528 C CE2 . PHE E  1 69  ? 120.630 2.098   -7.474  1.00   37.25  ? 69  PHE E CE2 1 
ATOM   12529 C CZ  . PHE E  1 69  ? 120.234 2.592   -6.248  1.00   36.64  ? 69  PHE E CZ  1 
ATOM   12530 N N   . CYS E  1 70  ? 118.735 7.777   -9.442  1.00   39.88  ? 70  CYS E N   1 
ATOM   12531 C CA  . CYS E  1 70  ? 118.463 8.921   -8.595  1.00   36.57  ? 70  CYS E CA  1 
ATOM   12532 C C   . CYS E  1 70  ? 118.365 8.522   -7.118  1.00   35.60  ? 70  CYS E C   1 
ATOM   12533 O O   . CYS E  1 70  ? 117.806 7.484   -6.801  1.00   34.62  ? 70  CYS E O   1 
ATOM   12534 C CB  . CYS E  1 70  ? 117.188 9.616   -9.032  1.00   37.24  ? 70  CYS E CB  1 
ATOM   12535 S SG  . CYS E  1 70  ? 117.190 11.284  -8.445  1.00   46.98  ? 70  CYS E SG  1 
ATOM   12536 N N   . HIS E  1 71  ? 118.922 9.357   -6.236  1.00   36.04  ? 71  HIS E N   1 
ATOM   12537 C CA  . HIS E  1 71  ? 118.950 9.136   -4.774  1.00   35.76  ? 71  HIS E CA  1 
ATOM   12538 C C   . HIS E  1 71  ? 119.929 8.033   -4.354  1.00   33.70  ? 71  HIS E C   1 
ATOM   12539 O O   . HIS E  1 71  ? 119.926 7.597   -3.193  1.00   34.27  ? 71  HIS E O   1 
ATOM   12540 C CB  . HIS E  1 71  ? 117.554 8.775   -4.217  1.00   39.59  ? 71  HIS E CB  1 
ATOM   12541 C CG  . HIS E  1 71  ? 116.433 9.655   -4.695  1.00   43.50  ? 71  HIS E CG  1 
ATOM   12542 N ND1 . HIS E  1 71  ? 116.356 11.002  -4.411  1.00   43.04  ? 71  HIS E ND1 1 
ATOM   12543 C CD2 . HIS E  1 71  ? 115.320 9.362   -5.409  1.00   44.96  ? 71  HIS E CD2 1 
ATOM   12544 C CE1 . HIS E  1 71  ? 115.259 11.502  -4.948  1.00   44.77  ? 71  HIS E CE1 1 
ATOM   12545 N NE2 . HIS E  1 71  ? 114.611 10.528  -5.558  1.00   45.29  ? 71  HIS E NE2 1 
ATOM   12546 N N   . SER E  1 72  ? 120.782 7.598   -5.279  1.00   34.04  ? 72  SER E N   1 
ATOM   12547 C CA  . SER E  1 72  ? 121.791 6.592   -4.969  1.00   32.83  ? 72  SER E CA  1 
ATOM   12548 C C   . SER E  1 72  ? 122.930 7.157   -4.136  1.00   33.20  ? 72  SER E C   1 
ATOM   12549 O O   . SER E  1 72  ? 123.087 8.366   -4.027  1.00   34.52  ? 72  SER E O   1 
ATOM   12550 C CB  . SER E  1 72  ? 122.347 6.008   -6.255  1.00   32.00  ? 72  SER E CB  1 
ATOM   12551 O OG  . SER E  1 72  ? 122.982 7.021   -7.007  1.00   33.43  ? 72  SER E OG  1 
ATOM   12552 N N   . THR E  1 73  ? 123.750 6.283   -3.573  1.00   33.74  ? 73  THR E N   1 
ATOM   12553 C CA  . THR E  1 73  ? 124.927 6.736   -2.857  1.00   35.32  ? 73  THR E CA  1 
ATOM   12554 C C   . THR E  1 73  ? 125.920 7.500   -3.761  1.00   35.95  ? 73  THR E C   1 
ATOM   12555 O O   . THR E  1 73  ? 126.583 8.438   -3.305  1.00   34.97  ? 73  THR E O   1 
ATOM   12556 C CB  . THR E  1 73  ? 125.661 5.554   -2.210  1.00   35.81  ? 73  THR E CB  1 
ATOM   12557 O OG1 . THR E  1 73  ? 125.885 4.554   -3.211  1.00   35.77  ? 73  THR E OG1 1 
ATOM   12558 C CG2 . THR E  1 73  ? 124.840 4.969   -1.093  1.00   29.97  ? 73  THR E CG2 1 
ATOM   12559 N N   . GLN E  1 74  ? 126.029 7.129   -5.036  1.00   34.12  ? 74  GLN E N   1 
ATOM   12560 C CA  . GLN E  1 74  ? 126.883 7.910   -5.909  1.00   31.28  ? 74  GLN E CA  1 
ATOM   12561 C C   . GLN E  1 74  ? 126.370 9.318   -6.064  1.00   31.41  ? 74  GLN E C   1 
ATOM   12562 O O   . GLN E  1 74  ? 127.147 10.263  -6.073  1.00   32.80  ? 74  GLN E O   1 
ATOM   12563 C CB  . GLN E  1 74  ? 127.006 7.299   -7.288  1.00   32.70  ? 74  GLN E CB  1 
ATOM   12564 C CG  . GLN E  1 74  ? 127.697 5.980   -7.287  1.00   34.41  ? 74  GLN E CG  1 
ATOM   12565 C CD  . GLN E  1 74  ? 126.713 4.862   -7.382  1.00   36.91  ? 74  GLN E CD  1 
ATOM   12566 O OE1 . GLN E  1 74  ? 125.569 4.980   -6.942  1.00   37.34  ? 74  GLN E OE1 1 
ATOM   12567 N NE2 . GLN E  1 74  ? 127.132 3.776   -8.010  1.00   39.78  ? 74  GLN E NE2 1 
ATOM   12568 N N   . CYS E  1 75  ? 125.059 9.462   -6.209  1.00   32.33  ? 75  CYS E N   1 
ATOM   12569 C CA  . CYS E  1 75  ? 124.457 10.781  -6.368  1.00   31.15  ? 75  CYS E CA  1 
ATOM   12570 C C   . CYS E  1 75  ? 124.629 11.586  -5.079  1.00   30.54  ? 75  CYS E C   1 
ATOM   12571 O O   . CYS E  1 75  ? 124.883 12.784  -5.106  1.00   31.41  ? 75  CYS E O   1 
ATOM   12572 C CB  . CYS E  1 75  ? 122.969 10.662  -6.728  1.00   33.36  ? 75  CYS E CB  1 
ATOM   12573 S SG  . CYS E  1 75  ? 122.583 9.844   -8.322  1.00   42.93  ? 75  CYS E SG  1 
ATOM   12574 N N   . SER E  1 76  ? 124.522 10.912  -3.949  1.00   29.14  ? 76  SER E N   1 
ATOM   12575 C CA  . SER E  1 76  ? 124.762 11.562  -2.678  1.00   33.34  ? 76  SER E CA  1 
ATOM   12576 C C   . SER E  1 76  ? 126.189 12.107  -2.604  1.00   35.41  ? 76  SER E C   1 
ATOM   12577 O O   . SER E  1 76  ? 126.422 13.256  -2.219  1.00   35.19  ? 76  SER E O   1 
ATOM   12578 C CB  . SER E  1 76  ? 124.507 10.590  -1.535  1.00   34.45  ? 76  SER E CB  1 
ATOM   12579 O OG  . SER E  1 76  ? 124.698 11.247  -0.301  1.00   40.22  ? 76  SER E OG  1 
ATOM   12580 N N   . ARG E  1 77  ? 127.153 11.282  -2.981  1.00   34.67  ? 77  ARG E N   1 
ATOM   12581 C CA  . ARG E  1 77  ? 128.528 11.719  -2.928  1.00   34.73  ? 77  ARG E CA  1 
ATOM   12582 C C   . ARG E  1 77  ? 128.768 12.933  -3.845  1.00   35.02  ? 77  ARG E C   1 
ATOM   12583 O O   . ARG E  1 77  ? 129.532 13.849  -3.506  1.00   31.87  ? 77  ARG E O   1 
ATOM   12584 C CB  . ARG E  1 77  ? 129.465 10.569  -3.277  1.00   35.13  ? 77  ARG E CB  1 
ATOM   12585 C CG  . ARG E  1 77  ? 130.888 10.957  -2.997  1.00   39.53  ? 77  ARG E CG  1 
ATOM   12586 C CD  . ARG E  1 77  ? 131.904 9.883   -3.274  1.00   43.86  ? 77  ARG E CD  1 
ATOM   12587 N NE  . ARG E  1 77  ? 133.236 10.435  -3.023  1.00   49.54  ? 77  ARG E NE  1 
ATOM   12588 C CZ  . ARG E  1 77  ? 134.376 9.903   -3.458  1.00   52.72  ? 77  ARG E CZ  1 
ATOM   12589 N NH1 . ARG E  1 77  ? 134.362 8.779   -4.166  1.00   49.26  ? 77  ARG E NH1 1 
ATOM   12590 N NH2 . ARG E  1 77  ? 135.531 10.505  -3.184  1.00   57.03  ? 77  ARG E NH2 1 
ATOM   12591 N N   . ALA E  1 78  ? 128.097 12.947  -4.994  1.00   33.37  ? 78  ALA E N   1 
ATOM   12592 C CA  . ALA E  1 78  ? 128.238 14.041  -5.935  1.00   30.76  ? 78  ALA E CA  1 
ATOM   12593 C C   . ALA E  1 78  ? 127.491 15.273  -5.465  1.00   33.75  ? 78  ALA E C   1 
ATOM   12594 O O   . ALA E  1 78  ? 127.601 16.316  -6.079  1.00   37.18  ? 78  ALA E O   1 
ATOM   12595 C CB  . ALA E  1 78  ? 127.743 13.624  -7.297  1.00   29.64  ? 78  ALA E CB  1 
ATOM   12596 N N   . ASN E  1 79  ? 126.719 15.146  -4.394  1.00   36.50  ? 79  ASN E N   1 
ATOM   12597 C CA  . ASN E  1 79  ? 125.962 16.268  -3.838  1.00   42.21  ? 79  ASN E CA  1 
ATOM   12598 C C   . ASN E  1 79  ? 124.915 16.787  -4.813  1.00   46.41  ? 79  ASN E C   1 
ATOM   12599 O O   . ASN E  1 79  ? 124.736 17.991  -4.961  1.00   45.61  ? 79  ASN E O   1 
ATOM   12600 C CB  . ASN E  1 79  ? 126.903 17.402  -3.423  1.00   46.20  ? 79  ASN E CB  1 
ATOM   12601 C CG  . ASN E  1 79  ? 126.236 18.420  -2.534  1.00   50.82  ? 79  ASN E CG  1 
ATOM   12602 O OD1 . ASN E  1 79  ? 125.270 18.119  -1.833  1.00   54.11  ? 79  ASN E OD1 1 
ATOM   12603 N ND2 . ASN E  1 79  ? 126.761 19.632  -2.542  1.00   51.99  ? 79  ASN E ND2 1 
ATOM   12604 N N   . THR E  1 80  ? 124.241 15.863  -5.490  1.00   51.12  ? 80  THR E N   1 
ATOM   12605 C CA  . THR E  1 80  ? 123.084 16.191  -6.312  1.00   56.93  ? 80  THR E CA  1 
ATOM   12606 C C   . THR E  1 80  ? 121.911 15.314  -5.928  1.00   67.47  ? 80  THR E C   1 
ATOM   12607 O O   . THR E  1 80  ? 121.999 14.090  -5.983  1.00   69.12  ? 80  THR E O   1 
ATOM   12608 C CB  . THR E  1 80  ? 123.347 16.011  -7.814  1.00   52.73  ? 80  THR E CB  1 
ATOM   12609 O OG1 . THR E  1 80  ? 122.094 16.043  -8.498  1.00   56.03  ? 80  THR E OG1 1 
ATOM   12610 C CG2 . THR E  1 80  ? 123.999 14.679  -8.113  1.00   47.57  ? 80  THR E CG2 1 
ATOM   12611 N N   . HIS E  1 81  ? 120.796 15.932  -5.559  1.00   76.55  ? 81  HIS E N   1 
ATOM   12612 C CA  . HIS E  1 81  ? 119.611 15.153  -5.195  1.00   82.51  ? 81  HIS E CA  1 
ATOM   12613 C C   . HIS E  1 81  ? 118.424 15.547  -6.084  1.00   81.55  ? 81  HIS E C   1 
ATOM   12614 O O   . HIS E  1 81  ? 117.262 15.266  -5.769  1.00   84.58  ? 81  HIS E O   1 
ATOM   12615 C CB  . HIS E  1 81  ? 119.296 15.332  -3.693  1.00   89.40  ? 81  HIS E CB  1 
ATOM   12616 C CG  . HIS E  1 81  ? 120.348 14.756  -2.780  1.00   93.22  ? 81  HIS E CG  1 
ATOM   12617 N ND1 . HIS E  1 81  ? 121.497 15.442  -2.433  1.00   94.38  ? 81  HIS E ND1 1 
ATOM   12618 C CD2 . HIS E  1 81  ? 120.430 13.553  -2.159  1.00   93.41  ? 81  HIS E CD2 1 
ATOM   12619 C CE1 . HIS E  1 81  ? 122.235 14.690  -1.634  1.00   93.88  ? 81  HIS E CE1 1 
ATOM   12620 N NE2 . HIS E  1 81  ? 121.611 13.539  -1.454  1.00   93.63  ? 81  HIS E NE2 1 
ATOM   12621 N N   . GLN E  1 82  ? 118.750 16.209  -7.194  1.00   76.52  ? 82  GLN E N   1 
ATOM   12622 C CA  . GLN E  1 82  ? 117.796 16.572  -8.233  1.00   72.07  ? 82  GLN E CA  1 
ATOM   12623 C C   . GLN E  1 82  ? 117.849 15.566  -9.388  1.00   62.91  ? 82  GLN E C   1 
ATOM   12624 O O   . GLN E  1 82  ? 118.873 15.435  -10.041 1.00   61.23  ? 82  GLN E O   1 
ATOM   12625 C CB  . GLN E  1 82  ? 118.099 17.988  -8.695  1.00   76.26  ? 82  GLN E CB  1 
ATOM   12626 C CG  . GLN E  1 82  ? 117.519 18.382  -10.019 1.00   83.96  ? 82  GLN E CG  1 
ATOM   12627 C CD  . GLN E  1 82  ? 117.654 19.873  -10.232 1.00   91.84  ? 82  GLN E CD  1 
ATOM   12628 O OE1 . GLN E  1 82  ? 117.556 20.655  -9.281  1.00   97.83  ? 82  GLN E OE1 1 
ATOM   12629 N NE2 . GLN E  1 82  ? 117.903 20.279  -11.468 1.00   91.88  ? 82  GLN E NE2 1 
ATOM   12630 N N   . CYS E  1 83  ? 116.730 14.911  -9.681  1.00   58.21  ? 83  CYS E N   1 
ATOM   12631 C CA  . CYS E  1 83  ? 116.719 13.791  -10.626 1.00   54.62  ? 83  CYS E CA  1 
ATOM   12632 C C   . CYS E  1 83  ? 116.803 14.158  -12.092 1.00   57.24  ? 83  CYS E C   1 
ATOM   12633 O O   . CYS E  1 83  ? 116.440 15.260  -12.487 1.00   62.21  ? 83  CYS E O   1 
ATOM   12634 C CB  . CYS E  1 83  ? 115.465 12.945  -10.426 1.00   53.74  ? 83  CYS E CB  1 
ATOM   12635 S SG  . CYS E  1 83  ? 115.398 12.092  -8.866  1.00   59.31  ? 83  CYS E SG  1 
ATOM   12636 N N   . PHE E  1 84  ? 117.288 13.220  -12.901 1.00   54.78  ? 84  PHE E N   1 
ATOM   12637 C CA  . PHE E  1 84  ? 117.488 13.501  -14.316 1.00   53.63  ? 84  PHE E CA  1 
ATOM   12638 C C   . PHE E  1 84  ? 116.448 12.811  -15.194 1.00   56.48  ? 84  PHE E C   1 
ATOM   12639 O O   . PHE E  1 84  ? 116.161 11.624  -15.039 1.00   57.14  ? 84  PHE E O   1 
ATOM   12640 C CB  . PHE E  1 84  ? 118.910 13.100  -14.757 1.00   49.33  ? 84  PHE E CB  1 
ATOM   12641 C CG  . PHE E  1 84  ? 119.228 13.472  -16.179 1.00   50.41  ? 84  PHE E CG  1 
ATOM   12642 C CD1 . PHE E  1 84  ? 119.755 14.718  -16.480 1.00   52.46  ? 84  PHE E CD1 1 
ATOM   12643 C CD2 . PHE E  1 84  ? 119.001 12.576  -17.215 1.00   50.11  ? 84  PHE E CD2 1 
ATOM   12644 C CE1 . PHE E  1 84  ? 120.029 15.069  -17.798 1.00   55.26  ? 84  PHE E CE1 1 
ATOM   12645 C CE2 . PHE E  1 84  ? 119.281 12.911  -18.518 1.00   52.45  ? 84  PHE E CE2 1 
ATOM   12646 C CZ  . PHE E  1 84  ? 119.787 14.154  -18.819 1.00   55.44  ? 84  PHE E CZ  1 
ATOM   12647 N N   . THR E  1 85  ? 115.917 13.576  -16.141 1.00   59.38  ? 85  THR E N   1 
ATOM   12648 C CA  . THR E  1 85  ? 114.978 13.071  -17.129 1.00   65.45  ? 85  THR E CA  1 
ATOM   12649 C C   . THR E  1 85  ? 115.490 13.423  -18.527 1.00   69.98  ? 85  THR E C   1 
ATOM   12650 O O   . THR E  1 85  ? 115.720 14.595  -18.823 1.00   72.65  ? 85  THR E O   1 
ATOM   12651 C CB  . THR E  1 85  ? 113.563 13.687  -16.967 1.00   76.26  ? 85  THR E CB  1 
ATOM   12652 O OG1 . THR E  1 85  ? 113.039 13.424  -15.661 1.00   75.49  ? 85  THR E OG1 1 
ATOM   12653 C CG2 . THR E  1 85  ? 112.620 13.131  -18.019 1.00   78.83  ? 85  THR E CG2 1 
ATOM   12654 N N   . CYS E  1 86  ? 115.685 12.431  -19.387 1.00   71.30  ? 86  CYS E N   1 
ATOM   12655 C CA  . CYS E  1 86  ? 116.159 12.729  -20.725 1.00   74.94  ? 86  CYS E CA  1 
ATOM   12656 C C   . CYS E  1 86  ? 115.182 12.363  -21.788 1.00   82.37  ? 86  CYS E C   1 
ATOM   12657 O O   . CYS E  1 86  ? 114.878 11.193  -22.025 1.00   84.68  ? 86  CYS E O   1 
ATOM   12658 C CB  . CYS E  1 86  ? 117.458 12.022  -21.039 1.00   73.28  ? 86  CYS E CB  1 
ATOM   12659 S SG  . CYS E  1 86  ? 118.212 12.633  -22.561 1.00   85.97  ? 86  CYS E SG  1 
ATOM   12660 N N   . THR E  1 87  ? 114.675 13.393  -22.441 1.00   87.14  ? 87  THR E N   1 
ATOM   12661 C CA  . THR E  1 87  ? 113.785 13.153  -23.562 1.00   93.36  ? 87  THR E CA  1 
ATOM   12662 C C   . THR E  1 87  ? 114.465 13.837  -24.761 1.00   95.02  ? 87  THR E C   1 
ATOM   12663 O O   . THR E  1 87  ? 113.812 14.120  -25.773 1.00   101.08 ? 87  THR E O   1 
ATOM   12664 C CB  . THR E  1 87  ? 112.314 13.605  -23.259 1.00   102.29 ? 87  THR E CB  1 
ATOM   12665 O OG1 . THR E  1 87  ? 111.380 13.019  -24.171 1.00   109.74 ? 87  THR E OG1 1 
ATOM   12666 C CG2 . THR E  1 87  ? 112.224 15.126  -23.204 1.00   101.34 ? 87  THR E CG2 1 
ATOM   12667 N N   . ASP E  1 88  ? 115.778 14.093  -24.621 1.00   89.86  ? 88  ASP E N   1 
ATOM   12668 C CA  . ASP E  1 88  ? 116.643 14.516  -25.739 1.00   91.35  ? 88  ASP E CA  1 
ATOM   12669 C C   . ASP E  1 88  ? 116.424 13.403  -26.709 1.00   93.95  ? 88  ASP E C   1 
ATOM   12670 O O   . ASP E  1 88  ? 115.524 13.473  -27.541 1.00   98.02  ? 88  ASP E O   1 
ATOM   12671 C CB  . ASP E  1 88  ? 118.129 14.724  -25.306 1.00   93.96  ? 88  ASP E CB  1 
ATOM   12672 C CG  . ASP E  1 88  ? 119.115 14.806  -26.486 1.00   96.04  ? 88  ASP E CG  1 
ATOM   12673 O OD1 . ASP E  1 88  ? 119.303 15.895  -27.060 1.00   97.38  ? 88  ASP E OD1 1 
ATOM   12674 O OD2 . ASP E  1 88  ? 119.708 13.767  -26.817 1.00   95.84  ? 88  ASP E OD2 1 
ATOM   12675 N N   . SER E  1 89  ? 117.262 12.394  -26.671 1.00   92.70  ? 89  SER E N   1 
ATOM   12676 C CA  . SER E  1 89  ? 116.837 11.184  -27.339 1.00   97.98  ? 89  SER E CA  1 
ATOM   12677 C C   . SER E  1 89  ? 115.729 10.573  -26.458 1.00   98.74  ? 89  SER E C   1 
ATOM   12678 O O   . SER E  1 89  ? 115.685 10.874  -25.258 1.00   95.83  ? 89  SER E O   1 
ATOM   12679 C CB  . SER E  1 89  ? 118.008 10.251  -27.528 1.00   96.49  ? 89  SER E CB  1 
ATOM   12680 O OG  . SER E  1 89  ? 117.604 8.894   -27.628 1.00   98.45  ? 89  SER E OG  1 
ATOM   12681 N N   . THR E  1 90  ? 114.845 9.758   -27.033 1.00   102.86 ? 90  THR E N   1 
ATOM   12682 C CA  . THR E  1 90  ? 113.884 8.996   -26.258 1.00   101.91 ? 90  THR E CA  1 
ATOM   12683 C C   . THR E  1 90  ? 114.260 7.483   -26.214 1.00   104.27 ? 90  THR E C   1 
ATOM   12684 O O   . THR E  1 90  ? 113.409 6.684   -25.858 1.00   106.18 ? 90  THR E O   1 
ATOM   12685 C CB  . THR E  1 90  ? 112.422 9.178   -26.751 1.00   116.64 ? 90  THR E CB  1 
ATOM   12686 O OG1 . THR E  1 90  ? 112.425 9.043   -28.149 1.00   124.58 ? 90  THR E OG1 1 
ATOM   12687 C CG2 . THR E  1 90  ? 111.868 10.550  -26.483 1.00   115.05 ? 90  THR E CG2 1 
ATOM   12688 N N   . THR E  1 91  ? 115.470 7.084   -26.649 1.00   101.52 ? 91  THR E N   1 
ATOM   12689 C CA  . THR E  1 91  ? 116.003 5.719   -26.409 1.00   96.71  ? 91  THR E CA  1 
ATOM   12690 C C   . THR E  1 91  ? 117.232 5.971   -25.551 1.00   87.07  ? 91  THR E C   1 
ATOM   12691 O O   . THR E  1 91  ? 117.841 7.031   -25.683 1.00   86.84  ? 91  THR E O   1 
ATOM   12692 C CB  . THR E  1 91  ? 116.378 4.954   -27.695 1.00   100.63 ? 91  THR E CB  1 
ATOM   12693 O OG1 . THR E  1 91  ? 115.358 5.136   -28.696 1.00   107.03 ? 91  THR E OG1 1 
ATOM   12694 C CG2 . THR E  1 91  ? 116.574 3.445   -27.375 1.00   94.81  ? 91  THR E CG2 1 
ATOM   12695 N N   . THR E  1 92  ? 117.688 4.999   -24.769 1.00   78.79  ? 92  THR E N   1 
ATOM   12696 C CA  . THR E  1 92  ? 118.775 5.325   -23.849 1.00   71.23  ? 92  THR E CA  1 
ATOM   12697 C C   . THR E  1 92  ? 120.155 5.274   -24.501 1.00   74.62  ? 92  THR E C   1 
ATOM   12698 O O   . THR E  1 92  ? 120.361 4.606   -25.510 1.00   80.54  ? 92  THR E O   1 
ATOM   12699 C CB  . THR E  1 92  ? 118.783 4.429   -22.596 1.00   63.28  ? 92  THR E CB  1 
ATOM   12700 O OG1 . THR E  1 92  ? 119.185 3.102   -22.942 1.00   62.82  ? 92  THR E OG1 1 
ATOM   12701 C CG2 . THR E  1 92  ? 117.436 4.412   -21.947 1.00   61.09  ? 92  THR E CG2 1 
ATOM   12702 N N   . ARG E  1 93  ? 121.078 6.037   -23.925 1.00   71.77  ? 93  ARG E N   1 
ATOM   12703 C CA  . ARG E  1 93  ? 122.463 6.141   -24.388 1.00   71.86  ? 93  ARG E CA  1 
ATOM   12704 C C   . ARG E  1 93  ? 123.240 6.730   -23.241 1.00   67.71  ? 93  ARG E C   1 
ATOM   12705 O O   . ARG E  1 93  ? 122.626 7.228   -22.302 1.00   66.03  ? 93  ARG E O   1 
ATOM   12706 C CB  . ARG E  1 93  ? 122.591 7.041   -25.616 1.00   72.57  ? 93  ARG E CB  1 
ATOM   12707 C CG  . ARG E  1 93  ? 122.108 8.429   -25.312 1.00   70.54  ? 93  ARG E CG  1 
ATOM   12708 C CD  . ARG E  1 93  ? 122.428 9.403   -26.407 1.00   75.45  ? 93  ARG E CD  1 
ATOM   12709 N NE  . ARG E  1 93  ? 121.742 10.668  -26.170 1.00   77.05  ? 93  ARG E NE  1 
ATOM   12710 C CZ  . ARG E  1 93  ? 122.255 11.684  -25.476 1.00   75.55  ? 93  ARG E CZ  1 
ATOM   12711 N NH1 . ARG E  1 93  ? 123.433 11.564  -24.870 1.00   70.56  ? 93  ARG E NH1 1 
ATOM   12712 N NH2 . ARG E  1 93  ? 121.562 12.807  -25.334 1.00   77.66  ? 93  ARG E NH2 1 
ATOM   12713 N N   . PRO E  1 94  ? 124.582 6.651   -23.286 1.00   66.10  ? 94  PRO E N   1 
ATOM   12714 C CA  . PRO E  1 94  ? 125.306 7.355   -22.230 1.00   59.42  ? 94  PRO E CA  1 
ATOM   12715 C C   . PRO E  1 94  ? 124.890 8.814   -22.233 1.00   55.28  ? 94  PRO E C   1 
ATOM   12716 O O   . PRO E  1 94  ? 124.943 9.451   -23.282 1.00   56.53  ? 94  PRO E O   1 
ATOM   12717 C CB  . PRO E  1 94  ? 126.773 7.169   -22.623 1.00   61.40  ? 94  PRO E CB  1 
ATOM   12718 C CG  . PRO E  1 94  ? 126.778 5.888   -23.399 1.00   66.40  ? 94  PRO E CG  1 
ATOM   12719 C CD  . PRO E  1 94  ? 125.490 5.901   -24.173 1.00   70.36  ? 94  PRO E CD  1 
ATOM   12720 N N   . GLY E  1 95  ? 124.469 9.325   -21.081 1.00   51.11  ? 95  GLY E N   1 
ATOM   12721 C CA  . GLY E  1 95  ? 124.017 10.702  -20.989 1.00   50.66  ? 95  GLY E CA  1 
ATOM   12722 C C   . GLY E  1 95  ? 122.514 10.961  -21.091 1.00   52.78  ? 95  GLY E C   1 
ATOM   12723 O O   . GLY E  1 95  ? 122.095 12.103  -20.876 1.00   52.83  ? 95  GLY E O   1 
ATOM   12724 N N   . CYS E  1 96  ? 121.717 9.952   -21.474 1.00   55.04  ? 96  CYS E N   1 
ATOM   12725 C CA  . CYS E  1 96  ? 120.249 10.096  -21.574 1.00   57.33  ? 96  CYS E CA  1 
ATOM   12726 C C   . CYS E  1 96  ? 119.523 8.813   -21.097 1.00   55.14  ? 96  CYS E C   1 
ATOM   12727 O O   . CYS E  1 96  ? 119.388 7.868   -21.886 1.00   55.67  ? 96  CYS E O   1 
ATOM   12728 C CB  . CYS E  1 96  ? 119.842 10.473  -23.018 1.00   64.18  ? 96  CYS E CB  1 
ATOM   12729 S SG  . CYS E  1 96  ? 118.050 10.751  -23.317 1.00   66.44  ? 96  CYS E SG  1 
ATOM   12730 N N   . HIS E  1 97  ? 119.100 8.785   -19.820 1.00   52.13  ? 97  HIS E N   1 
ATOM   12731 C CA  . HIS E  1 97  ? 118.281 7.719   -19.205 1.00   53.67  ? 97  HIS E CA  1 
ATOM   12732 C C   . HIS E  1 97  ? 117.252 8.477   -18.350 1.00   55.36  ? 97  HIS E C   1 
ATOM   12733 O O   . HIS E  1 97  ? 117.399 9.684   -18.175 1.00   52.97  ? 97  HIS E O   1 
ATOM   12734 C CB  . HIS E  1 97  ? 119.106 6.800   -18.289 1.00   50.19  ? 97  HIS E CB  1 
ATOM   12735 C CG  . HIS E  1 97  ? 120.426 6.368   -18.862 1.00   50.67  ? 97  HIS E CG  1 
ATOM   12736 N ND1 . HIS E  1 97  ? 120.605 5.218   -19.605 1.00   51.89  ? 97  HIS E ND1 1 
ATOM   12737 C CD2 . HIS E  1 97  ? 121.645 6.948   -18.781 1.00   50.12  ? 97  HIS E CD2 1 
ATOM   12738 C CE1 . HIS E  1 97  ? 121.876 5.113   -19.956 1.00   51.34  ? 97  HIS E CE1 1 
ATOM   12739 N NE2 . HIS E  1 97  ? 122.527 6.153   -19.471 1.00   50.44  ? 97  HIS E NE2 1 
ATOM   12740 N N   . ASN E  1 98  ? 116.222 7.825   -17.804 1.00   59.95  ? 98  ASN E N   1 
ATOM   12741 C CA  . ASN E  1 98  ? 115.521 8.547   -16.761 1.00   61.86  ? 98  ASN E CA  1 
ATOM   12742 C C   . ASN E  1 98  ? 115.774 7.814   -15.477 1.00   57.13  ? 98  ASN E C   1 
ATOM   12743 O O   . ASN E  1 98  ? 116.402 6.762   -15.484 1.00   55.79  ? 98  ASN E O   1 
ATOM   12744 C CB  . ASN E  1 98  ? 114.049 8.707   -16.949 1.00   69.76  ? 98  ASN E CB  1 
ATOM   12745 C CG  . ASN E  1 98  ? 113.679 9.221   -18.317 1.00   78.55  ? 98  ASN E CG  1 
ATOM   12746 O OD1 . ASN E  1 98  ? 112.759 8.610   -18.863 1.00   83.65  ? 98  ASN E OD1 1 
ATOM   12747 N ND2 . ASN E  1 98  ? 114.537 10.076  -18.994 1.00   80.03  ? 98  ASN E ND2 1 
ATOM   12748 N N   . ASN E  1 99  ? 115.261 8.376   -14.389 1.00   54.64  ? 99  ASN E N   1 
ATOM   12749 C CA  . ASN E  1 99  ? 115.463 7.901   -13.022 1.00   50.08  ? 99  ASN E CA  1 
ATOM   12750 C C   . ASN E  1 99  ? 116.974 7.909   -12.696 1.00   45.37  ? 99  ASN E C   1 
ATOM   12751 O O   . ASN E  1 99  ? 117.469 7.156   -11.847 1.00   45.26  ? 99  ASN E O   1 
ATOM   12752 C CB  . ASN E  1 99  ? 114.845 6.519   -12.815 1.00   52.78  ? 99  ASN E CB  1 
ATOM   12753 C CG  . ASN E  1 99  ? 114.459 6.280   -11.377 0.0000 52.05  ? 99  ASN E CG  1 
ATOM   12754 O OD1 . ASN E  1 99  ? 114.282 7.230   -10.605 0.0000 51.45  ? 99  ASN E OD1 1 
ATOM   12755 N ND2 . ASN E  1 99  ? 114.246 5.028   -11.027 0.0000 52.38  ? 99  ASN E ND2 1 
ATOM   12756 N N   . THR E  1 100 ? 117.690 8.835   -13.333 1.00   42.66  ? 100 THR E N   1 
ATOM   12757 C CA  . THR E  1 100 ? 119.081 9.111   -13.022 1.00   41.66  ? 100 THR E CA  1 
ATOM   12758 C C   . THR E  1 100 ? 119.153 10.441  -12.294 1.00   42.87  ? 100 THR E C   1 
ATOM   12759 O O   . THR E  1 100 ? 118.120 11.000  -11.951 1.00   47.49  ? 100 THR E O   1 
ATOM   12760 C CB  . THR E  1 100 ? 119.939 9.176   -14.299 1.00   43.55  ? 100 THR E CB  1 
ATOM   12761 O OG1 . THR E  1 100 ? 119.220 9.899   -15.302 1.00   46.63  ? 100 THR E OG1 1 
ATOM   12762 C CG2 . THR E  1 100 ? 120.202 7.791   -14.840 1.00   44.28  ? 100 THR E CG2 1 
ATOM   12763 N N   . CYS E  1 101 ? 120.354 10.974  -12.062 1.00   42.51  ? 101 CYS E N   1 
ATOM   12764 C CA  . CYS E  1 101 ? 120.441 12.291  -11.428 1.00   42.03  ? 101 CYS E CA  1 
ATOM   12765 C C   . CYS E  1 101 ? 121.272 13.328  -12.181 1.00   39.70  ? 101 CYS E C   1 
ATOM   12766 O O   . CYS E  1 101 ? 122.217 13.024  -12.896 1.00   40.42  ? 101 CYS E O   1 
ATOM   12767 C CB  . CYS E  1 101 ? 120.926 12.172  -9.989  1.00   43.40  ? 101 CYS E CB  1 
ATOM   12768 S SG  . CYS E  1 101 ? 122.394 11.260  -9.747  1.00   67.27  ? 101 CYS E SG  1 
ATOM   12769 N N   . GLY E  1 102 ? 120.857 14.572  -12.008 1.00   39.71  ? 102 GLY E N   1 
ATOM   12770 C CA  . GLY E  1 102 ? 121.381 15.710  -12.732 1.00   41.77  ? 102 GLY E CA  1 
ATOM   12771 C C   . GLY E  1 102 ? 122.460 16.532  -12.056 1.00   41.70  ? 102 GLY E C   1 
ATOM   12772 O O   . GLY E  1 102 ? 122.471 16.730  -10.839 1.00   41.74  ? 102 GLY E O   1 
ATOM   12773 N N   . LEU E  1 103 ? 123.370 17.030  -12.875 1.00   42.24  ? 103 LEU E N   1 
ATOM   12774 C CA  . LEU E  1 103 ? 124.513 17.773  -12.387 1.00   41.98  ? 103 LEU E CA  1 
ATOM   12775 C C   . LEU E  1 103 ? 124.736 19.023  -13.252 1.00   43.91  ? 103 LEU E C   1 
ATOM   12776 O O   . LEU E  1 103 ? 124.783 18.937  -14.482 1.00   47.15  ? 103 LEU E O   1 
ATOM   12777 C CB  . LEU E  1 103 ? 125.746 16.864  -12.388 1.00   39.65  ? 103 LEU E CB  1 
ATOM   12778 C CG  . LEU E  1 103 ? 126.950 17.301  -11.563 1.00   40.86  ? 103 LEU E CG  1 
ATOM   12779 C CD1 . LEU E  1 103 ? 126.539 17.660  -10.138 1.00   43.00  ? 103 LEU E CD1 1 
ATOM   12780 C CD2 . LEU E  1 103 ? 127.973 16.191  -11.550 1.00   38.99  ? 103 LEU E CD2 1 
ATOM   12781 N N   . LEU E  1 104 ? 124.842 20.187  -12.624 1.00   40.24  ? 104 LEU E N   1 
ATOM   12782 C CA  . LEU E  1 104 ? 125.102 21.381  -13.401 1.00   42.83  ? 104 LEU E CA  1 
ATOM   12783 C C   . LEU E  1 104 ? 126.595 21.518  -13.681 1.00   38.96  ? 104 LEU E C   1 
ATOM   12784 O O   . LEU E  1 104 ? 127.397 21.535  -12.754 1.00   37.90  ? 104 LEU E O   1 
ATOM   12785 C CB  . LEU E  1 104 ? 124.585 22.606  -12.682 1.00   48.62  ? 104 LEU E CB  1 
ATOM   12786 C CG  . LEU E  1 104 ? 124.338 23.774  -13.622 1.00   55.15  ? 104 LEU E CG  1 
ATOM   12787 C CD1 . LEU E  1 104 ? 123.212 23.451  -14.594 1.00   56.96  ? 104 LEU E CD1 1 
ATOM   12788 C CD2 . LEU E  1 104 ? 123.968 24.955  -12.770 1.00   59.57  ? 104 LEU E CD2 1 
ATOM   12789 N N   . SER E  1 105 ? 126.948 21.566  -14.966 1.00   38.10  ? 105 SER E N   1 
ATOM   12790 C CA  . SER E  1 105 ? 128.331 21.720  -15.413 1.00   36.47  ? 105 SER E CA  1 
ATOM   12791 C C   . SER E  1 105 ? 128.549 23.101  -16.011 1.00   37.75  ? 105 SER E C   1 
ATOM   12792 O O   . SER E  1 105 ? 127.679 23.619  -16.685 1.00   39.84  ? 105 SER E O   1 
ATOM   12793 C CB  . SER E  1 105 ? 128.672 20.641  -16.435 1.00   36.17  ? 105 SER E CB  1 
ATOM   12794 O OG  . SER E  1 105 ? 128.495 19.355  -15.865 1.00   36.49  ? 105 SER E OG  1 
ATOM   12795 N N   . SER E  1 106 ? 129.720 23.687  -15.814 1.00   39.21  ? 106 SER E N   1 
ATOM   12796 C CA  . SER E  1 106 ? 129.938 25.038  -16.322 1.00   41.40  ? 106 SER E CA  1 
ATOM   12797 C C   . SER E  1 106 ? 131.104 25.099  -17.308 1.00   41.59  ? 106 SER E C   1 
ATOM   12798 O O   . SER E  1 106 ? 132.174 24.524  -17.070 1.00   40.86  ? 106 SER E O   1 
ATOM   12799 C CB  A SER E  1 106 ? 130.166 26.018  -15.164 0.50   41.63  ? 106 SER E CB  1 
ATOM   12800 C CB  B SER E  1 106 ? 130.196 26.006  -15.163 0.50   41.59  ? 106 SER E CB  1 
ATOM   12801 O OG  A SER E  1 106 ? 130.121 27.368  -15.610 0.50   44.99  ? 106 SER E OG  1 
ATOM   12802 O OG  B SER E  1 106 ? 129.068 26.115  -14.313 0.50   41.74  ? 106 SER E OG  1 
ATOM   12803 N N   . ASN E  1 107 ? 130.883 25.800  -18.420 1.00   39.78  ? 107 ASN E N   1 
ATOM   12804 C CA  . ASN E  1 107 ? 131.957 26.152  -19.326 1.00   38.82  ? 107 ASN E CA  1 
ATOM   12805 C C   . ASN E  1 107 ? 132.605 27.383  -18.751 1.00   39.89  ? 107 ASN E C   1 
ATOM   12806 O O   . ASN E  1 107 ? 132.012 28.454  -18.716 1.00   42.10  ? 107 ASN E O   1 
ATOM   12807 C CB  . ASN E  1 107 ? 131.446 26.385  -20.743 1.00   40.50  ? 107 ASN E CB  1 
ATOM   12808 C CG  . ASN E  1 107 ? 132.554 26.743  -21.725 1.00   43.87  ? 107 ASN E CG  1 
ATOM   12809 O OD1 . ASN E  1 107 ? 133.502 27.444  -21.391 1.00   44.74  ? 107 ASN E OD1 1 
ATOM   12810 N ND2 . ASN E  1 107 ? 132.448 26.232  -22.939 1.00   46.88  ? 107 ASN E ND2 1 
ATOM   12811 N N   . PRO E  1 108 ? 133.836 27.226  -18.282 1.00   38.62  ? 108 PRO E N   1 
ATOM   12812 C CA  . PRO E  1 108 ? 134.492 28.268  -17.499 1.00   39.15  ? 108 PRO E CA  1 
ATOM   12813 C C   . PRO E  1 108 ? 134.921 29.453  -18.354 1.00   41.59  ? 108 PRO E C   1 
ATOM   12814 O O   . PRO E  1 108 ? 135.158 30.531  -17.827 1.00   45.24  ? 108 PRO E O   1 
ATOM   12815 C CB  . PRO E  1 108 ? 135.691 27.528  -16.907 1.00   37.86  ? 108 PRO E CB  1 
ATOM   12816 C CG  . PRO E  1 108 ? 135.998 26.463  -17.934 1.00   36.52  ? 108 PRO E CG  1 
ATOM   12817 C CD  . PRO E  1 108 ? 134.680 26.037  -18.470 1.00   36.88  ? 108 PRO E CD  1 
ATOM   12818 N N   . VAL E  1 109 ? 134.985 29.264  -19.665 1.00   41.38  ? 109 VAL E N   1 
ATOM   12819 C CA  . VAL E  1 109 ? 135.344 30.339  -20.577 1.00   41.85  ? 109 VAL E CA  1 
ATOM   12820 C C   . VAL E  1 109 ? 134.154 31.217  -20.892 1.00   43.98  ? 109 VAL E C   1 
ATOM   12821 O O   . VAL E  1 109 ? 134.235 32.444  -20.851 1.00   49.02  ? 109 VAL E O   1 
ATOM   12822 C CB  . VAL E  1 109 ? 135.919 29.802  -21.899 1.00   41.41  ? 109 VAL E CB  1 
ATOM   12823 C CG1 . VAL E  1 109 ? 136.068 30.925  -22.897 1.00   44.87  ? 109 VAL E CG1 1 
ATOM   12824 C CG2 . VAL E  1 109 ? 137.249 29.139  -21.666 1.00   39.47  ? 109 VAL E CG2 1 
ATOM   12825 N N   . THR E  1 110 ? 133.049 30.586  -21.250 1.00   44.75  ? 110 THR E N   1 
ATOM   12826 C CA  . THR E  1 110 ? 131.866 31.317  -21.671 1.00   47.87  ? 110 THR E CA  1 
ATOM   12827 C C   . THR E  1 110 ? 130.918 31.619  -20.531 1.00   50.49  ? 110 THR E C   1 
ATOM   12828 O O   . THR E  1 110 ? 130.005 32.420  -20.695 1.00   56.39  ? 110 THR E O   1 
ATOM   12829 C CB  . THR E  1 110 ? 131.135 30.544  -22.729 1.00   47.48  ? 110 THR E CB  1 
ATOM   12830 O OG1 . THR E  1 110 ? 130.615 29.351  -22.141 1.00   47.51  ? 110 THR E OG1 1 
ATOM   12831 C CG2 . THR E  1 110 ? 132.112 30.172  -23.845 1.00   46.49  ? 110 THR E CG2 1 
ATOM   12832 N N   . GLN E  1 111 ? 131.149 30.972  -19.392 1.00   46.60  ? 111 GLN E N   1 
ATOM   12833 C CA  . GLN E  1 111 ? 130.316 31.077  -18.197 1.00   48.85  ? 111 GLN E CA  1 
ATOM   12834 C C   . GLN E  1 111 ? 128.966 30.465  -18.362 1.00   50.39  ? 111 GLN E C   1 
ATOM   12835 O O   . GLN E  1 111 ? 128.166 30.473  -17.433 1.00   51.76  ? 111 GLN E O   1 
ATOM   12836 C CB  . GLN E  1 111 ? 130.141 32.538  -17.794 1.00   59.56  ? 111 GLN E CB  1 
ATOM   12837 C CG  . GLN E  1 111 ? 131.370 33.142  -17.199 1.00   69.59  ? 111 GLN E CG  1 
ATOM   12838 C CD  . GLN E  1 111 ? 131.666 32.505  -15.863 1.00   78.67  ? 111 GLN E CD  1 
ATOM   12839 O OE1 . GLN E  1 111 ? 132.551 31.654  -15.737 1.00   81.20  ? 111 GLN E OE1 1 
ATOM   12840 N NE2 . GLN E  1 111 ? 130.899 32.898  -14.849 1.00   82.70  ? 111 GLN E NE2 1 
ATOM   12841 N N   . GLU E  1 112 ? 128.736 29.852  -19.510 1.00   51.89  ? 112 GLU E N   1 
ATOM   12842 C CA  . GLU E  1 112 ? 127.544 29.051  -19.686 1.00   53.86  ? 112 GLU E CA  1 
ATOM   12843 C C   . GLU E  1 112 ? 127.618 27.829  -18.838 1.00   50.50  ? 112 GLU E C   1 
ATOM   12844 O O   . GLU E  1 112 ? 128.697 27.310  -18.569 1.00   47.61  ? 112 GLU E O   1 
ATOM   12845 C CB  . GLU E  1 112 ? 127.337 28.633  -21.125 1.00   60.80  ? 112 GLU E CB  1 
ATOM   12846 C CG  . GLU E  1 112 ? 126.850 29.745  -21.991 1.00   71.04  ? 112 GLU E CG  1 
ATOM   12847 C CD  . GLU E  1 112 ? 126.954 29.385  -23.436 1.00   78.52  ? 112 GLU E CD  1 
ATOM   12848 O OE1 . GLU E  1 112 ? 127.921 28.671  -23.790 1.00   77.98  ? 112 GLU E OE1 1 
ATOM   12849 O OE2 . GLU E  1 112 ? 126.070 29.809  -24.211 1.00   85.39  1 112 GLU E OE2 1 
ATOM   12850 N N   . SER E  1 113 ? 126.445 27.379  -18.423 1.00   51.71  ? 113 SER E N   1 
ATOM   12851 C CA  . SER E  1 113 ? 126.309 26.115  -17.736 1.00   51.49  ? 113 SER E CA  1 
ATOM   12852 C C   . SER E  1 113 ? 125.137 25.292  -18.284 1.00   49.05  ? 113 SER E C   1 
ATOM   12853 O O   . SER E  1 113 ? 124.265 25.813  -18.957 1.00   51.33  ? 113 SER E O   1 
ATOM   12854 C CB  . SER E  1 113 ? 126.187 26.368  -16.230 1.00   53.74  ? 113 SER E CB  1 
ATOM   12855 O OG  . SER E  1 113 ? 125.043 27.139  -15.940 1.00   57.21  ? 113 SER E OG  1 
ATOM   12856 N N   . GLY E  1 114 ? 125.142 23.993  -18.024 1.00   45.92  ? 114 GLY E N   1 
ATOM   12857 C CA  . GLY E  1 114 ? 124.108 23.130  -18.544 1.00   46.04  ? 114 GLY E CA  1 
ATOM   12858 C C   . GLY E  1 114 ? 123.929 21.965  -17.616 1.00   43.76  ? 114 GLY E C   1 
ATOM   12859 O O   . GLY E  1 114 ? 124.835 21.605  -16.890 1.00   42.14  ? 114 GLY E O   1 
ATOM   12860 N N   . LEU E  1 115 ? 122.740 21.392  -17.609 1.00   44.18  ? 115 LEU E N   1 
ATOM   12861 C CA  . LEU E  1 115 ? 122.485 20.269  -16.735 1.00   43.87  ? 115 LEU E CA  1 
ATOM   12862 C C   . LEU E  1 115 ? 122.845 18.944  -17.394 1.00   42.33  ? 115 LEU E C   1 
ATOM   12863 O O   . LEU E  1 115 ? 122.242 18.541  -18.384 1.00   42.07  ? 115 LEU E O   1 
ATOM   12864 C CB  . LEU E  1 115 ? 121.024 20.242  -16.301 1.00   46.70  ? 115 LEU E CB  1 
ATOM   12865 C CG  . LEU E  1 115 ? 120.858 19.289  -15.123 1.00   48.90  ? 115 LEU E CG  1 
ATOM   12866 C CD1 . LEU E  1 115 ? 121.288 19.973  -13.833 1.00   50.08  ? 115 LEU E CD1 1 
ATOM   12867 C CD2 . LEU E  1 115 ? 119.451 18.760  -15.008 1.00   51.63  ? 115 LEU E CD2 1 
ATOM   12868 N N   . GLY E  1 116 ? 123.825 18.262  -16.828 1.00   42.61  ? 116 GLY E N   1 
ATOM   12869 C CA  . GLY E  1 116 ? 124.220 16.959  -17.323 1.00   43.82  ? 116 GLY E CA  1 
ATOM   12870 C C   . GLY E  1 116 ? 123.738 15.812  -16.451 1.00   41.47  ? 116 GLY E C   1 
ATOM   12871 O O   . GLY E  1 116 ? 123.054 16.013  -15.458 1.00   41.10  ? 116 GLY E O   1 
ATOM   12872 N N   . GLU E  1 117 ? 124.106 14.599  -16.837 1.00   40.08  ? 117 GLU E N   1 
ATOM   12873 C CA  . GLU E  1 117 ? 123.741 13.398  -16.100 1.00   39.09  ? 117 GLU E CA  1 
ATOM   12874 C C   . GLU E  1 117 ? 124.972 12.815  -15.424 1.00   38.85  ? 117 GLU E C   1 
ATOM   12875 O O   . GLU E  1 117 ? 126.017 12.654  -16.065 1.00   40.33  ? 117 GLU E O   1 
ATOM   12876 C CB  . GLU E  1 117 ? 123.131 12.365  -17.053 1.00   39.05  ? 117 GLU E CB  1 
ATOM   12877 C CG  . GLU E  1 117 ? 122.538 11.145  -16.398 1.00   37.75  ? 117 GLU E CG  1 
ATOM   12878 C CD  . GLU E  1 117 ? 122.120 10.109  -17.414 1.00   43.04  ? 117 GLU E CD  1 
ATOM   12879 O OE1 . GLU E  1 117 ? 122.946 9.733   -18.266 1.00   45.70  ? 117 GLU E OE1 1 
ATOM   12880 O OE2 . GLU E  1 117 ? 120.960 9.667   -17.368 1.00   47.02  1 117 GLU E OE2 1 
ATOM   12881 N N   . LEU E  1 118 ? 124.854 12.478  -14.143 1.00   35.13  ? 118 LEU E N   1 
ATOM   12882 C CA  . LEU E  1 118 ? 125.971 11.866  -13.440 1.00   31.55  ? 118 LEU E CA  1 
ATOM   12883 C C   . LEU E  1 118 ? 126.329 10.538  -14.100 1.00   34.12  ? 118 LEU E C   1 
ATOM   12884 O O   . LEU E  1 118 ? 125.444 9.771   -14.475 1.00   33.62  ? 118 LEU E O   1 
ATOM   12885 C CB  . LEU E  1 118 ? 125.635 11.659  -11.969 1.00   29.80  ? 118 LEU E CB  1 
ATOM   12886 C CG  . LEU E  1 118 ? 126.775 11.171  -11.085 1.00   28.48  ? 118 LEU E CG  1 
ATOM   12887 C CD1 . LEU E  1 118 ? 127.862 12.212  -11.027 1.00   26.78  ? 118 LEU E CD1 1 
ATOM   12888 C CD2 . LEU E  1 118 ? 126.247 10.846  -9.702  1.00   27.59  ? 118 LEU E CD2 1 
ATOM   12889 N N   . ALA E  1 119 ? 127.629 10.294  -14.261 1.00   33.72  ? 119 ALA E N   1 
ATOM   12890 C CA  . ALA E  1 119 ? 128.144 9.103   -14.911 1.00   31.19  ? 119 ALA E CA  1 
ATOM   12891 C C   . ALA E  1 119 ? 129.236 8.508   -14.043 1.00   34.95  ? 119 ALA E C   1 
ATOM   12892 O O   . ALA E  1 119 ? 129.799 9.175   -13.177 1.00   36.69  ? 119 ALA E O   1 
ATOM   12893 C CB  . ALA E  1 119 ? 128.684 9.425   -16.296 1.00   28.06  ? 119 ALA E CB  1 
ATOM   12894 N N   . GLN E  1 120 ? 129.524 7.240   -14.289 1.00   36.91  ? 120 GLN E N   1 
ATOM   12895 C CA  . GLN E  1 120 ? 130.560 6.490   -13.593 1.00   37.33  ? 120 GLN E CA  1 
ATOM   12896 C C   . GLN E  1 120 ? 131.291 5.586   -14.595 1.00   37.11  ? 120 GLN E C   1 
ATOM   12897 O O   . GLN E  1 120 ? 130.651 4.878   -15.347 1.00   35.04  ? 120 GLN E O   1 
ATOM   12898 C CB  . GLN E  1 120 ? 129.930 5.673   -12.485 1.00   38.50  ? 120 GLN E CB  1 
ATOM   12899 C CG  . GLN E  1 120 ? 130.858 4.814   -11.726 1.00   39.86  ? 120 GLN E CG  1 
ATOM   12900 C CD  . GLN E  1 120 ? 130.097 3.920   -10.796 1.00   43.29  ? 120 GLN E CD  1 
ATOM   12901 O OE1 . GLN E  1 120 ? 129.588 4.360   -9.766  1.00   42.67  ? 120 GLN E OE1 1 
ATOM   12902 N NE2 . GLN E  1 120 ? 129.945 2.661   -11.195 1.00   45.70  ? 120 GLN E NE2 1 
ATOM   12903 N N   . ASP E  1 121 ? 132.617 5.602   -14.613 1.00   37.31  ? 121 ASP E N   1 
ATOM   12904 C CA  . ASP E  1 121 ? 133.350 4.759   -15.550 1.00   38.50  ? 121 ASP E CA  1 
ATOM   12905 C C   . ASP E  1 121 ? 134.761 4.642   -15.020 1.00   36.32  ? 121 ASP E C   1 
ATOM   12906 O O   . ASP E  1 121 ? 135.070 5.257   -14.005 1.00   33.85  ? 121 ASP E O   1 
ATOM   12907 C CB  . ASP E  1 121 ? 133.343 5.386   -16.950 1.00   41.46  ? 121 ASP E CB  1 
ATOM   12908 C CG  . ASP E  1 121 ? 133.401 4.367   -18.069 1.00   44.53  ? 121 ASP E CG  1 
ATOM   12909 O OD1 . ASP E  1 121 ? 133.940 3.261   -17.874 1.00   46.48  ? 121 ASP E OD1 1 
ATOM   12910 O OD2 . ASP E  1 121 ? 132.904 4.686   -19.167 1.00   45.30  1 121 ASP E OD2 1 
ATOM   12911 N N   . VAL E  1 122 ? 135.607 3.880   -15.713 1.00   36.05  ? 122 VAL E N   1 
ATOM   12912 C CA  . VAL E  1 122 ? 137.029 3.759   -15.393 1.00   32.21  ? 122 VAL E CA  1 
ATOM   12913 C C   . VAL E  1 122 ? 137.801 5.044   -15.775 1.00   33.39  ? 122 VAL E C   1 
ATOM   12914 O O   . VAL E  1 122 ? 137.607 5.574   -16.868 1.00   33.57  ? 122 VAL E O   1 
ATOM   12915 C CB  . VAL E  1 122 ? 137.656 2.555   -16.139 1.00   29.74  ? 122 VAL E CB  1 
ATOM   12916 C CG1 . VAL E  1 122 ? 139.151 2.526   -15.976 1.00   30.26  ? 122 VAL E CG1 1 
ATOM   12917 C CG2 . VAL E  1 122 ? 137.073 1.269   -15.640 1.00   31.06  ? 122 VAL E CG2 1 
ATOM   12918 N N   . LEU E  1 123 ? 138.634 5.560   -14.863 1.00   31.53  ? 123 LEU E N   1 
ATOM   12919 C CA  . LEU E  1 123 ? 139.696 6.531   -15.195 1.00   30.38  ? 123 LEU E CA  1 
ATOM   12920 C C   . LEU E  1 123 ? 141.066 5.936   -14.823 1.00   33.73  ? 123 LEU E C   1 
ATOM   12921 O O   . LEU E  1 123 ? 141.192 5.292   -13.776 1.00   33.82  ? 123 LEU E O   1 
ATOM   12922 C CB  . LEU E  1 123 ? 139.497 7.875   -14.470 1.00   28.45  ? 123 LEU E CB  1 
ATOM   12923 C CG  . LEU E  1 123 ? 140.573 8.979   -14.629 1.00   33.09  ? 123 LEU E CG  1 
ATOM   12924 C CD1 . LEU E  1 123 ? 139.986 10.400  -14.632 1.00   31.96  ? 123 LEU E CD1 1 
ATOM   12925 C CD2 . LEU E  1 123 ? 141.641 8.918   -13.551 1.00   32.00  ? 123 LEU E CD2 1 
ATOM   12926 N N   . ALA E  1 124 ? 142.080 6.141   -15.674 1.00   33.94  ? 124 ALA E N   1 
ATOM   12927 C CA  . ALA E  1 124 ? 143.442 5.697   -15.384 1.00   33.20  ? 124 ALA E CA  1 
ATOM   12928 C C   . ALA E  1 124 ? 144.429 6.857   -15.431 1.00   35.18  ? 124 ALA E C   1 
ATOM   12929 O O   . ALA E  1 124 ? 144.218 7.853   -16.136 1.00   35.18  ? 124 ALA E O   1 
ATOM   12930 C CB  . ALA E  1 124 ? 143.864 4.621   -16.344 1.00   33.94  ? 124 ALA E CB  1 
ATOM   12931 N N   . ILE E  1 125 ? 145.512 6.733   -14.675 1.00   33.08  ? 125 ILE E N   1 
ATOM   12932 C CA  . ILE E  1 125 ? 146.490 7.801   -14.616 1.00   31.08  ? 125 ILE E CA  1 
ATOM   12933 C C   . ILE E  1 125 ? 147.845 7.198   -14.283 1.00   33.86  ? 125 ILE E C   1 
ATOM   12934 O O   . ILE E  1 125 ? 147.910 6.161   -13.644 1.00   36.61  ? 125 ILE E O   1 
ATOM   12935 C CB  . ILE E  1 125 ? 146.083 8.882   -13.577 1.00   28.19  ? 125 ILE E CB  1 
ATOM   12936 C CG1 . ILE E  1 125 ? 146.999 10.100  -13.677 1.00   27.78  ? 125 ILE E CG1 1 
ATOM   12937 C CG2 . ILE E  1 125 ? 146.056 8.310   -12.178 1.00   27.71  ? 125 ILE E CG2 1 
ATOM   12938 C CD1 . ILE E  1 125 ? 146.656 11.201  -12.758 1.00   27.33  ? 125 ILE E CD1 1 
ATOM   12939 N N   . HIS E  1 126 ? 148.927 7.832   -14.722 1.00   34.19  ? 126 HIS E N   1 
ATOM   12940 C CA  . HIS E  1 126 ? 150.269 7.300   -14.483 1.00   34.56  ? 126 HIS E CA  1 
ATOM   12941 C C   . HIS E  1 126 ? 150.687 7.273   -13.019 1.00   34.60  ? 126 HIS E C   1 
ATOM   12942 O O   . HIS E  1 126 ? 150.419 8.200   -12.277 1.00   34.59  ? 126 HIS E O   1 
ATOM   12943 C CB  . HIS E  1 126 ? 151.296 8.100   -15.279 1.00   36.26  ? 126 HIS E CB  1 
ATOM   12944 C CG  . HIS E  1 126 ? 151.392 7.688   -16.709 1.00   40.87  ? 126 HIS E CG  1 
ATOM   12945 N ND1 . HIS E  1 126 ? 152.049 6.546   -17.111 1.00   46.64  ? 126 HIS E ND1 1 
ATOM   12946 C CD2 . HIS E  1 126 ? 150.873 8.236   -17.829 1.00   41.22  ? 126 HIS E CD2 1 
ATOM   12947 C CE1 . HIS E  1 126 ? 151.953 6.420   -18.421 1.00   46.04  ? 126 HIS E CE1 1 
ATOM   12948 N NE2 . HIS E  1 126 ? 151.241 7.431   -18.880 1.00   43.53  ? 126 HIS E NE2 1 
ATOM   12949 N N   . SER E  1 127 ? 151.319 6.181   -12.603 1.00   37.55  ? 127 SER E N   1 
ATOM   12950 C CA  . SER E  1 127 ? 152.061 6.167   -11.351 1.00   36.16  ? 127 SER E CA  1 
ATOM   12951 C C   . SER E  1 127 ? 153.510 6.522   -11.625 1.00   40.35  ? 127 SER E C   1 
ATOM   12952 O O   . SER E  1 127 ? 153.858 6.946   -12.732 1.00   43.04  ? 127 SER E O   1 
ATOM   12953 C CB  . SER E  1 127 ? 151.952 4.813   -10.678 1.00   35.07  ? 127 SER E CB  1 
ATOM   12954 O OG  . SER E  1 127 ? 152.315 3.788   -11.570 1.00   37.03  ? 127 SER E OG  1 
ATOM   12955 N N   . THR E  1 128 ? 154.373 6.344   -10.636 1.00   40.94  ? 128 THR E N   1 
ATOM   12956 C CA  . THR E  1 128 ? 155.783 6.582   -10.880 1.00   38.50  ? 128 THR E CA  1 
ATOM   12957 C C   . THR E  1 128 ? 156.611 5.359   -10.603 1.00   43.91  ? 128 THR E C   1 
ATOM   12958 O O   . THR E  1 128 ? 156.274 4.528   -9.771  1.00   45.41  ? 128 THR E O   1 
ATOM   12959 C CB  . THR E  1 128 ? 156.317 7.737   -10.034 1.00   38.36  ? 128 THR E CB  1 
ATOM   12960 O OG1 . THR E  1 128 ? 156.294 7.370   -8.652  1.00   40.67  ? 128 THR E OG1 1 
ATOM   12961 C CG2 . THR E  1 128 ? 155.468 8.987   -10.262 1.00   33.95  ? 128 THR E CG2 1 
ATOM   12962 N N   . HIS E  1 129 ? 157.723 5.272   -11.307 1.00   47.50  ? 129 HIS E N   1 
ATOM   12963 C CA  . HIS E  1 129 ? 158.620 4.154   -11.167 1.00   50.08  ? 129 HIS E CA  1 
ATOM   12964 C C   . HIS E  1 129 ? 160.049 4.638   -11.160 1.00   49.09  ? 129 HIS E C   1 
ATOM   12965 O O   . HIS E  1 129 ? 160.607 4.921   -12.211 1.00   48.70  ? 129 HIS E O   1 
ATOM   12966 C CB  . HIS E  1 129 ? 158.380 3.182   -12.308 1.00   54.12  ? 129 HIS E CB  1 
ATOM   12967 C CG  . HIS E  1 129 ? 159.167 1.923   -12.199 1.00   62.63  ? 129 HIS E CG  1 
ATOM   12968 N ND1 . HIS E  1 129 ? 159.101 1.101   -11.096 1.00   66.28  ? 129 HIS E ND1 1 
ATOM   12969 C CD2 . HIS E  1 129 ? 160.029 1.334   -13.061 1.00   68.22  ? 129 HIS E CD2 1 
ATOM   12970 C CE1 . HIS E  1 129 ? 159.900 0.064   -11.277 1.00   71.14  ? 129 HIS E CE1 1 
ATOM   12971 N NE2 . HIS E  1 129 ? 160.473 0.181   -12.462 1.00   72.77  ? 129 HIS E NE2 1 
ATOM   12972 N N   . GLY E  1 130 ? 160.648 4.725   -9.980  1.00   50.85  ? 130 GLY E N   1 
ATOM   12973 C CA  . GLY E  1 130 ? 161.971 5.317   -9.857  1.00   53.54  ? 130 GLY E CA  1 
ATOM   12974 C C   . GLY E  1 130 ? 161.962 6.777   -10.257 1.00   51.34  ? 130 GLY E C   1 
ATOM   12975 O O   . GLY E  1 130 ? 161.132 7.542   -9.771  1.00   49.54  ? 130 GLY E O   1 
ATOM   12976 N N   . SER E  1 131 ? 162.838 7.156   -11.178 1.00   51.01  ? 131 SER E N   1 
ATOM   12977 C CA  . SER E  1 131 ? 162.883 8.539   -11.609 1.00   51.30  ? 131 SER E CA  1 
ATOM   12978 C C   . SER E  1 131 ? 161.971 8.714   -12.804 1.00   50.41  ? 131 SER E C   1 
ATOM   12979 O O   . SER E  1 131 ? 161.860 9.804   -13.345 1.00   52.38  ? 131 SER E O   1 
ATOM   12980 C CB  . SER E  1 131 ? 164.304 8.969   -11.986 1.00   51.79  ? 131 SER E CB  1 
ATOM   12981 O OG  . SER E  1 131 ? 164.642 8.486   -13.275 1.00   52.95  ? 131 SER E OG  1 
ATOM   12982 N N   . LYS E  1 132 ? 161.306 7.640   -13.205 1.00   48.27  ? 132 LYS E N   1 
ATOM   12983 C CA  . LYS E  1 132 ? 160.501 7.647   -14.419 1.00   47.20  ? 132 LYS E CA  1 
ATOM   12984 C C   . LYS E  1 132 ? 159.004 7.567   -14.133 1.00   46.21  ? 132 LYS E C   1 
ATOM   12985 O O   . LYS E  1 132 ? 158.605 7.378   -12.992 1.00   46.41  ? 132 LYS E O   1 
ATOM   12986 C CB  . LYS E  1 132 ? 160.925 6.474   -15.291 1.00   48.76  ? 132 LYS E CB  1 
ATOM   12987 C CG  . LYS E  1 132 ? 162.428 6.438   -15.562 1.00   51.32  ? 132 LYS E CG  1 
ATOM   12988 C CD  . LYS E  1 132 ? 162.724 5.818   -16.904 1.00   53.58  ? 132 LYS E CD  1 
ATOM   12989 C CE  . LYS E  1 132 ? 164.188 5.442   -17.024 0.0000 56.64  ? 132 LYS E CE  1 
ATOM   12990 N NZ  . LYS E  1 132 ? 164.369 4.122   -17.697 0.0000 58.93  ? 132 LYS E NZ  1 
ATOM   12991 N N   . LEU E  1 133 ? 158.177 7.734   -15.164 1.00   45.31  ? 133 LEU E N   1 
ATOM   12992 C CA  . LEU E  1 133 ? 156.750 7.388   -15.073 1.00   44.35  ? 133 LEU E CA  1 
ATOM   12993 C C   . LEU E  1 133 ? 156.535 5.892   -14.912 1.00   47.62  ? 133 LEU E C   1 
ATOM   12994 O O   . LEU E  1 133 ? 157.245 5.091   -15.522 1.00   51.86  ? 133 LEU E O   1 
ATOM   12995 C CB  . LEU E  1 133 ? 155.970 7.848   -16.304 1.00   42.92  ? 133 LEU E CB  1 
ATOM   12996 C CG  . LEU E  1 133 ? 155.745 9.333   -16.486 1.00   40.80  ? 133 LEU E CG  1 
ATOM   12997 C CD1 . LEU E  1 133 ? 154.950 9.586   -17.746 1.00   41.09  ? 133 LEU E CD1 1 
ATOM   12998 C CD2 . LEU E  1 133 ? 155.025 9.827   -15.272 1.00   36.81  ? 133 LEU E CD2 1 
ATOM   12999 N N   . GLY E  1 134 ? 155.554 5.506   -14.103 1.00   45.10  ? 134 GLY E N   1 
ATOM   13000 C CA  . GLY E  1 134 ? 155.268 4.097   -13.918 1.00   47.90  ? 134 GLY E CA  1 
ATOM   13001 C C   . GLY E  1 134 ? 153.998 3.698   -14.639 1.00   49.47  ? 134 GLY E C   1 
ATOM   13002 O O   . GLY E  1 134 ? 153.456 4.463   -15.438 1.00   45.45  ? 134 GLY E O   1 
ATOM   13003 N N   . PRO E  1 135 ? 153.527 2.478   -14.382 1.00   55.07  ? 135 PRO E N   1 
ATOM   13004 C CA  . PRO E  1 135 ? 152.319 1.977   -15.048 1.00   54.93  ? 135 PRO E CA  1 
ATOM   13005 C C   . PRO E  1 135 ? 151.053 2.736   -14.658 1.00   48.92  ? 135 PRO E C   1 
ATOM   13006 O O   . PRO E  1 135 ? 151.001 3.332   -13.587 1.00   48.19  ? 135 PRO E O   1 
ATOM   13007 C CB  . PRO E  1 135 ? 152.260 0.512   -14.611 1.00   58.97  ? 135 PRO E CB  1 
ATOM   13008 C CG  . PRO E  1 135 ? 153.119 0.428   -13.395 1.00   60.40  ? 135 PRO E CG  1 
ATOM   13009 C CD  . PRO E  1 135 ? 154.191 1.444   -13.570 1.00   58.65  ? 135 PRO E CD  1 
ATOM   13010 N N   . MET E  1 136 ? 150.066 2.720   -15.549 1.00   45.42  ? 136 MET E N   1 
ATOM   13011 C CA  . MET E  1 136 ? 148.756 3.300   -15.312 1.00   41.50  ? 136 MET E CA  1 
ATOM   13012 C C   . MET E  1 136 ? 148.082 2.598   -14.174 1.00   40.23  ? 136 MET E C   1 
ATOM   13013 O O   . MET E  1 136 ? 148.164 1.386   -14.067 1.00   43.87  ? 136 MET E O   1 
ATOM   13014 C CB  . MET E  1 136 ? 147.880 3.163   -16.540 1.00   45.52  ? 136 MET E CB  1 
ATOM   13015 C CG  . MET E  1 136 ? 148.514 3.637   -17.806 1.00   49.62  ? 136 MET E CG  1 
ATOM   13016 S SD  . MET E  1 136 ? 148.300 5.385   -17.916 1.00   50.72  ? 136 MET E SD  1 
ATOM   13017 C CE  . MET E  1 136 ? 146.583 5.390   -18.288 1.00   46.74  ? 136 MET E CE  1 
ATOM   13018 N N   . VAL E  1 137 ? 147.421 3.368   -13.323 1.00   38.34  ? 137 VAL E N   1 
ATOM   13019 C CA  . VAL E  1 137 ? 146.580 2.834   -12.268 1.00   37.47  ? 137 VAL E CA  1 
ATOM   13020 C C   . VAL E  1 137 ? 145.167 3.362   -12.464 1.00   39.17  ? 137 VAL E C   1 
ATOM   13021 O O   . VAL E  1 137 ? 144.983 4.481   -12.963 1.00   39.10  ? 137 VAL E O   1 
ATOM   13022 C CB  . VAL E  1 137 ? 147.109 3.208   -10.880 1.00   33.81  ? 137 VAL E CB  1 
ATOM   13023 C CG1 . VAL E  1 137 ? 148.370 2.424   -10.584 1.00   35.12  ? 137 VAL E CG1 1 
ATOM   13024 C CG2 . VAL E  1 137 ? 147.385 4.694   -10.799 1.00   31.29  ? 137 VAL E CG2 1 
ATOM   13025 N N   . LYS E  1 138 ? 144.178 2.563   -12.056 1.00   40.15  ? 138 LYS E N   1 
ATOM   13026 C CA  . LYS E  1 138 ? 142.777 2.827   -12.391 1.00   38.72  ? 138 LYS E CA  1 
ATOM   13027 C C   . LYS E  1 138 ? 141.881 3.164   -11.208 1.00   35.90  ? 138 LYS E C   1 
ATOM   13028 O O   . LYS E  1 138 ? 142.045 2.622   -10.122 1.00   35.17  ? 138 LYS E O   1 
ATOM   13029 C CB  . LYS E  1 138 ? 142.192 1.616   -13.127 1.00   42.80  ? 138 LYS E CB  1 
ATOM   13030 C CG  . LYS E  1 138 ? 142.904 1.260   -14.424 1.00   47.59  ? 138 LYS E CG  1 
ATOM   13031 C CD  . LYS E  1 138 ? 142.290 0.031   -15.058 1.00   54.96  ? 138 LYS E CD  1 
ATOM   13032 C CE  . LYS E  1 138 ? 143.038 -0.369  -16.322 1.00   60.59  ? 138 LYS E CE  1 
ATOM   13033 N NZ  . LYS E  1 138 ? 144.256 -1.165  -15.996 1.00   63.85  ? 138 LYS E NZ  1 
ATOM   13034 N N   . VAL E  1 139 ? 140.932 4.070   -11.443 1.00   37.71  ? 139 VAL E N   1 
ATOM   13035 C CA  . VAL E  1 139 ? 139.753 4.250   -10.589 1.00   36.73  ? 139 VAL E CA  1 
ATOM   13036 C C   . VAL E  1 139 ? 138.547 3.708   -11.352 1.00   36.96  ? 139 VAL E C   1 
ATOM   13037 O O   . VAL E  1 139 ? 138.020 4.397   -12.227 1.00   39.94  ? 139 VAL E O   1 
ATOM   13038 C CB  . VAL E  1 139 ? 139.505 5.743   -10.228 1.00   28.02  ? 139 VAL E CB  1 
ATOM   13039 C CG1 . VAL E  1 139 ? 138.364 5.878   -9.226  1.00   27.06  ? 139 VAL E CG1 1 
ATOM   13040 C CG2 . VAL E  1 139 ? 140.766 6.397   -9.669  1.00   26.89  ? 139 VAL E CG2 1 
ATOM   13041 N N   . PRO E  1 140 ? 138.097 2.486   -11.021 1.00   37.26  ? 140 PRO E N   1 
ATOM   13042 C CA  . PRO E  1 140 ? 137.074 1.764   -11.788 1.00   37.83  ? 140 PRO E CA  1 
ATOM   13043 C C   . PRO E  1 140 ? 135.691 2.393   -11.704 1.00   40.37  ? 140 PRO E C   1 
ATOM   13044 O O   . PRO E  1 140 ? 134.878 2.154   -12.593 1.00   43.65  ? 140 PRO E O   1 
ATOM   13045 C CB  . PRO E  1 140 ? 137.059 0.378   -11.147 1.00   36.99  ? 140 PRO E CB  1 
ATOM   13046 C CG  . PRO E  1 140 ? 138.297 0.307   -10.353 1.00   37.47  ? 140 PRO E CG  1 
ATOM   13047 C CD  . PRO E  1 140 ? 138.587 1.681   -9.895  1.00   36.31  ? 140 PRO E CD  1 
ATOM   13048 N N   . GLN E  1 141 ? 135.449 3.182   -10.666 1.00   41.65  ? 141 GLN E N   1 
ATOM   13049 C CA  . GLN E  1 141 ? 134.174 3.859   -10.499 1.00   41.95  ? 141 GLN E CA  1 
ATOM   13050 C C   . GLN E  1 141 ? 134.364 5.370   -10.396 1.00   40.03  ? 141 GLN E C   1 
ATOM   13051 O O   . GLN E  1 141 ? 133.937 5.985   -9.423  1.00   40.01  ? 141 GLN E O   1 
ATOM   13052 C CB  . GLN E  1 141 ? 133.452 3.331   -9.257  1.00   44.16  ? 141 GLN E CB  1 
ATOM   13053 C CG  . GLN E  1 141 ? 133.031 1.875   -9.348  1.00   53.03  ? 141 GLN E CG  1 
ATOM   13054 C CD  . GLN E  1 141 ? 134.040 0.936   -8.721  1.00   62.82  ? 141 GLN E CD  1 
ATOM   13055 O OE1 . GLN E  1 141 ? 134.683 1.268   -7.726  1.00   63.89  ? 141 GLN E OE1 1 
ATOM   13056 N NE2 . GLN E  1 141 ? 134.186 -0.246  -9.303  1.00   68.30  ? 141 GLN E NE2 1 
ATOM   13057 N N   . PHE E  1 142 ? 135.004 5.971   -11.396 1.00   39.25  ? 142 PHE E N   1 
ATOM   13058 C CA  . PHE E  1 142 ? 135.194 7.432   -11.377 1.00   35.75  ? 142 PHE E CA  1 
ATOM   13059 C C   . PHE E  1 142 ? 133.882 8.174   -11.748 1.00   27.61  ? 142 PHE E C   1 
ATOM   13060 O O   . PHE E  1 142 ? 133.269 7.894   -12.770 1.00   26.67  ? 142 PHE E O   1 
ATOM   13061 C CB  . PHE E  1 142 ? 136.355 7.848   -12.315 1.00   31.29  ? 142 PHE E CB  1 
ATOM   13062 C CG  . PHE E  1 142 ? 136.707 9.320   -12.236 1.00   28.15  ? 142 PHE E CG  1 
ATOM   13063 C CD1 . PHE E  1 142 ? 137.510 9.809   -11.216 1.00   24.77  ? 142 PHE E CD1 1 
ATOM   13064 C CD2 . PHE E  1 142 ? 136.225 10.220  -13.180 1.00   28.81  ? 142 PHE E CD2 1 
ATOM   13065 C CE1 . PHE E  1 142 ? 137.827 11.168  -11.144 1.00   25.36  ? 142 PHE E CE1 1 
ATOM   13066 C CE2 . PHE E  1 142 ? 136.536 11.574  -13.108 1.00   25.53  ? 142 PHE E CE2 1 
ATOM   13067 C CZ  . PHE E  1 142 ? 137.337 12.047  -12.098 1.00   23.64  ? 142 PHE E CZ  1 
ATOM   13068 N N   . LEU E  1 143 ? 133.480 9.131   -10.910 1.00   27.43  ? 143 LEU E N   1 
ATOM   13069 C CA  . LEU E  1 143 ? 132.251 9.891   -11.138 1.00   29.32  ? 143 LEU E CA  1 
ATOM   13070 C C   . LEU E  1 143 ? 132.461 11.205  -11.892 1.00   32.13  ? 143 LEU E C   1 
ATOM   13071 O O   . LEU E  1 143 ? 133.350 12.012  -11.587 1.00   33.05  ? 143 LEU E O   1 
ATOM   13072 C CB  . LEU E  1 143 ? 131.553 10.174  -9.805  1.00   24.68  ? 143 LEU E CB  1 
ATOM   13073 C CG  . LEU E  1 143 ? 131.099 8.961   -9.001  1.00   25.15  ? 143 LEU E CG  1 
ATOM   13074 C CD1 . LEU E  1 143 ? 130.605 9.385   -7.627  1.00   25.21  ? 143 LEU E CD1 1 
ATOM   13075 C CD2 . LEU E  1 143 ? 130.007 8.225   -9.737  1.00   26.29  ? 143 LEU E CD2 1 
ATOM   13076 N N   . PHE E  1 144 ? 131.598 11.440  -12.862 1.00   31.23  ? 144 PHE E N   1 
ATOM   13077 C CA  . PHE E  1 144 ? 131.775 12.592  -13.703 1.00   31.67  ? 144 PHE E CA  1 
ATOM   13078 C C   . PHE E  1 144 ? 130.437 12.941  -14.312 1.00   33.11  ? 144 PHE E C   1 
ATOM   13079 O O   . PHE E  1 144 ? 129.450 12.305  -14.008 1.00   34.09  ? 144 PHE E O   1 
ATOM   13080 C CB  . PHE E  1 144 ? 132.840 12.304  -14.761 1.00   27.82  ? 144 PHE E CB  1 
ATOM   13081 C CG  . PHE E  1 144 ? 132.455 11.260  -15.760 1.00   30.19  ? 144 PHE E CG  1 
ATOM   13082 C CD1 . PHE E  1 144 ? 132.568 9.917   -15.461 1.00   31.33  ? 144 PHE E CD1 1 
ATOM   13083 C CD2 . PHE E  1 144 ? 132.052 11.617  -17.034 1.00   33.74  ? 144 PHE E CD2 1 
ATOM   13084 C CE1 . PHE E  1 144 ? 132.229 8.944   -16.396 1.00   32.71  ? 144 PHE E CE1 1 
ATOM   13085 C CE2 . PHE E  1 144 ? 131.714 10.646  -17.980 1.00   35.63  ? 144 PHE E CE2 1 
ATOM   13086 C CZ  . PHE E  1 144 ? 131.800 9.309   -17.661 1.00   35.03  ? 144 PHE E CZ  1 
ATOM   13087 N N   . SER E  1 145 ? 130.384 13.970  -15.140 1.00   33.68  ? 145 SER E N   1 
ATOM   13088 C CA  . SER E  1 145 ? 129.124 14.350  -15.735 1.00   33.84  ? 145 SER E CA  1 
ATOM   13089 C C   . SER E  1 145 ? 129.151 14.170  -17.228 1.00   32.78  ? 145 SER E C   1 
ATOM   13090 O O   . SER E  1 145 ? 130.094 14.568  -17.876 1.00   34.26  ? 145 SER E O   1 
ATOM   13091 C CB  . SER E  1 145 ? 128.789 15.793  -15.389 1.00   35.82  ? 145 SER E CB  1 
ATOM   13092 O OG  . SER E  1 145 ? 127.608 16.222  -16.053 1.00   39.52  ? 145 SER E OG  1 
ATOM   13093 N N   . CYS E  1 146 ? 128.115 13.558  -17.771 1.00   32.57  ? 146 CYS E N   1 
ATOM   13094 C CA  . CYS E  1 146 ? 127.906 13.591  -19.202 1.00   32.91  ? 146 CYS E CA  1 
ATOM   13095 C C   . CYS E  1 146 ? 127.148 14.876  -19.442 1.00   35.89  ? 146 CYS E C   1 
ATOM   13096 O O   . CYS E  1 146 ? 125.947 14.947  -19.181 1.00   38.79  ? 146 CYS E O   1 
ATOM   13097 C CB  . CYS E  1 146 ? 127.107 12.380  -19.679 1.00   34.59  ? 146 CYS E CB  1 
ATOM   13098 S SG  . CYS E  1 146 ? 128.031 10.841  -19.809 1.00   42.30  ? 146 CYS E SG  1 
ATOM   13099 N N   . ALA E  1 147 ? 127.842 15.893  -19.931 1.00   36.93  ? 147 ALA E N   1 
ATOM   13100 C CA  . ALA E  1 147 ? 127.275 17.230  -20.048 1.00   36.36  ? 147 ALA E CA  1 
ATOM   13101 C C   . ALA E  1 147 ? 126.575 17.381  -21.377 1.00   42.26  ? 147 ALA E C   1 
ATOM   13102 O O   . ALA E  1 147 ? 126.868 16.632  -22.315 1.00   45.01  ? 147 ALA E O   1 
ATOM   13103 C CB  . ALA E  1 147 ? 128.355 18.268  -19.907 1.00   35.27  ? 147 ALA E CB  1 
ATOM   13104 N N   . PRO E  1 148 ? 125.635 18.345  -21.468 1.00   44.52  ? 148 PRO E N   1 
ATOM   13105 C CA  . PRO E  1 148 ? 124.974 18.623  -22.757 1.00   47.37  ? 148 PRO E CA  1 
ATOM   13106 C C   . PRO E  1 148 ? 125.973 19.052  -23.844 1.00   52.09  ? 148 PRO E C   1 
ATOM   13107 O O   . PRO E  1 148 ? 126.952 19.730  -23.528 1.00   53.31  ? 148 PRO E O   1 
ATOM   13108 C CB  . PRO E  1 148 ? 123.977 19.741  -22.410 1.00   45.56  ? 148 PRO E CB  1 
ATOM   13109 C CG  . PRO E  1 148 ? 124.397 20.264  -21.045 1.00   43.54  ? 148 PRO E CG  1 
ATOM   13110 C CD  . PRO E  1 148 ? 125.048 19.121  -20.355 1.00   42.83  ? 148 PRO E CD  1 
ATOM   13111 N N   . SER E  1 149 ? 125.760 18.614  -25.086 1.00   56.84  ? 149 SER E N   1 
ATOM   13112 C CA  . SER E  1 149 ? 126.721 18.809  -26.183 1.00   61.07  ? 149 SER E CA  1 
ATOM   13113 C C   . SER E  1 149 ? 127.111 20.285  -26.452 1.00   64.87  ? 149 SER E C   1 
ATOM   13114 O O   . SER E  1 149 ? 128.255 20.578  -26.835 1.00   64.91  ? 149 SER E O   1 
ATOM   13115 C CB  . SER E  1 149 ? 126.182 18.153  -27.470 1.00   64.71  ? 149 SER E CB  1 
ATOM   13116 O OG  . SER E  1 149 ? 125.073 18.836  -28.008 1.00   67.96  ? 149 SER E OG  1 
ATOM   13117 N N   . PHE E  1 150 ? 126.163 21.201  -26.247 1.00   63.16  ? 150 PHE E N   1 
ATOM   13118 C CA  . PHE E  1 150 ? 126.378 22.613  -26.545 1.00   61.20  ? 150 PHE E CA  1 
ATOM   13119 C C   . PHE E  1 150 ? 127.508 23.197  -25.725 1.00   59.78  ? 150 PHE E C   1 
ATOM   13120 O O   . PHE E  1 150 ? 128.143 24.163  -26.129 1.00   64.03  ? 150 PHE E O   1 
ATOM   13121 C CB  . PHE E  1 150 ? 125.092 23.413  -26.295 1.00   60.40  ? 150 PHE E CB  1 
ATOM   13122 C CG  . PHE E  1 150 ? 124.828 23.741  -24.842 1.00   57.54  ? 150 PHE E CG  1 
ATOM   13123 C CD1 . PHE E  1 150 ? 125.332 24.895  -24.258 1.00   58.44  ? 150 PHE E CD1 1 
ATOM   13124 C CD2 . PHE E  1 150 ? 124.041 22.911  -24.069 1.00   53.90  ? 150 PHE E CD2 1 
ATOM   13125 C CE1 . PHE E  1 150 ? 125.078 25.193  -22.922 1.00   55.90  ? 150 PHE E CE1 1 
ATOM   13126 C CE2 . PHE E  1 150 ? 123.781 23.211  -22.730 1.00   51.65  ? 150 PHE E CE2 1 
ATOM   13127 C CZ  . PHE E  1 150 ? 124.303 24.349  -22.163 1.00   52.64  ? 150 PHE E CZ  1 
ATOM   13128 N N   . LEU E  1 151 ? 127.781 22.576  -24.590 1.00   54.86  ? 151 LEU E N   1 
ATOM   13129 C CA  . LEU E  1 151 ? 128.626 23.162  -23.564 1.00   52.81  ? 151 LEU E CA  1 
ATOM   13130 C C   . LEU E  1 151 ? 130.078 23.279  -24.012 1.00   51.44  ? 151 LEU E C   1 
ATOM   13131 O O   . LEU E  1 151 ? 130.777 24.196  -23.610 1.00   50.99  ? 151 LEU E O   1 
ATOM   13132 C CB  . LEU E  1 151 ? 128.514 22.330  -22.281 1.00   49.29  ? 151 LEU E CB  1 
ATOM   13133 C CG  . LEU E  1 151 ? 128.903 23.004  -20.976 1.00   46.66  ? 151 LEU E CG  1 
ATOM   13134 C CD1 . LEU E  1 151 ? 128.085 24.268  -20.793 1.00   50.51  ? 151 LEU E CD1 1 
ATOM   13135 C CD2 . LEU E  1 151 ? 128.615 22.069  -19.870 1.00   42.97  ? 151 LEU E CD2 1 
ATOM   13136 N N   . ALA E  1 152 ? 130.523 22.368  -24.867 1.00   52.96  ? 152 ALA E N   1 
ATOM   13137 C CA  . ALA E  1 152 ? 131.904 22.389  -25.342 1.00   55.03  ? 152 ALA E CA  1 
ATOM   13138 C C   . ALA E  1 152 ? 132.043 22.999  -26.747 1.00   61.65  ? 152 ALA E C   1 
ATOM   13139 O O   . ALA E  1 152 ? 133.123 23.026  -27.323 1.00   64.52  ? 152 ALA E O   1 
ATOM   13140 C CB  . ALA E  1 152 ? 132.478 20.987  -25.321 1.00   51.51  ? 152 ALA E CB  1 
ATOM   13141 N N   . GLN E  1 153 ? 130.944 23.510  -27.283 1.00   65.40  ? 153 GLN E N   1 
ATOM   13142 C CA  . GLN E  1 153 ? 130.882 23.929  -28.682 1.00   67.28  ? 153 GLN E CA  1 
ATOM   13143 C C   . GLN E  1 153 ? 131.537 25.310  -28.898 1.00   66.61  ? 153 GLN E C   1 
ATOM   13144 O O   . GLN E  1 153 ? 131.799 25.707  -30.039 1.00   69.56  ? 153 GLN E O   1 
ATOM   13145 C CB  . GLN E  1 153 ? 129.406 23.878  -29.120 1.00   71.83  ? 153 GLN E CB  1 
ATOM   13146 C CG  . GLN E  1 153 ? 128.863 25.006  -29.927 1.00   80.70  ? 153 GLN E CG  1 
ATOM   13147 C CD  . GLN E  1 153 ? 127.371 25.214  -29.704 1.00   87.29  ? 153 GLN E CD  1 
ATOM   13148 O OE1 . GLN E  1 153 ? 126.559 24.306  -29.892 1.00   87.66  ? 153 GLN E OE1 1 
ATOM   13149 N NE2 . GLN E  1 153 ? 127.005 26.432  -29.309 1.00   91.74  ? 153 GLN E NE2 1 
ATOM   13150 N N   . LYS E  1 154 ? 131.825 26.011  -27.793 1.00   64.38  ? 154 LYS E N   1 
ATOM   13151 C CA  . LYS E  1 154 ? 132.467 27.352  -27.782 1.00   66.44  ? 154 LYS E CA  1 
ATOM   13152 C C   . LYS E  1 154 ? 133.586 27.586  -26.728 1.00   68.57  ? 154 LYS E C   1 
ATOM   13153 O O   . LYS E  1 154 ? 133.424 27.261  -25.548 1.00   68.11  ? 154 LYS E O   1 
ATOM   13154 C CB  . LYS E  1 154 ? 131.419 28.466  -27.585 1.00   70.24  ? 154 LYS E CB  1 
ATOM   13155 C CG  . LYS E  1 154 ? 130.803 29.091  -28.847 1.00   76.87  ? 154 LYS E CG  1 
ATOM   13156 C CD  . LYS E  1 154 ? 129.939 28.174  -29.657 1.00   80.56  ? 154 LYS E CD  1 
ATOM   13157 C CE  . LYS E  1 154 ? 129.367 28.855  -30.888 1.00   85.36  ? 154 LYS E CE  1 
ATOM   13158 N NZ  . LYS E  1 154 ? 128.522 27.905  -31.660 1.00   86.01  ? 154 LYS E NZ  1 
ATOM   13159 N N   . GLY E  1 155 ? 134.701 28.185  -27.163 1.00   66.72  ? 155 GLY E N   1 
ATOM   13160 C CA  . GLY E  1 155 ? 135.729 28.692  -26.257 1.00   63.74  ? 155 GLY E CA  1 
ATOM   13161 C C   . GLY E  1 155 ? 136.928 27.807  -25.900 1.00   59.39  ? 155 GLY E C   1 
ATOM   13162 O O   . GLY E  1 155 ? 137.935 28.290  -25.374 1.00   57.25  ? 155 GLY E O   1 
ATOM   13163 N N   . LEU E  1 156 ? 136.831 26.517  -26.196 1.00   57.44  ? 156 LEU E N   1 
ATOM   13164 C CA  . LEU E  1 156 ? 137.831 25.545  -25.760 1.00   53.80  ? 156 LEU E CA  1 
ATOM   13165 C C   . LEU E  1 156 ? 138.853 25.297  -26.867 1.00   52.96  ? 156 LEU E C   1 
ATOM   13166 O O   . LEU E  1 156 ? 138.576 25.623  -28.024 1.00   58.02  ? 156 LEU E O   1 
ATOM   13167 C CB  . LEU E  1 156 ? 137.129 24.235  -25.376 1.00   51.39  ? 156 LEU E CB  1 
ATOM   13168 C CG  . LEU E  1 156 ? 135.890 24.381  -24.494 1.00   48.16  ? 156 LEU E CG  1 
ATOM   13169 C CD1 . LEU E  1 156 ? 135.320 23.022  -24.110 1.00   45.41  ? 156 LEU E CD1 1 
ATOM   13170 C CD2 . LEU E  1 156 ? 136.197 25.212  -23.261 1.00   47.73  ? 156 LEU E CD2 1 
ATOM   13171 N N   . PRO E  1 157 ? 140.038 24.739  -26.524 1.00   46.84  ? 157 PRO E N   1 
ATOM   13172 C CA  . PRO E  1 157 ? 140.940 24.336  -27.611 1.00   49.32  ? 157 PRO E CA  1 
ATOM   13173 C C   . PRO E  1 157 ? 140.217 23.360  -28.538 1.00   55.63  ? 157 PRO E C   1 
ATOM   13174 O O   . PRO E  1 157 ? 139.274 22.682  -28.099 1.00   55.46  ? 157 PRO E O   1 
ATOM   13175 C CB  . PRO E  1 157 ? 142.105 23.673  -26.878 1.00   44.17  ? 157 PRO E CB  1 
ATOM   13176 C CG  . PRO E  1 157 ? 142.103 24.312  -25.529 1.00   39.21  ? 157 PRO E CG  1 
ATOM   13177 C CD  . PRO E  1 157 ? 140.659 24.561  -25.199 1.00   40.28  ? 157 PRO E CD  1 
ATOM   13178 N N   . ASN E  1 158 ? 140.635 23.277  -29.794 1.00   61.63  ? 158 ASN E N   1 
ATOM   13179 C CA  . ASN E  1 158 ? 139.828 22.524  -30.741 1.00   66.36  ? 158 ASN E CA  1 
ATOM   13180 C C   . ASN E  1 158 ? 139.828 21.055  -30.382 1.00   63.45  ? 158 ASN E C   1 
ATOM   13181 O O   . ASN E  1 158 ? 140.837 20.495  -29.930 1.00   56.54  ? 158 ASN E O   1 
ATOM   13182 C CB  . ASN E  1 158 ? 140.279 22.754  -32.191 1.00   73.77  ? 158 ASN E CB  1 
ATOM   13183 C CG  . ASN E  1 158 ? 141.675 22.274  -32.452 1.00   78.62  ? 158 ASN E CG  1 
ATOM   13184 O OD1 . ASN E  1 158 ? 142.588 22.545  -31.674 1.00   82.23  ? 158 ASN E OD1 1 
ATOM   13185 N ND2 . ASN E  1 158 ? 141.866 21.584  -33.570 1.00   79.99  ? 158 ASN E ND2 1 
ATOM   13186 N N   . ASN E  1 159 ? 138.634 20.487  -30.504 1.00   69.65  ? 159 ASN E N   1 
ATOM   13187 C CA  . ASN E  1 159 ? 138.358 19.077  -30.259 1.00   72.21  ? 159 ASN E CA  1 
ATOM   13188 C C   . ASN E  1 159 ? 138.415 18.680  -28.789 1.00   62.82  ? 159 ASN E C   1 
ATOM   13189 O O   . ASN E  1 159 ? 138.261 17.512  -28.462 1.00   62.28  ? 159 ASN E O   1 
ATOM   13190 C CB  . ASN E  1 159 ? 139.299 18.197  -31.085 1.00   79.63  ? 159 ASN E CB  1 
ATOM   13191 C CG  . ASN E  1 159 ? 138.897 18.139  -32.558 1.00   87.28  ? 159 ASN E CG  1 
ATOM   13192 O OD1 . ASN E  1 159 ? 138.450 17.103  -33.056 1.00   89.79  ? 159 ASN E OD1 1 
ATOM   13193 N ND2 . ASN E  1 159 ? 139.060 19.260  -33.260 1.00   89.94  ? 159 ASN E ND2 1 
ATOM   13194 N N   . VAL E  1 160 ? 138.646 19.637  -27.903 1.00   55.94  ? 160 VAL E N   1 
ATOM   13195 C CA  . VAL E  1 160 ? 138.582 19.318  -26.484 1.00   49.63  ? 160 VAL E CA  1 
ATOM   13196 C C   . VAL E  1 160 ? 137.094 19.187  -26.222 1.00   49.11  ? 160 VAL E C   1 
ATOM   13197 O O   . VAL E  1 160 ? 136.313 19.992  -26.727 1.00   49.84  ? 160 VAL E O   1 
ATOM   13198 C CB  . VAL E  1 160 ? 139.257 20.384  -25.587 1.00   43.91  ? 160 VAL E CB  1 
ATOM   13199 C CG1 . VAL E  1 160 ? 138.791 20.265  -24.181 1.00   39.57  ? 160 VAL E CG1 1 
ATOM   13200 C CG2 . VAL E  1 160 ? 140.760 20.219  -25.631 1.00   40.77  ? 160 VAL E CG2 1 
ATOM   13201 N N   . GLN E  1 161 ? 136.701 18.140  -25.493 1.00   48.46  ? 161 GLN E N   1 
ATOM   13202 C CA  . GLN E  1 161 ? 135.304 17.751  -25.432 1.00   47.53  ? 161 GLN E CA  1 
ATOM   13203 C C   . GLN E  1 161 ? 134.767 17.844  -24.014 1.00   44.79  ? 161 GLN E C   1 
ATOM   13204 O O   . GLN E  1 161 ? 133.761 17.221  -23.694 1.00   43.60  ? 161 GLN E O   1 
ATOM   13205 C CB  . GLN E  1 161 ? 135.109 16.318  -25.944 1.00   50.46  ? 161 GLN E CB  1 
ATOM   13206 C CG  . GLN E  1 161 ? 135.296 16.114  -27.461 1.00   57.91  ? 161 GLN E CG  1 
ATOM   13207 C CD  . GLN E  1 161 ? 134.219 16.767  -28.329 1.00   64.45  ? 161 GLN E CD  1 
ATOM   13208 O OE1 . GLN E  1 161 ? 133.044 16.428  -28.240 1.00   67.07  ? 161 GLN E OE1 1 
ATOM   13209 N NE2 . GLN E  1 161 ? 134.642 17.659  -29.231 1.00   67.02  ? 161 GLN E NE2 1 
ATOM   13210 N N   . GLY E  1 162 ? 135.436 18.608  -23.157 1.00   41.35  ? 162 GLY E N   1 
ATOM   13211 C CA  . GLY E  1 162 ? 134.990 18.750  -21.782 1.00   37.30  ? 162 GLY E CA  1 
ATOM   13212 C C   . GLY E  1 162 ? 136.073 19.385  -20.957 1.00   33.63  ? 162 GLY E C   1 
ATOM   13213 O O   . GLY E  1 162 ? 136.984 19.954  -21.530 1.00   32.69  ? 162 GLY E O   1 
ATOM   13214 N N   . ALA E  1 163 ? 135.983 19.296  -19.634 1.00   32.58  ? 163 ALA E N   1 
ATOM   13215 C CA  . ALA E  1 163 ? 136.975 19.901  -18.737 1.00   31.10  ? 163 ALA E CA  1 
ATOM   13216 C C   . ALA E  1 163 ? 137.200 19.015  -17.529 1.00   31.55  ? 163 ALA E C   1 
ATOM   13217 O O   . ALA E  1 163 ? 136.295 18.287  -17.116 1.00   32.69  ? 163 ALA E O   1 
ATOM   13218 C CB  . ALA E  1 163 ? 136.542 21.282  -18.293 1.00   31.73  ? 163 ALA E CB  1 
ATOM   13219 N N   . LEU E  1 164 ? 138.410 19.056  -16.976 1.00   30.23  ? 164 LEU E N   1 
ATOM   13220 C CA  . LEU E  1 164 ? 138.687 18.377  -15.724 1.00   28.65  ? 164 LEU E CA  1 
ATOM   13221 C C   . LEU E  1 164 ? 138.821 19.416  -14.645 1.00   29.41  ? 164 LEU E C   1 
ATOM   13222 O O   . LEU E  1 164 ? 139.524 20.397  -14.806 1.00   32.47  ? 164 LEU E O   1 
ATOM   13223 C CB  . LEU E  1 164 ? 139.939 17.501  -15.835 1.00   31.07  ? 164 LEU E CB  1 
ATOM   13224 C CG  . LEU E  1 164 ? 141.231 18.225  -16.179 1.00   38.33  ? 164 LEU E CG  1 
ATOM   13225 C CD1 . LEU E  1 164 ? 142.168 18.258  -14.997 1.00   40.31  ? 164 LEU E CD1 1 
ATOM   13226 C CD2 . LEU E  1 164 ? 141.898 17.630  -17.404 1.00   41.93  ? 164 LEU E CD2 1 
ATOM   13227 N N   . GLY E  1 165 ? 138.090 19.220  -13.562 1.00   29.29  ? 165 GLY E N   1 
ATOM   13228 C CA  . GLY E  1 165 ? 138.039 20.202  -12.505 1.00   29.32  ? 165 GLY E CA  1 
ATOM   13229 C C   . GLY E  1 165 ? 138.849 19.778  -11.309 1.00   28.66  ? 165 GLY E C   1 
ATOM   13230 O O   . GLY E  1 165 ? 138.803 18.619  -10.902 1.00   30.77  ? 165 GLY E O   1 
ATOM   13231 N N   . LEU E  1 166 ? 139.605 20.718  -10.753 1.00   27.70  ? 166 LEU E N   1 
ATOM   13232 C CA  . LEU E  1 166 ? 140.423 20.453  -9.578  1.00   27.95  ? 166 LEU E CA  1 
ATOM   13233 C C   . LEU E  1 166 ? 140.000 21.326  -8.397  1.00   28.96  ? 166 LEU E C   1 
ATOM   13234 O O   . LEU E  1 166 ? 140.780 21.583  -7.491  1.00   30.61  ? 166 LEU E O   1 
ATOM   13235 C CB  . LEU E  1 166 ? 141.901 20.662  -9.893  1.00   27.47  ? 166 LEU E CB  1 
ATOM   13236 C CG  . LEU E  1 166 ? 142.550 19.778  -10.957 1.00   31.99  ? 166 LEU E CG  1 
ATOM   13237 C CD1 . LEU E  1 166 ? 143.935 20.260  -11.162 1.00   36.20  ? 166 LEU E CD1 1 
ATOM   13238 C CD2 . LEU E  1 166 ? 142.618 18.354  -10.522 1.00   32.44  ? 166 LEU E CD2 1 
ATOM   13239 N N   . GLY E  1 167 ? 138.753 21.766  -8.400  1.00   28.07  ? 167 GLY E N   1 
ATOM   13240 C CA  . GLY E  1 167 ? 138.291 22.683  -7.388  1.00   29.41  ? 167 GLY E CA  1 
ATOM   13241 C C   . GLY E  1 167 ? 138.106 21.974  -6.071  1.00   30.67  ? 167 GLY E C   1 
ATOM   13242 O O   . GLY E  1 167 ? 138.356 20.767  -5.956  1.00   31.79  ? 167 GLY E O   1 
ATOM   13243 N N   . GLN E  1 168 ? 137.765 22.751  -5.050  1.00   32.70  ? 168 GLN E N   1 
ATOM   13244 C CA  . GLN E  1 168 ? 137.421 22.226  -3.733  1.00   34.51  ? 168 GLN E CA  1 
ATOM   13245 C C   . GLN E  1 168 ? 135.962 21.792  -3.711  1.00   36.39  ? 168 GLN E C   1 
ATOM   13246 O O   . GLN E  1 168 ? 135.074 22.581  -3.408  1.00   39.72  ? 168 GLN E O   1 
ATOM   13247 C CB  . GLN E  1 168 ? 137.678 23.268  -2.663  1.00   36.61  ? 168 GLN E CB  1 
ATOM   13248 C CG  . GLN E  1 168 ? 139.122 23.436  -2.373  1.00   37.36  ? 168 GLN E CG  1 
ATOM   13249 C CD  . GLN E  1 168 ? 139.666 22.168  -1.821  1.00   42.12  ? 168 GLN E CD  1 
ATOM   13250 O OE1 . GLN E  1 168 ? 139.267 21.739  -0.745  1.00   45.84  ? 168 GLN E OE1 1 
ATOM   13251 N NE2 . GLN E  1 168 ? 140.548 21.523  -2.568  1.00   43.99  ? 168 GLN E NE2 1 
ATOM   13252 N N   . ALA E  1 169 ? 135.710 20.555  -4.109  1.00   33.46  ? 169 ALA E N   1 
ATOM   13253 C CA  . ALA E  1 169 ? 134.353 20.085  -4.260  1.00   29.63  ? 169 ALA E CA  1 
ATOM   13254 C C   . ALA E  1 169 ? 134.402 18.569  -4.227  1.00   26.16  ? 169 ALA E C   1 
ATOM   13255 O O   . ALA E  1 169 ? 135.400 17.993  -4.611  1.00   27.98  ? 169 ALA E O   1 
ATOM   13256 C CB  . ALA E  1 169 ? 133.758 20.613  -5.563  1.00   30.07  ? 169 ALA E CB  1 
ATOM   13257 N N   . PRO E  1 170 ? 133.323 17.920  -3.785  1.00   28.28  ? 170 PRO E N   1 
ATOM   13258 C CA  . PRO E  1 170 ? 133.398 16.497  -3.445  1.00   29.88  ? 170 PRO E CA  1 
ATOM   13259 C C   . PRO E  1 170 ? 133.754 15.511  -4.565  1.00   30.08  ? 170 PRO E C   1 
ATOM   13260 O O   . PRO E  1 170 ? 134.380 14.501  -4.244  1.00   27.59  ? 170 PRO E O   1 
ATOM   13261 C CB  . PRO E  1 170 ? 131.990 16.202  -2.899  1.00   32.14  ? 170 PRO E CB  1 
ATOM   13262 C CG  . PRO E  1 170 ? 131.138 17.313  -3.357  1.00   31.95  ? 170 PRO E CG  1 
ATOM   13263 C CD  . PRO E  1 170 ? 132.030 18.498  -3.387  1.00   29.02  ? 170 PRO E CD  1 
ATOM   13264 N N   . ILE E  1 171 ? 133.405 15.749  -5.824  1.00   31.06  ? 171 ILE E N   1 
ATOM   13265 C CA  . ILE E  1 171 ? 133.872 14.786  -6.818  1.00   28.18  ? 171 ILE E CA  1 
ATOM   13266 C C   . ILE E  1 171 ? 134.850 15.414  -7.815  1.00   30.39  ? 171 ILE E C   1 
ATOM   13267 O O   . ILE E  1 171 ? 134.916 15.014  -8.982  1.00   31.66  ? 171 ILE E O   1 
ATOM   13268 C CB  . ILE E  1 171 ? 132.685 14.086  -7.563  1.00   23.60  ? 171 ILE E CB  1 
ATOM   13269 C CG1 . ILE E  1 171 ? 131.761 15.056  -8.267  1.00   25.89  ? 171 ILE E CG1 1 
ATOM   13270 C CG2 . ILE E  1 171 ? 131.862 13.267  -6.595  1.00   23.08  ? 171 ILE E CG2 1 
ATOM   13271 C CD1 . ILE E  1 171 ? 130.953 14.376  -9.336  1.00   27.61  ? 171 ILE E CD1 1 
ATOM   13272 N N   . SER E  1 172 ? 135.647 16.364  -7.331  1.00   27.73  ? 172 SER E N   1 
ATOM   13273 C CA  . SER E  1 172 ? 136.729 16.912  -8.130  1.00   28.32  ? 172 SER E CA  1 
ATOM   13274 C C   . SER E  1 172 ? 137.731 15.804  -8.412  1.00   29.97  ? 172 SER E C   1 
ATOM   13275 O O   . SER E  1 172 ? 137.738 14.806  -7.725  1.00   32.19  ? 172 SER E O   1 
ATOM   13276 C CB  . SER E  1 172 ? 137.386 18.092  -7.429  1.00   28.32  ? 172 SER E CB  1 
ATOM   13277 O OG  . SER E  1 172 ? 137.963 17.703  -6.203  1.00   32.45  ? 172 SER E OG  1 
ATOM   13278 N N   . LEU E  1 173 ? 138.574 15.979  -9.420  1.00   28.89  ? 173 LEU E N   1 
ATOM   13279 C CA  . LEU E  1 173 ? 139.504 14.943  -9.794  1.00   27.80  ? 173 LEU E CA  1 
ATOM   13280 C C   . LEU E  1 173 ? 140.464 14.614  -8.668  1.00   29.94  ? 173 LEU E C   1 
ATOM   13281 O O   . LEU E  1 173 ? 140.616 13.457  -8.317  1.00   29.61  ? 173 LEU E O   1 
ATOM   13282 C CB  . LEU E  1 173 ? 140.273 15.348  -11.039 1.00   28.04  ? 173 LEU E CB  1 
ATOM   13283 C CG  . LEU E  1 173 ? 141.490 14.497  -11.409 1.00   29.65  ? 173 LEU E CG  1 
ATOM   13284 C CD1 . LEU E  1 173 ? 141.138 13.094  -11.726 1.00   29.18  ? 173 LEU E CD1 1 
ATOM   13285 C CD2 . LEU E  1 173 ? 142.142 15.105  -12.606 1.00   32.55  ? 173 LEU E CD2 1 
ATOM   13286 N N   . GLN E  1 174 ? 141.085 15.613  -8.067  1.00   32.16  ? 174 GLN E N   1 
ATOM   13287 C CA  . GLN E  1 174 ? 142.069 15.312  -7.037  1.00   32.12  ? 174 GLN E CA  1 
ATOM   13288 C C   . GLN E  1 174 ? 141.387 14.683  -5.819  1.00   32.64  ? 174 GLN E C   1 
ATOM   13289 O O   . GLN E  1 174 ? 141.944 13.769  -5.225  1.00   35.08  ? 174 GLN E O   1 
ATOM   13290 C CB  . GLN E  1 174 ? 142.869 16.570  -6.643  1.00   30.26  ? 174 GLN E CB  1 
ATOM   13291 C CG  . GLN E  1 174 ? 142.214 17.494  -5.621  1.00   29.40  ? 174 GLN E CG  1 
ATOM   13292 C CD  . GLN E  1 174 ? 141.150 18.347  -6.241  1.00   27.67  ? 174 GLN E CD  1 
ATOM   13293 O OE1 . GLN E  1 174 ? 140.942 18.290  -7.444  1.00   29.26  ? 174 GLN E OE1 1 
ATOM   13294 N NE2 . GLN E  1 174 ? 140.432 19.098  -5.428  1.00   27.40  ? 174 GLN E NE2 1 
ATOM   13295 N N   . ASN E  1 175 ? 140.186 15.136  -5.453  1.00   29.53  ? 175 ASN E N   1 
ATOM   13296 C CA  . ASN E  1 175 ? 139.512 14.580  -4.283  1.00   29.36  ? 175 ASN E CA  1 
ATOM   13297 C C   . ASN E  1 175 ? 139.241 13.088  -4.510  1.00   29.89  ? 175 ASN E C   1 
ATOM   13298 O O   . ASN E  1 175 ? 139.312 12.276  -3.587  1.00   30.52  ? 175 ASN E O   1 
ATOM   13299 C CB  A ASN E  1 175 ? 138.241 15.383  -3.930  0.70   30.09  ? 175 ASN E CB  1 
ATOM   13300 C CB  B ASN E  1 175 ? 138.199 15.324  -4.012  0.30   30.26  ? 175 ASN E CB  1 
ATOM   13301 C CG  A ASN E  1 175 ? 138.570 16.705  -3.201  0.70   30.27  ? 175 ASN E CG  1 
ATOM   13302 C CG  B ASN E  1 175 ? 137.484 14.828  -2.771  0.30   30.83  ? 175 ASN E CG  1 
ATOM   13303 O OD1 A ASN E  1 175 ? 139.580 16.792  -2.495  0.70   30.84  ? 175 ASN E OD1 1 
ATOM   13304 O OD1 B ASN E  1 175 ? 136.840 13.781  -2.782  0.30   29.84  ? 175 ASN E OD1 1 
ATOM   13305 N ND2 A ASN E  1 175 ? 137.742 17.737  -3.393  0.70   27.93  ? 175 ASN E ND2 1 
ATOM   13306 N ND2 B ASN E  1 175 ? 137.578 15.594  -1.695  0.30   33.58  ? 175 ASN E ND2 1 
ATOM   13307 N N   . GLN E  1 176 ? 138.946 12.711  -5.744  1.00   29.76  ? 176 GLN E N   1 
ATOM   13308 C CA  . GLN E  1 176 ? 138.695 11.306  -6.019  1.00   30.42  ? 176 GLN E CA  1 
ATOM   13309 C C   . GLN E  1 176 ? 139.978 10.484  -6.066  1.00   28.84  ? 176 GLN E C   1 
ATOM   13310 O O   . GLN E  1 176 ? 139.980 9.333   -5.627  1.00   29.30  ? 176 GLN E O   1 
ATOM   13311 C CB  . GLN E  1 176 ? 137.913 11.126  -7.327  1.00   30.74  ? 176 GLN E CB  1 
ATOM   13312 C CG  . GLN E  1 176 ? 136.455 11.586  -7.225  1.00   28.36  ? 176 GLN E CG  1 
ATOM   13313 C CD  . GLN E  1 176 ? 135.606 11.150  -8.397  1.00   29.44  ? 176 GLN E CD  1 
ATOM   13314 O OE1 . GLN E  1 176 ? 135.252 9.971   -8.517  1.00   30.80  ? 176 GLN E OE1 1 
ATOM   13315 N NE2 . GLN E  1 176 ? 135.235 12.101  -9.252  1.00   29.12  ? 176 GLN E NE2 1 
ATOM   13316 N N   . LEU E  1 177 ? 141.061 11.060  -6.578  1.00   23.88  ? 177 LEU E N   1 
ATOM   13317 C CA  . LEU E  1 177 ? 142.349 10.364  -6.590  1.00   24.83  ? 177 LEU E CA  1 
ATOM   13318 C C   . LEU E  1 177 ? 142.885 10.179  -5.180  1.00   25.52  ? 177 LEU E C   1 
ATOM   13319 O O   . LEU E  1 177 ? 143.392 9.119   -4.834  1.00   27.55  ? 177 LEU E O   1 
ATOM   13320 C CB  . LEU E  1 177 ? 143.356 11.122  -7.438  1.00   25.07  ? 177 LEU E CB  1 
ATOM   13321 C CG  . LEU E  1 177 ? 143.025 11.187  -8.924  1.00   22.32  ? 177 LEU E CG  1 
ATOM   13322 C CD1 . LEU E  1 177 ? 144.003 12.102  -9.564  1.00   23.62  ? 177 LEU E CD1 1 
ATOM   13323 C CD2 . LEU E  1 177 ? 143.100 9.823   -9.596  1.00   23.28  ? 177 LEU E CD2 1 
ATOM   13324 N N   . PHE E  1 178 ? 142.788 11.228  -4.376  1.00   26.32  ? 178 PHE E N   1 
ATOM   13325 C CA  . PHE E  1 178 ? 143.178 11.172  -2.982  1.00   25.41  ? 178 PHE E CA  1 
ATOM   13326 C C   . PHE E  1 178 ? 142.495 10.028  -2.258  1.00   25.63  ? 178 PHE E C   1 
ATOM   13327 O O   . PHE E  1 178 ? 143.111 9.253   -1.526  1.00   29.40  ? 178 PHE E O   1 
ATOM   13328 C CB  . PHE E  1 178 ? 142.805 12.476  -2.264  1.00   27.37  ? 178 PHE E CB  1 
ATOM   13329 C CG  . PHE E  1 178 ? 143.581 13.694  -2.702  1.00   28.20  ? 178 PHE E CG  1 
ATOM   13330 C CD1 . PHE E  1 178 ? 144.817 13.588  -3.305  1.00   30.46  ? 178 PHE E CD1 1 
ATOM   13331 C CD2 . PHE E  1 178 ? 143.053 14.962  -2.479  1.00   27.69  ? 178 PHE E CD2 1 
ATOM   13332 C CE1 . PHE E  1 178 ? 145.492 14.724  -3.683  1.00   29.25  ? 178 PHE E CE1 1 
ATOM   13333 C CE2 . PHE E  1 178 ? 143.723 16.088  -2.841  1.00   26.95  ? 178 PHE E CE2 1 
ATOM   13334 C CZ  . PHE E  1 178 ? 144.947 15.972  -3.443  1.00   28.05  ? 178 PHE E CZ  1 
ATOM   13335 N N   . SER E  1 179 ? 141.191 9.952   -2.421  1.00   26.66  ? 179 SER E N   1 
ATOM   13336 C CA  . SER E  1 179 ? 140.419 9.050   -1.595  1.00   32.56  ? 179 SER E CA  1 
ATOM   13337 C C   . SER E  1 179 ? 140.561 7.602   -2.084  1.00   28.39  ? 179 SER E C   1 
ATOM   13338 O O   . SER E  1 179 ? 140.616 6.675   -1.293  1.00   27.85  ? 179 SER E O   1 
ATOM   13339 C CB  . SER E  1 179 ? 138.940 9.491   -1.561  1.00   39.00  ? 179 SER E CB  1 
ATOM   13340 O OG  . SER E  1 179 ? 138.262 9.160   -2.757  1.00   42.79  ? 179 SER E OG  1 
ATOM   13341 N N   . HIS E  1 180 ? 140.670 7.400   -3.384  1.00   26.64  ? 180 HIS E N   1 
ATOM   13342 C CA  . HIS E  1 180 ? 140.782 6.040   -3.869  1.00   29.79  ? 180 HIS E CA  1 
ATOM   13343 C C   . HIS E  1 180 ? 142.139 5.427   -3.481  1.00   29.97  ? 180 HIS E C   1 
ATOM   13344 O O   . HIS E  1 180 ? 142.217 4.257   -3.147  1.00   30.40  ? 180 HIS E O   1 
ATOM   13345 C CB  . HIS E  1 180 ? 140.581 5.977   -5.383  1.00   32.12  ? 180 HIS E CB  1 
ATOM   13346 C CG  . HIS E  1 180 ? 140.389 4.583   -5.891  1.00   38.25  ? 180 HIS E CG  1 
ATOM   13347 N ND1 . HIS E  1 180 ? 141.404 3.846   -6.464  1.00   40.13  ? 180 HIS E ND1 1 
ATOM   13348 C CD2 . HIS E  1 180 ? 139.296 3.784   -5.899  1.00   42.10  ? 180 HIS E CD2 1 
ATOM   13349 C CE1 . HIS E  1 180 ? 140.944 2.657   -6.811  1.00   42.05  ? 180 HIS E CE1 1 
ATOM   13350 N NE2 . HIS E  1 180 ? 139.667 2.595   -6.478  1.00   43.93  ? 180 HIS E NE2 1 
ATOM   13351 N N   . PHE E  1 181 ? 143.207 6.219   -3.520  1.00   29.79  ? 181 PHE E N   1 
ATOM   13352 C CA  . PHE E  1 181 ? 144.550 5.680   -3.292  1.00   29.41  ? 181 PHE E CA  1 
ATOM   13353 C C   . PHE E  1 181 ? 145.137 5.990   -1.896  1.00   30.91  ? 181 PHE E C   1 
ATOM   13354 O O   . PHE E  1 181 ? 146.220 5.505   -1.551  1.00   32.43  ? 181 PHE E O   1 
ATOM   13355 C CB  . PHE E  1 181 ? 145.503 6.195   -4.371  1.00   27.84  ? 181 PHE E CB  1 
ATOM   13356 C CG  . PHE E  1 181 ? 145.151 5.730   -5.760  1.00   26.65  ? 181 PHE E CG  1 
ATOM   13357 C CD1 . PHE E  1 181 ? 145.396 4.439   -6.160  1.00   29.66  ? 181 PHE E CD1 1 
ATOM   13358 C CD2 . PHE E  1 181 ? 144.582 6.604   -6.667  1.00   27.08  ? 181 PHE E CD2 1 
ATOM   13359 C CE1 . PHE E  1 181 ? 145.063 4.022   -7.445  1.00   30.56  ? 181 PHE E CE1 1 
ATOM   13360 C CE2 . PHE E  1 181 ? 144.251 6.195   -7.942  1.00   25.07  ? 181 PHE E CE2 1 
ATOM   13361 C CZ  . PHE E  1 181 ? 144.495 4.908   -8.333  1.00   27.07  ? 181 PHE E CZ  1 
ATOM   13362 N N   . GLY E  1 182 ? 144.421 6.765   -1.091  1.00   28.71  ? 182 GLY E N   1 
ATOM   13363 C CA  . GLY E  1 182 ? 144.906 7.123   0.220   1.00   29.64  ? 182 GLY E CA  1 
ATOM   13364 C C   . GLY E  1 182 ? 146.119 8.028   0.145   1.00   30.39  ? 182 GLY E C   1 
ATOM   13365 O O   . GLY E  1 182 ? 147.036 7.882   0.959   1.00   32.55  ? 182 GLY E O   1 
ATOM   13366 N N   . LEU E  1 183 ? 146.126 8.952   -0.822  1.00   29.42  ? 183 LEU E N   1 
ATOM   13367 C CA  . LEU E  1 183 ? 147.245 9.882   -1.012  1.00   29.46  ? 183 LEU E CA  1 
ATOM   13368 C C   . LEU E  1 183 ? 147.170 10.988  0.002   1.00   31.60  ? 183 LEU E C   1 
ATOM   13369 O O   . LEU E  1 183 ? 146.085 11.327  0.460   1.00   33.89  ? 183 LEU E O   1 
ATOM   13370 C CB  . LEU E  1 183 ? 147.220 10.521  -2.394  1.00   28.52  ? 183 LEU E CB  1 
ATOM   13371 C CG  . LEU E  1 183 ? 147.176 9.693   -3.666  1.00   29.31  ? 183 LEU E CG  1 
ATOM   13372 C CD1 . LEU E  1 183 ? 146.978 10.639  -4.830  1.00   29.38  ? 183 LEU E CD1 1 
ATOM   13373 C CD2 . LEU E  1 183 ? 148.450 8.921   -3.835  1.00   31.75  ? 183 LEU E CD2 1 
ATOM   13374 N N   . LYS E  1 184 ? 148.305 11.595  0.317   1.00   31.09  ? 184 LYS E N   1 
ATOM   13375 C CA  . LYS E  1 184 ? 148.290 12.839  1.074   1.00   35.03  ? 184 LYS E CA  1 
ATOM   13376 C C   . LYS E  1 184 ? 147.521 13.879  0.234   1.00   34.26  ? 184 LYS E C   1 
ATOM   13377 O O   . LYS E  1 184 ? 147.588 13.820  -0.999  1.00   30.75  ? 184 LYS E O   1 
ATOM   13378 C CB  . LYS E  1 184 ? 149.720 13.311  1.397   1.00   40.51  ? 184 LYS E CB  1 
ATOM   13379 C CG  . LYS E  1 184 ? 149.803 14.736  1.946   1.00   44.42  ? 184 LYS E CG  1 
ATOM   13380 C CD  . LYS E  1 184 ? 151.148 15.083  2.607   1.00   48.69  ? 184 LYS E CD  1 
ATOM   13381 C CE  . LYS E  1 184 ? 151.173 16.553  3.102   1.00   63.40  ? 184 LYS E CE  1 
ATOM   13382 N NZ  . LYS E  1 184 ? 150.683 17.613  2.123   1.00   61.26  ? 184 LYS E NZ  1 
ATOM   13383 N N   . ARG E  1 185 ? 146.745 14.774  0.881   1.00   32.04  ? 185 ARG E N   1 
ATOM   13384 C CA  . ARG E  1 185 ? 145.941 15.786  0.169   1.00   27.38  ? 185 ARG E CA  1 
ATOM   13385 C C   . ARG E  1 185 ? 146.772 16.999  -0.277  1.00   28.19  ? 185 ARG E C   1 
ATOM   13386 O O   . ARG E  1 185 ? 146.848 18.014  0.413   1.00   30.63  ? 185 ARG E O   1 
ATOM   13387 C CB  . ARG E  1 185 ? 144.754 16.251  1.017   1.00   25.71  ? 185 ARG E CB  1 
ATOM   13388 C CG  . ARG E  1 185 ? 143.846 15.115  1.458   1.00   27.14  ? 185 ARG E CG  1 
ATOM   13389 C CD  . ARG E  1 185 ? 142.487 15.571  2.046   1.00   32.89  ? 185 ARG E CD  1 
ATOM   13390 N NE  . ARG E  1 185 ? 141.462 14.662  1.535   1.00   37.94  ? 185 ARG E NE  1 
ATOM   13391 C CZ  . ARG E  1 185 ? 140.501 14.982  0.677   1.00   43.11  ? 185 ARG E CZ  1 
ATOM   13392 N NH1 . ARG E  1 185 ? 140.358 16.225  0.247   1.00   45.50  ? 185 ARG E NH1 1 
ATOM   13393 N NH2 . ARG E  1 185 ? 139.660 14.045  0.270   1.00   48.52  ? 185 ARG E NH2 1 
ATOM   13394 N N   . GLN E  1 186 ? 147.397 16.876  -1.441  1.00   27.49  ? 186 GLN E N   1 
ATOM   13395 C CA  . GLN E  1 186 ? 148.302 17.894  -1.931  1.00   28.11  ? 186 GLN E CA  1 
ATOM   13396 C C   . GLN E  1 186 ? 148.416 17.715  -3.428  1.00   28.30  ? 186 GLN E C   1 
ATOM   13397 O O   . GLN E  1 186 ? 148.503 16.592  -3.890  1.00   30.08  ? 186 GLN E O   1 
ATOM   13398 C CB  . GLN E  1 186 ? 149.674 17.723  -1.295  1.00   30.50  ? 186 GLN E CB  1 
ATOM   13399 C CG  . GLN E  1 186 ? 150.670 18.815  -1.598  1.00   32.66  ? 186 GLN E CG  1 
ATOM   13400 C CD  . GLN E  1 186 ? 152.073 18.382  -1.299  1.00   35.44  ? 186 GLN E CD  1 
ATOM   13401 O OE1 . GLN E  1 186 ? 152.693 17.685  -2.097  1.00   38.94  ? 186 GLN E OE1 1 
ATOM   13402 N NE2 . GLN E  1 186 ? 152.534 18.666  -0.101  1.00   36.93  ? 186 GLN E NE2 1 
ATOM   13403 N N   . PHE E  1 187 ? 148.386 18.779  -4.210  1.00   26.96  ? 187 PHE E N   1 
ATOM   13404 C CA  . PHE E  1 187 ? 148.777 18.619  -5.597  1.00   25.05  ? 187 PHE E CA  1 
ATOM   13405 C C   . PHE E  1 187 ? 149.593 19.802  -6.044  1.00   28.39  ? 187 PHE E C   1 
ATOM   13406 O O   . PHE E  1 187 ? 149.527 20.856  -5.457  1.00   27.44  ? 187 PHE E O   1 
ATOM   13407 C CB  . PHE E  1 187 ? 147.573 18.410  -6.500  1.00   26.22  ? 187 PHE E CB  1 
ATOM   13408 C CG  . PHE E  1 187 ? 146.654 19.592  -6.605  1.00   28.87  ? 187 PHE E CG  1 
ATOM   13409 C CD1 . PHE E  1 187 ? 145.644 19.789  -5.669  1.00   29.27  ? 187 PHE E CD1 1 
ATOM   13410 C CD2 . PHE E  1 187 ? 146.742 20.468  -7.687  1.00   28.18  ? 187 PHE E CD2 1 
ATOM   13411 C CE1 . PHE E  1 187 ? 144.767 20.874  -5.796  1.00   26.76  ? 187 PHE E CE1 1 
ATOM   13412 C CE2 . PHE E  1 187 ? 145.875 21.551  -7.811  1.00   24.40  ? 187 PHE E CE2 1 
ATOM   13413 C CZ  . PHE E  1 187 ? 144.891 21.751  -6.872  1.00   24.83  ? 187 PHE E CZ  1 
ATOM   13414 N N   . SER E  1 188 ? 150.401 19.589  -7.066  1.00   32.00  ? 188 SER E N   1 
ATOM   13415 C CA  . SER E  1 188 ? 151.334 20.584  -7.543  1.00   32.93  ? 188 SER E CA  1 
ATOM   13416 C C   . SER E  1 188 ? 151.163 20.778  -9.041  1.00   33.57  ? 188 SER E C   1 
ATOM   13417 O O   . SER E  1 188 ? 151.087 19.813  -9.800  1.00   34.32  ? 188 SER E O   1 
ATOM   13418 C CB  . SER E  1 188 ? 152.784 20.164  -7.245  1.00   34.83  ? 188 SER E CB  1 
ATOM   13419 O OG  . SER E  1 188 ? 153.037 19.966  -5.860  1.00   33.99  ? 188 SER E OG  1 
ATOM   13420 N N   . VAL E  1 189 ? 151.159 22.034  -9.460  1.00   34.29  ? 189 VAL E N   1 
ATOM   13421 C CA  . VAL E  1 189 ? 150.955 22.404  -10.855 1.00   32.56  ? 189 VAL E CA  1 
ATOM   13422 C C   . VAL E  1 189 ? 152.167 23.069  -11.470 1.00   31.37  ? 189 VAL E C   1 
ATOM   13423 O O   . VAL E  1 189 ? 152.625 24.094  -10.982 1.00   33.68  ? 189 VAL E O   1 
ATOM   13424 C CB  . VAL E  1 189 ? 149.796 23.371  -10.994 1.00   29.49  ? 189 VAL E CB  1 
ATOM   13425 C CG1 . VAL E  1 189 ? 149.610 23.744  -12.442 1.00   27.04  ? 189 VAL E CG1 1 
ATOM   13426 C CG2 . VAL E  1 189 ? 148.534 22.793  -10.326 1.00   29.02  ? 189 VAL E CG2 1 
ATOM   13427 N N   . CYS E  1 190 ? 152.664 22.507  -12.561 1.00   31.10  ? 190 CYS E N   1 
ATOM   13428 C CA  . CYS E  1 190 ? 153.746 23.131  -13.275 1.00   31.21  ? 190 CYS E CA  1 
ATOM   13429 C C   . CYS E  1 190 ? 153.389 23.278  -14.757 1.00   33.34  ? 190 CYS E C   1 
ATOM   13430 O O   . CYS E  1 190 ? 153.667 22.396  -15.574 1.00   32.56  ? 190 CYS E O   1 
ATOM   13431 C CB  . CYS E  1 190 ? 155.038 22.335  -13.095 1.00   31.01  ? 190 CYS E CB  1 
ATOM   13432 S SG  . CYS E  1 190 ? 156.555 23.369  -13.160 1.00   40.66  ? 190 CYS E SG  1 
ATOM   13433 N N   . LEU E  1 191 ? 152.767 24.404  -15.101 1.00   31.73  ? 191 LEU E N   1 
ATOM   13434 C CA  . LEU E  1 191 ? 152.399 24.633  -16.484 1.00   32.61  ? 191 LEU E CA  1 
ATOM   13435 C C   . LEU E  1 191 ? 153.593 25.053  -17.338 1.00   33.79  ? 191 LEU E C   1 
ATOM   13436 O O   . LEU E  1 191 ? 154.447 25.822  -16.916 1.00   34.07  ? 191 LEU E O   1 
ATOM   13437 C CB  . LEU E  1 191 ? 151.312 25.688  -16.571 1.00   32.20  ? 191 LEU E CB  1 
ATOM   13438 C CG  . LEU E  1 191 ? 150.092 25.347  -15.729 1.00   35.07  ? 191 LEU E CG  1 
ATOM   13439 C CD1 . LEU E  1 191 ? 149.025 26.395  -15.958 1.00   35.41  ? 191 LEU E CD1 1 
ATOM   13440 C CD2 . LEU E  1 191 ? 149.562 23.942  -16.047 1.00   34.21  ? 191 LEU E CD2 1 
ATOM   13441 N N   . SER E  1 192 ? 153.625 24.547  -18.560 1.00   34.90  ? 192 SER E N   1 
ATOM   13442 C CA  . SER E  1 192 ? 154.653 24.896  -19.502 1.00   35.41  ? 192 SER E CA  1 
ATOM   13443 C C   . SER E  1 192 ? 154.243 26.072  -20.356 1.00   38.70  ? 192 SER E C   1 
ATOM   13444 O O   . SER E  1 192 ? 153.121 26.128  -20.861 1.00   38.72  ? 192 SER E O   1 
ATOM   13445 C CB  . SER E  1 192 ? 154.970 23.712  -20.401 1.00   34.84  ? 192 SER E CB  1 
ATOM   13446 O OG  . SER E  1 192 ? 155.902 24.080  -21.403 1.00   32.50  ? 192 SER E OG  1 
ATOM   13447 N N   . ARG E  1 193 ? 155.160 27.026  -20.479 1.00   38.97  ? 193 ARG E N   1 
ATOM   13448 C CA  . ARG E  1 193 ? 155.005 28.169  -21.353 1.00   36.66  ? 193 ARG E CA  1 
ATOM   13449 C C   . ARG E  1 193 ? 155.007 27.779  -22.825 1.00   38.64  ? 193 ARG E C   1 
ATOM   13450 O O   . ARG E  1 193 ? 154.473 28.502  -23.664 1.00   40.22  ? 193 ARG E O   1 
ATOM   13451 C CB  . ARG E  1 193 ? 156.104 29.190  -21.035 1.00   38.65  ? 193 ARG E CB  1 
ATOM   13452 C CG  . ARG E  1 193 ? 156.361 30.241  -22.071 1.00   43.43  ? 193 ARG E CG  1 
ATOM   13453 C CD  . ARG E  1 193 ? 157.428 31.187  -21.577 1.00   49.11  ? 193 ARG E CD  1 
ATOM   13454 N NE  . ARG E  1 193 ? 156.982 31.709  -20.289 1.00   55.81  ? 193 ARG E NE  1 
ATOM   13455 C CZ  . ARG E  1 193 ? 157.773 32.148  -19.317 1.00   60.22  ? 193 ARG E CZ  1 
ATOM   13456 N NH1 . ARG E  1 193 ? 159.088 32.125  -19.476 1.00   60.95  ? 193 ARG E NH1 1 
ATOM   13457 N NH2 . ARG E  1 193 ? 157.239 32.601  -18.176 1.00   60.08  ? 193 ARG E NH2 1 
ATOM   13458 N N   . TYR E  1 194 ? 155.589 26.625  -23.137 1.00   39.39  ? 194 TYR E N   1 
ATOM   13459 C CA  . TYR E  1 194 ? 155.808 26.214  -24.530 1.00   41.84  ? 194 TYR E CA  1 
ATOM   13460 C C   . TYR E  1 194 ? 154.805 25.203  -25.033 1.00   42.59  ? 194 TYR E C   1 
ATOM   13461 O O   . TYR E  1 194 ? 154.458 24.264  -24.336 1.00   41.71  ? 194 TYR E O   1 
ATOM   13462 C CB  . TYR E  1 194 ? 157.220 25.656  -24.694 1.00   38.91  ? 194 TYR E CB  1 
ATOM   13463 C CG  . TYR E  1 194 ? 158.206 26.542  -24.022 1.00   38.79  ? 194 TYR E CG  1 
ATOM   13464 C CD1 . TYR E  1 194 ? 158.644 27.692  -24.644 1.00   40.35  ? 194 TYR E CD1 1 
ATOM   13465 C CD2 . TYR E  1 194 ? 158.613 26.300  -22.723 1.00   37.17  ? 194 TYR E CD2 1 
ATOM   13466 C CE1 . TYR E  1 194 ? 159.522 28.548  -24.021 1.00   44.35  ? 194 TYR E CE1 1 
ATOM   13467 C CE2 . TYR E  1 194 ? 159.489 27.153  -22.084 1.00   37.20  ? 194 TYR E CE2 1 
ATOM   13468 C CZ  . TYR E  1 194 ? 159.937 28.275  -22.737 1.00   42.39  ? 194 TYR E CZ  1 
ATOM   13469 O OH  . TYR E  1 194 ? 160.811 29.137  -22.117 1.00   43.70  ? 194 TYR E OH  1 
ATOM   13470 N N   . SER E  1 195 ? 154.316 25.436  -26.245 1.00   45.98  ? 195 SER E N   1 
ATOM   13471 C CA  . SER E  1 195 ? 153.392 24.523  -26.893 1.00   47.15  ? 195 SER E CA  1 
ATOM   13472 C C   . SER E  1 195 ? 154.139 23.274  -27.332 1.00   48.92  ? 195 SER E C   1 
ATOM   13473 O O   . SER E  1 195 ? 153.517 22.249  -27.619 1.00   49.58  ? 195 SER E O   1 
ATOM   13474 C CB  . SER E  1 195 ? 152.695 25.187  -28.084 1.00   49.59  ? 195 SER E CB  1 
ATOM   13475 O OG  . SER E  1 195 ? 153.628 25.647  -29.029 1.00   53.27  ? 195 SER E OG  1 
ATOM   13476 N N   . THR E  1 196 ? 155.471 23.365  -27.393 1.00   47.91  ? 196 THR E N   1 
ATOM   13477 C CA  . THR E  1 196 ? 156.300 22.242  -27.853 1.00   47.99  ? 196 THR E CA  1 
ATOM   13478 C C   . THR E  1 196 ? 156.762 21.292  -26.731 1.00   45.41  ? 196 THR E C   1 
ATOM   13479 O O   . THR E  1 196 ? 157.298 20.230  -27.015 1.00   44.30  ? 196 THR E O   1 
ATOM   13480 C CB  . THR E  1 196 ? 157.561 22.735  -28.590 1.00   47.18  ? 196 THR E CB  1 
ATOM   13481 O OG1 . THR E  1 196 ? 158.375 23.487  -27.688 1.00   46.10  ? 196 THR E OG1 1 
ATOM   13482 C CG2 . THR E  1 196 ? 157.185 23.608  -29.751 1.00   50.32  ? 196 THR E CG2 1 
ATOM   13483 N N   . SER E  1 197 ? 156.497 21.624  -25.470 1.00   43.83  ? 197 SER E N   1 
ATOM   13484 C CA  . SER E  1 197 ? 156.830 20.719  -24.375 1.00   42.55  ? 197 SER E CA  1 
ATOM   13485 C C   . SER E  1 197 ? 155.769 20.789  -23.284 1.00   40.38  ? 197 SER E C   1 
ATOM   13486 O O   . SER E  1 197 ? 155.214 21.842  -23.021 1.00   45.07  ? 197 SER E O   1 
ATOM   13487 C CB  . SER E  1 197 ? 158.211 21.041  -23.782 1.00   42.74  ? 197 SER E CB  1 
ATOM   13488 O OG  . SER E  1 197 ? 158.284 22.339  -23.210 1.00   42.83  ? 197 SER E OG  1 
ATOM   13489 N N   . ASN E  1 198 ? 155.504 19.657  -22.644 1.00   40.08  ? 198 ASN E N   1 
ATOM   13490 C CA  . ASN E  1 198 ? 154.442 19.546  -21.654 1.00   38.51  ? 198 ASN E CA  1 
ATOM   13491 C C   . ASN E  1 198 ? 154.829 20.014  -20.273 1.00   35.07  ? 198 ASN E C   1 
ATOM   13492 O O   . ASN E  1 198 ? 155.997 20.062  -19.932 1.00   38.23  ? 198 ASN E O   1 
ATOM   13493 C CB  . ASN E  1 198 ? 153.955 18.104  -21.527 1.00   43.56  ? 198 ASN E CB  1 
ATOM   13494 C CG  . ASN E  1 198 ? 153.135 17.653  -22.702 1.00   48.88  ? 198 ASN E CG  1 
ATOM   13495 O OD1 . ASN E  1 198 ? 152.698 18.465  -23.511 1.00   54.22  ? 198 ASN E OD1 1 
ATOM   13496 N ND2 . ASN E  1 198 ? 152.859 16.356  -22.768 1.00   48.64  ? 198 ASN E ND2 1 
ATOM   13497 N N   . GLY E  1 199 ? 153.822 20.383  -19.500 1.00   31.59  ? 199 GLY E N   1 
ATOM   13498 C CA  . GLY E  1 199 ? 153.962 20.524  -18.068 1.00   35.36  ? 199 GLY E CA  1 
ATOM   13499 C C   . GLY E  1 199 ? 153.259 19.355  -17.364 1.00   34.76  ? 199 GLY E C   1 
ATOM   13500 O O   . GLY E  1 199 ? 152.903 18.369  -18.010 1.00   33.32  ? 199 GLY E O   1 
ATOM   13501 N N   . ALA E  1 200 ? 153.062 19.450  -16.046 1.00   33.87  ? 200 ALA E N   1 
ATOM   13502 C CA  . ALA E  1 200 ? 152.472 18.343  -15.286 1.00   34.79  ? 200 ALA E CA  1 
ATOM   13503 C C   . ALA E  1 200 ? 151.696 18.795  -14.042 1.00   36.67  ? 200 ALA E C   1 
ATOM   13504 O O   . ALA E  1 200 ? 151.929 19.888  -13.499 1.00   36.63  ? 200 ALA E O   1 
ATOM   13505 C CB  . ALA E  1 200 ? 153.559 17.349  -14.872 1.00   32.29  ? 200 ALA E CB  1 
ATOM   13506 N N   . ILE E  1 201 ? 150.781 17.928  -13.601 1.00   34.96  ? 201 ILE E N   1 
ATOM   13507 C CA  . ILE E  1 201 ? 150.168 18.004  -12.277 1.00   30.19  ? 201 ILE E CA  1 
ATOM   13508 C C   . ILE E  1 201 ? 150.613 16.768  -11.504 1.00   29.75  ? 201 ILE E C   1 
ATOM   13509 O O   . ILE E  1 201 ? 150.580 15.643  -12.025 1.00   29.51  ? 201 ILE E O   1 
ATOM   13510 C CB  . ILE E  1 201 ? 148.632 17.988  -12.304 1.00   29.52  ? 201 ILE E CB  1 
ATOM   13511 C CG1 . ILE E  1 201 ? 148.032 18.772  -13.484 1.00   28.56  ? 201 ILE E CG1 1 
ATOM   13512 C CG2 . ILE E  1 201 ? 148.061 18.377  -10.893 1.00   22.70  ? 201 ILE E CG2 1 
ATOM   13513 C CD1 . ILE E  1 201 ? 148.089 20.254  -13.377 1.00   27.78  ? 201 ILE E CD1 1 
ATOM   13514 N N   . LEU E  1 202 ? 151.026 16.965  -10.263 1.00   28.98  ? 202 LEU E N   1 
ATOM   13515 C CA  . LEU E  1 202 ? 151.488 15.864  -9.434  1.00   31.53  ? 202 LEU E CA  1 
ATOM   13516 C C   . LEU E  1 202 ? 150.529 15.720  -8.306  1.00   30.24  ? 202 LEU E C   1 
ATOM   13517 O O   . LEU E  1 202 ? 150.116 16.717  -7.730  1.00   31.34  ? 202 LEU E O   1 
ATOM   13518 C CB  . LEU E  1 202 ? 152.882 16.135  -8.901  1.00   36.75  ? 202 LEU E CB  1 
ATOM   13519 C CG  . LEU E  1 202 ? 154.040 15.714  -9.778  1.00   40.81  ? 202 LEU E CG  1 
ATOM   13520 C CD1 . LEU E  1 202 ? 154.025 16.467  -11.059 1.00   43.23  ? 202 LEU E CD1 1 
ATOM   13521 C CD2 . LEU E  1 202 ? 155.287 16.049  -9.026  1.00   42.58  ? 202 LEU E CD2 1 
ATOM   13522 N N   . PHE E  1 203 ? 150.133 14.493  -8.010  1.00   28.90  ? 203 PHE E N   1 
ATOM   13523 C CA  . PHE E  1 203 ? 149.164 14.249  -6.954  1.00   27.08  ? 203 PHE E CA  1 
ATOM   13524 C C   . PHE E  1 203 ? 149.800 13.395  -5.883  1.00   26.38  ? 203 PHE E C   1 
ATOM   13525 O O   . PHE E  1 203 ? 150.274 12.309  -6.158  1.00   29.52  ? 203 PHE E O   1 
ATOM   13526 C CB  . PHE E  1 203 ? 147.914 13.541  -7.483  1.00   30.31  ? 203 PHE E CB  1 
ATOM   13527 C CG  . PHE E  1 203 ? 147.202 14.257  -8.611  1.00   29.24  ? 203 PHE E CG  1 
ATOM   13528 C CD1 . PHE E  1 203 ? 146.220 15.199  -8.346  1.00   30.35  ? 203 PHE E CD1 1 
ATOM   13529 C CD2 . PHE E  1 203 ? 147.469 13.930  -9.930  1.00   29.62  ? 203 PHE E CD2 1 
ATOM   13530 C CE1 . PHE E  1 203 ? 145.549 15.839  -9.368  1.00   31.61  ? 203 PHE E CE1 1 
ATOM   13531 C CE2 . PHE E  1 203 ? 146.811 14.561  -10.960 1.00   30.49  ? 203 PHE E CE2 1 
ATOM   13532 C CZ  . PHE E  1 203 ? 145.845 15.510  -10.685 1.00   32.76  ? 203 PHE E CZ  1 
ATOM   13533 N N   . GLY E  1 204 ? 149.798 13.869  -4.652  1.00   28.17  ? 204 GLY E N   1 
ATOM   13534 C CA  . GLY E  1 204 ? 150.446 13.154  -3.574  1.00   27.27  ? 204 GLY E CA  1 
ATOM   13535 C C   . GLY E  1 204 ? 151.518 14.025  -2.964  1.00   30.93  ? 204 GLY E C   1 
ATOM   13536 O O   . GLY E  1 204 ? 151.712 15.178  -3.372  1.00   30.06  ? 204 GLY E O   1 
ATOM   13537 N N   . ASP E  1 205 ? 152.184 13.484  -1.952  1.00   34.03  ? 205 ASP E N   1 
ATOM   13538 C CA  . ASP E  1 205 ? 153.172 14.223  -1.193  1.00   36.24  ? 205 ASP E CA  1 
ATOM   13539 C C   . ASP E  1 205 ? 154.484 14.295  -1.946  1.00   39.55  ? 205 ASP E C   1 
ATOM   13540 O O   . ASP E  1 205 ? 155.092 13.265  -2.198  1.00   43.69  ? 205 ASP E O   1 
ATOM   13541 C CB  . ASP E  1 205 ? 153.377 13.568  0.151   1.00   39.33  ? 205 ASP E CB  1 
ATOM   13542 C CG  . ASP E  1 205 ? 154.239 14.375  1.050   1.00   45.64  ? 205 ASP E CG  1 
ATOM   13543 O OD1 . ASP E  1 205 ? 154.487 15.574  0.758   1.00   44.61  ? 205 ASP E OD1 1 
ATOM   13544 O OD2 . ASP E  1 205 ? 154.696 13.773  2.044   1.00   51.30  1 205 ASP E OD2 1 
ATOM   13545 N N   . ILE E  1 206 ? 154.988 15.486  -2.229  1.00   39.71  ? 206 ILE E N   1 
ATOM   13546 C CA  . ILE E  1 206 ? 156.226 15.530  -2.990  1.00   42.21  ? 206 ILE E CA  1 
ATOM   13547 C C   . ILE E  1 206 ? 157.415 15.525  -2.064  1.00   41.11  ? 206 ILE E C   1 
ATOM   13548 O O   . ILE E  1 206 ? 158.514 15.324  -2.515  1.00   43.67  ? 206 ILE E O   1 
ATOM   13549 C CB  . ILE E  1 206 ? 156.293 16.775  -3.847  1.00   43.16  ? 206 ILE E CB  1 
ATOM   13550 C CG1 . ILE E  1 206 ? 155.956 17.962  -2.973  1.00   43.31  ? 206 ILE E CG1 1 
ATOM   13551 C CG2 . ILE E  1 206 ? 155.305 16.707  -4.986  1.00   44.19  ? 206 ILE E CG2 1 
ATOM   13552 C CD1 . ILE E  1 206 ? 155.976 19.199  -3.698  1.00   45.26  ? 206 ILE E CD1 1 
ATOM   13553 N N   . ASN E  1 207 ? 157.163 15.606  -0.763  1.00   41.73  ? 207 ASN E N   1 
ATOM   13554 C CA  . ASN E  1 207 ? 158.224 15.665  0.227   1.00   46.76  ? 207 ASN E CA  1 
ATOM   13555 C C   . ASN E  1 207 ? 158.265 14.342  0.926   1.00   48.80  ? 207 ASN E C   1 
ATOM   13556 O O   . ASN E  1 207 ? 158.855 14.201  1.989   1.00   52.68  ? 207 ASN E O   1 
ATOM   13557 C CB  . ASN E  1 207 ? 157.956 16.750  1.274   1.00   53.32  ? 207 ASN E CB  1 
ATOM   13558 C CG  . ASN E  1 207 ? 157.849 18.141  0.686   1.00   56.34  ? 207 ASN E CG  1 
ATOM   13559 O OD1 . ASN E  1 207 ? 158.685 18.565  -0.112  1.00   59.58  ? 207 ASN E OD1 1 
ATOM   13560 N ND2 . ASN E  1 207 ? 156.807 18.860  1.075   1.00   54.78  ? 207 ASN E ND2 1 
ATOM   13561 N N   . ASP E  1 208 ? 157.714 13.349  0.258   1.00   49.13  ? 208 ASP E N   1 
ATOM   13562 C CA  . ASP E  1 208 ? 157.610 12.025  0.801   1.00   51.45  ? 208 ASP E CA  1 
ATOM   13563 C C   . ASP E  1 208 ? 158.812 11.329  0.238   1.00   58.39  ? 208 ASP E C   1 
ATOM   13564 O O   . ASP E  1 208 ? 158.968 11.251  -0.978  1.00   59.47  ? 208 ASP E O   1 
ATOM   13565 C CB  . ASP E  1 208 ? 156.296 11.339  0.407   1.00   51.26  ? 208 ASP E CB  1 
ATOM   13566 C CG  . ASP E  1 208 ? 156.145 9.925   1.001   1.00   55.56  ? 208 ASP E CG  1 
ATOM   13567 O OD1 . ASP E  1 208 ? 157.109 9.360   1.554   1.00   57.27  ? 208 ASP E OD1 1 
ATOM   13568 O OD2 . ASP E  1 208 ? 155.041 9.354   0.897   1.00   56.24  ? 208 ASP E OD2 1 
ATOM   13569 N N   . PRO E  1 209 ? 159.733 10.939  1.131   1.00   65.16  ? 209 PRO E N   1 
ATOM   13570 C CA  . PRO E  1 209 ? 160.984 10.228  0.839   1.00   67.79  ? 209 PRO E CA  1 
ATOM   13571 C C   . PRO E  1 209 ? 160.763 9.066   -0.126  1.00   64.63  ? 209 PRO E C   1 
ATOM   13572 O O   . PRO E  1 209 ? 161.677 8.704   -0.852  1.00   61.40  ? 209 PRO E O   1 
ATOM   13573 C CB  . PRO E  1 209 ? 161.449 9.740   2.215   1.00   71.82  ? 209 PRO E CB  1 
ATOM   13574 C CG  . PRO E  1 209 ? 160.243 9.881   3.117   1.00   71.71  ? 209 PRO E CG  1 
ATOM   13575 C CD  . PRO E  1 209 ? 159.514 11.078  2.580   1.00   68.18  ? 209 PRO E CD  1 
ATOM   13576 N N   . ASN E  1 210 ? 159.579 8.466   -0.123  1.00   66.05  ? 210 ASN E N   1 
ATOM   13577 C CA  . ASN E  1 210 ? 159.294 7.432   -1.117  1.00   68.02  ? 210 ASN E CA  1 
ATOM   13578 C C   . ASN E  1 210 ? 159.233 7.999   -2.536  1.00   65.59  ? 210 ASN E C   1 
ATOM   13579 O O   . ASN E  1 210 ? 159.515 7.302   -3.508  1.00   66.93  ? 210 ASN E O   1 
ATOM   13580 C CB  . ASN E  1 210 ? 157.998 6.672   -0.806  1.00   69.02  ? 210 ASN E CB  1 
ATOM   13581 C CG  . ASN E  1 210 ? 158.102 5.805   0.423   1.00   73.18  ? 210 ASN E CG  1 
ATOM   13582 O OD1 . ASN E  1 210 ? 157.356 6.005   1.382   1.00   74.33  ? 210 ASN E OD1 1 
ATOM   13583 N ND2 . ASN E  1 210 ? 159.023 4.835   0.409   1.00   74.47  ? 210 ASN E ND2 1 
ATOM   13584 N N   . ASN E  1 211 ? 158.900 9.270   -2.672  1.00   61.85  ? 211 ASN E N   1 
ATOM   13585 C CA  . ASN E  1 211 ? 158.800 9.797   -4.011  1.00   57.38  ? 211 ASN E CA  1 
ATOM   13586 C C   . ASN E  1 211 ? 160.086 10.449  -4.390  1.00   58.27  ? 211 ASN E C   1 
ATOM   13587 O O   . ASN E  1 211 ? 160.203 11.059  -5.435  1.00   56.65  ? 211 ASN E O   1 
ATOM   13588 C CB  . ASN E  1 211 ? 157.658 10.786  -4.098  1.00   51.73  ? 211 ASN E CB  1 
ATOM   13589 C CG  . ASN E  1 211 ? 156.364 10.150  -3.732  1.00   47.67  ? 211 ASN E CG  1 
ATOM   13590 O OD1 . ASN E  1 211 ? 156.162 8.986   -4.044  1.00   48.17  ? 211 ASN E OD1 1 
ATOM   13591 N ND2 . ASN E  1 211 ? 155.477 10.884  -3.073  1.00   46.53  ? 211 ASN E ND2 1 
ATOM   13592 N N   . ASN E  1 212 ? 161.090 10.199  -3.577  1.00   61.62  ? 212 ASN E N   1 
ATOM   13593 C CA  . ASN E  1 212 ? 162.324 10.941  -3.700  1.00   63.46  ? 212 ASN E CA  1 
ATOM   13594 C C   . ASN E  1 212 ? 163.035 10.827  -5.065  1.00   60.32  ? 212 ASN E C   1 
ATOM   13595 O O   . ASN E  1 212 ? 163.617 11.792  -5.511  1.00   57.20  ? 212 ASN E O   1 
ATOM   13596 C CB  . ASN E  1 212 ? 163.279 10.537  -2.579  1.00   68.73  ? 212 ASN E CB  1 
ATOM   13597 C CG  . ASN E  1 212 ? 164.305 11.595  -2.294  1.00   74.25  ? 212 ASN E CG  1 
ATOM   13598 O OD1 . ASN E  1 212 ? 164.718 12.298  -3.189  1.00   75.98  ? 212 ASN E OD1 1 
ATOM   13599 N ND2 . ASN E  1 212 ? 164.749 11.695  -1.044  1.00   77.61  ? 212 ASN E ND2 1 
ATOM   13600 N N   . ASN E  1 213 ? 163.012 9.678   -5.738  1.00   61.93  ? 213 ASN E N   1 
ATOM   13601 C CA  . ASN E  1 213 ? 163.796 9.655   -6.964  1.00   64.67  ? 213 ASN E CA  1 
ATOM   13602 C C   . ASN E  1 213 ? 163.083 10.385  -8.046  1.00   56.93  ? 213 ASN E C   1 
ATOM   13603 O O   . ASN E  1 213 ? 163.675 11.014  -8.946  1.00   54.54  ? 213 ASN E O   1 
ATOM   13604 C CB  . ASN E  1 213 ? 164.077 8.284   -7.510  1.00   72.36  ? 213 ASN E CB  1 
ATOM   13605 C CG  . ASN E  1 213 ? 164.992 7.480   -6.627  1.00   79.78  ? 213 ASN E CG  1 
ATOM   13606 O OD1 . ASN E  1 213 ? 165.125 6.300   -6.909  1.00   84.12  ? 213 ASN E OD1 1 
ATOM   13607 N ND2 . ASN E  1 213 ? 165.288 7.980   -5.403  1.00   80.91  ? 213 ASN E ND2 1 
ATOM   13608 N N   . TYR E  1 214 ? 161.776 10.305  -7.973  1.00   50.65  ? 214 TYR E N   1 
ATOM   13609 C CA  . TYR E  1 214 ? 161.030 10.890  -9.052  1.00   48.03  ? 214 TYR E CA  1 
ATOM   13610 C C   . TYR E  1 214 ? 161.203 12.409  -9.022  1.00   46.69  ? 214 TYR E C   1 
ATOM   13611 O O   . TYR E  1 214 ? 161.380 13.041  -10.066 1.00   47.22  ? 214 TYR E O   1 
ATOM   13612 C CB  . TYR E  1 214 ? 159.526 10.530  -9.005  1.00   42.81  ? 214 TYR E CB  1 
ATOM   13613 C CG  . TYR E  1 214 ? 158.858 11.034  -10.267 1.00   40.36  ? 214 TYR E CG  1 
ATOM   13614 C CD1 . TYR E  1 214 ? 158.949 10.314  -11.449 1.00   41.55  ? 214 TYR E CD1 1 
ATOM   13615 C CD2 . TYR E  1 214 ? 158.186 12.243  -10.289 1.00   40.84  ? 214 TYR E CD2 1 
ATOM   13616 C CE1 . TYR E  1 214 ? 158.374 10.778  -12.627 1.00   41.87  ? 214 TYR E CE1 1 
ATOM   13617 C CE2 . TYR E  1 214 ? 157.595 12.719  -11.452 1.00   40.93  ? 214 TYR E CE2 1 
ATOM   13618 C CZ  . TYR E  1 214 ? 157.695 11.988  -12.621 1.00   41.11  ? 214 TYR E CZ  1 
ATOM   13619 O OH  . TYR E  1 214 ? 157.104 12.497  -13.761 1.00   39.22  ? 214 TYR E OH  1 
ATOM   13620 N N   . ILE E  1 215 ? 161.249 12.985  -7.830  1.00   45.72  ? 215 ILE E N   1 
ATOM   13621 C CA  . ILE E  1 215 ? 161.307 14.429  -7.682  1.00   44.50  ? 215 ILE E CA  1 
ATOM   13622 C C   . ILE E  1 215 ? 162.730 14.924  -7.472  1.00   48.13  ? 215 ILE E C   1 
ATOM   13623 O O   . ILE E  1 215 ? 162.938 16.098  -7.212  1.00   46.86  ? 215 ILE E O   1 
ATOM   13624 C CB  . ILE E  1 215 ? 160.397 14.901  -6.508  1.00   36.44  ? 215 ILE E CB  1 
ATOM   13625 C CG1 . ILE E  1 215 ? 160.763 14.175  -5.227  1.00   39.27  ? 215 ILE E CG1 1 
ATOM   13626 C CG2 . ILE E  1 215 ? 158.922 14.584  -6.810  1.00   35.71  ? 215 ILE E CG2 1 
ATOM   13627 C CD1 . ILE E  1 215 ? 161.594 14.960  -4.296  1.00   41.41  ? 215 ILE E CD1 1 
ATOM   13628 N N   . HIS E  1 216 ? 163.715 14.042  -7.618  1.00   53.18  ? 216 HIS E N   1 
ATOM   13629 C CA  . HIS E  1 216 ? 165.089 14.401  -7.305  1.00   56.70  ? 216 HIS E CA  1 
ATOM   13630 C C   . HIS E  1 216 ? 165.616 15.621  -8.054  1.00   55.61  ? 216 HIS E C   1 
ATOM   13631 O O   . HIS E  1 216 ? 166.328 16.438  -7.476  1.00   56.67  ? 216 HIS E O   1 
ATOM   13632 C CB  . HIS E  1 216 ? 166.027 13.239  -7.586  1.00   63.99  ? 216 HIS E CB  1 
ATOM   13633 C CG  . HIS E  1 216 ? 167.453 13.525  -7.216  1.00   70.80  ? 216 HIS E CG  1 
ATOM   13634 N ND1 . HIS E  1 216 ? 167.954 13.322  -5.946  1.00   72.99  ? 216 HIS E ND1 1 
ATOM   13635 C CD2 . HIS E  1 216 ? 168.473 14.046  -7.942  1.00   71.46  ? 216 HIS E CD2 1 
ATOM   13636 C CE1 . HIS E  1 216 ? 169.228 13.672  -5.915  1.00   74.06  ? 216 HIS E CE1 1 
ATOM   13637 N NE2 . HIS E  1 216 ? 169.564 14.122  -7.110  1.00   73.56  ? 216 HIS E NE2 1 
ATOM   13638 N N   . ASN E  1 217 ? 165.285 15.752  -9.330  1.00   52.96  ? 217 ASN E N   1 
ATOM   13639 C CA  . ASN E  1 217 ? 165.777 16.884  -10.103 1.00   54.09  ? 217 ASN E CA  1 
ATOM   13640 C C   . ASN E  1 217 ? 165.145 18.232  -9.681  1.00   50.81  ? 217 ASN E C   1 
ATOM   13641 O O   . ASN E  1 217 ? 165.550 19.291  -10.152 1.00   49.43  ? 217 ASN E O   1 
ATOM   13642 C CB  . ASN E  1 217 ? 165.592 16.616  -11.600 1.00   58.53  ? 217 ASN E CB  1 
ATOM   13643 C CG  . ASN E  1 217 ? 166.178 17.722  -12.473 1.00   61.93  ? 217 ASN E CG  1 
ATOM   13644 O OD1 . ASN E  1 217 ? 167.383 17.955  -12.470 1.00   64.48  ? 217 ASN E OD1 1 
ATOM   13645 N ND2 . ASN E  1 217 ? 165.330 18.373  -13.254 1.00   61.44  ? 217 ASN E ND2 1 
ATOM   13646 N N   . SER E  1 218 ? 164.124 18.201  -8.828  1.00   49.29  ? 218 SER E N   1 
ATOM   13647 C CA  . SER E  1 218 ? 163.495 19.449  -8.395  1.00   44.16  ? 218 SER E CA  1 
ATOM   13648 C C   . SER E  1 218 ? 163.889 19.878  -6.973  1.00   44.75  ? 218 SER E C   1 
ATOM   13649 O O   . SER E  1 218 ? 163.353 20.841  -6.451  1.00   43.44  ? 218 SER E O   1 
ATOM   13650 C CB  . SER E  1 218 ? 161.977 19.343  -8.493  1.00   39.79  ? 218 SER E CB  1 
ATOM   13651 O OG  . SER E  1 218 ? 161.445 18.637  -7.403  1.00   37.89  ? 218 SER E OG  1 
ATOM   13652 N N   . LEU E  1 219 ? 164.843 19.189  -6.358  1.00   46.38  ? 219 LEU E N   1 
ATOM   13653 C CA  . LEU E  1 219 ? 165.124 19.380  -4.937  1.00   45.45  ? 219 LEU E CA  1 
ATOM   13654 C C   . LEU E  1 219 ? 165.622 20.759  -4.535  1.00   45.63  ? 219 LEU E C   1 
ATOM   13655 O O   . LEU E  1 219 ? 165.352 21.214  -3.436  1.00   44.74  ? 219 LEU E O   1 
ATOM   13656 C CB  . LEU E  1 219 ? 166.138 18.347  -4.476  1.00   45.40  ? 219 LEU E CB  1 
ATOM   13657 C CG  . LEU E  1 219 ? 165.550 16.969  -4.195  1.00   43.83  ? 219 LEU E CG  1 
ATOM   13658 C CD1 . LEU E  1 219 ? 166.655 15.967  -3.889  1.00   46.05  ? 219 LEU E CD1 1 
ATOM   13659 C CD2 . LEU E  1 219 ? 164.570 17.053  -3.041  1.00   39.62  ? 219 LEU E CD2 1 
ATOM   13660 N N   . ASP E  1 220 ? 166.372 21.418  -5.402  1.00   48.44  ? 220 ASP E N   1 
ATOM   13661 C CA  . ASP E  1 220 ? 166.861 22.737  -5.052  1.00   52.40  ? 220 ASP E CA  1 
ATOM   13662 C C   . ASP E  1 220 ? 165.713 23.711  -5.036  1.00   47.70  ? 220 ASP E C   1 
ATOM   13663 O O   . ASP E  1 220 ? 165.655 24.575  -4.176  1.00   50.83  ? 220 ASP E O   1 
ATOM   13664 C CB  . ASP E  1 220 ? 167.963 23.213  -6.001  1.00   60.33  ? 220 ASP E CB  1 
ATOM   13665 C CG  . ASP E  1 220 ? 169.224 22.366  -5.909  1.00   70.10  ? 220 ASP E CG  1 
ATOM   13666 O OD1 . ASP E  1 220 ? 169.588 21.956  -4.780  1.00   74.20  ? 220 ASP E OD1 1 
ATOM   13667 O OD2 . ASP E  1 220 ? 169.855 22.128  -6.966  1.00   72.25  ? 220 ASP E OD2 1 
ATOM   13668 N N   . VAL E  1 221 ? 164.787 23.544  -5.974  1.00   40.65  ? 221 VAL E N   1 
ATOM   13669 C CA  . VAL E  1 221 ? 163.597 24.380  -6.057  1.00   35.89  ? 221 VAL E CA  1 
ATOM   13670 C C   . VAL E  1 221 ? 162.698 24.304  -4.805  1.00   36.51  ? 221 VAL E C   1 
ATOM   13671 O O   . VAL E  1 221 ? 162.251 25.331  -4.288  1.00   37.24  ? 221 VAL E O   1 
ATOM   13672 C CB  . VAL E  1 221 ? 162.765 23.990  -7.301  1.00   32.84  ? 221 VAL E CB  1 
ATOM   13673 C CG1 . VAL E  1 221 ? 161.548 24.847  -7.418  1.00   31.62  ? 221 VAL E CG1 1 
ATOM   13674 C CG2 . VAL E  1 221 ? 163.615 24.120  -8.557  1.00   33.64  ? 221 VAL E CG2 1 
ATOM   13675 N N   . LEU E  1 222 ? 162.444 23.087  -4.332  1.00   35.34  ? 222 LEU E N   1 
ATOM   13676 C CA  . LEU E  1 222 ? 161.593 22.841  -3.172  1.00   34.89  ? 222 LEU E CA  1 
ATOM   13677 C C   . LEU E  1 222 ? 162.178 23.417  -1.904  1.00   39.06  ? 222 LEU E C   1 
ATOM   13678 O O   . LEU E  1 222 ? 161.462 23.833  -1.002  1.00   42.48  ? 222 LEU E O   1 
ATOM   13679 C CB  . LEU E  1 222 ? 161.364 21.351  -2.988  1.00   34.52  ? 222 LEU E CB  1 
ATOM   13680 C CG  . LEU E  1 222 ? 160.594 20.621  -4.078  1.00   34.06  ? 222 LEU E CG  1 
ATOM   13681 C CD1 . LEU E  1 222 ? 160.417 19.184  -3.656  1.00   38.05  ? 222 LEU E CD1 1 
ATOM   13682 C CD2 . LEU E  1 222 ? 159.268 21.247  -4.278  1.00   31.87  ? 222 LEU E CD2 1 
ATOM   13683 N N   . HIS E  1 223 ? 163.497 23.397  -1.844  1.00   43.07  ? 223 HIS E N   1 
ATOM   13684 C CA  . HIS E  1 223 ? 164.248 23.915  -0.712  1.00   49.78  ? 223 HIS E CA  1 
ATOM   13685 C C   . HIS E  1 223 ? 163.947 25.388  -0.505  1.00   49.05  ? 223 HIS E C   1 
ATOM   13686 O O   . HIS E  1 223 ? 163.922 25.876  0.622   1.00   51.26  ? 223 HIS E O   1 
ATOM   13687 C CB  . HIS E  1 223 ? 165.750 23.702  -0.962  1.00   54.50  ? 223 HIS E CB  1 
ATOM   13688 C CG  . HIS E  1 223 ? 166.645 24.207  0.128   1.00   63.30  ? 223 HIS E CG  1 
ATOM   13689 N ND1 . HIS E  1 223 ? 166.732 23.607  1.367   1.00   68.00  ? 223 HIS E ND1 1 
ATOM   13690 C CD2 . HIS E  1 223 ? 167.540 25.228  0.146   1.00   67.46  ? 223 HIS E CD2 1 
ATOM   13691 C CE1 . HIS E  1 223 ? 167.618 24.252  2.107   1.00   71.07  ? 223 HIS E CE1 1 
ATOM   13692 N NE2 . HIS E  1 223 ? 168.125 25.240  1.389   1.00   70.31  ? 223 HIS E NE2 1 
ATOM   13693 N N   . ASP E  1 224 ? 163.694 26.081  -1.609  1.00   46.12  ? 224 ASP E N   1 
ATOM   13694 C CA  . ASP E  1 224 ? 163.517 27.519  -1.583  1.00   45.78  ? 224 ASP E CA  1 
ATOM   13695 C C   . ASP E  1 224 ? 162.072 27.975  -1.731  1.00   40.61  ? 224 ASP E C   1 
ATOM   13696 O O   . ASP E  1 224 ? 161.830 29.178  -1.870  1.00   40.56  ? 224 ASP E O   1 
ATOM   13697 C CB  . ASP E  1 224 ? 164.343 28.176  -2.692  1.00   50.08  ? 224 ASP E CB  1 
ATOM   13698 C CG  . ASP E  1 224 ? 165.819 27.981  -2.509  1.00   56.83  ? 224 ASP E CG  1 
ATOM   13699 O OD1 . ASP E  1 224 ? 166.260 27.748  -1.363  1.00   61.65  ? 224 ASP E OD1 1 
ATOM   13700 O OD2 . ASP E  1 224 ? 166.550 28.101  -3.512  1.00   57.98  1 224 ASP E OD2 1 
ATOM   13701 N N   . LEU E  1 225 ? 161.121 27.042  -1.682  1.00   37.49  ? 225 LEU E N   1 
ATOM   13702 C CA  . LEU E  1 225 ? 159.725 27.417  -1.802  1.00   34.85  ? 225 LEU E CA  1 
ATOM   13703 C C   . LEU E  1 225 ? 159.278 28.390  -0.731  1.00   35.41  ? 225 LEU E C   1 
ATOM   13704 O O   . LEU E  1 225 ? 159.646 28.255  0.435   1.00   36.74  ? 225 LEU E O   1 
ATOM   13705 C CB  . LEU E  1 225 ? 158.797 26.226  -1.723  1.00   34.72  ? 225 LEU E CB  1 
ATOM   13706 C CG  . LEU E  1 225 ? 158.577 25.239  -2.849  1.00   34.69  ? 225 LEU E CG  1 
ATOM   13707 C CD1 . LEU E  1 225 ? 157.293 24.534  -2.498  1.00   34.40  ? 225 LEU E CD1 1 
ATOM   13708 C CD2 . LEU E  1 225 ? 158.509 25.822  -4.246  1.00   33.55  ? 225 LEU E CD2 1 
ATOM   13709 N N   . VAL E  1 226 ? 158.425 29.324  -1.143  1.00   34.25  ? 226 VAL E N   1 
ATOM   13710 C CA  . VAL E  1 226 ? 157.817 30.311  -0.271  1.00   34.31  ? 226 VAL E CA  1 
ATOM   13711 C C   . VAL E  1 226 ? 156.308 30.026  -0.180  1.00   33.66  ? 226 VAL E C   1 
ATOM   13712 O O   . VAL E  1 226 ? 155.682 29.665  -1.167  1.00   33.49  ? 226 VAL E O   1 
ATOM   13713 C CB  . VAL E  1 226 ? 158.079 31.752  -0.802  1.00   38.66  ? 226 VAL E CB  1 
ATOM   13714 C CG1 . VAL E  1 226 ? 157.157 32.758  -0.156  1.00   41.59  ? 226 VAL E CG1 1 
ATOM   13715 C CG2 . VAL E  1 226 ? 159.487 32.166  -0.523  1.00   37.75  ? 226 VAL E CG2 1 
ATOM   13716 N N   . TYR E  1 227 ? 155.736 30.172  1.008   1.00   33.85  ? 227 TYR E N   1 
ATOM   13717 C CA  . TYR E  1 227 ? 154.336 29.830  1.238   1.00   33.62  ? 227 TYR E CA  1 
ATOM   13718 C C   . TYR E  1 227 ? 153.479 31.023  1.653   1.00   32.34  ? 227 TYR E C   1 
ATOM   13719 O O   . TYR E  1 227 ? 153.976 31.976  2.241   1.00   33.68  ? 227 TYR E O   1 
ATOM   13720 C CB  . TYR E  1 227 ? 154.232 28.734  2.312   1.00   36.11  ? 227 TYR E CB  1 
ATOM   13721 C CG  . TYR E  1 227 ? 154.835 27.403  1.908   1.00   39.85  ? 227 TYR E CG  1 
ATOM   13722 C CD1 . TYR E  1 227 ? 154.095 26.476  1.178   1.00   40.62  ? 227 TYR E CD1 1 
ATOM   13723 C CD2 . TYR E  1 227 ? 156.146 27.080  2.247   1.00   46.43  ? 227 TYR E CD2 1 
ATOM   13724 C CE1 . TYR E  1 227 ? 154.633 25.273  0.803   1.00   44.42  ? 227 TYR E CE1 1 
ATOM   13725 C CE2 . TYR E  1 227 ? 156.700 25.869  1.878   1.00   49.89  ? 227 TYR E CE2 1 
ATOM   13726 C CZ  . TYR E  1 227 ? 155.939 24.973  1.153   1.00   50.52  ? 227 TYR E CZ  1 
ATOM   13727 O OH  . TYR E  1 227 ? 156.484 23.761  0.791   1.00   55.51  ? 227 TYR E OH  1 
ATOM   13728 N N   . THR E  1 228 ? 152.188 30.962  1.338   1.00   32.15  ? 228 THR E N   1 
ATOM   13729 C CA  . THR E  1 228 ? 151.224 31.974  1.791   1.00   35.13  ? 228 THR E CA  1 
ATOM   13730 C C   . THR E  1 228 ? 149.886 31.265  2.034   1.00   33.63  ? 228 THR E C   1 
ATOM   13731 O O   . THR E  1 228 ? 149.604 30.247  1.396   1.00   32.87  ? 228 THR E O   1 
ATOM   13732 C CB  . THR E  1 228 ? 151.071 33.152  0.765   1.00   34.26  ? 228 THR E CB  1 
ATOM   13733 O OG1 . THR E  1 228 ? 150.410 34.279  1.363   1.00   37.21  ? 228 THR E OG1 1 
ATOM   13734 C CG2 . THR E  1 228 ? 150.331 32.700  -0.463  1.00   30.13  ? 228 THR E CG2 1 
ATOM   13735 N N   . PRO E  1 229 ? 149.060 31.786  2.965   1.00   35.11  ? 229 PRO E N   1 
ATOM   13736 C CA  . PRO E  1 229 ? 147.811 31.083  3.290   1.00   33.99  ? 229 PRO E CA  1 
ATOM   13737 C C   . PRO E  1 229 ? 146.838 30.979  2.118   1.00   33.28  ? 229 PRO E C   1 
ATOM   13738 O O   . PRO E  1 229 ? 146.652 31.889  1.308   1.00   33.28  ? 229 PRO E O   1 
ATOM   13739 C CB  . PRO E  1 229 ? 147.208 31.944  4.407   1.00   34.64  ? 229 PRO E CB  1 
ATOM   13740 C CG  . PRO E  1 229 ? 148.392 32.645  5.027   1.00   36.07  ? 229 PRO E CG  1 
ATOM   13741 C CD  . PRO E  1 229 ? 149.290 32.941  3.858   1.00   34.85  ? 229 PRO E CD  1 
ATOM   13742 N N   . LEU E  1 230 ? 146.202 29.825  2.045   1.00   34.16  ? 230 LEU E N   1 
ATOM   13743 C CA  . LEU E  1 230 ? 145.231 29.554  1.005   1.00   33.60  ? 230 LEU E CA  1 
ATOM   13744 C C   . LEU E  1 230 ? 143.824 29.625  1.592   1.00   36.42  ? 230 LEU E C   1 
ATOM   13745 O O   . LEU E  1 230 ? 143.562 29.042  2.653   1.00   37.06  ? 230 LEU E O   1 
ATOM   13746 C CB  . LEU E  1 230 ? 145.475 28.183  0.401   1.00   30.56  ? 230 LEU E CB  1 
ATOM   13747 C CG  . LEU E  1 230 ? 144.543 27.675  -0.689  1.00   27.19  ? 230 LEU E CG  1 
ATOM   13748 C CD1 . LEU E  1 230 ? 144.691 28.542  -1.908  1.00   25.32  ? 230 LEU E CD1 1 
ATOM   13749 C CD2 . LEU E  1 230 ? 144.849 26.215  -0.998  1.00   25.41  ? 230 LEU E CD2 1 
ATOM   13750 N N   . THR E  1 231 ? 142.932 30.352  0.918   1.00   36.35  ? 231 THR E N   1 
ATOM   13751 C CA  . THR E  1 231 ? 141.525 30.405  1.305   1.00   36.46  ? 231 THR E CA  1 
ATOM   13752 C C   . THR E  1 231 ? 140.635 29.925  0.159   1.00   36.50  ? 231 THR E C   1 
ATOM   13753 O O   . THR E  1 231 ? 140.988 30.089  -1.012  1.00   36.07  ? 231 THR E O   1 
ATOM   13754 C CB  . THR E  1 231 ? 141.093 31.833  1.703   1.00   35.15  ? 231 THR E CB  1 
ATOM   13755 O OG1 . THR E  1 231 ? 141.554 32.771  0.719   1.00   33.44  ? 231 THR E OG1 1 
ATOM   13756 C CG2 . THR E  1 231 ? 141.631 32.200  3.085   1.00   33.74  ? 231 THR E CG2 1 
ATOM   13757 N N   . ILE E  1 232 ? 139.467 29.376  0.501   1.00   36.41  ? 232 ILE E N   1 
ATOM   13758 C CA  . ILE E  1 232 ? 138.588 28.719  -0.470  1.00   34.72  ? 232 ILE E CA  1 
ATOM   13759 C C   . ILE E  1 232 ? 137.222 29.375  -0.469  1.00   35.59  ? 232 ILE E C   1 
ATOM   13760 O O   . ILE E  1 232 ? 136.658 29.581  0.608   1.00   39.56  ? 232 ILE E O   1 
ATOM   13761 C CB  . ILE E  1 232 ? 138.417 27.228  -0.164  1.00   29.90  ? 232 ILE E CB  1 
ATOM   13762 C CG1 . ILE E  1 232 ? 139.782 26.554  -0.080  1.00   27.10  ? 232 ILE E CG1 1 
ATOM   13763 C CG2 . ILE E  1 232 ? 137.554 26.577  -1.228  1.00   29.97  ? 232 ILE E CG2 1 
ATOM   13764 C CD1 . ILE E  1 232 ? 140.557 26.603  -1.372  1.00   25.61  ? 232 ILE E CD1 1 
ATOM   13765 N N   . SER E  1 233 ? 136.681 29.711  -1.644  1.00   32.97  ? 233 SER E N   1 
ATOM   13766 C CA  . SER E  1 233 ? 135.362 30.356  -1.677  1.00   34.05  ? 233 SER E CA  1 
ATOM   13767 C C   . SER E  1 233 ? 134.269 29.336  -1.434  1.00   34.00  ? 233 SER E C   1 
ATOM   13768 O O   . SER E  1 233 ? 134.522 28.140  -1.481  1.00   32.58  ? 233 SER E O   1 
ATOM   13769 C CB  . SER E  1 233 ? 135.098 31.062  -3.009  1.00   32.46  ? 233 SER E CB  1 
ATOM   13770 O OG  . SER E  1 233 ? 134.791 30.135  -4.030  1.00   31.96  ? 233 SER E OG  1 
ATOM   13771 N N   . LYS E  1 234 ? 133.045 29.818  -1.222  1.00   38.49  ? 234 LYS E N   1 
ATOM   13772 C CA  . LYS E  1 234 ? 131.909 28.940  -0.972  1.00   44.50  ? 234 LYS E CA  1 
ATOM   13773 C C   . LYS E  1 234 ? 131.635 28.078  -2.210  1.00   48.65  ? 234 LYS E C   1 
ATOM   13774 O O   . LYS E  1 234 ? 130.907 27.089  -2.143  1.00   49.10  ? 234 LYS E O   1 
ATOM   13775 C CB  . LYS E  1 234 ? 130.670 29.736  -0.543  1.00   48.28  ? 234 LYS E CB  1 
ATOM   13776 C CG  . LYS E  1 234 ? 129.709 30.079  -1.655  1.00   51.31  ? 234 LYS E CG  1 
ATOM   13777 C CD  . LYS E  1 234 ? 128.765 31.199  -1.243  0.0000 53.47  ? 234 LYS E CD  1 
ATOM   13778 C CE  . LYS E  1 234 ? 127.928 31.692  -2.416  0.0000 52.84  ? 234 LYS E CE  1 
ATOM   13779 N NZ  . LYS E  1 234 ? 128.745 31.916  -3.640  0.0000 49.28  ? 234 LYS E NZ  1 
ATOM   13780 N N   . GLN E  1 235 ? 132.225 28.452  -3.342  1.00   51.63  ? 235 GLN E N   1 
ATOM   13781 C CA  . GLN E  1 235 ? 132.083 27.646  -4.547  1.00   51.22  ? 235 GLN E CA  1 
ATOM   13782 C C   . GLN E  1 235 ? 133.325 26.784  -4.879  1.00   43.73  ? 235 GLN E C   1 
ATOM   13783 O O   . GLN E  1 235 ? 133.417 26.147  -5.940  1.00   41.59  ? 235 GLN E O   1 
ATOM   13784 C CB  . GLN E  1 235 ? 131.656 28.537  -5.686  1.00   58.34  ? 235 GLN E CB  1 
ATOM   13785 C CG  . GLN E  1 235 ? 130.202 28.189  -5.992  1.00   68.49  ? 235 GLN E CG  1 
ATOM   13786 C CD  . GLN E  1 235 ? 129.612 28.984  -7.117  1.00   78.10  ? 235 GLN E CD  1 
ATOM   13787 O OE1 . GLN E  1 235 ? 130.198 29.984  -7.538  1.00   80.67  ? 235 GLN E OE1 1 
ATOM   13788 N NE2 . GLN E  1 235 ? 128.433 28.576  -7.595  1.00   82.99  ? 235 GLN E NE2 1 
ATOM   13789 N N   . GLY E  1 236 ? 134.281 26.769  -3.958  1.00   36.36  ? 236 GLY E N   1 
ATOM   13790 C CA  . GLY E  1 236 ? 135.408 25.874  -4.073  1.00   31.41  ? 236 GLY E CA  1 
ATOM   13791 C C   . GLY E  1 236 ? 136.595 26.374  -4.872  1.00   29.46  ? 236 GLY E C   1 
ATOM   13792 O O   . GLY E  1 236 ? 137.426 25.581  -5.308  1.00   27.50  ? 236 GLY E O   1 
ATOM   13793 N N   . GLU E  1 237 ? 136.675 27.683  -5.069  1.00   31.02  ? 237 GLU E N   1 
ATOM   13794 C CA  . GLU E  1 237 ? 137.779 28.303  -5.812  1.00   30.53  ? 237 GLU E CA  1 
ATOM   13795 C C   . GLU E  1 237 ? 138.962 28.641  -4.904  1.00   30.82  ? 237 GLU E C   1 
ATOM   13796 O O   . GLU E  1 237 ? 138.799 28.861  -3.705  1.00   32.07  ? 237 GLU E O   1 
ATOM   13797 C CB  . GLU E  1 237 ? 137.317 29.580  -6.530  1.00   32.21  ? 237 GLU E CB  1 
ATOM   13798 C CG  . GLU E  1 237 ? 136.176 29.439  -7.528  1.00   34.56  ? 237 GLU E CG  1 
ATOM   13799 C CD  . GLU E  1 237 ? 135.391 30.719  -7.684  1.00   40.11  ? 237 GLU E CD  1 
ATOM   13800 O OE1 . GLU E  1 237 ? 134.763 31.139  -6.693  1.00   43.22  ? 237 GLU E OE1 1 
ATOM   13801 O OE2 . GLU E  1 237 ? 135.431 31.333  -8.774  1.00   43.19  1 237 GLU E OE2 1 
ATOM   13802 N N   . TYR E  1 238 ? 140.149 28.672  -5.491  1.00   28.88  ? 238 TYR E N   1 
ATOM   13803 C CA  . TYR E  1 238 ? 141.383 28.957  -4.761  1.00   28.17  ? 238 TYR E CA  1 
ATOM   13804 C C   . TYR E  1 238 ? 141.742 30.440  -4.760  1.00   27.89  ? 238 TYR E C   1 
ATOM   13805 O O   . TYR E  1 238 ? 141.802 31.063  -5.811  1.00   26.28  ? 238 TYR E O   1 
ATOM   13806 C CB  . TYR E  1 238 ? 142.520 28.164  -5.376  1.00   26.27  ? 238 TYR E CB  1 
ATOM   13807 C CG  . TYR E  1 238 ? 142.293 26.665  -5.348  1.00   28.01  ? 238 TYR E CG  1 
ATOM   13808 C CD1 . TYR E  1 238 ? 142.493 25.929  -4.191  1.00   28.15  ? 238 TYR E CD1 1 
ATOM   13809 C CD2 . TYR E  1 238 ? 141.831 26.000  -6.467  1.00   25.88  ? 238 TYR E CD2 1 
ATOM   13810 C CE1 . TYR E  1 238 ? 142.290 24.558  -4.166  1.00   26.97  ? 238 TYR E CE1 1 
ATOM   13811 C CE2 . TYR E  1 238 ? 141.617 24.651  -6.446  1.00   26.23  ? 238 TYR E CE2 1 
ATOM   13812 C CZ  . TYR E  1 238 ? 141.850 23.933  -5.293  1.00   26.37  ? 238 TYR E CZ  1 
ATOM   13813 O OH  . TYR E  1 238 ? 141.632 22.582  -5.279  1.00   26.16  ? 238 TYR E OH  1 
ATOM   13814 N N   . PHE E  1 239 ? 141.972 30.994  -3.570  1.00   28.80  ? 239 PHE E N   1 
ATOM   13815 C CA  . PHE E  1 239 ? 142.288 32.400  -3.400  1.00   30.51  ? 239 PHE E CA  1 
ATOM   13816 C C   . PHE E  1 239 ? 143.533 32.562  -2.546  1.00   30.30  ? 239 PHE E C   1 
ATOM   13817 O O   . PHE E  1 239 ? 143.767 31.774  -1.653  1.00   30.53  ? 239 PHE E O   1 
ATOM   13818 C CB  . PHE E  1 239 ? 141.132 33.172  -2.723  1.00   30.93  ? 239 PHE E CB  1 
ATOM   13819 C CG  . PHE E  1 239 ? 139.969 33.505  -3.636  1.00   31.97  ? 239 PHE E CG  1 
ATOM   13820 C CD1 . PHE E  1 239 ? 138.923 32.602  -3.820  1.00   31.88  ? 239 PHE E CD1 1 
ATOM   13821 C CD2 . PHE E  1 239 ? 139.921 34.721  -4.314  1.00   31.63  ? 239 PHE E CD2 1 
ATOM   13822 C CE1 . PHE E  1 239 ? 137.857 32.908  -4.660  1.00   31.86  ? 239 PHE E CE1 1 
ATOM   13823 C CE2 . PHE E  1 239 ? 138.857 35.029  -5.158  1.00   32.35  ? 239 PHE E CE2 1 
ATOM   13824 C CZ  . PHE E  1 239 ? 137.826 34.123  -5.331  1.00   31.12  ? 239 PHE E CZ  1 
ATOM   13825 N N   . ILE E  1 240 ? 144.328 33.592  -2.816  1.00   31.09  ? 240 ILE E N   1 
ATOM   13826 C CA  . ILE E  1 240 ? 145.351 34.027  -1.875  1.00   30.22  ? 240 ILE E CA  1 
ATOM   13827 C C   . ILE E  1 240 ? 145.198 35.523  -1.607  1.00   33.69  ? 240 ILE E C   1 
ATOM   13828 O O   . ILE E  1 240 ? 144.412 36.181  -2.269  1.00   38.27  ? 240 ILE E O   1 
ATOM   13829 C CB  . ILE E  1 240 ? 146.748 33.746  -2.383  1.00   27.29  ? 240 ILE E CB  1 
ATOM   13830 C CG1 . ILE E  1 240 ? 146.914 34.353  -3.773  1.00   28.59  ? 240 ILE E CG1 1 
ATOM   13831 C CG2 . ILE E  1 240 ? 146.988 32.247  -2.417  1.00   27.73  ? 240 ILE E CG2 1 
ATOM   13832 C CD1 . ILE E  1 240 ? 148.335 34.411  -4.265  1.00   28.55  ? 240 ILE E CD1 1 
ATOM   13833 N N   . GLN E  1 241 ? 145.943 36.055  -0.643  1.00   33.59  ? 241 GLN E N   1 
ATOM   13834 C CA  . GLN E  1 241 ? 145.867 37.475  -0.291  1.00   36.49  ? 241 GLN E CA  1 
ATOM   13835 C C   . GLN E  1 241 ? 147.012 38.307  -0.858  1.00   37.74  ? 241 GLN E C   1 
ATOM   13836 O O   . GLN E  1 241 ? 148.177 38.060  -0.568  1.00   36.88  ? 241 GLN E O   1 
ATOM   13837 C CB  . GLN E  1 241 ? 145.838 37.644  1.235   1.00   39.70  ? 241 GLN E CB  1 
ATOM   13838 C CG  . GLN E  1 241 ? 145.994 39.084  1.739   1.00   43.29  ? 241 GLN E CG  1 
ATOM   13839 C CD  . GLN E  1 241 ? 144.927 40.006  1.198   1.00   44.46  ? 241 GLN E CD  1 
ATOM   13840 O OE1 . GLN E  1 241 ? 143.854 39.553  0.818   1.00   44.48  ? 241 GLN E OE1 1 
ATOM   13841 N NE2 . GLN E  1 241 ? 145.215 41.307  1.159   1.00   43.86  ? 241 GLN E NE2 1 
ATOM   13842 N N   . VAL E  1 242 ? 146.669 39.286  -1.689  1.00   37.28  ? 242 VAL E N   1 
ATOM   13843 C CA  . VAL E  1 242 ? 147.642 40.262  -2.195  1.00   35.06  ? 242 VAL E CA  1 
ATOM   13844 C C   . VAL E  1 242 ? 147.390 41.595  -1.515  1.00   36.96  ? 242 VAL E C   1 
ATOM   13845 O O   . VAL E  1 242 ? 146.329 42.214  -1.677  1.00   37.85  ? 242 VAL E O   1 
ATOM   13846 C CB  . VAL E  1 242 ? 147.574 40.391  -3.730  1.00   32.60  ? 242 VAL E CB  1 
ATOM   13847 C CG1 . VAL E  1 242 ? 148.449 41.509  -4.231  1.00   32.33  ? 242 VAL E CG1 1 
ATOM   13848 C CG2 . VAL E  1 242 ? 147.984 39.077  -4.368  1.00   31.29  ? 242 VAL E CG2 1 
ATOM   13849 N N   . ASN E  1 243 ? 148.356 41.997  -0.697  1.00   39.17  ? 243 ASN E N   1 
ATOM   13850 C CA  . ASN E  1 243 ? 148.285 43.253  0.031   1.00   40.21  ? 243 ASN E CA  1 
ATOM   13851 C C   . ASN E  1 243 ? 148.560 44.449  -0.853  1.00   36.20  ? 243 ASN E C   1 
ATOM   13852 O O   . ASN E  1 243 ? 148.057 45.532  -0.595  1.00   36.10  ? 243 ASN E O   1 
ATOM   13853 C CB  . ASN E  1 243 ? 149.271 43.247  1.193   1.00   43.09  ? 243 ASN E CB  1 
ATOM   13854 C CG  . ASN E  1 243 ? 148.710 42.587  2.424   1.00   45.16  ? 243 ASN E CG  1 
ATOM   13855 O OD1 . ASN E  1 243 ? 147.573 42.103  2.433   1.00   47.27  ? 243 ASN E OD1 1 
ATOM   13856 N ND2 . ASN E  1 243 ? 149.508 42.553  3.474   1.00   45.39  ? 243 ASN E ND2 1 
ATOM   13857 N N   . ALA E  1 244 ? 149.385 44.246  -1.875  1.00   34.47  ? 244 ALA E N   1 
ATOM   13858 C CA  . ALA E  1 244 ? 149.741 45.304  -2.809  1.00   33.81  ? 244 ALA E CA  1 
ATOM   13859 C C   . ALA E  1 244 ? 150.377 44.741  -4.070  1.00   33.64  ? 244 ALA E C   1 
ATOM   13860 O O   . ALA E  1 244 ? 150.950 43.659  -4.066  1.00   34.79  ? 244 ALA E O   1 
ATOM   13861 C CB  . ALA E  1 244 ? 150.691 46.306  -2.153  1.00   33.39  ? 244 ALA E CB  1 
ATOM   13862 N N   . ILE E  1 245 ? 150.276 45.497  -5.148  1.00   35.17  ? 245 ILE E N   1 
ATOM   13863 C CA  . ILE E  1 245 ? 151.079 45.273  -6.335  1.00   36.83  ? 245 ILE E CA  1 
ATOM   13864 C C   . ILE E  1 245 ? 152.167 46.354  -6.427  1.00   38.84  ? 245 ILE E C   1 
ATOM   13865 O O   . ILE E  1 245 ? 151.855 47.543  -6.606  1.00   38.20  ? 245 ILE E O   1 
ATOM   13866 C CB  . ILE E  1 245 ? 150.201 45.306  -7.574  1.00   37.57  ? 245 ILE E CB  1 
ATOM   13867 C CG1 . ILE E  1 245 ? 149.018 44.371  -7.367  1.00   39.07  ? 245 ILE E CG1 1 
ATOM   13868 C CG2 . ILE E  1 245 ? 150.994 44.951  -8.803  1.00   36.87  ? 245 ILE E CG2 1 
ATOM   13869 C CD1 . ILE E  1 245 ? 147.923 44.574  -8.358  1.00   40.93  ? 245 ILE E CD1 1 
ATOM   13870 N N   . ARG E  1 246 ? 153.437 45.939  -6.357  1.00   41.32  ? 246 ARG E N   1 
ATOM   13871 C CA  . ARG E  1 246 ? 154.565 46.884  -6.346  1.00   44.48  ? 246 ARG E CA  1 
ATOM   13872 C C   . ARG E  1 246 ? 155.240 47.016  -7.701  1.00   42.70  ? 246 ARG E C   1 
ATOM   13873 O O   . ARG E  1 246 ? 155.572 46.017  -8.314  1.00   42.61  ? 246 ARG E O   1 
ATOM   13874 C CB  . ARG E  1 246 ? 155.604 46.460  -5.314  1.00   47.35  ? 246 ARG E CB  1 
ATOM   13875 C CG  . ARG E  1 246 ? 156.816 47.371  -5.229  1.00   54.01  ? 246 ARG E CG  1 
ATOM   13876 C CD  . ARG E  1 246 ? 158.069 46.573  -4.821  1.00   59.93  ? 246 ARG E CD  1 
ATOM   13877 N NE  . ARG E  1 246 ? 158.151 46.246  -3.394  1.00   61.25  ? 246 ARG E NE  1 
ATOM   13878 C CZ  . ARG E  1 246 ? 158.737 45.152  -2.903  1.00   62.31  ? 246 ARG E CZ  1 
ATOM   13879 N NH1 . ARG E  1 246 ? 159.279 44.255  -3.717  1.00   60.66  ? 246 ARG E NH1 1 
ATOM   13880 N NH2 . ARG E  1 246 ? 158.772 44.946  -1.590  1.00   64.18  ? 246 ARG E NH2 1 
ATOM   13881 N N   . VAL E  1 247 ? 155.418 48.252  -8.161  1.00   43.72  ? 247 VAL E N   1 
ATOM   13882 C CA  . VAL E  1 247 ? 156.214 48.571  -9.343  1.00   43.00  ? 247 VAL E CA  1 
ATOM   13883 C C   . VAL E  1 247 ? 157.273 49.571  -8.921  1.00   44.66  ? 247 VAL E C   1 
ATOM   13884 O O   . VAL E  1 247 ? 156.941 50.698  -8.562  1.00   46.04  ? 247 VAL E O   1 
ATOM   13885 C CB  . VAL E  1 247 ? 155.376 49.180  -10.497 1.00   43.79  ? 247 VAL E CB  1 
ATOM   13886 C CG1 . VAL E  1 247 ? 156.256 49.406  -11.723 1.00   45.42  ? 247 VAL E CG1 1 
ATOM   13887 C CG2 . VAL E  1 247 ? 154.198 48.301  -10.849 1.00   40.70  ? 247 VAL E CG2 1 
ATOM   13888 N N   . ASN E  1 248 ? 158.532 49.148  -8.930  1.00   47.74  ? 248 ASN E N   1 
ATOM   13889 C CA  . ASN E  1 248 ? 159.624 49.926  -8.378  1.00   50.59  ? 248 ASN E CA  1 
ATOM   13890 C C   . ASN E  1 248 ? 159.265 50.330  -6.958  1.00   50.97  ? 248 ASN E C   1 
ATOM   13891 O O   . ASN E  1 248 ? 159.088 49.470  -6.103  1.00   50.82  ? 248 ASN E O   1 
ATOM   13892 C CB  . ASN E  1 248 ? 159.904 51.144  -9.241  1.00   58.30  ? 248 ASN E CB  1 
ATOM   13893 C CG  . ASN E  1 248 ? 160.452 50.773  -10.601 1.00   63.02  ? 248 ASN E CG  1 
ATOM   13894 O OD1 . ASN E  1 248 ? 160.957 49.668  -10.796 1.00   63.01  ? 248 ASN E OD1 1 
ATOM   13895 N ND2 . ASN E  1 248 ? 160.363 51.699  -11.550 1.00   66.91  ? 248 ASN E ND2 1 
ATOM   13896 N N   . LYS E  1 249 ? 159.070 51.617  -6.707  1.00   52.03  ? 249 LYS E N   1 
ATOM   13897 C CA  . LYS E  1 249 ? 158.676 52.016  -5.363  1.00   51.60  ? 249 LYS E CA  1 
ATOM   13898 C C   . LYS E  1 249 ? 157.222 52.508  -5.286  1.00   50.28  ? 249 LYS E C   1 
ATOM   13899 O O   . LYS E  1 249 ? 156.843 53.187  -4.332  1.00   48.45  ? 249 LYS E O   1 
ATOM   13900 C CB  . LYS E  1 249 ? 159.623 53.089  -4.813  1.00   55.04  ? 249 LYS E CB  1 
ATOM   13901 C CG  . LYS E  1 249 ? 161.117 52.718  -4.858  1.00   57.00  ? 249 LYS E CG  1 
ATOM   13902 C CD  . LYS E  1 249 ? 161.941 53.760  -4.118  1.00   59.46  ? 249 LYS E CD  1 
ATOM   13903 C CE  . LYS E  1 249 ? 163.432 53.676  -4.380  1.00   60.67  ? 249 LYS E CE  1 
ATOM   13904 N NZ  . LYS E  1 249 ? 164.181 54.685  -3.547  1.00   60.98  ? 249 LYS E NZ  1 
ATOM   13905 N N   . HIS E  1 250 ? 156.392 52.124  -6.252  1.00   48.82  ? 250 HIS E N   1 
ATOM   13906 C CA  . HIS E  1 250 ? 154.985 52.492  -6.195  1.00   48.00  ? 250 HIS E CA  1 
ATOM   13907 C C   . HIS E  1 250 ? 154.148 51.272  -5.794  1.00   47.61  ? 250 HIS E C   1 
ATOM   13908 O O   . HIS E  1 250 ? 154.209 50.241  -6.449  1.00   48.29  ? 250 HIS E O   1 
ATOM   13909 C CB  . HIS E  1 250 ? 154.558 53.046  -7.556  1.00   47.99  ? 250 HIS E CB  1 
ATOM   13910 C CG  . HIS E  1 250 ? 155.244 54.334  -7.915  1.00   50.63  ? 250 HIS E CG  1 
ATOM   13911 N ND1 . HIS E  1 250 ? 155.154 54.911  -9.163  1.00   50.07  ? 250 HIS E ND1 1 
ATOM   13912 C CD2 . HIS E  1 250 ? 156.065 55.131  -7.194  1.00   49.89  ? 250 HIS E CD2 1 
ATOM   13913 C CE1 . HIS E  1 250 ? 155.868 56.021  -9.188  1.00   53.32  ? 250 HIS E CE1 1 
ATOM   13914 N NE2 . HIS E  1 250 ? 156.438 56.174  -8.007  1.00   53.18  ? 250 HIS E NE2 1 
ATOM   13915 N N   . LEU E  1 251 ? 153.334 51.395  -4.745  1.00   47.25  ? 251 LEU E N   1 
ATOM   13916 C CA  . LEU E  1 251 ? 152.501 50.278  -4.279  1.00   43.07  ? 251 LEU E CA  1 
ATOM   13917 C C   . LEU E  1 251 ? 151.014 50.513  -4.426  1.00   37.03  ? 251 LEU E C   1 
ATOM   13918 O O   . LEU E  1 251 ? 150.454 51.352  -3.760  1.00   38.60  ? 251 LEU E O   1 
ATOM   13919 C CB  . LEU E  1 251 ? 152.802 49.968  -2.817  1.00   42.16  ? 251 LEU E CB  1 
ATOM   13920 C CG  . LEU E  1 251 ? 154.157 49.329  -2.510  1.00   43.27  ? 251 LEU E CG  1 
ATOM   13921 C CD1 . LEU E  1 251 ? 155.193 50.361  -2.168  1.00   46.39  ? 251 LEU E CD1 1 
ATOM   13922 C CD2 . LEU E  1 251 ? 154.026 48.327  -1.380  1.00   42.39  ? 251 LEU E CD2 1 
ATOM   13923 N N   . VAL E  1 252 ? 150.377 49.655  -5.210  1.00   36.98  ? 252 VAL E N   1 
ATOM   13924 C CA  . VAL E  1 252 ? 148.945 49.689  -5.479  1.00   37.35  ? 252 VAL E CA  1 
ATOM   13925 C C   . VAL E  1 252 ? 148.178 48.773  -4.548  1.00   37.56  ? 252 VAL E C   1 
ATOM   13926 O O   . VAL E  1 252 ? 148.450 47.581  -4.513  1.00   41.19  ? 252 VAL E O   1 
ATOM   13927 C CB  . VAL E  1 252 ? 148.663 49.304  -6.947  1.00   35.28  ? 252 VAL E CB  1 
ATOM   13928 C CG1 . VAL E  1 252 ? 147.208 49.327  -7.232  1.00   35.03  ? 252 VAL E CG1 1 
ATOM   13929 C CG2 . VAL E  1 252 ? 149.393 50.259  -7.873  1.00   37.84  ? 252 VAL E CG2 1 
ATOM   13930 N N   . ILE E  1 253 ? 147.243 49.329  -3.784  1.00   37.63  ? 253 ILE E N   1 
ATOM   13931 C CA  . ILE E  1 253 ? 146.533 48.580  -2.750  1.00   40.33  ? 253 ILE E CA  1 
ATOM   13932 C C   . ILE E  1 253 ? 145.172 48.170  -3.291  1.00   44.12  ? 253 ILE E C   1 
ATOM   13933 O O   . ILE E  1 253 ? 144.297 49.020  -3.474  1.00   46.97  ? 253 ILE E O   1 
ATOM   13934 C CB  . ILE E  1 253 ? 146.327 49.404  -1.462  1.00   40.84  ? 253 ILE E CB  1 
ATOM   13935 C CG1 . ILE E  1 253 ? 147.610 50.119  -1.063  1.00   37.98  ? 253 ILE E CG1 1 
ATOM   13936 C CG2 . ILE E  1 253 ? 145.727 48.541  -0.345  1.00   40.95  ? 253 ILE E CG2 1 
ATOM   13937 C CD1 . ILE E  1 253 ? 148.798 49.235  -1.012  1.00   36.23  ? 253 ILE E CD1 1 
ATOM   13938 N N   . PRO E  1 254 ? 145.002 46.859  -3.575  1.00   43.71  ? 254 PRO E N   1 
ATOM   13939 C CA  . PRO E  1 254 ? 143.812 46.282  -4.200  1.00   46.86  ? 254 PRO E CA  1 
ATOM   13940 C C   . PRO E  1 254 ? 142.525 46.289  -3.380  1.00   53.87  ? 254 PRO E C   1 
ATOM   13941 O O   . PRO E  1 254 ? 142.566 46.104  -2.159  1.00   53.20  ? 254 PRO E O   1 
ATOM   13942 C CB  . PRO E  1 254 ? 144.237 44.826  -4.458  1.00   39.86  ? 254 PRO E CB  1 
ATOM   13943 C CG  . PRO E  1 254 ? 145.674 44.786  -4.308  1.00   35.03  ? 254 PRO E CG  1 
ATOM   13944 C CD  . PRO E  1 254 ? 145.981 45.805  -3.277  1.00   38.20  ? 254 PRO E CD  1 
ATOM   13945 N N   . THR E  1 255 ? 141.421 46.585  -4.076  1.00   60.77  ? 255 THR E N   1 
ATOM   13946 C CA  . THR E  1 255 ? 140.020 46.379  -3.660  1.00   64.22  ? 255 THR E CA  1 
ATOM   13947 C C   . THR E  1 255 ? 139.111 46.876  -4.785  1.00   64.73  ? 255 THR E C   1 
ATOM   13948 O O   . THR E  1 255 ? 139.335 47.955  -5.350  1.00   65.24  ? 255 THR E O   1 
ATOM   13949 C CB  . THR E  1 255 ? 139.619 47.075  -2.334  1.00   83.22  ? 255 THR E CB  1 
ATOM   13950 O OG1 . THR E  1 255 ? 140.682 46.978  -1.374  1.00   85.31  ? 255 THR E OG1 1 
ATOM   13951 C CG2 . THR E  1 255 ? 138.342 46.438  -1.764  1.00   81.09  ? 255 THR E CG2 1 
ATOM   13952 N N   . GLY E  1 271 ? 140.257 35.624  9.296   1.00   83.48  ? 271 GLY E N   1 
ATOM   13953 C CA  . GLY E  1 271 ? 139.181 34.940  8.601   1.00   81.28  ? 271 GLY E CA  1 
ATOM   13954 C C   . GLY E  1 271 ? 138.413 35.817  7.622   1.00   77.60  ? 271 GLY E C   1 
ATOM   13955 O O   . GLY E  1 271 ? 137.226 36.108  7.808   1.00   79.16  ? 271 GLY E O   1 
ATOM   13956 N N   . GLU E  1 272 ? 139.109 36.216  6.561   1.00   72.11  ? 272 GLU E N   1 
ATOM   13957 C CA  . GLU E  1 272 ? 138.560 36.974  5.436   1.00   68.58  ? 272 GLU E CA  1 
ATOM   13958 C C   . GLU E  1 272 ? 139.154 36.293  4.213   1.00   62.84  ? 272 GLU E C   1 
ATOM   13959 O O   . GLU E  1 272 ? 140.320 35.928  4.250   1.00   63.87  ? 272 GLU E O   1 
ATOM   13960 C CB  . GLU E  1 272 ? 138.923 38.465  5.502   1.00   71.07  ? 272 GLU E CB  1 
ATOM   13961 C CG  . GLU E  1 272 ? 137.765 39.430  5.839   1.00   78.43  ? 272 GLU E CG  1 
ATOM   13962 C CD  . GLU E  1 272 ? 136.684 39.470  4.750   1.00   82.92  ? 272 GLU E CD  1 
ATOM   13963 O OE1 . GLU E  1 272 ? 136.962 39.016  3.615   1.00   82.93  ? 272 GLU E OE1 1 
ATOM   13964 O OE2 . GLU E  1 272 ? 135.566 39.974  5.013   1.00   85.84  ? 272 GLU E OE2 1 
ATOM   13965 N N   . ILE E  1 273 ? 138.377 36.079  3.152   1.00   59.25  ? 273 ILE E N   1 
ATOM   13966 C CA  . ILE E  1 273 ? 138.918 35.395  1.972   1.00   56.04  ? 273 ILE E CA  1 
ATOM   13967 C C   . ILE E  1 273 ? 139.935 36.307  1.286   1.00   54.72  ? 273 ILE E C   1 
ATOM   13968 O O   . ILE E  1 273 ? 139.768 37.529  1.277   1.00   57.07  ? 273 ILE E O   1 
ATOM   13969 C CB  . ILE E  1 273 ? 137.807 34.982  0.948   1.00   51.81  ? 273 ILE E CB  1 
ATOM   13970 C CG1 . ILE E  1 273 ? 136.741 34.141  1.619   1.00   61.74  ? 273 ILE E CG1 1 
ATOM   13971 C CG2 . ILE E  1 273 ? 138.361 34.147  -0.200  1.00   44.46  ? 273 ILE E CG2 1 
ATOM   13972 C CD1 . ILE E  1 273 ? 135.724 33.579  0.646   1.00   66.66  ? 273 ILE E CD1 1 
ATOM   13973 N N   . GLY E  1 274 ? 141.003 35.719  0.747   1.00   50.55  ? 274 GLY E N   1 
ATOM   13974 C CA  . GLY E  1 274 ? 141.982 36.482  -0.007  1.00   46.81  ? 274 GLY E CA  1 
ATOM   13975 C C   . GLY E  1 274 ? 141.343 37.140  -1.224  1.00   46.60  ? 274 GLY E C   1 
ATOM   13976 O O   . GLY E  1 274 ? 140.283 36.729  -1.681  1.00   46.49  ? 274 GLY E O   1 
ATOM   13977 N N   . GLY E  1 275 ? 141.999 38.152  -1.775  1.00   46.27  ? 275 GLY E N   1 
ATOM   13978 C CA  . GLY E  1 275 ? 141.438 38.892  -2.889  1.00   44.82  ? 275 GLY E CA  1 
ATOM   13979 C C   . GLY E  1 275 ? 141.906 38.478  -4.273  1.00   41.89  ? 275 GLY E C   1 
ATOM   13980 O O   . GLY E  1 275 ? 141.414 39.003  -5.272  1.00   43.56  ? 275 GLY E O   1 
ATOM   13981 N N   . ALA E  1 276 ? 142.876 37.576  -4.351  1.00   37.83  ? 276 ALA E N   1 
ATOM   13982 C CA  . ALA E  1 276 ? 143.412 37.200  -5.643  1.00   31.56  ? 276 ALA E CA  1 
ATOM   13983 C C   . ALA E  1 276 ? 142.977 35.779  -5.995  1.00   33.60  ? 276 ALA E C   1 
ATOM   13984 O O   . ALA E  1 276 ? 143.313 34.815  -5.313  1.00   32.13  ? 276 ALA E O   1 
ATOM   13985 C CB  . ALA E  1 276 ? 144.927 37.337  -5.639  1.00   25.64  ? 276 ALA E CB  1 
ATOM   13986 N N   . LEU E  1 277 ? 142.188 35.666  -7.052  1.00   34.61  ? 277 LEU E N   1 
ATOM   13987 C CA  . LEU E  1 277 ? 141.762 34.370  -7.529  1.00   32.04  ? 277 LEU E CA  1 
ATOM   13988 C C   . LEU E  1 277 ? 142.906 33.754  -8.276  1.00   33.47  ? 277 LEU E C   1 
ATOM   13989 O O   . LEU E  1 277 ? 143.611 34.448  -8.982  1.00   37.00  ? 277 LEU E O   1 
ATOM   13990 C CB  . LEU E  1 277 ? 140.551 34.495  -8.448  1.00   31.53  ? 277 LEU E CB  1 
ATOM   13991 C CG  . LEU E  1 277 ? 140.127 33.206  -9.146  1.00   31.13  ? 277 LEU E CG  1 
ATOM   13992 C CD1 . LEU E  1 277 ? 139.474 32.277  -8.166  1.00   29.66  ? 277 LEU E CD1 1 
ATOM   13993 C CD2 . LEU E  1 277 ? 139.218 33.469  -10.324 1.00   32.26  ? 277 LEU E CD2 1 
ATOM   13994 N N   . ILE E  1 278 ? 143.091 32.449  -8.137  1.00   33.02  ? 278 ILE E N   1 
ATOM   13995 C CA  . ILE E  1 278 ? 143.980 31.719  -9.028  1.00   30.91  ? 278 ILE E CA  1 
ATOM   13996 C C   . ILE E  1 278 ? 143.181 30.807  -9.957  1.00   32.81  ? 278 ILE E C   1 
ATOM   13997 O O   . ILE E  1 278 ? 142.367 30.009  -9.494  1.00   34.74  ? 278 ILE E O   1 
ATOM   13998 C CB  . ILE E  1 278 ? 144.958 30.899  -8.249  1.00   29.76  ? 278 ILE E CB  1 
ATOM   13999 C CG1 . ILE E  1 278 ? 145.664 31.775  -7.213  1.00   27.39  ? 278 ILE E CG1 1 
ATOM   14000 C CG2 . ILE E  1 278 ? 145.912 30.257  -9.188  1.00   31.27  ? 278 ILE E CG2 1 
ATOM   14001 C CD1 . ILE E  1 278 ? 146.488 30.995  -6.225  1.00   27.39  ? 278 ILE E CD1 1 
ATOM   14002 N N   . THR E  1 279 ? 143.422 30.922  -11.264 1.00   33.38  ? 279 THR E N   1 
ATOM   14003 C CA  . THR E  1 279 ? 142.637 30.206  -12.279 1.00   31.55  ? 279 THR E CA  1 
ATOM   14004 C C   . THR E  1 279 ? 143.469 29.812  -13.493 1.00   33.07  ? 279 THR E C   1 
ATOM   14005 O O   . THR E  1 279 ? 144.486 30.436  -13.778 1.00   34.09  ? 279 THR E O   1 
ATOM   14006 C CB  . THR E  1 279 ? 141.477 31.052  -12.793 1.00   31.92  ? 279 THR E CB  1 
ATOM   14007 O OG1 . THR E  1 279 ? 140.720 30.298  -13.743 1.00   34.88  ? 279 THR E OG1 1 
ATOM   14008 C CG2 . THR E  1 279 ? 142.012 32.308  -13.466 1.00   31.22  ? 279 THR E CG2 1 
ATOM   14009 N N   . THR E  1 280 ? 143.019 28.803  -14.231 1.00   33.23  ? 280 THR E N   1 
ATOM   14010 C CA  . THR E  1 280 ? 143.719 28.366  -15.431 1.00   34.16  ? 280 THR E CA  1 
ATOM   14011 C C   . THR E  1 280 ? 142.898 28.611  -16.701 1.00   34.94  ? 280 THR E C   1 
ATOM   14012 O O   . THR E  1 280 ? 143.286 28.206  -17.792 1.00   37.27  ? 280 THR E O   1 
ATOM   14013 C CB  . THR E  1 280 ? 144.075 26.861  -15.358 1.00   34.90  ? 280 THR E CB  1 
ATOM   14014 O OG1 . THR E  1 280 ? 142.895 26.069  -15.175 1.00   35.94  ? 280 THR E OG1 1 
ATOM   14015 C CG2 . THR E  1 280 ? 145.053 26.579  -14.232 1.00   32.85  ? 280 THR E CG2 1 
ATOM   14016 N N   . THR E  1 281 ? 141.760 29.271  -16.568 1.00   34.87  ? 281 THR E N   1 
ATOM   14017 C CA  . THR E  1 281 ? 140.824 29.325  -17.684 1.00   37.17  ? 281 THR E CA  1 
ATOM   14018 C C   . THR E  1 281 ? 140.835 30.649  -18.458 1.00   39.81  ? 281 THR E C   1 
ATOM   14019 O O   . THR E  1 281 ? 139.970 30.891  -19.308 1.00   42.29  ? 281 THR E O   1 
ATOM   14020 C CB  . THR E  1 281 ? 139.397 28.999  -17.205 1.00   37.39  ? 281 THR E CB  1 
ATOM   14021 O OG1 . THR E  1 281 ? 139.055 29.820  -16.076 1.00   35.99  ? 281 THR E OG1 1 
ATOM   14022 C CG2 . THR E  1 281 ? 139.340 27.533  -16.789 1.00   37.34  ? 281 THR E CG2 1 
ATOM   14023 N N   . HIS E  1 282 ? 141.805 31.507  -18.145 1.00   38.46  ? 282 HIS E N   1 
ATOM   14024 C CA  . HIS E  1 282 ? 142.243 32.560  -19.060 1.00   37.93  ? 282 HIS E CA  1 
ATOM   14025 C C   . HIS E  1 282 ? 143.744 32.770  -18.877 1.00   35.43  ? 282 HIS E C   1 
ATOM   14026 O O   . HIS E  1 282 ? 144.242 32.652  -17.762 1.00   33.92  ? 282 HIS E O   1 
ATOM   14027 C CB  . HIS E  1 282 ? 141.460 33.851  -18.840 1.00   40.76  ? 282 HIS E CB  1 
ATOM   14028 C CG  . HIS E  1 282 ? 141.433 34.331  -17.419 1.00   43.31  ? 282 HIS E CG  1 
ATOM   14029 N ND1 . HIS E  1 282 ? 142.559 34.757  -16.747 1.00   43.68  ? 282 HIS E ND1 1 
ATOM   14030 C CD2 . HIS E  1 282 ? 140.394 34.526  -16.569 1.00   44.70  ? 282 HIS E CD2 1 
ATOM   14031 C CE1 . HIS E  1 282 ? 142.224 35.153  -15.531 1.00   42.08  ? 282 HIS E CE1 1 
ATOM   14032 N NE2 . HIS E  1 282 ? 140.915 35.022  -15.398 1.00   43.73  ? 282 HIS E NE2 1 
ATOM   14033 N N   . PRO E  1 283 ? 144.468 33.077  -19.972 1.00   36.50  ? 283 PRO E N   1 
ATOM   14034 C CA  . PRO E  1 283 ? 145.931 33.209  -20.008 1.00   35.74  ? 283 PRO E CA  1 
ATOM   14035 C C   . PRO E  1 283 ? 146.480 34.432  -19.283 1.00   38.20  ? 283 PRO E C   1 
ATOM   14036 O O   . PRO E  1 283 ? 147.439 34.328  -18.518 1.00   38.36  ? 283 PRO E O   1 
ATOM   14037 C CB  . PRO E  1 283 ? 146.243 33.295  -21.505 1.00   39.89  ? 283 PRO E CB  1 
ATOM   14038 C CG  . PRO E  1 283 ? 144.994 33.710  -22.141 1.00   42.01  ? 283 PRO E CG  1 
ATOM   14039 C CD  . PRO E  1 283 ? 143.888 33.126  -21.322 1.00   39.55  ? 283 PRO E CD  1 
ATOM   14040 N N   . TYR E  1 284 ? 145.893 35.591  -19.520 1.00   40.62  ? 284 TYR E N   1 
ATOM   14041 C CA  . TYR E  1 284 ? 146.456 36.803  -18.967 1.00   41.27  ? 284 TYR E CA  1 
ATOM   14042 C C   . TYR E  1 284 ? 145.833 37.099  -17.623 1.00   39.69  ? 284 TYR E C   1 
ATOM   14043 O O   . TYR E  1 284 ? 144.791 36.563  -17.285 1.00   42.18  ? 284 TYR E O   1 
ATOM   14044 C CB  . TYR E  1 284 ? 146.273 37.966  -19.944 1.00   44.72  ? 284 TYR E CB  1 
ATOM   14045 C CG  . TYR E  1 284 ? 146.856 37.663  -21.299 1.00   47.41  ? 284 TYR E CG  1 
ATOM   14046 C CD1 . TYR E  1 284 ? 148.213 37.381  -21.437 1.00   49.62  ? 284 TYR E CD1 1 
ATOM   14047 C CD2 . TYR E  1 284 ? 146.058 37.617  -22.434 1.00   48.25  ? 284 TYR E CD2 1 
ATOM   14048 C CE1 . TYR E  1 284 ? 148.765 37.089  -22.671 1.00   52.29  ? 284 TYR E CE1 1 
ATOM   14049 C CE2 . TYR E  1 284 ? 146.604 37.315  -23.676 1.00   51.70  ? 284 TYR E CE2 1 
ATOM   14050 C CZ  . TYR E  1 284 ? 147.960 37.047  -23.787 1.00   54.09  ? 284 TYR E CZ  1 
ATOM   14051 O OH  . TYR E  1 284 ? 148.519 36.745  -25.016 1.00   59.02  ? 284 TYR E OH  1 
ATOM   14052 N N   . THR E  1 285 ? 146.513 37.905  -16.827 1.00   37.36  ? 285 THR E N   1 
ATOM   14053 C CA  . THR E  1 285 ? 145.988 38.297  -15.536 1.00   33.06  ? 285 THR E CA  1 
ATOM   14054 C C   . THR E  1 285 ? 144.929 39.403  -15.680 1.00   35.36  ? 285 THR E C   1 
ATOM   14055 O O   . THR E  1 285 ? 145.101 40.365  -16.438 1.00   37.43  ? 285 THR E O   1 
ATOM   14056 C CB  . THR E  1 285 ? 147.109 38.726  -14.602 1.00   31.30  ? 285 THR E CB  1 
ATOM   14057 O OG1 . THR E  1 285 ? 147.981 37.604  -14.384 1.00   34.31  ? 285 THR E OG1 1 
ATOM   14058 C CG2 . THR E  1 285 ? 146.528 39.165  -13.280 1.00   29.59  ? 285 THR E CG2 1 
ATOM   14059 N N   . VAL E  1 286 ? 143.811 39.219  -14.975 1.00   36.03  ? 286 VAL E N   1 
ATOM   14060 C CA  . VAL E  1 286 ? 142.635 40.070  -15.094 1.00   36.60  ? 286 VAL E CA  1 
ATOM   14061 C C   . VAL E  1 286 ? 142.422 40.933  -13.842 1.00   37.49  ? 286 VAL E C   1 
ATOM   14062 O O   . VAL E  1 286 ? 142.396 40.432  -12.714 1.00   35.96  ? 286 VAL E O   1 
ATOM   14063 C CB  . VAL E  1 286 ? 141.384 39.217  -15.357 1.00   35.91  ? 286 VAL E CB  1 
ATOM   14064 C CG1 . VAL E  1 286 ? 140.145 40.088  -15.422 1.00   36.61  ? 286 VAL E CG1 1 
ATOM   14065 C CG2 . VAL E  1 286 ? 141.539 38.436  -16.654 1.00   36.44  ? 286 VAL E CG2 1 
ATOM   14066 N N   . LEU E  1 287 ? 142.259 42.234  -14.064 1.00   40.36  ? 287 LEU E N   1 
ATOM   14067 C CA  . LEU E  1 287 ? 142.064 43.200  -12.993 1.00   38.38  ? 287 LEU E CA  1 
ATOM   14068 C C   . LEU E  1 287 ? 140.708 43.858  -13.059 1.00   40.10  ? 287 LEU E C   1 
ATOM   14069 O O   . LEU E  1 287 ? 140.223 44.159  -14.150 1.00   43.71  ? 287 LEU E O   1 
ATOM   14070 C CB  . LEU E  1 287 ? 143.152 44.275  -13.057 1.00   36.29  ? 287 LEU E CB  1 
ATOM   14071 C CG  . LEU E  1 287 ? 144.545 43.659  -13.072 1.00   34.25  ? 287 LEU E CG  1 
ATOM   14072 C CD1 . LEU E  1 287 ? 145.637 44.683  -13.324 1.00   34.83  ? 287 LEU E CD1 1 
ATOM   14073 C CD2 . LEU E  1 287 ? 144.739 42.971  -11.746 1.00   32.51  ? 287 LEU E CD2 1 
ATOM   14074 N N   . SER E  1 288 ? 140.097 44.085  -11.899 1.00   41.03  ? 288 SER E N   1 
ATOM   14075 C CA  . SER E  1 288 ? 138.833 44.816  -11.853 1.00   46.45  ? 288 SER E CA  1 
ATOM   14076 C C   . SER E  1 288 ? 139.113 46.223  -12.352 1.00   49.42  ? 288 SER E C   1 
ATOM   14077 O O   . SER E  1 288 ? 140.249 46.679  -12.288 1.00   48.58  ? 288 SER E O   1 
ATOM   14078 C CB  . SER E  1 288 ? 138.235 44.843  -10.441 1.00   49.71  ? 288 SER E CB  1 
ATOM   14079 O OG  . SER E  1 288 ? 139.044 45.554  -9.517  1.00   50.82  ? 288 SER E OG  1 
ATOM   14080 N N   . HIS E  1 289 ? 138.104 46.905  -12.877 1.00   53.30  ? 289 HIS E N   1 
ATOM   14081 C CA  . HIS E  1 289 ? 138.370 48.175  -13.549 1.00   58.80  ? 289 HIS E CA  1 
ATOM   14082 C C   . HIS E  1 289 ? 139.106 49.207  -12.669 1.00   56.06  ? 289 HIS E C   1 
ATOM   14083 O O   . HIS E  1 289 ? 140.042 49.846  -13.138 1.00   56.32  ? 289 HIS E O   1 
ATOM   14084 C CB  . HIS E  1 289 ? 137.084 48.781  -14.099 1.00   66.22  ? 289 HIS E CB  1 
ATOM   14085 C CG  . HIS E  1 289 ? 137.305 50.076  -14.820 1.00   73.76  ? 289 HIS E CG  1 
ATOM   14086 N ND1 . HIS E  1 289 ? 137.972 50.150  -16.023 1.00   76.76  ? 289 HIS E ND1 1 
ATOM   14087 C CD2 . HIS E  1 289 ? 136.977 51.349  -14.495 1.00   78.02  ? 289 HIS E CD2 1 
ATOM   14088 C CE1 . HIS E  1 289 ? 138.036 51.411  -16.415 1.00   80.49  ? 289 HIS E CE1 1 
ATOM   14089 N NE2 . HIS E  1 289 ? 137.440 52.159  -15.506 1.00   81.47  ? 289 HIS E NE2 1 
ATOM   14090 N N   . SER E  1 290 ? 138.707 49.357  -11.405 1.00   54.53  ? 290 SER E N   1 
ATOM   14091 C CA  . SER E  1 290 ? 139.318 50.372  -10.545 1.00   56.47  ? 290 SER E CA  1 
ATOM   14092 C C   . SER E  1 290 ? 140.801 50.107  -10.336 1.00   49.51  ? 290 SER E C   1 
ATOM   14093 O O   . SER E  1 290 ? 141.615 51.020  -10.379 1.00   52.45  ? 290 SER E O   1 
ATOM   14094 C CB  . SER E  1 290 ? 138.632 50.430  -9.176  1.00   61.52  ? 290 SER E CB  1 
ATOM   14095 O OG  . SER E  1 290 ? 138.806 49.216  -8.463  1.00   61.49  ? 290 SER E OG  1 
ATOM   14096 N N   . ILE E  1 291 ? 141.147 48.850  -10.120 1.00   42.62  ? 291 ILE E N   1 
ATOM   14097 C CA  . ILE E  1 291 ? 142.538 48.451  -9.969  1.00   38.48  ? 291 ILE E CA  1 
ATOM   14098 C C   . ILE E  1 291 ? 143.308 48.531  -11.285 1.00   40.18  ? 291 ILE E C   1 
ATOM   14099 O O   . ILE E  1 291 ? 144.444 49.016  -11.317 1.00   38.01  ? 291 ILE E O   1 
ATOM   14100 C CB  . ILE E  1 291 ? 142.609 47.058  -9.407  1.00   35.09  ? 291 ILE E CB  1 
ATOM   14101 C CG1 . ILE E  1 291 ? 141.987 47.068  -8.012  1.00   35.96  ? 291 ILE E CG1 1 
ATOM   14102 C CG2 . ILE E  1 291 ? 144.030 46.571  -9.385  1.00   33.75  ? 291 ILE E CG2 1 
ATOM   14103 C CD1 . ILE E  1 291 ? 141.926 45.721  -7.380  1.00   36.21  ? 291 ILE E CD1 1 
ATOM   14104 N N   . PHE E  1 292 ? 142.673 48.076  -12.363 1.00   42.60  ? 292 PHE E N   1 
ATOM   14105 C CA  . PHE E  1 292 ? 143.271 48.126  -13.696 1.00   46.12  ? 292 PHE E CA  1 
ATOM   14106 C C   . PHE E  1 292 ? 143.692 49.536  -14.130 1.00   51.95  ? 292 PHE E C   1 
ATOM   14107 O O   . PHE E  1 292 ? 144.841 49.758  -14.508 1.00   54.88  ? 292 PHE E O   1 
ATOM   14108 C CB  . PHE E  1 292 ? 142.289 47.549  -14.732 1.00   45.70  ? 292 PHE E CB  1 
ATOM   14109 C CG  . PHE E  1 292 ? 142.729 47.733  -16.164 1.00   47.14  ? 292 PHE E CG  1 
ATOM   14110 C CD1 . PHE E  1 292 ? 143.647 46.876  -16.746 1.00   45.06  ? 292 PHE E CD1 1 
ATOM   14111 C CD2 . PHE E  1 292 ? 142.219 48.773  -16.932 1.00   50.74  ? 292 PHE E CD2 1 
ATOM   14112 C CE1 . PHE E  1 292 ? 144.046 47.057  -18.071 1.00   45.27  ? 292 PHE E CE1 1 
ATOM   14113 C CE2 . PHE E  1 292 ? 142.611 48.949  -18.257 1.00   51.96  ? 292 PHE E CE2 1 
ATOM   14114 C CZ  . PHE E  1 292 ? 143.525 48.086  -18.822 1.00   48.32  ? 292 PHE E CZ  1 
ATOM   14115 N N   . GLU E  1 293 ? 142.786 50.497  -14.024 1.00   53.86  ? 293 GLU E N   1 
ATOM   14116 C CA  . GLU E  1 293 ? 143.085 51.840  -14.495 1.00   58.71  ? 293 GLU E CA  1 
ATOM   14117 C C   . GLU E  1 293 ? 144.227 52.440  -13.665 1.00   56.29  ? 293 GLU E C   1 
ATOM   14118 O O   . GLU E  1 293 ? 145.105 53.121  -14.201 1.00   56.00  ? 293 GLU E O   1 
ATOM   14119 C CB  . GLU E  1 293 ? 141.838 52.720  -14.465 1.00   68.80  ? 293 GLU E CB  1 
ATOM   14120 C CG  . GLU E  1 293 ? 141.361 53.115  -13.093 1.00   78.74  ? 293 GLU E CG  1 
ATOM   14121 C CD  . GLU E  1 293 ? 140.805 54.535  -13.048 1.00   92.05  ? 293 GLU E CD  1 
ATOM   14122 O OE1 . GLU E  1 293 ? 140.833 55.240  -14.087 1.00   98.53  ? 293 GLU E OE1 1 
ATOM   14123 O OE2 . GLU E  1 293 ? 140.360 54.952  -11.956 1.00   95.00  1 293 GLU E OE2 1 
ATOM   14124 N N   . VAL E  1 294 ? 144.211 52.195  -12.358 1.00   52.16  ? 294 VAL E N   1 
ATOM   14125 C CA  . VAL E  1 294 ? 145.257 52.707  -11.496 1.00   48.98  ? 294 VAL E CA  1 
ATOM   14126 C C   . VAL E  1 294 ? 146.584 52.006  -11.752 1.00   45.62  ? 294 VAL E C   1 
ATOM   14127 O O   . VAL E  1 294 ? 147.623 52.651  -11.871 1.00   48.46  ? 294 VAL E O   1 
ATOM   14128 C CB  . VAL E  1 294 ? 144.903 52.517  -10.026 1.00   47.68  ? 294 VAL E CB  1 
ATOM   14129 C CG1 . VAL E  1 294 ? 146.113 52.865  -9.143  1.00   48.51  ? 294 VAL E CG1 1 
ATOM   14130 C CG2 . VAL E  1 294 ? 143.661 53.345  -9.653  1.00   46.11  ? 294 VAL E CG2 1 
ATOM   14131 N N   . PHE E  1 295 ? 146.544 50.682  -11.837 1.00   42.70  ? 295 PHE E N   1 
ATOM   14132 C CA  . PHE E  1 295 ? 147.760 49.914  -12.032 1.00   40.91  ? 295 PHE E CA  1 
ATOM   14133 C C   . PHE E  1 295 ? 148.437 50.233  -13.340 1.00   42.57  ? 295 PHE E C   1 
ATOM   14134 O O   . PHE E  1 295 ? 149.661 50.319  -13.407 1.00   42.81  ? 295 PHE E O   1 
ATOM   14135 C CB  . PHE E  1 295 ? 147.508 48.415  -11.970 1.00   40.58  ? 295 PHE E CB  1 
ATOM   14136 C CG  . PHE E  1 295 ? 148.696 47.599  -12.439 1.00   44.47  ? 295 PHE E CG  1 
ATOM   14137 C CD1 . PHE E  1 295 ? 149.818 47.431  -11.620 1.00   45.79  ? 295 PHE E CD1 1 
ATOM   14138 C CD2 . PHE E  1 295 ? 148.709 47.023  -13.700 1.00   44.47  ? 295 PHE E CD2 1 
ATOM   14139 C CE1 . PHE E  1 295 ? 150.926 46.701  -12.054 1.00   44.99  ? 295 PHE E CE1 1 
ATOM   14140 C CE2 . PHE E  1 295 ? 149.814 46.301  -14.138 1.00   45.10  ? 295 PHE E CE2 1 
ATOM   14141 C CZ  . PHE E  1 295 ? 150.918 46.134  -13.311 1.00   45.10  ? 295 PHE E CZ  1 
ATOM   14142 N N   . THR E  1 296 ? 147.646 50.345  -14.395 1.00   44.90  ? 296 THR E N   1 
ATOM   14143 C CA  . THR E  1 296 ? 148.210 50.579  -15.716 1.00   51.28  ? 296 THR E CA  1 
ATOM   14144 C C   . THR E  1 296 ? 148.916 51.930  -15.803 1.00   57.02  ? 296 THR E C   1 
ATOM   14145 O O   . THR E  1 296 ? 149.971 52.063  -16.436 1.00   61.19  ? 296 THR E O   1 
ATOM   14146 C CB  . THR E  1 296 ? 147.121 50.507  -16.774 1.00   53.69  ? 296 THR E CB  1 
ATOM   14147 O OG1 . THR E  1 296 ? 146.606 49.176  -16.805 1.00   54.45  ? 296 THR E OG1 1 
ATOM   14148 C CG2 . THR E  1 296 ? 147.677 50.840  -18.124 1.00   57.69  ? 296 THR E CG2 1 
ATOM   14149 N N   . GLN E  1 297 ? 148.355 52.915  -15.112 1.00   57.55  ? 297 GLN E N   1 
ATOM   14150 C CA  . GLN E  1 297 ? 148.913 54.252  -15.091 1.00   58.94  ? 297 GLN E CA  1 
ATOM   14151 C C   . GLN E  1 297 ? 150.200 54.242  -14.296 1.00   55.60  ? 297 GLN E C   1 
ATOM   14152 O O   . GLN E  1 297 ? 151.190 54.808  -14.727 1.00   56.74  ? 297 GLN E O   1 
ATOM   14153 C CB  . GLN E  1 297 ? 147.902 55.240  -14.504 1.00   62.44  ? 297 GLN E CB  1 
ATOM   14154 C CG  . GLN E  1 297 ? 148.342 56.706  -14.485 1.00   67.60  ? 297 GLN E CG  1 
ATOM   14155 C CD  . GLN E  1 297 ? 148.633 57.281  -15.857 1.00   71.72  ? 297 GLN E CD  1 
ATOM   14156 O OE1 . GLN E  1 297 ? 147.780 57.258  -16.743 1.00   76.60  ? 297 GLN E OE1 1 
ATOM   14157 N NE2 . GLN E  1 297 ? 149.836 57.819  -16.033 1.00   70.16  ? 297 GLN E NE2 1 
ATOM   14158 N N   . VAL E  1 298 ? 150.187 53.580  -13.144 1.00   52.02  ? 298 VAL E N   1 
ATOM   14159 C CA  . VAL E  1 298 ? 151.381 53.452  -12.324 1.00   50.37  ? 298 VAL E CA  1 
ATOM   14160 C C   . VAL E  1 298 ? 152.520 52.822  -13.102 1.00   52.91  ? 298 VAL E C   1 
ATOM   14161 O O   . VAL E  1 298 ? 153.674 53.241  -13.009 1.00   58.00  ? 298 VAL E O   1 
ATOM   14162 C CB  . VAL E  1 298 ? 151.110 52.611  -11.080 1.00   45.30  ? 298 VAL E CB  1 
ATOM   14163 C CG1 . VAL E  1 298 ? 152.414 52.232  -10.395 1.00   43.57  ? 298 VAL E CG1 1 
ATOM   14164 C CG2 . VAL E  1 298 ? 150.251 53.387  -10.133 1.00   45.29  ? 298 VAL E CG2 1 
ATOM   14165 N N   . PHE E  1 299 ? 152.192 51.820  -13.895 1.00   50.36  ? 299 PHE E N   1 
ATOM   14166 C CA  . PHE E  1 299 ? 153.217 51.148  -14.653 1.00   53.03  ? 299 PHE E CA  1 
ATOM   14167 C C   . PHE E  1 299 ? 153.841 52.071  -15.672 1.00   58.04  ? 299 PHE E C   1 
ATOM   14168 O O   . PHE E  1 299 ? 155.065 52.193  -15.741 1.00   61.22  ? 299 PHE E O   1 
ATOM   14169 C CB  . PHE E  1 299 ? 152.649 49.909  -15.337 1.00   54.94  ? 299 PHE E CB  1 
ATOM   14170 C CG  . PHE E  1 299 ? 153.700 49.043  -15.951 1.00   56.87  ? 299 PHE E CG  1 
ATOM   14171 C CD1 . PHE E  1 299 ? 154.342 48.078  -15.195 1.00   52.72  ? 299 PHE E CD1 1 
ATOM   14172 C CD2 . PHE E  1 299 ? 154.074 49.216  -17.276 1.00   61.62  ? 299 PHE E CD2 1 
ATOM   14173 C CE1 . PHE E  1 299 ? 155.324 47.290  -15.754 1.00   53.07  ? 299 PHE E CE1 1 
ATOM   14174 C CE2 . PHE E  1 299 ? 155.054 48.434  -17.837 1.00   60.94  ? 299 PHE E CE2 1 
ATOM   14175 C CZ  . PHE E  1 299 ? 155.677 47.469  -17.075 1.00   57.34  ? 299 PHE E CZ  1 
ATOM   14176 N N   . ALA E  1 300 ? 152.983 52.760  -16.416 1.00   60.09  ? 300 ALA E N   1 
ATOM   14177 C CA  . ALA E  1 300 ? 153.411 53.675  -17.465 1.00   65.13  ? 300 ALA E CA  1 
ATOM   14178 C C   . ALA E  1 300 ? 154.339 54.749  -16.919 1.00   68.71  ? 300 ALA E C   1 
ATOM   14179 O O   . ALA E  1 300 ? 155.268 55.204  -17.604 1.00   64.79  ? 300 ALA E O   1 
ATOM   14180 C CB  . ALA E  1 300 ? 152.202 54.312  -18.115 1.00   65.64  ? 300 ALA E CB  1 
ATOM   14181 N N   . ASN E  1 301 ? 154.087 55.122  -15.667 1.00   67.55  ? 301 ASN E N   1 
ATOM   14182 C CA  . ASN E  1 301 ? 154.891 56.105  -14.952 1.00   68.71  ? 301 ASN E CA  1 
ATOM   14183 C C   . ASN E  1 301 ? 156.270 55.576  -14.608 1.00   66.00  ? 301 ASN E C   1 
ATOM   14184 O O   . ASN E  1 301 ? 157.165 56.351  -14.291 1.00   62.66  ? 301 ASN E O   1 
ATOM   14185 C CB  . ASN E  1 301 ? 154.192 56.528  -13.657 1.00   69.44  ? 301 ASN E CB  1 
ATOM   14186 C CG  . ASN E  1 301 ? 152.917 57.320  -13.897 1.00   72.02  ? 301 ASN E CG  1 
ATOM   14187 O OD1 . ASN E  1 301 ? 152.656 57.797  -15.002 1.00   76.58  ? 301 ASN E OD1 1 
ATOM   14188 N ND2 . ASN E  1 301 ? 152.118 57.469  -12.847 1.00   68.94  ? 301 ASN E ND2 1 
ATOM   14189 N N   . ASN E  1 302 ? 156.428 54.254  -14.622 1.00   65.04  ? 302 ASN E N   1 
ATOM   14190 C CA  . ASN E  1 302 ? 157.730 53.664  -14.345 1.00   66.62  ? 302 ASN E CA  1 
ATOM   14191 C C   . ASN E  1 302 ? 158.403 53.144  -15.620 1.00   69.79  ? 302 ASN E C   1 
ATOM   14192 O O   . ASN E  1 302 ? 159.299 52.297  -15.589 1.00   71.56  ? 302 ASN E O   1 
ATOM   14193 C CB  . ASN E  1 302 ? 157.596 52.571  -13.287 1.00   52.94  ? 302 ASN E CB  1 
ATOM   14194 C CG  . ASN E  1 302 ? 157.376 53.151  -11.905 1.00   51.72  ? 302 ASN E CG  1 
ATOM   14195 O OD1 . ASN E  1 302 ? 158.321 53.404  -11.151 1.00   52.44  ? 302 ASN E OD1 1 
ATOM   14196 N ND2 . ASN E  1 302 ? 156.118 53.371  -11.567 1.00   52.99  ? 302 ASN E ND2 1 
ATOM   14197 N N   . MET E  1 303 ? 157.998 53.717  -16.739 1.00   70.73  ? 303 MET E N   1 
ATOM   14198 C CA  . MET E  1 303 ? 158.511 53.308  -18.016 1.00   73.92  ? 303 MET E CA  1 
ATOM   14199 C C   . MET E  1 303 ? 158.824 54.493  -18.865 1.00   82.05  ? 303 MET E C   1 
ATOM   14200 O O   . MET E  1 303 ? 158.293 55.581  -18.630 1.00   85.67  ? 303 MET E O   1 
ATOM   14201 C CB  . MET E  1 303 ? 157.505 52.425  -18.732 1.00   71.74  ? 303 MET E CB  1 
ATOM   14202 C CG  . MET E  1 303 ? 157.388 51.071  -18.135 1.00   67.37  ? 303 MET E CG  1 
ATOM   14203 S SD  . MET E  1 303 ? 158.955 50.345  -18.582 1.00   108.57 ? 303 MET E SD  1 
ATOM   14204 C CE  . MET E  1 303 ? 158.659 50.007  -20.308 1.00   66.57  ? 303 MET E CE  1 
ATOM   14205 N N   . PRO E  1 304 ? 159.660 54.280  -19.890 1.00   86.14  ? 304 PRO E N   1 
ATOM   14206 C CA  . PRO E  1 304 ? 159.860 55.382  -20.837 1.00   90.52  ? 304 PRO E CA  1 
ATOM   14207 C C   . PRO E  1 304 ? 158.539 55.777  -21.512 1.00   89.58  ? 304 PRO E C   1 
ATOM   14208 O O   . PRO E  1 304 ? 157.928 54.989  -22.219 1.00   87.63  ? 304 PRO E O   1 
ATOM   14209 C CB  . PRO E  1 304 ? 160.870 54.805  -21.821 1.00   94.26  ? 304 PRO E CB  1 
ATOM   14210 C CG  . PRO E  1 304 ? 160.775 53.285  -21.668 1.00   90.69  ? 304 PRO E CG  1 
ATOM   14211 C CD  . PRO E  1 304 ? 160.500 53.104  -20.199 1.00   85.87  ? 304 PRO E CD  1 
ATOM   14212 N N   . LYS E  1 305 ? 158.110 56.998  -21.207 1.00   90.80  ? 305 LYS E N   1 
ATOM   14213 C CA  . LYS E  1 305 ? 156.770 57.470  -21.519 1.00   91.10  ? 305 LYS E CA  1 
ATOM   14214 C C   . LYS E  1 305 ? 156.435 57.625  -23.007 1.00   96.85  ? 305 LYS E C   1 
ATOM   14215 O O   . LYS E  1 305 ? 155.286 57.478  -23.399 1.00   98.21  ? 305 LYS E O   1 
ATOM   14216 C CB  . LYS E  1 305 ? 156.579 58.805  -20.829 0.0000 91.64  ? 305 LYS E CB  1 
ATOM   14217 C CG  . LYS E  1 305 ? 157.892 59.492  -20.603 0.0000 93.94  ? 305 LYS E CG  1 
ATOM   14218 C CD  . LYS E  1 305 ? 157.703 60.896  -20.136 0.0000 95.83  ? 305 LYS E CD  1 
ATOM   14219 C CE  . LYS E  1 305 ? 159.043 61.488  -19.722 0.0000 97.82  ? 305 LYS E CE  1 
ATOM   14220 N NZ  . LYS E  1 305 ? 159.936 61.565  -20.909 0.0000 102.85 ? 305 LYS E NZ  1 
ATOM   14221 N N   . GLN E  1 306 ? 157.452 57.879  -23.844 1.00   102.01 ? 306 GLN E N   1 
ATOM   14222 C CA  . GLN E  1 306 ? 157.267 58.075  -25.329 1.00   107.53 ? 306 GLN E CA  1 
ATOM   14223 C C   . GLN E  1 306 ? 157.602 56.867  -26.193 1.00   107.64 ? 306 GLN E C   1 
ATOM   14224 O O   . GLN E  1 306 ? 158.036 57.023  -27.316 1.00   112.69 ? 306 GLN E O   1 
ATOM   14225 C CB  . GLN E  1 306 ? 158.076 59.269  -25.908 0.0000 110.15 ? 306 GLN E CB  1 
ATOM   14226 C CG  . GLN E  1 306 ? 159.479 59.452  -25.426 0.0000 111.03 ? 306 GLN E CG  1 
ATOM   14227 C CD  . GLN E  1 306 ? 159.580 59.874  -24.009 0.0000 107.47 ? 306 GLN E CD  1 
ATOM   14228 O OE1 . GLN E  1 306 ? 158.585 60.221  -23.438 0.0000 104.99 ? 306 GLN E OE1 1 
ATOM   14229 N NE2 . GLN E  1 306 ? 160.790 59.905  -23.445 0.0000 107.85 ? 306 GLN E NE2 1 
ATOM   14230 N N   . ALA E  1 307 ? 157.511 55.680  -25.630 1.00   103.06 ? 307 ALA E N   1 
ATOM   14231 C CA  . ALA E  1 307 ? 157.728 54.484  -26.402 1.00   104.13 ? 307 ALA E CA  1 
ATOM   14232 C C   . ALA E  1 307 ? 156.379 53.823  -26.612 1.00   101.18 ? 307 ALA E C   1 
ATOM   14233 O O   . ALA E  1 307 ? 156.268 52.772  -27.237 1.00   100.90 ? 307 ALA E O   1 
ATOM   14234 C CB  . ALA E  1 307 ? 158.697 53.557  -25.682 1.00   101.47 ? 307 ALA E CB  1 
ATOM   14235 N N   . GLN E  1 308 ? 155.357 54.428  -26.028 1.00   98.70  ? 308 GLN E N   1 
ATOM   14236 C CA  . GLN E  1 308 ? 154.035 53.856  -26.065 1.00   96.15  ? 308 GLN E CA  1 
ATOM   14237 C C   . GLN E  1 308 ? 153.392 53.862  -27.462 1.00   102.25 ? 308 GLN E C   1 
ATOM   14238 O O   . GLN E  1 308 ? 153.651 54.728  -28.294 1.00   106.35 ? 308 GLN E O   1 
ATOM   14239 C CB  . GLN E  1 308 ? 153.173 54.600  -25.056 1.00   92.32  ? 308 GLN E CB  1 
ATOM   14240 C CG  . GLN E  1 308 ? 153.857 54.625  -23.690 1.00   88.07  ? 308 GLN E CG  1 
ATOM   14241 C CD  . GLN E  1 308 ? 153.029 55.253  -22.610 1.00   84.35  ? 308 GLN E CD  1 
ATOM   14242 O OE1 . GLN E  1 308 ? 151.882 55.607  -22.842 1.00   85.09  ? 308 GLN E OE1 1 
ATOM   14243 N NE2 . GLN E  1 308 ? 153.599 55.377  -21.405 1.00   79.95  ? 308 GLN E NE2 1 
ATOM   14244 N N   . VAL E  1 309 ? 152.525 52.878  -27.678 1.00   103.49 ? 309 VAL E N   1 
ATOM   14245 C CA  . VAL E  1 309 ? 151.775 52.713  -28.916 1.00   108.05 ? 309 VAL E CA  1 
ATOM   14246 C C   . VAL E  1 309 ? 150.303 52.614  -28.534 1.00   103.66 ? 309 VAL E C   1 
ATOM   14247 O O   . VAL E  1 309 ? 149.970 52.198  -27.413 1.00   96.33  ? 309 VAL E O   1 
ATOM   14248 C CB  . VAL E  1 309 ? 152.243 51.425  -29.682 1.00   94.27  ? 309 VAL E CB  1 
ATOM   14249 C CG1 . VAL E  1 309 ? 151.299 51.048  -30.807 1.00   96.83  ? 309 VAL E CG1 1 
ATOM   14250 C CG2 . VAL E  1 309 ? 153.670 51.595  -30.195 1.00   97.92  ? 309 VAL E CG2 1 
ATOM   14251 N N   . LYS E  1 310 ? 149.427 53.022  -29.447 1.00   106.98 ? 310 LYS E N   1 
ATOM   14252 C CA  . LYS E  1 310 ? 148.002 52.861  -29.237 1.00   104.14 ? 310 LYS E CA  1 
ATOM   14253 C C   . LYS E  1 310 ? 147.761 51.387  -28.974 1.00   100.12 ? 310 LYS E C   1 
ATOM   14254 O O   . LYS E  1 310 ? 148.244 50.523  -29.725 1.00   101.60 ? 310 LYS E O   1 
ATOM   14255 C CB  . LYS E  1 310 ? 147.190 53.408  -30.407 1.00   109.34 ? 310 LYS E CB  1 
ATOM   14256 C CG  . LYS E  1 310 ? 147.503 54.905  -30.669 1.00   133.28 ? 310 LYS E CG  1 
ATOM   14257 C CD  . LYS E  1 310 ? 146.882 55.918  -29.662 1.00   116.73 ? 310 LYS E CD  1 
ATOM   14258 C CE  . LYS E  1 310 ? 145.397 55.712  -29.382 1.00   114.18 ? 310 LYS E CE  1 
ATOM   14259 N NZ  . LYS E  1 310 ? 144.795 56.948  -28.787 1.00   114.06 ? 310 LYS E NZ  1 
ATOM   14260 N N   . ALA E  1 311 ? 147.055 51.120  -27.877 1.00   94.93  ? 311 ALA E N   1 
ATOM   14261 C CA  . ALA E  1 311 ? 146.806 49.765  -27.399 1.00   89.78  ? 311 ALA E CA  1 
ATOM   14262 C C   . ALA E  1 311 ? 146.219 48.829  -28.441 1.00   91.78  ? 311 ALA E C   1 
ATOM   14263 O O   . ALA E  1 311 ? 145.385 49.226  -29.253 1.00   95.07  ? 311 ALA E O   1 
ATOM   14264 C CB  . ALA E  1 311 ? 145.890 49.824  -26.195 1.00   85.64  ? 311 ALA E CB  1 
ATOM   14265 N N   . VAL E  1 312 ? 146.659 47.572  -28.386 1.00   90.29  ? 312 VAL E N   1 
ATOM   14266 C CA  . VAL E  1 312 ? 146.292 46.575  -29.380 1.00   92.12  ? 312 VAL E CA  1 
ATOM   14267 C C   . VAL E  1 312 ? 145.805 45.317  -28.688 1.00   86.61  ? 312 VAL E C   1 
ATOM   14268 O O   . VAL E  1 312 ? 146.205 45.010  -27.561 1.00   84.30  ? 312 VAL E O   1 
ATOM   14269 C CB  . VAL E  1 312 ? 147.481 46.199  -30.308 1.00   81.87  ? 312 VAL E CB  1 
ATOM   14270 C CG1 . VAL E  1 312 ? 147.980 47.418  -31.051 1.00   87.69  ? 312 VAL E CG1 1 
ATOM   14271 C CG2 . VAL E  1 312 ? 148.613 45.580  -29.515 1.00   78.11  ? 312 VAL E CG2 1 
ATOM   14272 N N   . GLY E  1 313 ? 144.885 44.625  -29.345 1.00   88.12  ? 313 GLY E N   1 
ATOM   14273 C CA  . GLY E  1 313 ? 144.387 43.376  -28.824 1.00   83.25  ? 313 GLY E CA  1 
ATOM   14274 C C   . GLY E  1 313 ? 143.518 43.729  -27.648 1.00   78.66  ? 313 GLY E C   1 
ATOM   14275 O O   . GLY E  1 313 ? 142.828 44.747  -27.662 1.00   78.94  ? 313 GLY E O   1 
ATOM   14276 N N   . PRO E  1 314 ? 143.586 42.904  -26.604 1.00   74.17  ? 314 PRO E N   1 
ATOM   14277 C CA  . PRO E  1 314 ? 142.874 43.041  -25.330 1.00   70.18  ? 314 PRO E CA  1 
ATOM   14278 C C   . PRO E  1 314 ? 143.548 44.014  -24.344 1.00   66.71  ? 314 PRO E C   1 
ATOM   14279 O O   . PRO E  1 314 ? 143.017 44.293  -23.261 1.00   63.36  ? 314 PRO E O   1 
ATOM   14280 C CB  . PRO E  1 314 ? 142.909 41.621  -24.780 1.00   69.21  ? 314 PRO E CB  1 
ATOM   14281 C CG  . PRO E  1 314 ? 144.207 41.074  -25.307 1.00   71.41  ? 314 PRO E CG  1 
ATOM   14282 C CD  . PRO E  1 314 ? 144.389 41.672  -26.665 1.00   74.18  ? 314 PRO E CD  1 
ATOM   14283 N N   . PHE E  1 315 ? 144.702 44.541  -24.730 1.00   67.52  ? 315 PHE E N   1 
ATOM   14284 C CA  . PHE E  1 315 ? 145.528 45.303  -23.814 1.00   64.96  ? 315 PHE E CA  1 
ATOM   14285 C C   . PHE E  1 315 ? 145.211 46.776  -23.787 1.00   65.80  ? 315 PHE E C   1 
ATOM   14286 O O   . PHE E  1 315 ? 144.624 47.304  -24.724 1.00   69.09  ? 315 PHE E O   1 
ATOM   14287 C CB  . PHE E  1 315 ? 146.985 45.109  -24.176 1.00   66.98  ? 315 PHE E CB  1 
ATOM   14288 C CG  . PHE E  1 315 ? 147.383 43.692  -24.206 1.00   66.26  ? 315 PHE E CG  1 
ATOM   14289 C CD1 . PHE E  1 315 ? 147.369 42.946  -23.047 1.00   63.40  ? 315 PHE E CD1 1 
ATOM   14290 C CD2 . PHE E  1 315 ? 147.726 43.084  -25.388 1.00   70.47  ? 315 PHE E CD2 1 
ATOM   14291 C CE1 . PHE E  1 315 ? 147.718 41.617  -23.060 1.00   66.07  ? 315 PHE E CE1 1 
ATOM   14292 C CE2 . PHE E  1 315 ? 148.076 41.757  -25.411 1.00   72.09  ? 315 PHE E CE2 1 
ATOM   14293 C CZ  . PHE E  1 315 ? 148.070 41.022  -24.244 1.00   70.70  ? 315 PHE E CZ  1 
ATOM   14294 N N   . GLY E  1 316 ? 145.586 47.417  -22.684 1.00   64.59  ? 316 GLY E N   1 
ATOM   14295 C CA  . GLY E  1 316 ? 145.353 48.835  -22.474 1.00   68.96  ? 316 GLY E CA  1 
ATOM   14296 C C   . GLY E  1 316 ? 146.611 49.692  -22.576 1.00   72.93  ? 316 GLY E C   1 
ATOM   14297 O O   . GLY E  1 316 ? 146.539 50.910  -22.743 1.00   76.72  ? 316 GLY E O   1 
ATOM   14298 N N   . LEU E  1 317 ? 147.771 49.062  -22.434 1.00   71.76  ? 317 LEU E N   1 
ATOM   14299 C CA  . LEU E  1 317 ? 149.045 49.773  -22.483 1.00   73.75  ? 317 LEU E CA  1 
ATOM   14300 C C   . LEU E  1 317 ? 150.120 49.007  -23.276 1.00   78.75  ? 317 LEU E C   1 
ATOM   14301 O O   . LEU E  1 317 ? 150.624 47.976  -22.823 1.00   77.64  ? 317 LEU E O   1 
ATOM   14302 C CB  . LEU E  1 317 ? 149.533 50.072  -21.067 1.00   68.87  ? 317 LEU E CB  1 
ATOM   14303 C CG  . LEU E  1 317 ? 150.855 50.826  -20.934 1.00   70.43  ? 317 LEU E CG  1 
ATOM   14304 C CD1 . LEU E  1 317 ? 150.806 52.175  -21.644 1.00   73.02  ? 317 LEU E CD1 1 
ATOM   14305 C CD2 . LEU E  1 317 ? 151.228 50.979  -19.459 1.00   68.80  ? 317 LEU E CD2 1 
ATOM   14306 N N   . CYS E  1 318 ? 150.468 49.516  -24.458 1.00   84.02  ? 318 CYS E N   1 
ATOM   14307 C CA  . CYS E  1 318 ? 151.457 48.873  -25.321 1.00   85.88  ? 318 CYS E CA  1 
ATOM   14308 C C   . CYS E  1 318 ? 152.629 49.789  -25.609 1.00   90.71  ? 318 CYS E C   1 
ATOM   14309 O O   . CYS E  1 318 ? 152.501 51.011  -25.541 1.00   93.29  ? 318 CYS E O   1 
ATOM   14310 C CB  . CYS E  1 318 ? 150.828 48.418  -26.634 1.00   88.35  ? 318 CYS E CB  1 
ATOM   14311 S SG  . CYS E  1 318 ? 149.644 47.091  -26.439 1.00   75.43  ? 318 CYS E SG  1 
ATOM   14312 N N   . TYR E  1 319 ? 153.775 49.184  -25.916 1.00   92.04  ? 319 TYR E N   1 
ATOM   14313 C CA  . TYR E  1 319 ? 155.014 49.917  -26.176 1.00   94.85  ? 319 TYR E CA  1 
ATOM   14314 C C   . TYR E  1 319 ? 155.645 49.599  -27.537 1.00   100.70 ? 319 TYR E C   1 
ATOM   14315 O O   . TYR E  1 319 ? 155.231 48.688  -28.247 1.00   101.86 ? 319 TYR E O   1 
ATOM   14316 C CB  . TYR E  1 319 ? 156.053 49.709  -25.056 1.00   93.14  ? 319 TYR E CB  1 
ATOM   14317 C CG  . TYR E  1 319 ? 155.745 50.418  -23.732 1.00   90.62  ? 319 TYR E CG  1 
ATOM   14318 C CD1 . TYR E  1 319 ? 154.520 50.261  -23.085 1.00   85.06  ? 319 TYR E CD1 1 
ATOM   14319 C CD2 . TYR E  1 319 ? 156.679 51.284  -23.154 1.00   93.69  ? 319 TYR E CD2 1 
ATOM   14320 C CE1 . TYR E  1 319 ? 154.241 50.919  -21.896 1.00   82.88  ? 319 TYR E CE1 1 
ATOM   14321 C CE2 . TYR E  1 319 ? 156.404 51.955  -21.966 1.00   92.52  ? 319 TYR E CE2 1 
ATOM   14322 C CZ  . TYR E  1 319 ? 155.181 51.760  -21.340 1.00   88.36  ? 319 TYR E CZ  1 
ATOM   14323 O OH  . TYR E  1 319 ? 154.879 52.406  -20.163 1.00   88.11  ? 319 TYR E OH  1 
ATOM   14324 N N   . ASP E  1 320 ? 156.632 50.425  -27.874 1.00   105.18 ? 320 ASP E N   1 
ATOM   14325 C CA  . ASP E  1 320 ? 157.438 50.406  -29.099 1.00   110.44 ? 320 ASP E CA  1 
ATOM   14326 C C   . ASP E  1 320 ? 158.400 49.212  -29.267 1.00   111.24 ? 320 ASP E C   1 
ATOM   14327 O O   . ASP E  1 320 ? 158.570 48.375  -28.381 1.00   104.14 ? 320 ASP E O   1 
ATOM   14328 C CB  . ASP E  1 320 ? 158.203 51.756  -29.107 0.0000 104.25 ? 320 ASP E CB  1 
ATOM   14329 C CG  . ASP E  1 320 ? 159.259 51.889  -30.193 0.0000 112.16 ? 320 ASP E CG  1 
ATOM   14330 O OD1 . ASP E  1 320 ? 159.316 51.071  -31.132 0.0000 115.09 ? 320 ASP E OD1 1 
ATOM   14331 O OD2 . ASP E  1 320 ? 160.044 52.858  -30.107 0.0000 116.06 ? 320 ASP E OD2 1 
ATOM   14332 N N   . SER E  1 321 ? 158.962 49.103  -30.464 1.00   120.92 ? 321 SER E N   1 
ATOM   14333 C CA  . SER E  1 321 ? 159.854 48.005  -30.780 1.00   123.19 ? 321 SER E CA  1 
ATOM   14334 C C   . SER E  1 321 ? 161.115 48.193  -29.981 1.00   123.22 ? 321 SER E C   1 
ATOM   14335 O O   . SER E  1 321 ? 161.708 47.229  -29.527 1.00   123.50 ? 321 SER E O   1 
ATOM   14336 C CB  . SER E  1 321 ? 160.163 47.961  -32.279 1.00   129.20 ? 321 SER E CB  1 
ATOM   14337 O OG  . SER E  1 321 ? 161.203 47.036  -32.537 1.00   132.20 ? 321 SER E OG  1 
ATOM   14338 N N   . ARG E  1 322 ? 161.506 49.463  -29.875 0.0000 123.12 ? 322 ARG E N   1 
ATOM   14339 C CA  . ARG E  1 322 ? 162.597 49.932  -29.021 0.0000 122.07 ? 322 ARG E CA  1 
ATOM   14340 C C   . ARG E  1 322 ? 162.778 48.827  -27.964 0.0000 115.62 ? 322 ARG E C   1 
ATOM   14341 O O   . ARG E  1 322 ? 161.959 48.710  -27.043 0.0000 108.00 ? 322 ARG E O   1 
ATOM   14342 C CB  . ARG E  1 322 ? 162.195 51.322  -28.452 0.0000 115.02 ? 322 ARG E CB  1 
ATOM   14343 C CG  . ARG E  1 322 ? 162.459 51.638  -27.011 0.0000 110.86 ? 322 ARG E CG  1 
ATOM   14344 C CD  . ARG E  1 322 ? 163.916 51.434  -26.715 0.0000 115.32 ? 322 ARG E CD  1 
ATOM   14345 N NE  . ARG E  1 322 ? 164.121 51.097  -25.331 0.0000 110.59 ? 322 ARG E NE  1 
ATOM   14346 C CZ  . ARG E  1 322 ? 165.260 50.587  -24.914 0.0000 113.39 ? 322 ARG E CZ  1 
ATOM   14347 N NH1 . ARG E  1 322 ? 165.414 50.260  -23.650 0.0000 109.51 ? 322 ARG E NH1 1 
ATOM   14348 N NH2 . ARG E  1 322 ? 166.244 50.420  -25.788 0.0000 120.79 ? 322 ARG E NH2 1 
ATOM   14349 N N   . LYS E  1 323 ? 163.802 47.994  -28.199 0.0000 119.50 ? 323 LYS E N   1 
ATOM   14350 C CA  . LYS E  1 323 ? 164.023 46.699  -27.534 0.0000 115.94 ? 323 LYS E CA  1 
ATOM   14351 C C   . LYS E  1 323 ? 163.319 46.561  -26.185 0.0000 107.53 ? 323 LYS E C   1 
ATOM   14352 O O   . LYS E  1 323 ? 162.294 45.871  -26.136 0.0000 102.21 ? 323 LYS E O   1 
ATOM   14353 C CB  . LYS E  1 323 ? 165.532 46.414  -27.449 0.0000 121.78 ? 323 LYS E CB  1 
ATOM   14354 C CG  . LYS E  1 323 ? 166.357 47.444  -26.701 0.0000 123.13 ? 323 LYS E CG  1 
ATOM   14355 C CD  . LYS E  1 323 ? 167.849 47.244  -26.777 0.0000 130.06 ? 323 LYS E CD  1 
ATOM   14356 C CE  . LYS E  1 323 ? 168.496 47.613  -25.484 0.0000 128.80 ? 323 LYS E CE  1 
ATOM   14357 N NZ  . LYS E  1 323 ? 168.891 49.048  -25.540 0.0000 132.50 ? 323 LYS E NZ  1 
ATOM   14358 N N   . ILE E  1 324 ? 163.795 47.346  -25.207 1.00   106.73 ? 324 ILE E N   1 
ATOM   14359 C CA  . ILE E  1 324 ? 163.257 47.593  -23.842 1.00   100.49 ? 324 ILE E CA  1 
ATOM   14360 C C   . ILE E  1 324 ? 164.204 47.326  -22.631 1.00   116.88 ? 324 ILE E C   1 
ATOM   14361 O O   . ILE E  1 324 ? 163.880 47.694  -21.496 1.00   111.73 ? 324 ILE E O   1 
ATOM   14362 C CB  . ILE E  1 324 ? 161.890 46.895  -23.635 1.00   94.49  ? 324 ILE E CB  1 
ATOM   14363 C CG1 . ILE E  1 324 ? 160.842 47.916  -24.057 1.00   95.75  ? 324 ILE E CG1 1 
ATOM   14364 C CG2 . ILE E  1 324 ? 161.529 46.545  -22.231 1.00   87.02  ? 324 ILE E CG2 1 
ATOM   14365 C CD1 . ILE E  1 324 ? 161.078 49.288  -23.423 1.00   98.31  ? 324 ILE E CD1 1 
ATOM   14366 N N   . SER E  1 325 ? 165.425 46.844  -22.846 1.00   123.80 ? 325 SER E N   1 
ATOM   14367 C CA  . SER E  1 325 ? 166.351 46.732  -21.713 1.00   126.55 ? 325 SER E CA  1 
ATOM   14368 C C   . SER E  1 325 ? 166.796 48.127  -21.247 1.00   130.51 ? 325 SER E C   1 
ATOM   14369 O O   . SER E  1 325 ? 167.956 48.366  -21.023 1.00   136.43 ? 325 SER E O   1 
ATOM   14370 C CB  . SER E  1 325 ? 167.573 45.903  -22.078 1.00   133.52 ? 325 SER E CB  1 
ATOM   14371 O OG  . SER E  1 325 ? 168.570 46.720  -22.660 1.00   141.57 ? 325 SER E OG  1 
ATOM   14372 N N   . GLY E  1 326 ? 165.844 49.043  -21.109 1.00   127.84 ? 326 GLY E N   1 
ATOM   14373 C CA  . GLY E  1 326 ? 166.066 50.367  -20.561 1.00   129.58 ? 326 GLY E CA  1 
ATOM   14374 C C   . GLY E  1 326 ? 165.293 50.608  -19.286 1.00   122.76 ? 326 GLY E C   1 
ATOM   14375 O O   . GLY E  1 326 ? 165.710 51.419  -18.472 1.00   124.37 ? 326 GLY E O   1 
ATOM   14376 N N   . GLY E  1 327 ? 164.193 49.903  -19.059 1.00   115.62 ? 327 GLY E N   1 
ATOM   14377 C CA  . GLY E  1 327 ? 163.578 50.043  -17.756 1.00   111.89 ? 327 GLY E CA  1 
ATOM   14378 C C   . GLY E  1 327 ? 162.339 49.253  -17.409 1.00   108.00 ? 327 GLY E C   1 
ATOM   14379 O O   . GLY E  1 327 ? 161.586 49.722  -16.556 1.00   109.36 ? 327 GLY E O   1 
ATOM   14380 N N   . ALA E  1 328 ? 162.111 48.094  -18.043 1.00   103.06 ? 328 ALA E N   1 
ATOM   14381 C CA  . ALA E  1 328 ? 160.988 47.208  -17.660 1.00   91.87  ? 328 ALA E CA  1 
ATOM   14382 C C   . ALA E  1 328 ? 161.073 46.915  -16.177 1.00   85.17  ? 328 ALA E C   1 
ATOM   14383 O O   . ALA E  1 328 ? 161.964 46.194  -15.734 1.00   86.13  ? 328 ALA E O   1 
ATOM   14384 C CB  . ALA E  1 328 ? 161.004 45.928  -18.454 1.00   90.82  ? 328 ALA E CB  1 
ATOM   14385 N N   . PRO E  1 329 ? 160.155 47.502  -15.401 1.00   78.44  ? 329 PRO E N   1 
ATOM   14386 C CA  . PRO E  1 329 ? 160.281 47.448  -13.945 1.00   75.86  ? 329 PRO E CA  1 
ATOM   14387 C C   . PRO E  1 329 ? 159.838 46.180  -13.223 1.00   72.67  ? 329 PRO E C   1 
ATOM   14388 O O   . PRO E  1 329 ? 159.193 45.250  -13.733 1.00   67.72  ? 329 PRO E O   1 
ATOM   14389 C CB  . PRO E  1 329 ? 159.395 48.600  -13.481 1.00   72.53  ? 329 PRO E CB  1 
ATOM   14390 C CG  . PRO E  1 329 ? 158.407 48.769  -14.528 1.00   71.37  ? 329 PRO E CG  1 
ATOM   14391 C CD  . PRO E  1 329 ? 159.045 48.375  -15.823 1.00   74.82  ? 329 PRO E CD  1 
ATOM   14392 N N   . SER E  1 330 ? 160.225 46.226  -11.959 1.00   75.52  ? 330 SER E N   1 
ATOM   14393 C CA  . SER E  1 330 ? 159.754 45.367  -10.906 1.00   73.14  ? 330 SER E CA  1 
ATOM   14394 C C   . SER E  1 330 ? 158.260 45.205  -10.905 1.00   67.66  ? 330 SER E C   1 
ATOM   14395 O O   . SER E  1 330 ? 157.595 46.201  -10.834 1.00   71.91  ? 330 SER E O   1 
ATOM   14396 C CB  . SER E  1 330 ? 160.152 46.033  -9.575  1.00   74.97  ? 330 SER E CB  1 
ATOM   14397 O OG  . SER E  1 330 ? 159.526 45.480  -8.436  1.00   71.83  ? 330 SER E OG  1 
ATOM   14398 N N   . VAL E  1 331 ? 157.737 43.988  -11.023 1.00   57.93  ? 331 VAL E N   1 
ATOM   14399 C CA  . VAL E  1 331 ? 156.346 43.777  -10.673 1.00   50.23  ? 331 VAL E CA  1 
ATOM   14400 C C   . VAL E  1 331 ? 156.246 42.672  -9.628  1.00   47.96  ? 331 VAL E C   1 
ATOM   14401 O O   . VAL E  1 331 ? 156.471 41.511  -9.919  1.00   48.94  ? 331 VAL E O   1 
ATOM   14402 C CB  . VAL E  1 331 ? 155.464 43.437  -11.880 1.00   47.33  ? 331 VAL E CB  1 
ATOM   14403 C CG1 . VAL E  1 331 ? 154.015 43.211  -11.439 1.00   39.57  ? 331 VAL E CG1 1 
ATOM   14404 C CG2 . VAL E  1 331 ? 155.475 44.522  -12.871 1.00   49.03  ? 331 VAL E CG2 1 
ATOM   14405 N N   . ASP E  1 332 ? 155.893 43.049  -8.410  1.00   45.13  ? 332 ASP E N   1 
ATOM   14406 C CA  . ASP E  1 332 ? 155.856 42.114  -7.305  1.00   43.37  ? 332 ASP E CA  1 
ATOM   14407 C C   . ASP E  1 332 ? 154.529 42.145  -6.597  1.00   38.86  ? 332 ASP E C   1 
ATOM   14408 O O   . ASP E  1 332 ? 153.987 43.213  -6.328  1.00   36.48  ? 332 ASP E O   1 
ATOM   14409 C CB  . ASP E  1 332 ? 156.948 42.427  -6.298  1.00   47.53  ? 332 ASP E CB  1 
ATOM   14410 C CG  . ASP E  1 332 ? 158.311 42.452  -6.926  1.00   50.90  ? 332 ASP E CG  1 
ATOM   14411 O OD1 . ASP E  1 332 ? 158.483 41.757  -7.949  1.00   50.16  ? 332 ASP E OD1 1 
ATOM   14412 O OD2 . ASP E  1 332 ? 159.205 43.156  -6.410  1.00   53.08  ? 332 ASP E OD2 1 
ATOM   14413 N N   . LEU E  1 333 ? 154.044 40.961  -6.254  1.00   38.63  ? 333 LEU E N   1 
ATOM   14414 C CA  . LEU E  1 333 ? 152.880 40.830  -5.416  1.00   35.61  ? 333 LEU E CA  1 
ATOM   14415 C C   . LEU E  1 333 ? 153.306 40.770  -3.977  1.00   37.34  ? 333 LEU E C   1 
ATOM   14416 O O   . LEU E  1 333 ? 154.035 39.881  -3.579  1.00   38.97  ? 333 LEU E O   1 
ATOM   14417 C CB  . LEU E  1 333 ? 152.118 39.577  -5.785  1.00   36.64  ? 333 LEU E CB  1 
ATOM   14418 C CG  . LEU E  1 333 ? 151.868 39.446  -7.286  1.00   36.44  ? 333 LEU E CG  1 
ATOM   14419 C CD1 . LEU E  1 333 ? 151.057 38.210  -7.567  1.00   38.20  ? 333 LEU E CD1 1 
ATOM   14420 C CD2 . LEU E  1 333 ? 151.185 40.676  -7.828  1.00   33.94  ? 333 LEU E CD2 1 
ATOM   14421 N N   . ILE E  1 334 ? 152.856 41.720  -3.185  1.00   41.17  ? 334 ILE E N   1 
ATOM   14422 C CA  . ILE E  1 334 ? 153.146 41.648  -1.777  1.00   42.58  ? 334 ILE E CA  1 
ATOM   14423 C C   . ILE E  1 334 ? 152.045 40.834  -1.153  1.00   39.73  ? 334 ILE E C   1 
ATOM   14424 O O   . ILE E  1 334 ? 150.884 41.161  -1.277  1.00   38.24  ? 334 ILE E O   1 
ATOM   14425 C CB  . ILE E  1 334 ? 153.231 43.016  -1.131  1.00   43.04  ? 334 ILE E CB  1 
ATOM   14426 C CG1 . ILE E  1 334 ? 154.001 43.981  -2.041  1.00   42.80  ? 334 ILE E CG1 1 
ATOM   14427 C CG2 . ILE E  1 334 ? 153.835 42.887  0.254   1.00   45.23  ? 334 ILE E CG2 1 
ATOM   14428 C CD1 . ILE E  1 334 ? 155.382 43.522  -2.382  1.00   43.16  ? 334 ILE E CD1 1 
ATOM   14429 N N   . LEU E  1 335 ? 152.410 39.755  -0.496  1.00   40.48  ? 335 LEU E N   1 
ATOM   14430 C CA  . LEU E  1 335 ? 151.412 38.800  -0.087  1.00   39.61  ? 335 LEU E CA  1 
ATOM   14431 C C   . LEU E  1 335 ? 150.966 38.986  1.340   1.00   44.76  ? 335 LEU E C   1 
ATOM   14432 O O   . LEU E  1 335 ? 151.287 39.975  1.986   1.00   46.36  ? 335 LEU E O   1 
ATOM   14433 C CB  . LEU E  1 335 ? 151.914 37.378  -0.273  1.00   37.35  ? 335 LEU E CB  1 
ATOM   14434 C CG  . LEU E  1 335 ? 152.340 37.113  -1.704  1.00   35.74  ? 335 LEU E CG  1 
ATOM   14435 C CD1 . LEU E  1 335 ? 152.759 35.679  -1.833  1.00   36.60  ? 335 LEU E CD1 1 
ATOM   14436 C CD2 . LEU E  1 335 ? 151.190 37.458  -2.619  1.00   34.40  ? 335 LEU E CD2 1 
ATOM   14437 N N   . ASP E  1 336 ? 150.154 38.031  1.774   1.00   48.75  ? 336 ASP E N   1 
ATOM   14438 C CA  . ASP E  1 336 ? 149.538 38.016  3.079   1.00   54.54  ? 336 ASP E CA  1 
ATOM   14439 C C   . ASP E  1 336 ? 150.537 38.431  4.153   1.00   59.42  ? 336 ASP E C   1 
ATOM   14440 O O   . ASP E  1 336 ? 151.597 37.822  4.324   1.00   62.04  ? 336 ASP E O   1 
ATOM   14441 C CB  . ASP E  1 336 ? 149.019 36.602  3.349   1.00   55.98  ? 336 ASP E CB  1 
ATOM   14442 C CG  . ASP E  1 336 ? 148.228 36.493  4.625   1.00   58.98  ? 336 ASP E CG  1 
ATOM   14443 O OD1 . ASP E  1 336 ? 148.832 36.353  5.712   1.00   64.44  ? 336 ASP E OD1 1 
ATOM   14444 O OD2 . ASP E  1 336 ? 146.990 36.494  4.533   1.00   57.75  ? 336 ASP E OD2 1 
ATOM   14445 N N   . LYS E  1 337 ? 150.186 39.501  4.850   1.00   61.48  ? 337 LYS E N   1 
ATOM   14446 C CA  . LYS E  1 337 ? 150.931 40.026  5.997   1.00   66.24  ? 337 LYS E CA  1 
ATOM   14447 C C   . LYS E  1 337 ? 152.367 40.439  5.645   1.00   65.36  ? 337 LYS E C   1 
ATOM   14448 O O   . LYS E  1 337 ? 153.244 40.519  6.512   1.00   68.44  ? 337 LYS E O   1 
ATOM   14449 C CB  . LYS E  1 337 ? 150.896 39.056  7.173   1.00   71.74  ? 337 LYS E CB  1 
ATOM   14450 C CG  . LYS E  1 337 ? 149.548 39.150  7.882   1.00   74.30  ? 337 LYS E CG  1 
ATOM   14451 C CD  . LYS E  1 337 ? 149.470 38.368  9.178   1.00   81.42  ? 337 LYS E CD  1 
ATOM   14452 C CE  . LYS E  1 337 ? 150.375 37.165  9.208   1.00   85.62  ? 337 LYS E CE  1 
ATOM   14453 N NZ  . LYS E  1 337 ? 150.916 36.996  10.601  1.00   91.39  ? 337 LYS E NZ  1 
ATOM   14454 N N   . ASN E  1 338 ? 152.582 40.691  4.356   1.00   62.73  ? 338 ASN E N   1 
ATOM   14455 C CA  . ASN E  1 338 ? 153.882 41.036  3.800   1.00   65.43  ? 338 ASN E CA  1 
ATOM   14456 C C   . ASN E  1 338 ? 154.957 39.993  4.104   1.00   70.41  ? 338 ASN E C   1 
ATOM   14457 O O   . ASN E  1 338 ? 156.153 40.300  4.043   1.00   74.96  ? 338 ASN E O   1 
ATOM   14458 C CB  . ASN E  1 338 ? 154.356 42.392  4.354   1.00   69.71  ? 338 ASN E CB  1 
ATOM   14459 C CG  . ASN E  1 338 ? 153.268 43.469  4.342   1.00   68.34  ? 338 ASN E CG  1 
ATOM   14460 O OD1 . ASN E  1 338 ? 152.456 43.544  3.427   1.00   66.16  ? 338 ASN E OD1 1 
ATOM   14461 N ND2 . ASN E  1 338 ? 153.299 44.350  5.340   1.00   70.07  ? 338 ASN E ND2 1 
ATOM   14462 N N   . ASP E  1 339 ? 154.549 38.761  4.402   1.00   69.88  ? 339 ASP E N   1 
ATOM   14463 C CA  . ASP E  1 339 ? 155.518 37.722  4.758   1.00   73.27  ? 339 ASP E CA  1 
ATOM   14464 C C   . ASP E  1 339 ? 156.224 37.166  3.550   1.00   69.18  ? 339 ASP E C   1 
ATOM   14465 O O   . ASP E  1 339 ? 157.311 36.605  3.657   1.00   73.30  ? 339 ASP E O   1 
ATOM   14466 C CB  . ASP E  1 339 ? 154.827 36.594  5.519   1.00   74.75  ? 339 ASP E CB  1 
ATOM   14467 C CG  . ASP E  1 339 ? 154.433 37.002  6.919   1.00   79.39  ? 339 ASP E CG  1 
ATOM   14468 O OD1 . ASP E  1 339 ? 155.200 37.750  7.576   1.00   85.73  ? 339 ASP E OD1 1 
ATOM   14469 O OD2 . ASP E  1 339 ? 153.331 36.611  7.348   1.00   77.38  1 339 ASP E OD2 1 
ATOM   14470 N N   . ALA E  1 340 ? 155.600 37.326  2.399   1.00   60.23  ? 340 ALA E N   1 
ATOM   14471 C CA  . ALA E  1 340 ? 156.122 36.717  1.207   1.00   56.20  ? 340 ALA E CA  1 
ATOM   14472 C C   . ALA E  1 340 ? 155.890 37.637  0.044   1.00   49.35  ? 340 ALA E C   1 
ATOM   14473 O O   . ALA E  1 340 ? 155.020 38.498  0.084   1.00   48.13  ? 340 ALA E O   1 
ATOM   14474 C CB  . ALA E  1 340 ? 155.462 35.390  0.973   1.00   56.03  ? 340 ALA E CB  1 
ATOM   14475 N N   . VAL E  1 341 ? 156.638 37.420  -1.015  1.00   47.04  ? 341 VAL E N   1 
ATOM   14476 C CA  . VAL E  1 341 ? 156.552 38.289  -2.162  1.00   45.50  ? 341 VAL E CA  1 
ATOM   14477 C C   . VAL E  1 341 ? 156.563 37.344  -3.328  1.00   42.50  ? 341 VAL E C   1 
ATOM   14478 O O   . VAL E  1 341 ? 157.322 36.397  -3.341  1.00   45.26  ? 341 VAL E O   1 
ATOM   14479 C CB  . VAL E  1 341 ? 157.726 39.314  -2.230  1.00   48.59  ? 341 VAL E CB  1 
ATOM   14480 C CG1 . VAL E  1 341 ? 157.801 39.979  -3.585  1.00   47.45  ? 341 VAL E CG1 1 
ATOM   14481 C CG2 . VAL E  1 341 ? 157.566 40.367  -1.169  1.00   51.61  ? 341 VAL E CG2 1 
ATOM   14482 N N   . TRP E  1 342 ? 155.662 37.549  -4.266  1.00   42.49  ? 342 TRP E N   1 
ATOM   14483 C CA  . TRP E  1 342 ? 155.715 36.829  -5.517  1.00   43.18  ? 342 TRP E CA  1 
ATOM   14484 C C   . TRP E  1 342 ? 156.168 37.744  -6.648  1.00   44.30  ? 342 TRP E C   1 
ATOM   14485 O O   . TRP E  1 342 ? 155.381 38.517  -7.188  1.00   43.78  ? 342 TRP E O   1 
ATOM   14486 C CB  . TRP E  1 342 ? 154.360 36.216  -5.838  1.00   43.04  ? 342 TRP E CB  1 
ATOM   14487 C CG  . TRP E  1 342 ? 154.450 35.086  -6.802  1.00   46.63  ? 342 TRP E CG  1 
ATOM   14488 C CD1 . TRP E  1 342 ? 155.494 34.792  -7.630  1.00   53.28  ? 342 TRP E CD1 1 
ATOM   14489 C CD2 . TRP E  1 342 ? 153.474 34.064  -7.012  1.00   45.26  ? 342 TRP E CD2 1 
ATOM   14490 N NE1 . TRP E  1 342 ? 155.220 33.658  -8.358  1.00   53.48  ? 342 TRP E NE1 1 
ATOM   14491 C CE2 . TRP E  1 342 ? 153.986 33.191  -7.993  1.00   48.61  ? 342 TRP E CE2 1 
ATOM   14492 C CE3 . TRP E  1 342 ? 152.212 33.806  -6.472  1.00   43.99  ? 342 TRP E CE3 1 
ATOM   14493 C CZ2 . TRP E  1 342 ? 153.281 32.075  -8.445  1.00   49.26  ? 342 TRP E CZ2 1 
ATOM   14494 C CZ3 . TRP E  1 342 ? 151.509 32.694  -6.927  1.00   45.13  ? 342 TRP E CZ3 1 
ATOM   14495 C CH2 . TRP E  1 342 ? 152.050 31.843  -7.903  1.00   46.81  ? 342 TRP E CH2 1 
ATOM   14496 N N   . ARG E  1 343 ? 157.442 37.661  -6.996  1.00   48.59  ? 343 ARG E N   1 
ATOM   14497 C CA  . ARG E  1 343 ? 158.002 38.487  -8.052  1.00   52.46  ? 343 ARG E CA  1 
ATOM   14498 C C   . ARG E  1 343 ? 157.541 38.002  -9.405  1.00   50.41  ? 343 ARG E C   1 
ATOM   14499 O O   . ARG E  1 343 ? 157.569 36.821  -9.668  1.00   51.61  ? 343 ARG E O   1 
ATOM   14500 C CB  . ARG E  1 343 ? 159.519 38.458  -7.971  1.00   61.17  ? 343 ARG E CB  1 
ATOM   14501 C CG  . ARG E  1 343 ? 160.040 39.234  -6.778  1.00   69.22  ? 343 ARG E CG  1 
ATOM   14502 C CD  . ARG E  1 343 ? 161.255 38.582  -6.113  1.00   78.75  ? 343 ARG E CD  1 
ATOM   14503 N NE  . ARG E  1 343 ? 161.501 39.194  -4.805  1.00   83.13  ? 343 ARG E NE  1 
ATOM   14504 C CZ  . ARG E  1 343 ? 161.699 38.519  -3.672  1.00   86.23  ? 343 ARG E CZ  1 
ATOM   14505 N NH1 . ARG E  1 343 ? 161.692 37.190  -3.672  1.00   86.37  ? 343 ARG E NH1 1 
ATOM   14506 N NH2 . ARG E  1 343 ? 161.900 39.180  -2.533  1.00   88.60  ? 343 ARG E NH2 1 
ATOM   14507 N N   . ILE E  1 344 ? 157.116 38.899  -10.272 1.00   49.29  ? 344 ILE E N   1 
ATOM   14508 C CA  . ILE E  1 344 ? 156.734 38.476  -11.602 1.00   49.61  ? 344 ILE E CA  1 
ATOM   14509 C C   . ILE E  1 344 ? 157.776 38.930  -12.595 1.00   57.28  ? 344 ILE E C   1 
ATOM   14510 O O   . ILE E  1 344 ? 158.112 40.114  -12.662 1.00   60.00  ? 344 ILE E O   1 
ATOM   14511 C CB  . ILE E  1 344 ? 155.393 39.004  -12.006 1.00   46.54  ? 344 ILE E CB  1 
ATOM   14512 C CG1 . ILE E  1 344 ? 154.352 38.554  -10.985 1.00   44.13  ? 344 ILE E CG1 1 
ATOM   14513 C CG2 . ILE E  1 344 ? 155.039 38.447  -13.362 1.00   49.31  ? 344 ILE E CG2 1 
ATOM   14514 C CD1 . ILE E  1 344 ? 152.972 39.108  -11.227 1.00   40.49  ? 344 ILE E CD1 1 
ATOM   14515 N N   . SER E  1 345 ? 158.278 37.971  -13.368 1.00   62.10  ? 345 SER E N   1 
ATOM   14516 C CA  . SER E  1 345 ? 159.370 38.223  -14.281 1.00   68.21  ? 345 SER E CA  1 
ATOM   14517 C C   . SER E  1 345 ? 158.913 39.206  -15.320 1.00   67.94  ? 345 SER E C   1 
ATOM   14518 O O   . SER E  1 345 ? 157.781 39.147  -15.795 1.00   64.61  ? 345 SER E O   1 
ATOM   14519 C CB  . SER E  1 345 ? 159.845 36.929  -14.949 1.00   74.56  ? 345 SER E CB  1 
ATOM   14520 O OG  . SER E  1 345 ? 159.952 35.872  -14.011 1.00   75.33  ? 345 SER E OG  1 
ATOM   14521 N N   . SER E  1 346 ? 159.835 40.070  -15.717 1.00   74.18  ? 346 SER E N   1 
ATOM   14522 C CA  . SER E  1 346 ? 159.520 41.181  -16.591 1.00   77.77  ? 346 SER E CA  1 
ATOM   14523 C C   . SER E  1 346 ? 159.072 40.800  -17.997 1.00   80.82  ? 346 SER E C   1 
ATOM   14524 O O   . SER E  1 346 ? 158.656 41.670  -18.745 1.00   80.87  ? 346 SER E O   1 
ATOM   14525 C CB  . SER E  1 346 ? 160.715 42.134  -16.653 1.00   82.71  ? 346 SER E CB  1 
ATOM   14526 O OG  . SER E  1 346 ? 161.745 41.571  -17.430 1.00   88.22  ? 346 SER E OG  1 
ATOM   14527 N N   . GLU E  1 347 ? 159.170 39.537  -18.386 1.00   83.95  ? 347 GLU E N   1 
ATOM   14528 C CA  . GLU E  1 347 ? 158.554 39.164  -19.646 1.00   87.67  ? 347 GLU E CA  1 
ATOM   14529 C C   . GLU E  1 347 ? 157.546 38.057  -19.343 1.00   89.23  ? 347 GLU E C   1 
ATOM   14530 O O   . GLU E  1 347 ? 156.813 37.601  -20.222 1.00   91.44  ? 347 GLU E O   1 
ATOM   14531 C CB  . GLU E  1 347 ? 159.548 38.761  -20.730 0.0000 90.97  ? 347 GLU E CB  1 
ATOM   14532 C CG  . GLU E  1 347 ? 158.824 38.625  -22.084 0.0000 89.93  ? 347 GLU E CG  1 
ATOM   14533 C CD  . GLU E  1 347 ? 159.569 37.865  -23.168 0.0000 94.65  ? 347 GLU E CD  1 
ATOM   14534 O OE1 . GLU E  1 347 ? 160.756 38.163  -23.399 0.0000 99.08  ? 347 GLU E OE1 1 
ATOM   14535 O OE2 . GLU E  1 347 ? 158.947 36.979  -23.805 0.0000 94.94  ? 347 GLU E OE2 1 
ATOM   14536 N N   . ASN E  1 348 ? 157.524 37.594  -18.100 1.00   88.39  ? 348 ASN E N   1 
ATOM   14537 C CA  . ASN E  1 348 ? 156.408 36.771  -17.693 1.00   86.02  ? 348 ASN E CA  1 
ATOM   14538 C C   . ASN E  1 348 ? 155.200 37.676  -17.961 1.00   80.70  ? 348 ASN E C   1 
ATOM   14539 O O   . ASN E  1 348 ? 154.179 37.210  -18.470 1.00   83.49  ? 348 ASN E O   1 
ATOM   14540 C CB  . ASN E  1 348 ? 156.521 36.297  -16.241 1.00   85.79  ? 348 ASN E CB  1 
ATOM   14541 C CG  . ASN E  1 348 ? 155.395 35.350  -15.841 1.00   84.34  ? 348 ASN E CG  1 
ATOM   14542 O OD1 . ASN E  1 348 ? 154.214 35.701  -15.911 1.00   81.71  ? 348 ASN E OD1 1 
ATOM   14543 N ND2 . ASN E  1 348 ? 155.758 34.112  -15.501 1.00   86.27  ? 348 ASN E ND2 1 
ATOM   14544 N N   . PHE E  1 349 ? 155.304 38.958  -17.594 1.00   72.13  ? 349 PHE E N   1 
ATOM   14545 C CA  . PHE E  1 349 ? 154.180 39.883  -17.791 1.00   63.00  ? 349 PHE E CA  1 
ATOM   14546 C C   . PHE E  1 349 ? 154.221 40.729  -19.084 1.00   64.32  ? 349 PHE E C   1 
ATOM   14547 O O   . PHE E  1 349 ? 153.245 41.398  -19.404 1.00   64.17  ? 349 PHE E O   1 
ATOM   14548 C CB  . PHE E  1 349 ? 154.008 40.801  -16.563 1.00   57.69  ? 349 PHE E CB  1 
ATOM   14549 C CG  . PHE E  1 349 ? 155.140 41.766  -16.298 1.00   57.69  ? 349 PHE E CG  1 
ATOM   14550 C CD1 . PHE E  1 349 ? 155.311 42.907  -17.068 1.00   58.71  ? 349 PHE E CD1 1 
ATOM   14551 C CD2 . PHE E  1 349 ? 155.998 41.558  -15.224 1.00   56.34  ? 349 PHE E CD2 1 
ATOM   14552 C CE1 . PHE E  1 349 ? 156.343 43.804  -16.796 1.00   59.97  ? 349 PHE E CE1 1 
ATOM   14553 C CE2 . PHE E  1 349 ? 157.028 42.451  -14.944 1.00   58.12  ? 349 PHE E CE2 1 
ATOM   14554 C CZ  . PHE E  1 349 ? 157.204 43.574  -15.735 1.00   60.33  ? 349 PHE E CZ  1 
ATOM   14555 N N   . MET E  1 350 ? 155.319 40.712  -19.835 1.00   65.91  ? 350 MET E N   1 
ATOM   14556 C CA  . MET E  1 350 ? 155.315 41.389  -21.135 1.00   68.02  ? 350 MET E CA  1 
ATOM   14557 C C   . MET E  1 350 ? 155.033 40.431  -22.258 1.00   70.53  ? 350 MET E C   1 
ATOM   14558 O O   . MET E  1 350 ? 155.772 39.492  -22.473 1.00   70.71  ? 350 MET E O   1 
ATOM   14559 C CB  . MET E  1 350 ? 156.647 42.082  -21.434 1.00   71.60  ? 350 MET E CB  1 
ATOM   14560 C CG  . MET E  1 350 ? 157.017 43.263  -20.547 1.00   71.30  ? 350 MET E CG  1 
ATOM   14561 S SD  . MET E  1 350 ? 155.788 44.571  -20.393 1.00   74.30  ? 350 MET E SD  1 
ATOM   14562 C CE  . MET E  1 350 ? 155.567 45.061  -22.098 1.00   67.01  ? 350 MET E CE  1 
ATOM   14563 N N   . VAL E  1 351 ? 153.986 40.701  -23.010 1.00   74.30  ? 351 VAL E N   1 
ATOM   14564 C CA  . VAL E  1 351 ? 153.607 39.817  -24.098 1.00   80.66  ? 351 VAL E CA  1 
ATOM   14565 C C   . VAL E  1 351 ? 153.810 40.531  -25.427 1.00   83.66  ? 351 VAL E C   1 
ATOM   14566 O O   . VAL E  1 351 ? 153.742 41.753  -25.504 1.00   84.19  ? 351 VAL E O   1 
ATOM   14567 C CB  . VAL E  1 351 ? 152.154 39.292  -23.947 1.00   95.05  ? 351 VAL E CB  1 
ATOM   14568 C CG1 . VAL E  1 351 ? 151.659 39.483  -22.521 1.00   88.44  ? 351 VAL E CG1 1 
ATOM   14569 C CG2 . VAL E  1 351 ? 151.218 39.965  -24.937 1.00   97.71  ? 351 VAL E CG2 1 
ATOM   14570 N N   . GLN E  1 352 ? 154.128 39.766  -26.459 1.00   87.28  ? 352 GLN E N   1 
ATOM   14571 C CA  . GLN E  1 352 ? 154.398 40.348  -27.761 1.00   94.43  ? 352 GLN E CA  1 
ATOM   14572 C C   . GLN E  1 352 ? 153.184 40.349  -28.717 1.00   97.25  ? 352 GLN E C   1 
ATOM   14573 O O   . GLN E  1 352 ? 152.698 41.414  -29.123 1.00   97.22  ? 352 GLN E O   1 
ATOM   14574 C CB  . GLN E  1 352 ? 155.570 39.601  -28.376 1.00   101.76 ? 352 GLN E CB  1 
ATOM   14575 C CG  . GLN E  1 352 ? 155.911 40.040  -29.740 1.00   111.39 ? 352 GLN E CG  1 
ATOM   14576 C CD  . GLN E  1 352 ? 156.562 41.407  -29.732 1.00   115.72 ? 352 GLN E CD  1 
ATOM   14577 O OE1 . GLN E  1 352 ? 156.441 42.181  -30.686 1.00   119.33 ? 352 GLN E OE1 1 
ATOM   14578 N NE2 . GLN E  1 352 ? 157.251 41.722  -28.629 1.00   115.26 ? 352 GLN E NE2 1 
ATOM   14579 N N   . ALA E  1 353 ? 152.727 39.158  -29.102 1.00   100.75 ? 353 ALA E N   1 
ATOM   14580 C CA  . ALA E  1 353 ? 151.507 38.977  -29.910 1.00   103.06 ? 353 ALA E CA  1 
ATOM   14581 C C   . ALA E  1 353 ? 151.564 39.580  -31.312 1.00   107.73 ? 353 ALA E C   1 
ATOM   14582 O O   . ALA E  1 353 ? 150.717 39.293  -32.159 1.00   110.55 ? 353 ALA E O   1 
ATOM   14583 C CB  . ALA E  1 353 ? 150.311 39.544  -29.165 1.00   98.63  ? 353 ALA E CB  1 
ATOM   14584 N N   . GLN E  1 354 ? 152.584 40.385  -31.555 1.00   108.70 ? 354 GLN E N   1 
ATOM   14585 C CA  . GLN E  1 354 ? 152.745 41.085  -32.810 1.00   113.77 ? 354 GLN E CA  1 
ATOM   14586 C C   . GLN E  1 354 ? 154.216 41.039  -33.177 1.00   120.30 ? 354 GLN E C   1 
ATOM   14587 O O   . GLN E  1 354 ? 155.033 40.531  -32.436 1.00   119.57 ? 354 GLN E O   1 
ATOM   14588 C CB  . GLN E  1 354 ? 152.239 42.522  -32.729 1.00   110.26 ? 354 GLN E CB  1 
ATOM   14589 C CG  . GLN E  1 354 ? 151.286 42.891  -33.862 1.00   113.66 ? 354 GLN E CG  1 
ATOM   14590 C CD  . GLN E  1 354 ? 150.671 44.254  -33.671 1.00   112.62 ? 354 GLN E CD  1 
ATOM   14591 O OE1 . GLN E  1 354 ? 151.310 45.147  -33.124 1.00   112.84 ? 354 GLN E OE1 1 
ATOM   14592 N NE2 . GLN E  1 354 ? 149.431 44.427  -34.125 1.00   112.49 ? 354 GLN E NE2 1 
ATOM   14593 N N   . ASP E  1 355 ? 154.516 41.470  -34.391 1.00   128.01 ? 355 ASP E N   1 
ATOM   14594 C CA  . ASP E  1 355 ? 155.888 41.692  -34.869 1.00   132.89 ? 355 ASP E CA  1 
ATOM   14595 C C   . ASP E  1 355 ? 156.881 42.312  -33.864 1.00   126.13 ? 355 ASP E C   1 
ATOM   14596 O O   . ASP E  1 355 ? 157.711 41.613  -33.287 1.00   124.21 ? 355 ASP E O   1 
ATOM   14597 C CB  . ASP E  1 355 ? 155.849 42.571  -36.135 1.00   140.99 ? 355 ASP E CB  1 
ATOM   14598 C CG  . ASP E  1 355 ? 154.989 43.817  -35.962 1.00   139.35 ? 355 ASP E CG  1 
ATOM   14599 O OD1 . ASP E  1 355 ? 154.980 44.405  -34.855 1.00   134.17 ? 355 ASP E OD1 1 
ATOM   14600 O OD2 . ASP E  1 355 ? 154.308 44.195  -36.931 1.00   143.47 ? 355 ASP E OD2 1 
ATOM   14601 N N   . GLY E  1 356 ? 156.790 43.623  -33.669 1.00   123.05 ? 356 GLY E N   1 
ATOM   14602 C CA  . GLY E  1 356 ? 157.704 44.332  -32.799 1.00   121.11 ? 356 GLY E CA  1 
ATOM   14603 C C   . GLY E  1 356 ? 157.008 45.157  -31.737 1.00   115.38 ? 356 GLY E C   1 
ATOM   14604 O O   . GLY E  1 356 ? 157.541 46.151  -31.267 1.00   115.29 ? 356 GLY E O   1 
ATOM   14605 N N   . VAL E  1 357 ? 155.818 44.736  -31.335 1.00   111.12 ? 357 VAL E N   1 
ATOM   14606 C CA  . VAL E  1 357 ? 155.106 45.437  -30.279 1.00   104.09 ? 357 VAL E CA  1 
ATOM   14607 C C   . VAL E  1 357 ? 154.943 44.548  -29.088 1.00   95.53  ? 357 VAL E C   1 
ATOM   14608 O O   . VAL E  1 357 ? 154.367 43.473  -29.173 1.00   93.37  ? 357 VAL E O   1 
ATOM   14609 C CB  . VAL E  1 357 ? 153.717 45.915  -30.721 1.00   104.04 ? 357 VAL E CB  1 
ATOM   14610 C CG1 . VAL E  1 357 ? 152.960 46.490  -29.543 1.00   96.52  ? 357 VAL E CG1 1 
ATOM   14611 C CG2 . VAL E  1 357 ? 153.833 46.924  -31.852 1.00   110.55 ? 357 VAL E CG2 1 
ATOM   14612 N N   . SER E  1 358 ? 155.423 45.041  -27.961 1.00   92.32  ? 358 SER E N   1 
ATOM   14613 C CA  . SER E  1 358 ? 155.420 44.279  -26.736 1.00   88.90  ? 358 SER E CA  1 
ATOM   14614 C C   . SER E  1 358 ? 154.463 44.939  -25.744 1.00   87.38  ? 358 SER E C   1 
ATOM   14615 O O   . SER E  1 358 ? 154.569 46.134  -25.475 1.00   90.01  ? 358 SER E O   1 
ATOM   14616 C CB  . SER E  1 358 ? 156.852 44.195  -26.196 1.00   87.86  ? 358 SER E CB  1 
ATOM   14617 O OG  . SER E  1 358 ? 156.921 43.608  -24.914 1.00   82.47  ? 358 SER E OG  1 
ATOM   14618 N N   . CYS E  1 359 ? 153.477 44.175  -25.273 1.00   83.08  ? 359 CYS E N   1 
ATOM   14619 C CA  . CYS E  1 359 ? 152.410 44.715  -24.426 1.00   77.02  ? 359 CYS E CA  1 
ATOM   14620 C C   . CYS E  1 359 ? 152.406 44.208  -22.988 1.00   68.60  ? 359 CYS E C   1 
ATOM   14621 O O   . CYS E  1 359 ? 152.840 43.091  -22.686 1.00   68.33  ? 359 CYS E O   1 
ATOM   14622 C CB  . CYS E  1 359 ? 151.041 44.448  -25.056 1.00   78.60  ? 359 CYS E CB  1 
ATOM   14623 S SG  . CYS E  1 359 ? 150.742 45.378  -26.577 1.00   100.36 ? 359 CYS E SG  1 
ATOM   14624 N N   . LEU E  1 360 ? 151.917 45.071  -22.106 1.00   64.72  ? 360 LEU E N   1 
ATOM   14625 C CA  . LEU E  1 360 ? 151.723 44.732  -20.706 1.00   61.35  ? 360 LEU E CA  1 
ATOM   14626 C C   . LEU E  1 360 ? 150.578 43.758  -20.601 1.00   60.76  ? 360 LEU E C   1 
ATOM   14627 O O   . LEU E  1 360 ? 149.436 44.117  -20.889 1.00   60.44  ? 360 LEU E O   1 
ATOM   14628 C CB  . LEU E  1 360 ? 151.425 45.978  -19.879 1.00   60.72  ? 360 LEU E CB  1 
ATOM   14629 C CG  . LEU E  1 360 ? 151.192 45.730  -18.390 1.00   57.42  ? 360 LEU E CG  1 
ATOM   14630 C CD1 . LEU E  1 360 ? 152.450 45.137  -17.759 1.00   56.76  ? 360 LEU E CD1 1 
ATOM   14631 C CD2 . LEU E  1 360 ? 150.767 47.014  -17.689 1.00   57.92  ? 360 LEU E CD2 1 
ATOM   14632 N N   . GLY E  1 361 ? 150.889 42.534  -20.176 1.00   62.39  ? 361 GLY E N   1 
ATOM   14633 C CA  . GLY E  1 361 ? 149.949 41.429  -20.235 1.00   63.19  ? 361 GLY E CA  1 
ATOM   14634 C C   . GLY E  1 361 ? 148.952 41.365  -19.102 1.00   56.65  ? 361 GLY E C   1 
ATOM   14635 O O   . GLY E  1 361 ? 148.730 40.295  -18.525 1.00   57.86  ? 361 GLY E O   1 
ATOM   14636 N N   . PHE E  1 362 ? 148.335 42.499  -18.794 1.00   51.53  ? 362 PHE E N   1 
ATOM   14637 C CA  . PHE E  1 362 ? 147.267 42.540  -17.809 1.00   48.07  ? 362 PHE E CA  1 
ATOM   14638 C C   . PHE E  1 362 ? 146.029 43.118  -18.451 1.00   50.35  ? 362 PHE E C   1 
ATOM   14639 O O   . PHE E  1 362 ? 146.125 44.111  -19.179 1.00   54.47  ? 362 PHE E O   1 
ATOM   14640 C CB  . PHE E  1 362 ? 147.653 43.394  -16.604 1.00   46.07  ? 362 PHE E CB  1 
ATOM   14641 C CG  . PHE E  1 362 ? 148.840 42.885  -15.845 1.00   48.62  ? 362 PHE E CG  1 
ATOM   14642 C CD1 . PHE E  1 362 ? 150.116 43.035  -16.346 1.00   53.92  ? 362 PHE E CD1 1 
ATOM   14643 C CD2 . PHE E  1 362 ? 148.684 42.275  -14.620 1.00   48.96  ? 362 PHE E CD2 1 
ATOM   14644 C CE1 . PHE E  1 362 ? 151.223 42.583  -15.647 1.00   55.87  ? 362 PHE E CE1 1 
ATOM   14645 C CE2 . PHE E  1 362 ? 149.786 41.814  -13.920 1.00   50.47  ? 362 PHE E CE2 1 
ATOM   14646 C CZ  . PHE E  1 362 ? 151.057 41.973  -14.437 1.00   54.09  ? 362 PHE E CZ  1 
ATOM   14647 N N   . VAL E  1 363 ? 144.867 42.527  -18.175 1.00   47.85  ? 363 VAL E N   1 
ATOM   14648 C CA  . VAL E  1 363 ? 143.643 42.983  -18.825 1.00   49.60  ? 363 VAL E CA  1 
ATOM   14649 C C   . VAL E  1 363 ? 142.529 43.419  -17.845 1.00   49.68  ? 363 VAL E C   1 
ATOM   14650 O O   . VAL E  1 363 ? 142.430 42.947  -16.708 1.00   49.45  ? 363 VAL E O   1 
ATOM   14651 C CB  . VAL E  1 363 ? 143.115 41.906  -19.807 1.00   52.05  ? 363 VAL E CB  1 
ATOM   14652 C CG1 . VAL E  1 363 ? 144.120 41.631  -20.910 1.00   55.97  ? 363 VAL E CG1 1 
ATOM   14653 C CG2 . VAL E  1 363 ? 142.791 40.649  -19.085 1.00   50.47  ? 363 VAL E CG2 1 
ATOM   14654 N N   . ASP E  1 364 ? 141.704 44.348  -18.314 1.00   50.65  ? 364 ASP E N   1 
ATOM   14655 C CA  . ASP E  1 364 ? 140.627 44.946  -17.548 1.00   47.66  ? 364 ASP E CA  1 
ATOM   14656 C C   . ASP E  1 364 ? 139.465 43.960  -17.469 1.00   49.40  ? 364 ASP E C   1 
ATOM   14657 O O   . ASP E  1 364 ? 138.943 43.553  -18.503 1.00   53.24  ? 364 ASP E O   1 
ATOM   14658 C CB  . ASP E  1 364 ? 140.184 46.244  -18.230 1.00   54.46  ? 364 ASP E CB  1 
ATOM   14659 C CG  . ASP E  1 364 ? 139.357 47.150  -17.334 1.00   53.61  ? 364 ASP E CG  1 
ATOM   14660 O OD1 . ASP E  1 364 ? 138.903 46.733  -16.258 1.00   48.71  ? 364 ASP E OD1 1 
ATOM   14661 O OD2 . ASP E  1 364 ? 139.132 48.303  -17.740 1.00   58.33  1 364 ASP E OD2 1 
ATOM   14662 N N   . GLY E  1 365 ? 139.067 43.576  -16.257 1.00   47.07  ? 365 GLY E N   1 
ATOM   14663 C CA  . GLY E  1 365 ? 137.953 42.659  -16.052 1.00   49.24  ? 365 GLY E CA  1 
ATOM   14664 C C   . GLY E  1 365 ? 136.559 43.275  -16.098 1.00   56.73  ? 365 GLY E C   1 
ATOM   14665 O O   . GLY E  1 365 ? 135.562 42.581  -15.919 1.00   57.78  ? 365 GLY E O   1 
ATOM   14666 N N   . GLY E  1 366 ? 136.483 44.579  -16.343 1.00   58.37  ? 366 GLY E N   1 
ATOM   14667 C CA  . GLY E  1 366 ? 135.214 45.284  -16.396 1.00   62.83  ? 366 GLY E CA  1 
ATOM   14668 C C   . GLY E  1 366 ? 134.798 45.685  -15.000 1.00   63.12  ? 366 GLY E C   1 
ATOM   14669 O O   . GLY E  1 366 ? 135.588 45.603  -14.062 1.00   59.74  ? 366 GLY E O   1 
ATOM   14670 N N   . VAL E  1 367 ? 133.569 46.147  -14.852 1.00   68.53  ? 367 VAL E N   1 
ATOM   14671 C CA  . VAL E  1 367 ? 133.148 46.647  -13.558 1.00   69.06  ? 367 VAL E CA  1 
ATOM   14672 C C   . VAL E  1 367 ? 132.472 45.558  -12.751 1.00   70.19  ? 367 VAL E C   1 
ATOM   14673 O O   . VAL E  1 367 ? 132.362 45.654  -11.532 1.00   68.66  ? 367 VAL E O   1 
ATOM   14674 C CB  . VAL E  1 367 ? 132.209 47.826  -13.722 1.00   72.19  ? 367 VAL E CB  1 
ATOM   14675 C CG1 . VAL E  1 367 ? 132.959 48.950  -14.392 1.00   72.73  ? 367 VAL E CG1 1 
ATOM   14676 C CG2 . VAL E  1 367 ? 130.985 47.423  -14.550 1.00   75.66  ? 367 VAL E CG2 1 
ATOM   14677 N N   . HIS E  1 368 ? 132.076 44.490  -13.434 1.00   73.03  ? 368 HIS E N   1 
ATOM   14678 C CA  . HIS E  1 368 ? 131.461 43.348  -12.774 1.00   75.13  ? 368 HIS E CA  1 
ATOM   14679 C C   . HIS E  1 368 ? 132.350 42.125  -12.905 1.00   75.75  ? 368 HIS E C   1 
ATOM   14680 O O   . HIS E  1 368 ? 131.874 41.029  -13.192 1.00   80.35  ? 368 HIS E O   1 
ATOM   14681 C CB  . HIS E  1 368 ? 130.059 43.067  -13.342 1.00   79.84  ? 368 HIS E CB  1 
ATOM   14682 C CG  . HIS E  1 368 ? 129.085 44.190  -13.134 1.00   85.98  ? 368 HIS E CG  1 
ATOM   14683 N ND1 . HIS E  1 368 ? 128.658 44.581  -11.882 1.00   87.38  ? 368 HIS E ND1 1 
ATOM   14684 C CD2 . HIS E  1 368 ? 128.469 45.011  -14.017 1.00   90.97  ? 368 HIS E CD2 1 
ATOM   14685 C CE1 . HIS E  1 368 ? 127.817 45.592  -12.004 1.00   92.96  ? 368 HIS E CE1 1 
ATOM   14686 N NE2 . HIS E  1 368 ? 127.685 45.873  -13.287 1.00   95.40  ? 368 HIS E NE2 1 
ATOM   14687 N N   . ALA E  1 369 ? 133.654 42.339  -12.738 1.00   71.95  ? 369 ALA E N   1 
ATOM   14688 C CA  . ALA E  1 369 ? 134.639 41.257  -12.723 1.00   67.23  ? 369 ALA E CA  1 
ATOM   14689 C C   . ALA E  1 369 ? 134.460 40.409  -11.475 1.00   62.77  ? 369 ALA E C   1 
ATOM   14690 O O   . ALA E  1 369 ? 134.022 40.908  -10.440 1.00   62.11  ? 369 ALA E O   1 
ATOM   14691 C CB  . ALA E  1 369 ? 136.051 41.805  -12.795 1.00   65.23  ? 369 ALA E CB  1 
ATOM   14692 N N   . ARG E  1 370 ? 134.817 39.134  -11.568 1.00   59.86  ? 370 ARG E N   1 
ATOM   14693 C CA  . ARG E  1 370 ? 134.583 38.203  -10.470 1.00   59.28  ? 370 ARG E CA  1 
ATOM   14694 C C   . ARG E  1 370 ? 135.416 38.561  -9.236  1.00   54.60  ? 370 ARG E C   1 
ATOM   14695 O O   . ARG E  1 370 ? 134.912 38.534  -8.116  1.00   55.42  ? 370 ARG E O   1 
ATOM   14696 C CB  . ARG E  1 370 ? 134.879 36.764  -10.937 1.00   62.55  ? 370 ARG E CB  1 
ATOM   14697 C CG  . ARG E  1 370 ? 134.991 35.652  -9.870  1.00   65.56  ? 370 ARG E CG  1 
ATOM   14698 C CD  . ARG E  1 370 ? 133.664 35.453  -9.112  1.00   72.63  ? 370 ARG E CD  1 
ATOM   14699 N NE  . ARG E  1 370 ? 133.707 34.445  -8.042  1.00   74.89  ? 370 ARG E NE  1 
ATOM   14700 C CZ  . ARG E  1 370 ? 134.060 34.677  -6.776  1.00   73.83  ? 370 ARG E CZ  1 
ATOM   14701 N NH1 . ARG E  1 370 ? 134.459 35.887  -6.396  1.00   72.57  ? 370 ARG E NH1 1 
ATOM   14702 N NH2 . ARG E  1 370 ? 134.041 33.687  -5.889  1.00   73.64  ? 370 ARG E NH2 1 
ATOM   14703 N N   . ALA E  1 371 ? 136.678 38.924  -9.441  1.00   49.46  ? 371 ALA E N   1 
ATOM   14704 C CA  . ALA E  1 371 ? 137.554 39.307  -8.334  1.00   44.00  ? 371 ALA E CA  1 
ATOM   14705 C C   . ALA E  1 371 ? 138.443 40.496  -8.707  1.00   42.71  ? 371 ALA E C   1 
ATOM   14706 O O   . ALA E  1 371 ? 138.574 40.837  -9.890  1.00   44.48  ? 371 ALA E O   1 
ATOM   14707 C CB  . ALA E  1 371 ? 138.399 38.114  -7.894  1.00   41.95  ? 371 ALA E CB  1 
ATOM   14708 N N   . GLY E  1 372 ? 139.058 41.128  -7.705  1.00   40.80  ? 372 GLY E N   1 
ATOM   14709 C CA  . GLY E  1 372 ? 139.914 42.280  -7.949  1.00   39.67  ? 372 GLY E CA  1 
ATOM   14710 C C   . GLY E  1 372 ? 141.132 41.923  -8.774  1.00   39.00  ? 372 GLY E C   1 
ATOM   14711 O O   . GLY E  1 372 ? 141.532 42.673  -9.652  1.00   40.69  ? 372 GLY E O   1 
ATOM   14712 N N   . ILE E  1 373 ? 141.704 40.759  -8.478  1.00   39.74  ? 373 ILE E N   1 
ATOM   14713 C CA  . ILE E  1 373 ? 142.833 40.194  -9.198  1.00   35.80  ? 373 ILE E CA  1 
ATOM   14714 C C   . ILE E  1 373 ? 142.541 38.750  -9.563  1.00   33.98  ? 373 ILE E C   1 
ATOM   14715 O O   . ILE E  1 373 ? 142.157 37.967  -8.707  1.00   34.68  ? 373 ILE E O   1 
ATOM   14716 C CB  . ILE E  1 373 ? 144.118 40.236  -8.350  1.00   33.62  ? 373 ILE E CB  1 
ATOM   14717 C CG1 . ILE E  1 373 ? 144.437 41.668  -7.900  1.00   34.22  ? 373 ILE E CG1 1 
ATOM   14718 C CG2 . ILE E  1 373 ? 145.275 39.650  -9.110  1.00   30.93  ? 373 ILE E CG2 1 
ATOM   14719 C CD1 . ILE E  1 373 ? 145.583 41.753  -6.901  1.00   33.22  ? 373 ILE E CD1 1 
ATOM   14720 N N   . ALA E  1 374 ? 142.705 38.391  -10.828 1.00   34.38  ? 374 ALA E N   1 
ATOM   14721 C CA  . ALA E  1 374 ? 142.603 36.986  -11.201 1.00   33.90  ? 374 ALA E CA  1 
ATOM   14722 C C   . ALA E  1 374 ? 143.851 36.559  -11.926 1.00   33.24  ? 374 ALA E C   1 
ATOM   14723 O O   . ALA E  1 374 ? 144.019 36.867  -13.084 1.00   36.83  ? 374 ALA E O   1 
ATOM   14724 C CB  . ALA E  1 374 ? 141.394 36.733  -12.067 1.00   36.28  ? 374 ALA E CB  1 
ATOM   14725 N N   . LEU E  1 375 ? 144.712 35.833  -11.231 1.00   31.85  ? 375 LEU E N   1 
ATOM   14726 C CA  . LEU E  1 375 ? 145.971 35.341  -11.771 1.00   29.73  ? 375 LEU E CA  1 
ATOM   14727 C C   . LEU E  1 375 ? 145.696 34.147  -12.677 1.00   33.54  ? 375 LEU E C   1 
ATOM   14728 O O   . LEU E  1 375 ? 145.081 33.181  -12.228 1.00   34.93  ? 375 LEU E O   1 
ATOM   14729 C CB  . LEU E  1 375 ? 146.899 34.940  -10.630 1.00   25.23  ? 375 LEU E CB  1 
ATOM   14730 C CG  . LEU E  1 375 ? 147.113 35.989  -9.543  1.00   27.72  ? 375 LEU E CG  1 
ATOM   14731 C CD1 . LEU E  1 375 ? 147.783 35.368  -8.357  1.00   29.74  ? 375 LEU E CD1 1 
ATOM   14732 C CD2 . LEU E  1 375 ? 147.988 37.071  -10.073 1.00   29.33  ? 375 LEU E CD2 1 
ATOM   14733 N N   . GLY E  1 376 ? 146.146 34.219  -13.937 1.00   34.18  ? 376 GLY E N   1 
ATOM   14734 C CA  . GLY E  1 376 ? 145.794 33.240  -14.961 1.00   33.49  ? 376 GLY E CA  1 
ATOM   14735 C C   . GLY E  1 376 ? 146.905 32.315  -15.395 1.00   30.50  ? 376 GLY E C   1 
ATOM   14736 O O   . GLY E  1 376 ? 147.887 32.177  -14.703 1.00   31.24  ? 376 GLY E O   1 
ATOM   14737 N N   . ALA E  1 377 ? 146.757 31.705  -16.562 1.00   33.20  ? 377 ALA E N   1 
ATOM   14738 C CA  . ALA E  1 377 ? 147.694 30.681  -17.028 1.00   34.02  ? 377 ALA E CA  1 
ATOM   14739 C C   . ALA E  1 377 ? 149.129 31.169  -17.236 1.00   36.00  ? 377 ALA E C   1 
ATOM   14740 O O   . ALA E  1 377 ? 150.073 30.460  -16.894 1.00   36.77  ? 377 ALA E O   1 
ATOM   14741 C CB  . ALA E  1 377 ? 147.181 30.067  -18.314 1.00   33.67  ? 377 ALA E CB  1 
ATOM   14742 N N   . HIS E  1 378 ? 149.289 32.370  -17.793 1.00   38.47  ? 378 HIS E N   1 
ATOM   14743 C CA  . HIS E  1 378 ? 150.615 32.915  -18.070 1.00   37.67  ? 378 HIS E CA  1 
ATOM   14744 C C   . HIS E  1 378 ? 151.396 33.180  -16.810 1.00   36.25  ? 378 HIS E C   1 
ATOM   14745 O O   . HIS E  1 378 ? 152.617 33.034  -16.779 1.00   36.84  ? 378 HIS E O   1 
ATOM   14746 C CB  . HIS E  1 378 ? 150.507 34.179  -18.898 1.00   42.51  ? 378 HIS E CB  1 
ATOM   14747 C CG  . HIS E  1 378 ? 150.331 33.905  -20.357 1.00   49.06  ? 378 HIS E CG  1 
ATOM   14748 N ND1 . HIS E  1 378 ? 150.622 34.830  -21.333 1.00   54.02  ? 378 HIS E ND1 1 
ATOM   14749 C CD2 . HIS E  1 378 ? 149.921 32.788  -21.007 1.00   50.47  ? 378 HIS E CD2 1 
ATOM   14750 C CE1 . HIS E  1 378 ? 150.375 34.303  -22.521 1.00   57.49  ? 378 HIS E CE1 1 
ATOM   14751 N NE2 . HIS E  1 378 ? 149.949 33.064  -22.351 1.00   54.16  ? 378 HIS E NE2 1 
ATOM   14752 N N   . HIS E  1 379 ? 150.680 33.600  -15.779 1.00   35.91  ? 379 HIS E N   1 
ATOM   14753 C CA  . HIS E  1 379 ? 151.260 33.790  -14.469 1.00   34.91  ? 379 HIS E CA  1 
ATOM   14754 C C   . HIS E  1 379 ? 151.796 32.467  -13.894 1.00   34.62  ? 379 HIS E C   1 
ATOM   14755 O O   . HIS E  1 379 ? 152.870 32.403  -13.299 1.00   34.74  ? 379 HIS E O   1 
ATOM   14756 C CB  . HIS E  1 379 ? 150.221 34.390  -13.532 1.00   34.53  ? 379 HIS E CB  1 
ATOM   14757 C CG  . HIS E  1 379 ? 150.733 34.611  -12.145 1.00   33.18  ? 379 HIS E CG  1 
ATOM   14758 N ND1 . HIS E  1 379 ? 151.387 35.765  -11.770 1.00   35.15  ? 379 HIS E ND1 1 
ATOM   14759 C CD2 . HIS E  1 379 ? 150.703 33.825  -11.046 1.00   31.17  ? 379 HIS E CD2 1 
ATOM   14760 C CE1 . HIS E  1 379 ? 151.733 35.684  -10.497 1.00   31.99  ? 379 HIS E CE1 1 
ATOM   14761 N NE2 . HIS E  1 379 ? 151.333 34.516  -10.036 1.00   31.92  ? 379 HIS E NE2 1 
ATOM   14762 N N   . LEU E  1 380 ? 151.040 31.399  -14.058 1.00   33.58  ? 380 LEU E N   1 
ATOM   14763 C CA  . LEU E  1 380 ? 151.459 30.132  -13.497 1.00   31.38  ? 380 LEU E CA  1 
ATOM   14764 C C   . LEU E  1 380 ? 152.550 29.418  -14.291 1.00   29.87  ? 380 LEU E C   1 
ATOM   14765 O O   . LEU E  1 380 ? 153.285 28.605  -13.732 1.00   30.15  ? 380 LEU E O   1 
ATOM   14766 C CB  . LEU E  1 380 ? 150.254 29.211  -13.362 1.00   32.15  ? 380 LEU E CB  1 
ATOM   14767 C CG  . LEU E  1 380 ? 149.125 29.656  -12.446 1.00   29.96  ? 380 LEU E CG  1 
ATOM   14768 C CD1 . LEU E  1 380 ? 147.964 28.766  -12.684 1.00   31.62  ? 380 LEU E CD1 1 
ATOM   14769 C CD2 . LEU E  1 380 ? 149.564 29.485  -11.027 1.00   29.36  ? 380 LEU E CD2 1 
ATOM   14770 N N   . GLU E  1 381 ? 152.611 29.668  -15.594 1.00   28.15  ? 381 GLU E N   1 
ATOM   14771 C CA  . GLU E  1 381 ? 153.543 28.942  -16.447 1.00   29.67  ? 381 GLU E CA  1 
ATOM   14772 C C   . GLU E  1 381 ? 154.977 29.153  -16.011 1.00   32.78  ? 381 GLU E C   1 
ATOM   14773 O O   . GLU E  1 381 ? 155.393 30.264  -15.679 1.00   33.58  ? 381 GLU E O   1 
ATOM   14774 C CB  . GLU E  1 381 ? 153.391 29.350  -17.895 1.00   29.84  ? 381 GLU E CB  1 
ATOM   14775 C CG  . GLU E  1 381 ? 152.158 28.822  -18.507 1.00   32.15  ? 381 GLU E CG  1 
ATOM   14776 C CD  . GLU E  1 381 ? 151.855 29.528  -19.784 1.00   40.02  ? 381 GLU E CD  1 
ATOM   14777 O OE1 . GLU E  1 381 ? 152.680 30.376  -20.190 1.00   44.36  ? 381 GLU E OE1 1 
ATOM   14778 O OE2 . GLU E  1 381 ? 150.771 29.284  -20.357 1.00   42.61  1 381 GLU E OE2 1 
ATOM   14779 N N   . GLU E  1 382 ? 155.722 28.061  -16.035 1.00   30.38  ? 382 GLU E N   1 
ATOM   14780 C CA  . GLU E  1 382 ? 157.113 28.030  -15.630 1.00   32.81  ? 382 GLU E CA  1 
ATOM   14781 C C   . GLU E  1 382 ? 157.264 28.351  -14.169 1.00   32.15  ? 382 GLU E C   1 
ATOM   14782 O O   . GLU E  1 382 ? 158.313 28.823  -13.751 1.00   33.93  ? 382 GLU E O   1 
ATOM   14783 C CB  . GLU E  1 382 ? 157.951 28.989  -16.474 1.00   32.04  ? 382 GLU E CB  1 
ATOM   14784 C CG  . GLU E  1 382 ? 157.881 28.636  -17.945 1.00   35.19  ? 382 GLU E CG  1 
ATOM   14785 C CD  . GLU E  1 382 ? 158.201 27.186  -18.215 1.00   37.81  ? 382 GLU E CD  1 
ATOM   14786 O OE1 . GLU E  1 382 ? 159.142 26.664  -17.596 1.00   38.46  ? 382 GLU E OE1 1 
ATOM   14787 O OE2 . GLU E  1 382 ? 157.482 26.543  -19.013 1.00   38.66  1 382 GLU E OE2 1 
ATOM   14788 N N   . ASN E  1 383 ? 156.207 28.089  -13.406 1.00   31.72  ? 383 ASN E N   1 
ATOM   14789 C CA  . ASN E  1 383 ? 156.256 28.109  -11.951 1.00   31.17  ? 383 ASN E CA  1 
ATOM   14790 C C   . ASN E  1 383 ? 155.774 26.785  -11.406 1.00   30.98  ? 383 ASN E C   1 
ATOM   14791 O O   . ASN E  1 383 ? 154.848 26.185  -11.933 1.00   32.66  ? 383 ASN E O   1 
ATOM   14792 C CB  . ASN E  1 383 ? 155.399 29.237  -11.375 1.00   32.62  ? 383 ASN E CB  1 
ATOM   14793 C CG  . ASN E  1 383 ? 155.969 30.610  -11.656 1.00   38.19  ? 383 ASN E CG  1 
ATOM   14794 O OD1 . ASN E  1 383 ? 157.003 30.980  -11.101 1.00   42.66  ? 383 ASN E OD1 1 
ATOM   14795 N ND2 . ASN E  1 383 ? 155.323 31.364  -12.547 1.00   39.18  ? 383 ASN E ND2 1 
ATOM   14796 N N   . LEU E  1 384 ? 156.413 26.340  -10.337 1.00   30.51  ? 384 LEU E N   1 
ATOM   14797 C CA  . LEU E  1 384 ? 155.956 25.201  -9.586  1.00   30.84  ? 384 LEU E CA  1 
ATOM   14798 C C   . LEU E  1 384 ? 155.140 25.721  -8.428  1.00   32.83  ? 384 LEU E C   1 
ATOM   14799 O O   . LEU E  1 384 ? 155.660 26.408  -7.538  1.00   33.94  ? 384 LEU E O   1 
ATOM   14800 C CB  . LEU E  1 384 ? 157.129 24.365  -9.083  1.00   35.29  ? 384 LEU E CB  1 
ATOM   14801 C CG  . LEU E  1 384 ? 156.772 23.164  -8.194  1.00   38.40  ? 384 LEU E CG  1 
ATOM   14802 C CD1 . LEU E  1 384 ? 156.081 22.023  -8.968  1.00   34.92  ? 384 LEU E CD1 1 
ATOM   14803 C CD2 . LEU E  1 384 ? 158.024 22.672  -7.497  1.00   41.51  ? 384 LEU E CD2 1 
ATOM   14804 N N   . VAL E  1 385 ? 153.857 25.383  -8.442  1.00   30.61  ? 385 VAL E N   1 
ATOM   14805 C CA  . VAL E  1 385 ? 152.917 25.897  -7.472  1.00   27.92  ? 385 VAL E CA  1 
ATOM   14806 C C   . VAL E  1 385 ? 152.306 24.742  -6.693  1.00   27.87  ? 385 VAL E C   1 
ATOM   14807 O O   . VAL E  1 385 ? 151.660 23.872  -7.266  1.00   27.71  ? 385 VAL E O   1 
ATOM   14808 C CB  . VAL E  1 385 ? 151.838 26.714  -8.166  1.00   26.62  ? 385 VAL E CB  1 
ATOM   14809 C CG1 . VAL E  1 385 ? 150.915 27.329  -7.140  1.00   26.89  ? 385 VAL E CG1 1 
ATOM   14810 C CG2 . VAL E  1 385 ? 152.468 27.800  -9.036  1.00   24.81  ? 385 VAL E CG2 1 
ATOM   14811 N N   . VAL E  1 386 ? 152.556 24.715  -5.389  1.00   27.08  ? 386 VAL E N   1 
ATOM   14812 C CA  . VAL E  1 386 ? 152.116 23.613  -4.533  1.00   26.62  ? 386 VAL E CA  1 
ATOM   14813 C C   . VAL E  1 386 ? 150.858 23.941  -3.736  1.00   30.69  ? 386 VAL E C   1 
ATOM   14814 O O   . VAL E  1 386 ? 150.843 24.862  -2.933  1.00   31.89  ? 386 VAL E O   1 
ATOM   14815 C CB  . VAL E  1 386 ? 153.228 23.208  -3.542  1.00   28.99  ? 386 VAL E CB  1 
ATOM   14816 C CG1 . VAL E  1 386 ? 152.772 22.091  -2.643  1.00   29.87  ? 386 VAL E CG1 1 
ATOM   14817 C CG2 . VAL E  1 386 ? 154.453 22.781  -4.306  1.00   30.88  ? 386 VAL E CG2 1 
ATOM   14818 N N   . PHE E  1 387 ? 149.800 23.170  -3.962  1.00   31.85  ? 387 PHE E N   1 
ATOM   14819 C CA  . PHE E  1 387 ? 148.561 23.328  -3.226  1.00   31.15  ? 387 PHE E CA  1 
ATOM   14820 C C   . PHE E  1 387 ? 148.515 22.336  -2.090  1.00   33.89  ? 387 PHE E C   1 
ATOM   14821 O O   . PHE E  1 387 ? 148.146 21.171  -2.265  1.00   33.86  ? 387 PHE E O   1 
ATOM   14822 C CB  . PHE E  1 387 ? 147.359 23.139  -4.140  1.00   30.01  ? 387 PHE E CB  1 
ATOM   14823 C CG  . PHE E  1 387 ? 147.241 24.187  -5.161  1.00   31.56  ? 387 PHE E CG  1 
ATOM   14824 C CD1 . PHE E  1 387 ? 147.995 24.133  -6.300  1.00   33.37  ? 387 PHE E CD1 1 
ATOM   14825 C CD2 . PHE E  1 387 ? 146.411 25.262  -4.969  1.00   34.10  ? 387 PHE E CD2 1 
ATOM   14826 C CE1 . PHE E  1 387 ? 147.903 25.132  -7.250  1.00   33.96  ? 387 PHE E CE1 1 
ATOM   14827 C CE2 . PHE E  1 387 ? 146.316 26.270  -5.915  1.00   32.08  ? 387 PHE E CE2 1 
ATOM   14828 C CZ  . PHE E  1 387 ? 147.058 26.204  -7.047  1.00   32.45  ? 387 PHE E CZ  1 
ATOM   14829 N N   . ASP E  1 388 ? 148.898 22.810  -0.918  1.00   36.48  ? 388 ASP E N   1 
ATOM   14830 C CA  . ASP E  1 388 ? 148.946 21.970  0.255   1.00   39.23  ? 388 ASP E CA  1 
ATOM   14831 C C   . ASP E  1 388 ? 147.607 22.053  1.007   1.00   40.80  ? 388 ASP E C   1 
ATOM   14832 O O   . ASP E  1 388 ? 147.382 22.941  1.831   1.00   39.56  ? 388 ASP E O   1 
ATOM   14833 C CB  . ASP E  1 388 ? 150.118 22.392  1.136   1.00   41.75  ? 388 ASP E CB  1 
ATOM   14834 C CG  . ASP E  1 388 ? 150.412 21.397  2.223   1.00   46.48  ? 388 ASP E CG  1 
ATOM   14835 O OD1 . ASP E  1 388 ? 149.614 20.443  2.411   1.00   48.87  ? 388 ASP E OD1 1 
ATOM   14836 O OD2 . ASP E  1 388 ? 151.447 21.583  2.892   1.00   48.29  1 388 ASP E OD2 1 
ATOM   14837 N N   . LEU E  1 389 ? 146.707 21.128  0.718   1.00   41.03  ? 389 LEU E N   1 
ATOM   14838 C CA  . LEU E  1 389 ? 145.395 21.233  1.290   1.00   38.72  ? 389 LEU E CA  1 
ATOM   14839 C C   . LEU E  1 389 ? 145.416 20.876  2.763   1.00   40.80  ? 389 LEU E C   1 
ATOM   14840 O O   . LEU E  1 389 ? 144.567 21.322  3.516   1.00   42.75  ? 389 LEU E O   1 
ATOM   14841 C CB  . LEU E  1 389 ? 144.415 20.352  0.532   1.00   41.03  ? 389 LEU E CB  1 
ATOM   14842 C CG  . LEU E  1 389 ? 144.534 20.526  -0.981  1.00   38.92  ? 389 LEU E CG  1 
ATOM   14843 C CD1 . LEU E  1 389 ? 143.746 19.435  -1.634  1.00   43.57  ? 389 LEU E CD1 1 
ATOM   14844 C CD2 . LEU E  1 389 ? 144.032 21.861  -1.413  1.00   27.14  ? 389 LEU E CD2 1 
ATOM   14845 N N   . GLU E  1 390 ? 146.394 20.097  3.198   1.00   41.18  ? 390 GLU E N   1 
ATOM   14846 C CA  . GLU E  1 390 ? 146.446 19.710  4.610   1.00   44.29  ? 390 GLU E CA  1 
ATOM   14847 C C   . GLU E  1 390 ? 146.804 20.862  5.548   1.00   44.85  ? 390 GLU E C   1 
ATOM   14848 O O   . GLU E  1 390 ? 146.443 20.842  6.726   1.00   46.64  ? 390 GLU E O   1 
ATOM   14849 C CB  . GLU E  1 390 ? 147.453 18.587  4.835   1.00   46.40  ? 390 GLU E CB  1 
ATOM   14850 C CG  . GLU E  1 390 ? 147.132 17.338  4.111   1.00   49.42  ? 390 GLU E CG  1 
ATOM   14851 C CD  . GLU E  1 390 ? 147.840 16.172  4.718   1.00   58.30  ? 390 GLU E CD  1 
ATOM   14852 O OE1 . GLU E  1 390 ? 148.807 16.416  5.482   1.00   59.86  ? 390 GLU E OE1 1 
ATOM   14853 O OE2 . GLU E  1 390 ? 147.430 15.019  4.430   1.00   62.87  ? 390 GLU E OE2 1 
ATOM   14854 N N   . ARG E  1 391 ? 147.563 21.828  5.031   1.00   44.54  ? 391 ARG E N   1 
ATOM   14855 C CA  . ARG E  1 391 ? 148.001 22.970  5.819   1.00   44.68  ? 391 ARG E CA  1 
ATOM   14856 C C   . ARG E  1 391 ? 147.316 24.250  5.357   1.00   40.80  ? 391 ARG E C   1 
ATOM   14857 O O   . ARG E  1 391 ? 147.552 25.307  5.923   1.00   42.11  ? 391 ARG E O   1 
ATOM   14858 C CB  . ARG E  1 391 ? 149.530 23.144  5.714   1.00   45.73  ? 391 ARG E CB  1 
ATOM   14859 C CG  . ARG E  1 391 ? 150.415 21.965  6.199   1.00   64.58  ? 391 ARG E CG  1 
ATOM   14860 C CD  . ARG E  1 391 ? 151.079 22.235  7.558   1.00   70.43  ? 391 ARG E CD  1 
ATOM   14861 N NE  . ARG E  1 391 ? 151.950 23.414  7.559   1.00   71.74  ? 391 ARG E NE  1 
ATOM   14862 C CZ  . ARG E  1 391 ? 152.353 24.055  8.656   1.00   76.99  ? 391 ARG E CZ  1 
ATOM   14863 N NH1 . ARG E  1 391 ? 151.967 23.638  9.857   1.00   83.37  ? 391 ARG E NH1 1 
ATOM   14864 N NH2 . ARG E  1 391 ? 153.139 25.121  8.554   1.00   76.15  ? 391 ARG E NH2 1 
ATOM   14865 N N   . SER E  1 392 ? 146.452 24.131  4.348   1.00   37.00  ? 392 SER E N   1 
ATOM   14866 C CA  . SER E  1 392 ? 145.719 25.254  3.745   1.00   34.85  ? 392 SER E CA  1 
ATOM   14867 C C   . SER E  1 392 ? 146.643 26.414  3.321   1.00   34.20  ? 392 SER E C   1 
ATOM   14868 O O   . SER E  1 392 ? 146.456 27.574  3.715   1.00   35.09  ? 392 SER E O   1 
ATOM   14869 C CB  . SER E  1 392 ? 144.626 25.765  4.692   1.00   35.64  ? 392 SER E CB  1 
ATOM   14870 O OG  . SER E  1 392 ? 143.688 26.556  3.975   1.00   34.23  ? 392 SER E OG  1 
ATOM   14871 N N   . ARG E  1 393 ? 147.620 26.085  2.482   1.00   33.91  ? 393 ARG E N   1 
ATOM   14872 C CA  . ARG E  1 393 ? 148.601 27.047  2.003   1.00   33.92  ? 393 ARG E CA  1 
ATOM   14873 C C   . ARG E  1 393 ? 149.049 26.667  0.608   1.00   32.45  ? 393 ARG E C   1 
ATOM   14874 O O   . ARG E  1 393 ? 148.941 25.509  0.207   1.00   32.29  ? 393 ARG E O   1 
ATOM   14875 C CB  . ARG E  1 393 ? 149.807 27.098  2.932   1.00   33.53  ? 393 ARG E CB  1 
ATOM   14876 C CG  . ARG E  1 393 ? 150.580 25.806  2.912   1.00   33.65  ? 393 ARG E CG  1 
ATOM   14877 C CD  . ARG E  1 393 ? 151.641 25.759  3.984   1.00   36.91  ? 393 ARG E CD  1 
ATOM   14878 N NE  . ARG E  1 393 ? 152.482 24.585  3.795   1.00   36.45  ? 393 ARG E NE  1 
ATOM   14879 C CZ  . ARG E  1 393 ? 153.662 24.419  4.366   1.00   41.47  ? 393 ARG E CZ  1 
ATOM   14880 N NH1 . ARG E  1 393 ? 154.125 25.322  5.212   1.00   46.95  ? 393 ARG E NH1 1 
ATOM   14881 N NH2 . ARG E  1 393 ? 154.362 23.328  4.118   1.00   45.52  ? 393 ARG E NH2 1 
ATOM   14882 N N   . VAL E  1 394 ? 149.562 27.658  -0.105  1.00   30.69  ? 394 VAL E N   1 
ATOM   14883 C CA  . VAL E  1 394 ? 150.137 27.494  -1.421  1.00   29.69  ? 394 VAL E CA  1 
ATOM   14884 C C   . VAL E  1 394 ? 151.611 27.795  -1.346  1.00   29.21  ? 394 VAL E C   1 
ATOM   14885 O O   . VAL E  1 394 ? 151.992 28.698  -0.634  1.00   31.53  ? 394 VAL E O   1 
ATOM   14886 C CB  . VAL E  1 394 ? 149.515 28.427  -2.437  1.00   30.49  ? 394 VAL E CB  1 
ATOM   14887 C CG1 . VAL E  1 394 ? 150.121 28.179  -3.769  1.00   32.68  ? 394 VAL E CG1 1 
ATOM   14888 C CG2 . VAL E  1 394 ? 148.108 28.146  -2.563  1.00   28.05  ? 394 VAL E CG2 1 
ATOM   14889 N N   . GLY E  1 395 ? 152.440 27.001  -2.018  1.00   29.89  ? 395 GLY E N   1 
ATOM   14890 C CA  . GLY E  1 395 ? 153.873 27.248  -2.105  1.00   33.00  ? 395 GLY E CA  1 
ATOM   14891 C C   . GLY E  1 395 ? 154.277 27.520  -3.532  1.00   31.66  ? 395 GLY E C   1 
ATOM   14892 O O   . GLY E  1 395 ? 153.619 27.019  -4.440  1.00   28.47  ? 395 GLY E O   1 
ATOM   14893 N N   . PHE E  1 396 ? 155.327 28.326  -3.733  1.00   32.81  ? 396 PHE E N   1 
ATOM   14894 C CA  . PHE E  1 396 ? 155.835 28.617  -5.084  1.00   31.13  ? 396 PHE E CA  1 
ATOM   14895 C C   . PHE E  1 396 ? 157.360 28.840  -5.078  1.00   33.70  ? 396 PHE E C   1 
ATOM   14896 O O   . PHE E  1 396 ? 157.966 29.174  -4.055  1.00   34.37  ? 396 PHE E O   1 
ATOM   14897 C CB  . PHE E  1 396 ? 155.142 29.851  -5.694  1.00   30.08  ? 396 PHE E CB  1 
ATOM   14898 C CG  . PHE E  1 396 ? 155.227 31.098  -4.826  1.00   34.77  ? 396 PHE E CG  1 
ATOM   14899 C CD1 . PHE E  1 396 ? 156.337 31.933  -4.883  1.00   39.46  ? 396 PHE E CD1 1 
ATOM   14900 C CD2 . PHE E  1 396 ? 154.210 31.438  -3.959  1.00   34.86  ? 396 PHE E CD2 1 
ATOM   14901 C CE1 . PHE E  1 396 ? 156.432 33.076  -4.078  1.00   41.33  ? 396 PHE E CE1 1 
ATOM   14902 C CE2 . PHE E  1 396 ? 154.303 32.588  -3.160  1.00   36.51  ? 396 PHE E CE2 1 
ATOM   14903 C CZ  . PHE E  1 396 ? 155.410 33.395  -3.223  1.00   38.53  ? 396 PHE E CZ  1 
ATOM   14904 N N   . ASN E  1 397 ? 157.979 28.680  -6.238  1.00   35.47  ? 397 ASN E N   1 
ATOM   14905 C CA  . ASN E  1 397 ? 159.407 28.900  -6.348  1.00   34.72  ? 397 ASN E CA  1 
ATOM   14906 C C   . ASN E  1 397 ? 159.735 30.355  -6.076  1.00   36.06  ? 397 ASN E C   1 
ATOM   14907 O O   . ASN E  1 397 ? 159.096 31.252  -6.636  1.00   38.47  ? 397 ASN E O   1 
ATOM   14908 C CB  . ASN E  1 397 ? 159.910 28.477  -7.735  1.00   36.86  ? 397 ASN E CB  1 
ATOM   14909 C CG  . ASN E  1 397 ? 159.009 28.954  -8.878  1.00   36.20  ? 397 ASN E CG  1 
ATOM   14910 O OD1 . ASN E  1 397 ? 157.871 28.499  -9.025  1.00   37.63  ? 397 ASN E OD1 1 
ATOM   14911 N ND2 . ASN E  1 397 ? 159.517 29.876  -9.688  1.00   36.92  ? 397 ASN E ND2 1 
ATOM   14912 N N   . SER E  1 398 ? 160.718 30.596  -5.210  1.00   33.77  ? 398 SER E N   1 
ATOM   14913 C CA  . SER E  1 398 ? 161.045 31.954  -4.830  1.00   37.47  ? 398 SER E CA  1 
ATOM   14914 C C   . SER E  1 398 ? 162.046 32.605  -5.792  1.00   44.59  ? 398 SER E C   1 
ATOM   14915 O O   . SER E  1 398 ? 162.232 33.827  -5.760  1.00   49.39  ? 398 SER E O   1 
ATOM   14916 C CB  . SER E  1 398 ? 161.599 31.995  -3.396  1.00   42.05  ? 398 SER E CB  1 
ATOM   14917 O OG  . SER E  1 398 ? 162.759 31.195  -3.229  1.00   44.05  ? 398 SER E OG  1 
ATOM   14918 N N   . ASN E  1 399 ? 162.675 31.793  -6.646  1.00   44.27  ? 399 ASN E N   1 
ATOM   14919 C CA  . ASN E  1 399 ? 163.515 32.260  -7.760  1.00   42.15  ? 399 ASN E CA  1 
ATOM   14920 C C   . ASN E  1 399 ? 162.972 31.600  -9.030  1.00   40.68  ? 399 ASN E C   1 
ATOM   14921 O O   . ASN E  1 399 ? 162.277 30.591  -8.940  1.00   39.98  ? 399 ASN E O   1 
ATOM   14922 C CB  . ASN E  1 399 ? 165.002 31.903  -7.559  1.00   44.61  ? 399 ASN E CB  1 
ATOM   14923 C CG  . ASN E  1 399 ? 165.639 32.552  -6.326  1.00   50.77  ? 399 ASN E CG  1 
ATOM   14924 O OD1 . ASN E  1 399 ? 165.982 33.734  -6.334  1.00   54.94  ? 399 ASN E OD1 1 
ATOM   14925 N ND2 . ASN E  1 399 ? 165.824 31.766  -5.273  1.00   52.12  ? 399 ASN E ND2 1 
ATOM   14926 N N   . SER E  1 400 ? 163.268 32.152  -10.207 1.00   40.90  ? 400 SER E N   1 
ATOM   14927 C CA  . SER E  1 400 ? 162.749 31.580  -11.455 1.00   38.62  ? 400 SER E CA  1 
ATOM   14928 C C   . SER E  1 400 ? 163.319 30.190  -11.662 1.00   40.04  ? 400 SER E C   1 
ATOM   14929 O O   . SER E  1 400 ? 164.420 29.910  -11.226 1.00   43.83  ? 400 SER E O   1 
ATOM   14930 C CB  . SER E  1 400 ? 163.104 32.425  -12.667 1.00   37.31  ? 400 SER E CB  1 
ATOM   14931 O OG  . SER E  1 400 ? 164.463 32.209  -12.993 1.00   40.61  ? 400 SER E OG  1 
ATOM   14932 N N   . LEU E  1 401 ? 162.562 29.331  -12.330 1.00   40.02  ? 401 LEU E N   1 
ATOM   14933 C CA  . LEU E  1 401 ? 163.009 27.992  -12.666 1.00   38.56  ? 401 LEU E CA  1 
ATOM   14934 C C   . LEU E  1 401 ? 164.271 28.113  -13.504 1.00   41.23  ? 401 LEU E C   1 
ATOM   14935 O O   . LEU E  1 401 ? 165.229 27.362  -13.345 1.00   43.23  ? 401 LEU E O   1 
ATOM   14936 C CB  . LEU E  1 401 ? 161.895 27.230  -13.408 1.00   36.69  ? 401 LEU E CB  1 
ATOM   14937 C CG  . LEU E  1 401 ? 160.632 26.882  -12.613 1.00   34.48  ? 401 LEU E CG  1 
ATOM   14938 C CD1 . LEU E  1 401 ? 159.739 25.941  -13.379 1.00   31.43  ? 401 LEU E CD1 1 
ATOM   14939 C CD2 . LEU E  1 401 ? 161.011 26.258  -11.288 1.00   35.14  ? 401 LEU E CD2 1 
ATOM   14940 N N   . LYS E  1 402 ? 164.273 29.124  -14.360 1.00   42.02  ? 402 LYS E N   1 
ATOM   14941 C CA  . LYS E  1 402 ? 165.373 29.374  -15.266 1.00   43.88  ? 402 LYS E CA  1 
ATOM   14942 C C   . LYS E  1 402 ? 166.657 29.665  -14.491 1.00   44.63  ? 402 LYS E C   1 
ATOM   14943 O O   . LYS E  1 402 ? 167.742 29.325  -14.949 1.00   47.16  ? 402 LYS E O   1 
ATOM   14944 C CB  . LYS E  1 402 ? 165.001 30.522  -16.197 1.00   47.20  ? 402 LYS E CB  1 
ATOM   14945 C CG  . LYS E  1 402 ? 166.119 31.488  -16.457 1.00   60.40  ? 402 LYS E CG  1 
ATOM   14946 C CD  . LYS E  1 402 ? 165.670 32.670  -17.322 1.00   70.44  ? 402 LYS E CD  1 
ATOM   14947 C CE  . LYS E  1 402 ? 166.687 33.822  -17.320 1.00   80.34  ? 402 LYS E CE  1 
ATOM   14948 N NZ  . LYS E  1 402 ? 166.894 34.508  -18.632 1.00   85.80  ? 402 LYS E NZ  1 
ATOM   14949 N N   . SER E  1 403 ? 166.535 30.233  -13.295 1.00   42.40  ? 403 SER E N   1 
ATOM   14950 C CA  . SER E  1 403 ? 167.710 30.468  -12.467 1.00   44.34  ? 403 SER E CA  1 
ATOM   14951 C C   . SER E  1 403 ? 168.280 29.162  -11.912 1.00   44.65  ? 403 SER E C   1 
ATOM   14952 O O   . SER E  1 403 ? 169.400 29.128  -11.410 1.00   47.69  ? 403 SER E O   1 
ATOM   14953 C CB  . SER E  1 403 ? 167.387 31.437  -11.325 1.00   45.04  ? 403 SER E CB  1 
ATOM   14954 O OG  . SER E  1 403 ? 166.877 30.783  -10.185 1.00   42.86  ? 403 SER E OG  1 
ATOM   14955 N N   . TYR E  1 404 ? 167.491 28.099  -11.981 1.00   44.43  ? 404 TYR E N   1 
ATOM   14956 C CA  . TYR E  1 404 ? 167.951 26.777  -11.599 1.00   46.57  ? 404 TYR E CA  1 
ATOM   14957 C C   . TYR E  1 404 ? 168.392 25.974  -12.803 1.00   50.13  ? 404 TYR E C   1 
ATOM   14958 O O   . TYR E  1 404 ? 168.823 24.829  -12.672 1.00   54.17  ? 404 TYR E O   1 
ATOM   14959 C CB  . TYR E  1 404 ? 166.852 26.026  -10.873 1.00   42.64  ? 404 TYR E CB  1 
ATOM   14960 C CG  . TYR E  1 404 ? 166.426 26.678  -9.596  1.00   43.18  ? 404 TYR E CG  1 
ATOM   14961 C CD1 . TYR E  1 404 ? 167.114 26.452  -8.412  1.00   46.11  ? 404 TYR E CD1 1 
ATOM   14962 C CD2 . TYR E  1 404 ? 165.329 27.526  -9.566  1.00   41.60  ? 404 TYR E CD2 1 
ATOM   14963 C CE1 . TYR E  1 404 ? 166.706 27.060  -7.226  1.00   45.70  ? 404 TYR E CE1 1 
ATOM   14964 C CE2 . TYR E  1 404 ? 164.920 28.140  -8.396  1.00   40.40  ? 404 TYR E CE2 1 
ATOM   14965 C CZ  . TYR E  1 404 ? 165.604 27.904  -7.226  1.00   41.83  ? 404 TYR E CZ  1 
ATOM   14966 O OH  . TYR E  1 404 ? 165.181 28.510  -6.058  1.00   41.30  ? 404 TYR E OH  1 
ATOM   14967 N N   . GLY E  1 405 ? 168.258 26.554  -13.985 1.00   49.03  ? 405 GLY E N   1 
ATOM   14968 C CA  . GLY E  1 405 ? 168.533 25.793  -15.185 1.00   46.06  ? 405 GLY E CA  1 
ATOM   14969 C C   . GLY E  1 405 ? 167.386 24.843  -15.483 1.00   48.99  ? 405 GLY E C   1 
ATOM   14970 O O   . GLY E  1 405 ? 167.572 23.839  -16.170 1.00   49.58  ? 405 GLY E O   1 
ATOM   14971 N N   . LYS E  1 406 ? 166.203 25.141  -14.947 1.00   46.52  ? 406 LYS E N   1 
ATOM   14972 C CA  . LYS E  1 406 ? 165.062 24.234  -15.088 1.00   44.41  ? 406 LYS E CA  1 
ATOM   14973 C C   . LYS E  1 406 ? 163.894 24.838  -15.855 1.00   41.96  ? 406 LYS E C   1 
ATOM   14974 O O   . LYS E  1 406 ? 163.783 26.051  -16.000 1.00   41.19  ? 406 LYS E O   1 
ATOM   14975 C CB  . LYS E  1 406 ? 164.579 23.762  -13.713 1.00   46.23  ? 406 LYS E CB  1 
ATOM   14976 C CG  . LYS E  1 406 ? 165.669 23.172  -12.816 1.00   53.28  ? 406 LYS E CG  1 
ATOM   14977 C CD  . LYS E  1 406 ? 166.117 21.795  -13.296 1.00   60.90  ? 406 LYS E CD  1 
ATOM   14978 C CE  . LYS E  1 406 ? 167.390 21.320  -12.600 1.00   68.10  ? 406 LYS E CE  1 
ATOM   14979 N NZ  . LYS E  1 406 ? 167.381 21.584  -11.133 1.00   70.34  ? 406 LYS E NZ  1 
ATOM   14980 N N   . THR E  1 407 ? 163.019 23.967  -16.344 1.00   41.81  ? 407 THR E N   1 
ATOM   14981 C CA  . THR E  1 407 ? 161.748 24.368  -16.921 1.00   37.82  ? 407 THR E CA  1 
ATOM   14982 C C   . THR E  1 407 ? 160.689 23.467  -16.331 1.00   38.34  ? 407 THR E C   1 
ATOM   14983 O O   . THR E  1 407 ? 161.021 22.474  -15.695 1.00   38.53  ? 407 THR E O   1 
ATOM   14984 C CB  . THR E  1 407 ? 161.730 24.240  -18.439 1.00   37.34  ? 407 THR E CB  1 
ATOM   14985 O OG1 . THR E  1 407 ? 161.774 22.853  -18.787 1.00   40.54  ? 407 THR E OG1 1 
ATOM   14986 C CG2 . THR E  1 407 ? 162.927 24.914  -19.040 1.00   40.72  ? 407 THR E CG2 1 
ATOM   14987 N N   . CYS E  1 408 ? 159.416 23.786  -16.552 1.00   36.23  ? 408 CYS E N   1 
ATOM   14988 C CA  . CYS E  1 408 ? 158.363 22.922  -16.068 1.00   34.58  ? 408 CYS E CA  1 
ATOM   14989 C C   . CYS E  1 408 ? 158.405 21.619  -16.829 1.00   35.27  ? 408 CYS E C   1 
ATOM   14990 O O   . CYS E  1 408 ? 158.025 20.580  -16.315 1.00   36.20  ? 408 CYS E O   1 
ATOM   14991 C CB  . CYS E  1 408 ? 156.992 23.586  -16.229 1.00   31.86  ? 408 CYS E CB  1 
ATOM   14992 S SG  . CYS E  1 408 ? 156.515 24.551  -14.805 1.00   35.46  ? 408 CYS E SG  1 
ATOM   14993 N N   . SER E  1 409 ? 158.989 21.658  -18.011 1.00   31.93  ? 409 SER E N   1 
ATOM   14994 C CA  . SER E  1 409 ? 159.085 20.473  -18.822 1.00   34.11  ? 409 SER E CA  1 
ATOM   14995 C C   . SER E  1 409 ? 160.199 19.518  -18.403 1.00   42.49  ? 409 SER E C   1 
ATOM   14996 O O   . SER E  1 409 ? 160.077 18.324  -18.626 1.00   42.82  ? 409 SER E O   1 
ATOM   14997 C CB  . SER E  1 409 ? 159.268 20.864  -20.287 1.00   37.11  ? 409 SER E CB  1 
ATOM   14998 O OG  . SER E  1 409 ? 158.164 21.625  -20.723 1.00   37.91  ? 409 SER E OG  1 
ATOM   14999 N N   . ASN E  1 410 ? 161.297 19.998  -17.824 1.00   43.02  ? 410 ASN E N   1 
ATOM   15000 C CA  . ASN E  1 410 ? 162.362 19.047  -17.503 1.00   43.06  ? 410 ASN E CA  1 
ATOM   15001 C C   . ASN E  1 410 ? 162.591 18.869  -16.011 1.00   42.98  ? 410 ASN E C   1 
ATOM   15002 O O   . ASN E  1 410 ? 163.561 18.224  -15.604 1.00   50.19  ? 410 ASN E O   1 
ATOM   15003 C CB  . ASN E  1 410 ? 163.692 19.412  -18.179 1.00   44.36  ? 410 ASN E CB  1 
ATOM   15004 C CG  . ASN E  1 410 ? 164.288 20.711  -17.686 1.00   45.39  ? 410 ASN E CG  1 
ATOM   15005 O OD1 . ASN E  1 410 ? 164.146 21.090  -16.527 1.00   43.70  ? 410 ASN E OD1 1 
ATOM   15006 N ND2 . ASN E  1 410 ? 165.017 21.379  -18.568 1.00   48.36  ? 410 ASN E ND2 1 
ATOM   15007 N N   . LEU E  1 411 ? 161.726 19.456  -15.199 1.00   35.76  ? 411 LEU E N   1 
ATOM   15008 C CA  . LEU E  1 411 ? 161.816 19.265  -13.766 1.00   35.50  ? 411 LEU E CA  1 
ATOM   15009 C C   . LEU E  1 411 ? 161.573 17.810  -13.418 1.00   41.68  ? 411 LEU E C   1 
ATOM   15010 O O   . LEU E  1 411 ? 162.200 17.257  -12.517 1.00   46.70  ? 411 LEU E O   1 
ATOM   15011 C CB  . LEU E  1 411 ? 160.808 20.139  -13.040 1.00   34.93  ? 411 LEU E CB  1 
ATOM   15012 C CG  . LEU E  1 411 ? 161.298 21.314  -12.204 1.00   36.68  ? 411 LEU E CG  1 
ATOM   15013 C CD1 . LEU E  1 411 ? 160.177 21.743  -11.248 1.00   35.48  ? 411 LEU E CD1 1 
ATOM   15014 C CD2 . LEU E  1 411 ? 162.614 21.030  -11.493 1.00   36.05  ? 411 LEU E CD2 1 
ATOM   15015 N N   . PHE E  1 412 ? 160.638 17.195  -14.138 1.00   42.15  ? 412 PHE E N   1 
ATOM   15016 C CA  . PHE E  1 412 ? 160.295 15.803  -13.921 1.00   42.37  ? 412 PHE E CA  1 
ATOM   15017 C C   . PHE E  1 412 ? 160.383 15.016  -15.213 1.00   47.59  ? 412 PHE E C   1 
ATOM   15018 O O   . PHE E  1 412 ? 160.246 15.579  -16.298 1.00   49.80  ? 412 PHE E O   1 
ATOM   15019 C CB  . PHE E  1 412 ? 158.880 15.687  -13.325 1.00   39.53  ? 412 PHE E CB  1 
ATOM   15020 C CG  . PHE E  1 412 ? 158.650 16.598  -12.161 1.00   36.82  ? 412 PHE E CG  1 
ATOM   15021 C CD1 . PHE E  1 412 ? 159.191 16.313  -10.922 1.00   36.01  ? 412 PHE E CD1 1 
ATOM   15022 C CD2 . PHE E  1 412 ? 157.898 17.748  -12.309 1.00   36.25  ? 412 PHE E CD2 1 
ATOM   15023 C CE1 . PHE E  1 412 ? 159.006 17.162  -9.858  1.00   32.69  ? 412 PHE E CE1 1 
ATOM   15024 C CE2 . PHE E  1 412 ? 157.708 18.612  -11.240 1.00   35.77  ? 412 PHE E CE2 1 
ATOM   15025 C CZ  . PHE E  1 412 ? 158.264 18.310  -10.011 1.00   33.69  ? 412 PHE E CZ  1 
ATOM   15026 N N   . ASP E  1 413 ? 160.603 13.709  -15.082 1.00   49.88  ? 413 ASP E N   1 
ATOM   15027 C CA  . ASP E  1 413 ? 160.638 12.807  -16.216 1.00   52.63  ? 413 ASP E CA  1 
ATOM   15028 C C   . ASP E  1 413 ? 159.211 12.557  -16.662 1.00   50.88  ? 413 ASP E C   1 
ATOM   15029 O O   . ASP E  1 413 ? 158.468 11.859  -15.987 1.00   50.13  ? 413 ASP E O   1 
ATOM   15030 C CB  . ASP E  1 413 ? 161.330 11.495  -15.826 1.00   56.32  ? 413 ASP E CB  1 
ATOM   15031 C CG  . ASP E  1 413 ? 161.644 10.611  -17.015 1.00   59.62  ? 413 ASP E CG  1 
ATOM   15032 O OD1 . ASP E  1 413 ? 160.873 10.649  -17.987 1.00   59.10  ? 413 ASP E OD1 1 
ATOM   15033 O OD2 . ASP E  1 413 ? 162.654 9.867   -16.971 1.00   63.39  1 413 ASP E OD2 1 
ATOM   15034 N N   . LEU E  1 414 ? 158.840 13.087  -17.820 1.00   50.24  ? 414 LEU E N   1 
ATOM   15035 C CA  . LEU E  1 414 ? 157.482 12.918  -18.313 1.00   51.34  ? 414 LEU E CA  1 
ATOM   15036 C C   . LEU E  1 414 ? 157.473 11.947  -19.476 1.00   60.14  ? 414 LEU E C   1 
ATOM   15037 O O   . LEU E  1 414 ? 156.513 11.880  -20.247 1.00   63.68  ? 414 LEU E O   1 
ATOM   15038 C CB  . LEU E  1 414 ? 156.862 14.256  -18.716 1.00   44.81  ? 414 LEU E CB  1 
ATOM   15039 C CG  . LEU E  1 414 ? 156.740 15.274  -17.584 1.00   39.87  ? 414 LEU E CG  1 
ATOM   15040 C CD1 . LEU E  1 414 ? 156.182 16.602  -18.047 1.00   36.22  ? 414 LEU E CD1 1 
ATOM   15041 C CD2 . LEU E  1 414 ? 155.860 14.697  -16.500 1.00   40.03  ? 414 LEU E CD2 1 
ATOM   15042 N N   . ASN E  1 415 ? 158.552 11.185  -19.592 1.00   62.79  ? 415 ASN E N   1 
ATOM   15043 C CA  . ASN E  1 415 ? 158.605 10.140  -20.585 1.00   66.51  ? 415 ASN E CA  1 
ATOM   15044 C C   . ASN E  1 415 ? 157.892 8.936   -20.027 1.00   64.61  ? 415 ASN E C   1 
ATOM   15045 O O   . ASN E  1 415 ? 158.164 8.534   -18.892 1.00   60.35  ? 415 ASN E O   1 
ATOM   15046 C CB  . ASN E  1 415 ? 160.051 9.796   -20.949 1.00   71.68  ? 415 ASN E CB  1 
ATOM   15047 C CG  . ASN E  1 415 ? 160.807 10.981  -21.509 1.00   72.09  ? 415 ASN E CG  1 
ATOM   15048 O OD1 . ASN E  1 415 ? 160.287 11.702  -22.357 1.00   72.96  ? 415 ASN E OD1 1 
ATOM   15049 N ND2 . ASN E  1 415 ? 162.034 11.194  -21.037 1.00   72.45  ? 415 ASN E ND2 1 
ATOM   15050 N N   . ASN E  1 416 ? 157.001 8.375   -20.850 1.00   67.96  ? 416 ASN E N   1 
ATOM   15051 C CA  . ASN E  1 416 ? 156.178 7.193   -20.549 1.00   72.08  ? 416 ASN E CA  1 
ATOM   15052 C C   . ASN E  1 416 ? 156.896 5.948   -20.013 1.00   74.37  ? 416 ASN E C   1 
ATOM   15053 O O   . ASN E  1 416 ? 156.252 4.964   -19.627 1.00   73.98  ? 416 ASN E O   1 
ATOM   15054 C CB  . ASN E  1 416 ? 155.429 6.824   -21.813 1.00   76.24  ? 416 ASN E CB  1 
ATOM   15055 C CG  . ASN E  1 416 ? 156.217 7.173   -23.043 1.00   79.72  ? 416 ASN E CG  1 
ATOM   15056 O OD1 . ASN E  1 416 ? 157.246 6.563   -23.334 1.00   81.66  ? 416 ASN E OD1 1 
ATOM   15057 N ND2 . ASN E  1 416 ? 155.765 8.192   -23.753 1.00   80.01  ? 416 ASN E ND2 1 
ATOM   15058 N N   . SER F  1 10  ? 122.546 96.139  9.305   1.00   86.29  ? 10  SER F N   1 
ATOM   15059 C CA  . SER F  1 10  ? 122.616 95.500  10.613  1.00   85.26  ? 10  SER F CA  1 
ATOM   15060 C C   . SER F  1 10  ? 122.888 93.985  10.494  1.00   79.64  ? 10  SER F C   1 
ATOM   15061 O O   . SER F  1 10  ? 122.858 93.274  11.502  1.00   78.78  ? 10  SER F O   1 
ATOM   15062 C CB  . SER F  1 10  ? 121.329 95.749  11.413  1.00   87.76  ? 10  SER F CB  1 
ATOM   15063 O OG  . SER F  1 10  ? 120.457 94.627  11.367  1.00   86.07  ? 10  SER F OG  1 
ATOM   15064 N N   . LYS F  1 11  ? 123.180 93.510  9.277   1.00   74.47  ? 11  LYS F N   1 
ATOM   15065 C CA  . LYS F  1 11  ? 123.349 92.073  9.014   1.00   67.50  ? 11  LYS F CA  1 
ATOM   15066 C C   . LYS F  1 11  ? 124.817 91.752  8.767   1.00   55.83  ? 11  LYS F C   1 
ATOM   15067 O O   . LYS F  1 11  ? 125.446 92.295  7.858   1.00   56.43  ? 11  LYS F O   1 
ATOM   15068 C CB  . LYS F  1 11  ? 122.497 91.591  7.825   1.00   71.81  ? 11  LYS F CB  1 
ATOM   15069 C CG  . LYS F  1 11  ? 123.179 90.474  6.976   1.00   82.54  ? 11  LYS F CG  1 
ATOM   15070 C CD  . LYS F  1 11  ? 122.888 90.629  5.468   1.00   80.37  ? 11  LYS F CD  1 
ATOM   15071 C CE  . LYS F  1 11  ? 123.777 89.743  4.567   1.00   72.04  ? 11  LYS F CE  1 
ATOM   15072 N NZ  . LYS F  1 11  ? 123.363 89.806  3.119   1.00   69.53  ? 11  LYS F NZ  1 
ATOM   15073 N N   . PRO F  1 12  ? 125.392 90.932  9.643   1.00   44.45  ? 12  PRO F N   1 
ATOM   15074 C CA  . PRO F  1 12  ? 126.809 90.585  9.621   1.00   45.20  ? 12  PRO F CA  1 
ATOM   15075 C C   . PRO F  1 12  ? 127.158 89.763  8.394   1.00   47.53  ? 12  PRO F C   1 
ATOM   15076 O O   . PRO F  1 12  ? 126.319 89.033  7.861   1.00   47.79  ? 12  PRO F O   1 
ATOM   15077 C CB  . PRO F  1 12  ? 126.985 89.768  10.888  1.00   34.96  ? 12  PRO F CB  1 
ATOM   15078 C CG  . PRO F  1 12  ? 125.675 89.208  11.139  1.00   33.97  ? 12  PRO F CG  1 
ATOM   15079 C CD  . PRO F  1 12  ? 124.667 90.197  10.680  1.00   41.07  ? 12  PRO F CD  1 
ATOM   15080 N N   . ASN F  1 13  ? 128.402 89.895  7.948   1.00   48.81  ? 13  ASN F N   1 
ATOM   15081 C CA  . ASN F  1 13  ? 128.843 89.196  6.772   1.00   49.07  ? 13  ASN F CA  1 
ATOM   15082 C C   . ASN F  1 13  ? 129.754 88.047  7.151   1.00   43.83  ? 13  ASN F C   1 
ATOM   15083 O O   . ASN F  1 13  ? 130.158 87.270  6.301   1.00   40.33  ? 13  ASN F O   1 
ATOM   15084 C CB  . ASN F  1 13  ? 129.567 90.165  5.852   1.00   57.71  ? 13  ASN F CB  1 
ATOM   15085 C CG  . ASN F  1 13  ? 128.618 91.105  5.145   1.00   67.87  ? 13  ASN F CG  1 
ATOM   15086 O OD1 . ASN F  1 13  ? 127.870 90.703  4.250   1.00   71.47  ? 13  ASN F OD1 1 
ATOM   15087 N ND2 . ASN F  1 13  ? 128.641 92.373  5.550   1.00   71.52  ? 13  ASN F ND2 1 
ATOM   15088 N N   . LEU F  1 14  ? 130.057 87.948  8.438   1.00   32.24  ? 14  LEU F N   1 
ATOM   15089 C CA  . LEU F  1 14  ? 130.933 86.911  8.950   1.00   29.93  ? 14  LEU F CA  1 
ATOM   15090 C C   . LEU F  1 14  ? 130.606 86.664  10.413  1.00   28.77  ? 14  LEU F C   1 
ATOM   15091 O O   . LEU F  1 14  ? 130.392 87.604  11.162  1.00   31.64  ? 14  LEU F O   1 
ATOM   15092 C CB  . LEU F  1 14  ? 132.410 87.279  8.761   1.00   30.72  ? 14  LEU F CB  1 
ATOM   15093 C CG  . LEU F  1 14  ? 133.437 86.146  9.011   1.00   28.72  ? 14  LEU F CG  1 
ATOM   15094 C CD1 . LEU F  1 14  ? 133.424 85.094  7.940   1.00   27.60  ? 14  LEU F CD1 1 
ATOM   15095 C CD2 . LEU F  1 14  ? 134.818 86.725  9.110   1.00   29.89  ? 14  LEU F CD2 1 
ATOM   15096 N N   . LEU F  1 15  ? 130.500 85.389  10.784  1.00   26.56  ? 15  LEU F N   1 
ATOM   15097 C CA  . LEU F  1 15  ? 130.206 84.981  12.148  1.00   27.73  ? 15  LEU F CA  1 
ATOM   15098 C C   . LEU F  1 15  ? 131.313 84.091  12.629  1.00   29.23  ? 15  LEU F C   1 
ATOM   15099 O O   . LEU F  1 15  ? 131.979 83.455  11.834  1.00   29.09  ? 15  LEU F O   1 
ATOM   15100 C CB  . LEU F  1 15  ? 128.885 84.239  12.245  1.00   27.85  ? 15  LEU F CB  1 
ATOM   15101 C CG  . LEU F  1 15  ? 127.665 84.876  11.587  1.00   29.95  ? 15  LEU F CG  1 
ATOM   15102 C CD1 . LEU F  1 15  ? 126.568 83.858  11.609  1.00   27.34  ? 15  LEU F CD1 1 
ATOM   15103 C CD2 . LEU F  1 15  ? 127.266 86.149  12.313  1.00   27.46  ? 15  LEU F CD2 1 
ATOM   15104 N N   . VAL F  1 16  ? 131.544 84.082  13.931  1.00   30.63  ? 16  VAL F N   1 
ATOM   15105 C CA  . VAL F  1 16  ? 132.685 83.354  14.460  1.00   31.77  ? 16  VAL F CA  1 
ATOM   15106 C C   . VAL F  1 16  ? 132.343 82.536  15.694  1.00   29.62  ? 16  VAL F C   1 
ATOM   15107 O O   . VAL F  1 16  ? 131.799 83.043  16.674  1.00   29.49  ? 16  VAL F O   1 
ATOM   15108 C CB  . VAL F  1 16  ? 133.858 84.304  14.822  1.00   35.57  ? 16  VAL F CB  1 
ATOM   15109 C CG1 . VAL F  1 16  ? 135.023 83.512  15.365  1.00   33.59  ? 16  VAL F CG1 1 
ATOM   15110 C CG2 . VAL F  1 16  ? 134.296 85.168  13.611  1.00   30.19  ? 16  VAL F CG2 1 
ATOM   15111 N N   . LEU F  1 17  ? 132.726 81.272  15.655  1.00   28.19  ? 17  LEU F N   1 
ATOM   15112 C CA  . LEU F  1 17  ? 132.506 80.393  16.774  1.00   28.85  ? 17  LEU F CA  1 
ATOM   15113 C C   . LEU F  1 17  ? 133.837 79.839  17.282  1.00   32.60  ? 17  LEU F C   1 
ATOM   15114 O O   . LEU F  1 17  ? 134.499 79.041  16.612  1.00   31.98  ? 17  LEU F O   1 
ATOM   15115 C CB  . LEU F  1 17  ? 131.584 79.263  16.355  1.00   30.10  ? 17  LEU F CB  1 
ATOM   15116 C CG  . LEU F  1 17  ? 131.264 78.306  17.469  1.00   30.50  ? 17  LEU F CG  1 
ATOM   15117 C CD1 . LEU F  1 17  ? 130.331 78.995  18.465  1.00   30.80  ? 17  LEU F CD1 1 
ATOM   15118 C CD2 . LEU F  1 17  ? 130.664 77.107  16.845  1.00   30.65  ? 17  LEU F CD2 1 
ATOM   15119 N N   . PRO F  1 18  ? 134.257 80.294  18.462  1.00   34.22  ? 18  PRO F N   1 
ATOM   15120 C CA  . PRO F  1 18  ? 135.460 79.754  19.084  1.00   34.15  ? 18  PRO F CA  1 
ATOM   15121 C C   . PRO F  1 18  ? 135.245 78.323  19.564  1.00   34.76  ? 18  PRO F C   1 
ATOM   15122 O O   . PRO F  1 18  ? 134.205 77.988  20.131  1.00   31.78  ? 18  PRO F O   1 
ATOM   15123 C CB  . PRO F  1 18  ? 135.702 80.701  20.254  1.00   36.32  ? 18  PRO F CB  1 
ATOM   15124 C CG  . PRO F  1 18  ? 134.944 81.940  19.907  1.00   35.80  ? 18  PRO F CG  1 
ATOM   15125 C CD  . PRO F  1 18  ? 133.733 81.451  19.198  1.00   35.31  ? 18  PRO F CD  1 
ATOM   15126 N N   . VAL F  1 19  ? 136.254 77.493  19.324  1.00   36.58  ? 19  VAL F N   1 
ATOM   15127 C CA  . VAL F  1 19  ? 136.220 76.082  19.655  1.00   39.33  ? 19  VAL F CA  1 
ATOM   15128 C C   . VAL F  1 19  ? 137.481 75.737  20.463  1.00   41.66  ? 19  VAL F C   1 
ATOM   15129 O O   . VAL F  1 19  ? 138.508 76.403  20.306  1.00   40.89  ? 19  VAL F O   1 
ATOM   15130 C CB  A VAL F  1 19  ? 136.127 75.246  18.341  0.50   33.19  ? 19  VAL F CB  1 
ATOM   15131 C CB  B VAL F  1 19  ? 136.115 75.167  18.401  0.50   33.22  ? 19  VAL F CB  1 
ATOM   15132 C CG1 A VAL F  1 19  ? 136.429 73.786  18.560  0.50   34.43  ? 19  VAL F CG1 1 
ATOM   15133 C CG1 B VAL F  1 19  ? 134.883 75.511  17.597  0.50   31.54  ? 19  VAL F CG1 1 
ATOM   15134 C CG2 A VAL F  1 19  ? 134.763 75.419  17.702  0.50   31.52  ? 19  VAL F CG2 1 
ATOM   15135 C CG2 B VAL F  1 19  ? 137.364 75.253  17.538  0.50   32.94  ? 19  VAL F CG2 1 
ATOM   15136 N N   . GLN F  1 20  ? 137.395 74.721  21.331  1.00   41.15  ? 20  GLN F N   1 
ATOM   15137 C CA  . GLN F  1 20  ? 138.501 74.307  22.198  1.00   40.14  ? 20  GLN F CA  1 
ATOM   15138 C C   . GLN F  1 20  ? 138.805 72.790  22.169  1.00   37.72  ? 20  GLN F C   1 
ATOM   15139 O O   . GLN F  1 20  ? 137.883 71.983  22.157  1.00   39.45  ? 20  GLN F O   1 
ATOM   15140 C CB  . GLN F  1 20  ? 138.192 74.717  23.626  1.00   42.61  ? 20  GLN F CB  1 
ATOM   15141 C CG  . GLN F  1 20  ? 139.368 74.544  24.546  1.00   47.30  ? 20  GLN F CG  1 
ATOM   15142 C CD  . GLN F  1 20  ? 139.119 75.110  25.908  1.00   50.50  ? 20  GLN F CD  1 
ATOM   15143 O OE1 . GLN F  1 20  ? 139.034 74.367  26.880  1.00   53.19  ? 20  GLN F OE1 1 
ATOM   15144 N NE2 . GLN F  1 20  ? 139.010 76.429  25.997  1.00   50.20  ? 20  GLN F NE2 1 
ATOM   15145 N N   . GLU F  1 21  ? 140.081 72.403  22.209  1.00   35.51  ? 21  GLU F N   1 
ATOM   15146 C CA  . GLU F  1 21  ? 140.465 70.988  22.265  1.00   35.39  ? 21  GLU F CA  1 
ATOM   15147 C C   . GLU F  1 21  ? 140.385 70.378  23.662  1.00   37.98  ? 21  GLU F C   1 
ATOM   15148 O O   . GLU F  1 21  ? 140.832 70.977  24.630  1.00   40.10  ? 21  GLU F O   1 
ATOM   15149 C CB  . GLU F  1 21  ? 141.884 70.800  21.740  1.00   36.48  ? 21  GLU F CB  1 
ATOM   15150 C CG  . GLU F  1 21  ? 142.220 69.366  21.355  1.00   40.77  ? 21  GLU F CG  1 
ATOM   15151 C CD  . GLU F  1 21  ? 143.015 68.645  22.431  1.00   49.86  ? 21  GLU F CD  1 
ATOM   15152 O OE1 . GLU F  1 21  ? 143.262 69.263  23.484  1.00   52.33  ? 21  GLU F OE1 1 
ATOM   15153 O OE2 . GLU F  1 21  ? 143.416 67.473  22.228  1.00   53.04  ? 21  GLU F OE2 1 
ATOM   15154 N N   . ASP F  1 22  ? 139.828 69.176  23.768  1.00   38.73  ? 22  ASP F N   1 
ATOM   15155 C CA  . ASP F  1 22  ? 139.818 68.470  25.043  1.00   41.30  ? 22  ASP F CA  1 
ATOM   15156 C C   . ASP F  1 22  ? 140.965 67.478  25.065  1.00   44.56  ? 22  ASP F C   1 
ATOM   15157 O O   . ASP F  1 22  ? 140.980 66.547  24.267  1.00   45.06  ? 22  ASP F O   1 
ATOM   15158 C CB  . ASP F  1 22  ? 138.486 67.756  25.250  1.00   41.51  ? 22  ASP F CB  1 
ATOM   15159 C CG  . ASP F  1 22  ? 138.439 66.964  26.533  1.00   46.77  ? 22  ASP F CG  1 
ATOM   15160 O OD1 . ASP F  1 22  ? 138.533 67.585  27.612  1.00   48.54  ? 22  ASP F OD1 1 
ATOM   15161 O OD2 . ASP F  1 22  ? 138.313 65.718  26.467  1.00   49.45  1 22  ASP F OD2 1 
ATOM   15162 N N   . ALA F  1 23  ? 141.921 67.677  25.974  1.00   47.19  ? 23  ALA F N   1 
ATOM   15163 C CA  . ALA F  1 23  ? 143.157 66.908  25.994  1.00   51.32  ? 23  ALA F CA  1 
ATOM   15164 C C   . ALA F  1 23  ? 142.940 65.422  26.236  1.00   54.27  ? 23  ALA F C   1 
ATOM   15165 O O   . ALA F  1 23  ? 143.595 64.570  25.625  1.00   54.23  ? 23  ALA F O   1 
ATOM   15166 C CB  . ALA F  1 23  ? 144.084 67.462  27.039  1.00   58.03  ? 23  ALA F CB  1 
ATOM   15167 N N   . SER F  1 24  ? 142.030 65.127  27.153  1.00   56.13  ? 24  SER F N   1 
ATOM   15168 C CA  . SER F  1 24  ? 141.738 63.760  27.532  1.00   59.24  ? 24  SER F CA  1 
ATOM   15169 C C   . SER F  1 24  ? 141.320 62.927  26.334  1.00   57.17  ? 24  SER F C   1 
ATOM   15170 O O   . SER F  1 24  ? 141.914 61.887  26.065  1.00   58.99  ? 24  SER F O   1 
ATOM   15171 C CB  . SER F  1 24  ? 140.623 63.750  28.574  1.00   62.84  ? 24  SER F CB  1 
ATOM   15172 O OG  . SER F  1 24  ? 140.178 62.442  28.858  1.00   68.15  ? 24  SER F OG  1 
ATOM   15173 N N   . THR F  1 25  ? 140.336 63.421  25.588  1.00   52.56  ? 25  THR F N   1 
ATOM   15174 C CA  . THR F  1 25  ? 139.734 62.675  24.490  1.00   50.14  ? 25  THR F CA  1 
ATOM   15175 C C   . THR F  1 25  ? 140.297 63.058  23.122  1.00   48.58  ? 25  THR F C   1 
ATOM   15176 O O   . THR F  1 25  ? 140.196 62.299  22.164  1.00   47.35  ? 25  THR F O   1 
ATOM   15177 C CB  . THR F  1 25  ? 138.228 62.903  24.449  1.00   45.54  ? 25  THR F CB  1 
ATOM   15178 O OG1 . THR F  1 25  ? 137.987 64.279  24.184  1.00   44.31  ? 25  THR F OG1 1 
ATOM   15179 C CG2 . THR F  1 25  ? 137.603 62.556  25.772  1.00   54.80  ? 25  THR F CG2 1 
ATOM   15180 N N   . GLY F  1 26  ? 140.890 64.236  23.028  1.00   43.43  ? 26  GLY F N   1 
ATOM   15181 C CA  . GLY F  1 26  ? 141.393 64.709  21.759  1.00   41.02  ? 26  GLY F CA  1 
ATOM   15182 C C   . GLY F  1 26  ? 140.314 65.310  20.882  1.00   40.40  ? 26  GLY F C   1 
ATOM   15183 O O   . GLY F  1 26  ? 140.558 65.643  19.725  1.00   40.14  ? 26  GLY F O   1 
ATOM   15184 N N   . LEU F  1 27  ? 139.117 65.476  21.435  1.00   39.22  ? 27  LEU F N   1 
ATOM   15185 C CA  . LEU F  1 27  ? 138.016 66.034  20.676  1.00   33.91  ? 27  LEU F CA  1 
ATOM   15186 C C   . LEU F  1 27  ? 137.893 67.505  20.951  1.00   37.68  ? 27  LEU F C   1 
ATOM   15187 O O   . LEU F  1 27  ? 138.509 68.011  21.889  1.00   40.14  ? 27  LEU F O   1 
ATOM   15188 C CB  . LEU F  1 27  ? 136.720 65.313  21.011  1.00   34.30  ? 27  LEU F CB  1 
ATOM   15189 C CG  . LEU F  1 27  ? 136.812 63.821  20.698  1.00   38.14  ? 27  LEU F CG  1 
ATOM   15190 C CD1 . LEU F  1 27  ? 135.586 63.067  21.146  1.00   39.01  ? 27  LEU F CD1 1 
ATOM   15191 C CD2 . LEU F  1 27  ? 137.043 63.603  19.208  1.00   36.59  ? 27  LEU F CD2 1 
ATOM   15192 N N   . HIS F  1 28  ? 137.101 68.180  20.118  1.00   33.17  ? 28  HIS F N   1 
ATOM   15193 C CA  . HIS F  1 28  ? 136.900 69.617  20.205  1.00   30.94  ? 28  HIS F CA  1 
ATOM   15194 C C   . HIS F  1 28  ? 135.433 69.917  20.505  1.00   31.72  ? 28  HIS F C   1 
ATOM   15195 O O   . HIS F  1 28  ? 134.553 69.174  20.103  1.00   32.07  ? 28  HIS F O   1 
ATOM   15196 C CB  . HIS F  1 28  ? 137.345 70.299  18.913  1.00   29.06  ? 28  HIS F CB  1 
ATOM   15197 C CG  . HIS F  1 28  ? 138.816 70.187  18.644  1.00   27.51  ? 28  HIS F CG  1 
ATOM   15198 N ND1 . HIS F  1 28  ? 139.675 71.260  18.735  1.00   30.59  ? 28  HIS F ND1 1 
ATOM   15199 C CD2 . HIS F  1 28  ? 139.573 69.129  18.269  1.00   28.67  ? 28  HIS F CD2 1 
ATOM   15200 C CE1 . HIS F  1 28  ? 140.904 70.863  18.445  1.00   31.68  ? 28  HIS F CE1 1 
ATOM   15201 N NE2 . HIS F  1 28  ? 140.869 69.575  18.160  1.00   29.35  ? 28  HIS F NE2 1 
ATOM   15202 N N   . TRP F  1 29  ? 135.189 70.987  21.256  1.00   32.67  ? 29  TRP F N   1 
ATOM   15203 C CA  . TRP F  1 29  ? 133.850 71.354  21.682  1.00   31.89  ? 29  TRP F CA  1 
ATOM   15204 C C   . TRP F  1 29  ? 133.744 72.886  21.722  1.00   33.52  ? 29  TRP F C   1 
ATOM   15205 O O   . TRP F  1 29  ? 134.763 73.564  21.704  1.00   34.59  ? 29  TRP F O   1 
ATOM   15206 C CB  . TRP F  1 29  ? 133.554 70.768  23.051  1.00   32.00  ? 29  TRP F CB  1 
ATOM   15207 C CG  . TRP F  1 29  ? 134.413 71.366  24.078  1.00   36.42  ? 29  TRP F CG  1 
ATOM   15208 C CD1 . TRP F  1 29  ? 135.705 71.030  24.372  1.00   40.87  ? 29  TRP F CD1 1 
ATOM   15209 C CD2 . TRP F  1 29  ? 134.056 72.421  24.975  1.00   39.05  ? 29  TRP F CD2 1 
ATOM   15210 N NE1 . TRP F  1 29  ? 136.172 71.816  25.395  1.00   42.63  ? 29  TRP F NE1 1 
ATOM   15211 C CE2 . TRP F  1 29  ? 135.178 72.679  25.781  1.00   42.48  ? 29  TRP F CE2 1 
ATOM   15212 C CE3 . TRP F  1 29  ? 132.893 73.167  25.178  1.00   39.14  ? 29  TRP F CE3 1 
ATOM   15213 C CZ2 . TRP F  1 29  ? 135.171 73.653  26.772  1.00   42.97  ? 29  TRP F CZ2 1 
ATOM   15214 C CZ3 . TRP F  1 29  ? 132.890 74.133  26.154  1.00   39.13  ? 29  TRP F CZ3 1 
ATOM   15215 C CH2 . TRP F  1 29  ? 134.020 74.365  26.943  1.00   42.07  ? 29  TRP F CH2 1 
ATOM   15216 N N   . ALA F  1 30  ? 132.529 73.431  21.779  1.00   33.46  ? 30  ALA F N   1 
ATOM   15217 C CA  . ALA F  1 30  ? 132.322 74.888  21.865  1.00   30.41  ? 30  ALA F CA  1 
ATOM   15218 C C   . ALA F  1 30  ? 131.205 75.217  22.850  1.00   30.32  ? 30  ALA F C   1 
ATOM   15219 O O   . ALA F  1 30  ? 130.237 74.468  22.957  1.00   32.77  ? 30  ALA F O   1 
ATOM   15220 C CB  . ALA F  1 30  ? 131.994 75.469  20.480  1.00   29.61  ? 30  ALA F CB  1 
ATOM   15221 N N   . ASN F  1 31  ? 131.315 76.332  23.558  1.00   32.39  ? 31  ASN F N   1 
ATOM   15222 C CA  . ASN F  1 31  ? 130.155 76.835  24.281  1.00   34.79  ? 31  ASN F CA  1 
ATOM   15223 C C   . ASN F  1 31  ? 129.238 77.554  23.324  1.00   36.96  ? 31  ASN F C   1 
ATOM   15224 O O   . ASN F  1 31  ? 129.619 78.568  22.744  1.00   41.62  ? 31  ASN F O   1 
ATOM   15225 C CB  . ASN F  1 31  ? 130.547 77.784  25.399  1.00   34.46  ? 31  ASN F CB  1 
ATOM   15226 C CG  . ASN F  1 31  ? 130.850 77.079  26.681  1.00   37.49  ? 31  ASN F CG  1 
ATOM   15227 O OD1 . ASN F  1 31  ? 130.129 76.193  27.112  1.00   38.83  ? 31  ASN F OD1 1 
ATOM   15228 N ND2 . ASN F  1 31  ? 131.931 77.472  27.305  1.00   41.15  ? 31  ASN F ND2 1 
ATOM   15229 N N   . ILE F  1 32  ? 128.031 77.025  23.147  1.00   34.48  ? 32  ILE F N   1 
ATOM   15230 C CA  . ILE F  1 32  ? 127.032 77.656  22.275  1.00   34.74  ? 32  ILE F CA  1 
ATOM   15231 C C   . ILE F  1 32  ? 125.976 78.410  23.077  1.00   32.34  ? 32  ILE F C   1 
ATOM   15232 O O   . ILE F  1 32  ? 125.494 77.924  24.107  1.00   31.32  ? 32  ILE F O   1 
ATOM   15233 C CB  . ILE F  1 32  ? 126.323 76.631  21.366  1.00   37.05  ? 32  ILE F CB  1 
ATOM   15234 C CG1 . ILE F  1 32  ? 127.344 75.812  20.577  1.00   37.22  ? 32  ILE F CG1 1 
ATOM   15235 C CG2 . ILE F  1 32  ? 125.390 77.341  20.398  1.00   36.61  ? 32  ILE F CG2 1 
ATOM   15236 C CD1 . ILE F  1 32  ? 128.043 76.588  19.532  1.00   36.92  ? 32  ILE F CD1 1 
ATOM   15237 N N   . HIS F  1 33  ? 125.627 79.605  22.610  1.00   31.75  ? 33  HIS F N   1 
ATOM   15238 C CA  . HIS F  1 33  ? 124.636 80.413  23.290  1.00   31.20  ? 33  HIS F CA  1 
ATOM   15239 C C   . HIS F  1 33  ? 123.233 80.162  22.799  1.00   29.14  ? 33  HIS F C   1 
ATOM   15240 O O   . HIS F  1 33  ? 122.959 80.274  21.618  1.00   28.28  ? 33  HIS F O   1 
ATOM   15241 C CB  . HIS F  1 33  ? 124.979 81.875  23.136  1.00   34.41  ? 33  HIS F CB  1 
ATOM   15242 C CG  . HIS F  1 33  ? 126.278 82.243  23.771  1.00   40.32  ? 33  HIS F CG  1 
ATOM   15243 N ND1 . HIS F  1 33  ? 127.495 81.870  23.238  1.00   44.45  ? 33  HIS F ND1 1 
ATOM   15244 C CD2 . HIS F  1 33  ? 126.553 82.903  24.919  1.00   41.19  ? 33  HIS F CD2 1 
ATOM   15245 C CE1 . HIS F  1 33  ? 128.463 82.312  24.019  1.00   45.63  ? 33  HIS F CE1 1 
ATOM   15246 N NE2 . HIS F  1 33  ? 127.918 82.938  25.047  1.00   43.22  ? 33  HIS F NE2 1 
ATOM   15247 N N   . LYS F  1 34  ? 122.352 79.814  23.730  1.00   30.42  ? 34  LYS F N   1 
ATOM   15248 C CA  . LYS F  1 34  ? 120.970 79.483  23.433  1.00   29.15  ? 34  LYS F CA  1 
ATOM   15249 C C   . LYS F  1 34  ? 120.002 80.046  24.454  1.00   28.74  ? 34  LYS F C   1 
ATOM   15250 O O   . LYS F  1 34  ? 120.396 80.422  25.538  1.00   29.45  ? 34  LYS F O   1 
ATOM   15251 C CB  . LYS F  1 34  ? 120.760 77.976  23.392  1.00   30.69  ? 34  LYS F CB  1 
ATOM   15252 C CG  . LYS F  1 34  ? 121.684 77.237  22.484  1.00   35.02  ? 34  LYS F CG  1 
ATOM   15253 C CD  . LYS F  1 34  ? 121.081 77.126  21.067  1.00   35.29  ? 34  LYS F CD  1 
ATOM   15254 C CE  . LYS F  1 34  ? 119.775 76.363  21.014  1.00   31.57  ? 34  LYS F CE  1 
ATOM   15255 N NZ  . LYS F  1 34  ? 120.048 74.957  21.283  1.00   32.12  ? 34  LYS F NZ  1 
ATOM   15256 N N   . ARG F  1 35  ? 118.733 80.088  24.064  1.00   29.59  ? 35  ARG F N   1 
ATOM   15257 C CA  . ARG F  1 35  ? 117.594 80.382  24.938  1.00   29.28  ? 35  ARG F CA  1 
ATOM   15258 C C   . ARG F  1 35  ? 117.407 81.845  25.293  1.00   32.65  ? 35  ARG F C   1 
ATOM   15259 O O   . ARG F  1 35  ? 118.260 82.693  25.002  1.00   36.15  ? 35  ARG F O   1 
ATOM   15260 C CB  . ARG F  1 35  ? 117.699 79.562  26.216  1.00   30.99  ? 35  ARG F CB  1 
ATOM   15261 C CG  . ARG F  1 35  ? 117.789 78.081  25.918  1.00   30.47  ? 35  ARG F CG  1 
ATOM   15262 C CD  . ARG F  1 35  ? 118.148 77.263  27.125  1.00   36.43  ? 35  ARG F CD  1 
ATOM   15263 N NE  . ARG F  1 35  ? 118.714 75.996  26.695  1.00   38.64  ? 35  ARG F NE  1 
ATOM   15264 C CZ  . ARG F  1 35  ? 119.062 75.005  27.504  1.00   46.32  ? 35  ARG F CZ  1 
ATOM   15265 N NH1 . ARG F  1 35  ? 118.885 75.114  28.816  1.00   50.84  ? 35  ARG F NH1 1 
ATOM   15266 N NH2 . ARG F  1 35  ? 119.590 73.898  26.993  1.00   48.84  ? 35  ARG F NH2 1 
ATOM   15267 N N   . THR F  1 36  ? 116.258 82.127  25.900  1.00   31.05  ? 36  THR F N   1 
ATOM   15268 C CA  . THR F  1 36  ? 115.983 83.420  26.501  1.00   31.82  ? 36  THR F CA  1 
ATOM   15269 C C   . THR F  1 36  ? 115.546 83.184  27.943  1.00   33.39  ? 36  THR F C   1 
ATOM   15270 O O   . THR F  1 36  ? 114.518 82.578  28.179  1.00   36.36  ? 36  THR F O   1 
ATOM   15271 C CB  . THR F  1 36  ? 114.894 84.172  25.766  1.00   32.99  ? 36  THR F CB  1 
ATOM   15272 O OG1 . THR F  1 36  ? 115.195 84.209  24.370  1.00   36.18  ? 36  THR F OG1 1 
ATOM   15273 C CG2 . THR F  1 36  ? 114.775 85.588  26.300  1.00   34.86  ? 36  THR F CG2 1 
ATOM   15274 N N   . PRO F  1 37  ? 116.328 83.642  28.916  1.00   34.66  ? 37  PRO F N   1 
ATOM   15275 C CA  . PRO F  1 37  ? 117.577 84.392  28.780  1.00   35.41  ? 37  PRO F CA  1 
ATOM   15276 C C   . PRO F  1 37  ? 118.736 83.553  28.226  1.00   36.52  ? 37  PRO F C   1 
ATOM   15277 O O   . PRO F  1 37  ? 118.761 82.329  28.348  1.00   37.06  ? 37  PRO F O   1 
ATOM   15278 C CB  . PRO F  1 37  ? 117.839 84.874  30.208  1.00   37.24  ? 37  PRO F CB  1 
ATOM   15279 C CG  . PRO F  1 37  ? 117.131 83.925  31.061  1.00   37.61  ? 37  PRO F CG  1 
ATOM   15280 C CD  . PRO F  1 37  ? 115.916 83.510  30.322  1.00   37.70  ? 37  PRO F CD  1 
ATOM   15281 N N   . LEU F  1 38  ? 119.671 84.229  27.572  1.00   35.11  ? 38  LEU F N   1 
ATOM   15282 C CA  . LEU F  1 38  ? 120.739 83.552  26.872  1.00   31.74  ? 38  LEU F CA  1 
ATOM   15283 C C   . LEU F  1 38  ? 121.660 82.848  27.841  1.00   34.51  ? 38  LEU F C   1 
ATOM   15284 O O   . LEU F  1 38  ? 122.019 83.395  28.869  1.00   37.23  ? 38  LEU F O   1 
ATOM   15285 C CB  . LEU F  1 38  ? 121.496 84.555  26.024  1.00   31.76  ? 38  LEU F CB  1 
ATOM   15286 C CG  . LEU F  1 38  ? 122.184 84.091  24.743  1.00   33.61  ? 38  LEU F CG  1 
ATOM   15287 C CD1 . LEU F  1 38  ? 121.235 83.498  23.731  1.00   31.96  ? 38  LEU F CD1 1 
ATOM   15288 C CD2 . LEU F  1 38  ? 122.791 85.329  24.160  1.00   36.70  ? 38  LEU F CD2 1 
ATOM   15289 N N   . MET F  1 39  ? 122.055 81.633  27.511  1.00   32.32  ? 39  MET F N   1 
ATOM   15290 C CA  . MET F  1 39  ? 123.008 80.917  28.341  1.00   35.93  ? 39  MET F CA  1 
ATOM   15291 C C   . MET F  1 39  ? 123.896 80.040  27.458  1.00   37.53  ? 39  MET F C   1 
ATOM   15292 O O   . MET F  1 39  ? 123.676 79.945  26.253  1.00   38.90  ? 39  MET F O   1 
ATOM   15293 C CB  . MET F  1 39  ? 122.282 80.078  29.406  1.00   34.35  ? 39  MET F CB  1 
ATOM   15294 C CG  . MET F  1 39  ? 121.141 79.239  28.864  1.00   32.82  ? 39  MET F CG  1 
ATOM   15295 S SD  . MET F  1 39  ? 121.618 77.720  27.975  1.00   42.63  ? 39  MET F SD  1 
ATOM   15296 C CE  . MET F  1 39  ? 122.215 76.726  29.349  1.00   36.97  ? 39  MET F CE  1 
ATOM   15297 N N   . GLN F  1 40  ? 124.927 79.448  28.050  1.00   38.54  ? 40  GLN F N   1 
ATOM   15298 C CA  . GLN F  1 40  ? 125.884 78.635  27.310  1.00   37.42  ? 40  GLN F CA  1 
ATOM   15299 C C   . GLN F  1 40  ? 125.740 77.136  27.515  1.00   38.00  ? 40  GLN F C   1 
ATOM   15300 O O   . GLN F  1 40  ? 125.601 76.673  28.641  1.00   38.96  ? 40  GLN F O   1 
ATOM   15301 C CB  . GLN F  1 40  ? 127.303 79.022  27.666  1.00   40.99  ? 40  GLN F CB  1 
ATOM   15302 C CG  . GLN F  1 40  ? 127.693 80.371  27.200  1.00   44.27  ? 40  GLN F CG  1 
ATOM   15303 C CD  . GLN F  1 40  ? 129.128 80.659  27.525  1.00   47.17  ? 40  GLN F CD  1 
ATOM   15304 O OE1 . GLN F  1 40  ? 129.962 80.723  26.623  1.00   47.60  ? 40  GLN F OE1 1 
ATOM   15305 N NE2 . GLN F  1 40  ? 129.439 80.810  28.815  1.00   48.62  ? 40  GLN F NE2 1 
ATOM   15306 N N   . VAL F  1 41  ? 125.800 76.390  26.416  1.00   37.59  ? 41  VAL F N   1 
ATOM   15307 C CA  . VAL F  1 41  ? 125.764 74.930  26.426  1.00   40.65  ? 41  VAL F CA  1 
ATOM   15308 C C   . VAL F  1 41  ? 127.049 74.327  25.832  1.00   39.51  ? 41  VAL F C   1 
ATOM   15309 O O   . VAL F  1 41  ? 127.375 74.602  24.683  1.00   38.63  ? 41  VAL F O   1 
ATOM   15310 C CB  . VAL F  1 41  ? 124.572 74.386  25.608  1.00   43.74  ? 41  VAL F CB  1 
ATOM   15311 C CG1 . VAL F  1 41  ? 124.346 72.894  25.912  1.00   45.47  ? 41  VAL F CG1 1 
ATOM   15312 C CG2 . VAL F  1 41  ? 123.319 75.175  25.903  1.00   46.88  ? 41  VAL F CG2 1 
ATOM   15313 N N   . PRO F  1 42  ? 127.792 73.512  26.605  1.00   38.03  ? 42  PRO F N   1 
ATOM   15314 C CA  . PRO F  1 42  ? 128.955 72.896  25.961  1.00   35.52  ? 42  PRO F CA  1 
ATOM   15315 C C   . PRO F  1 42  ? 128.576 71.741  25.022  1.00   32.06  ? 42  PRO F C   1 
ATOM   15316 O O   . PRO F  1 42  ? 127.951 70.775  25.458  1.00   34.23  ? 42  PRO F O   1 
ATOM   15317 C CB  . PRO F  1 42  ? 129.777 72.390  27.155  1.00   37.34  ? 42  PRO F CB  1 
ATOM   15318 C CG  . PRO F  1 42  ? 128.790 72.159  28.219  1.00   37.71  ? 42  PRO F CG  1 
ATOM   15319 C CD  . PRO F  1 42  ? 127.702 73.167  28.037  1.00   36.79  ? 42  PRO F CD  1 
ATOM   15320 N N   . LEU F  1 43  ? 128.961 71.834  23.753  1.00   30.53  ? 43  LEU F N   1 
ATOM   15321 C CA  . LEU F  1 43  ? 128.600 70.810  22.769  1.00   31.47  ? 43  LEU F CA  1 
ATOM   15322 C C   . LEU F  1 43  ? 129.813 70.347  21.928  1.00   33.87  ? 43  LEU F C   1 
ATOM   15323 O O   . LEU F  1 43  ? 130.685 71.148  21.596  1.00   31.10  ? 43  LEU F O   1 
ATOM   15324 C CB  . LEU F  1 43  ? 127.515 71.313  21.824  1.00   26.24  ? 43  LEU F CB  1 
ATOM   15325 C CG  . LEU F  1 43  ? 126.157 71.785  22.334  1.00   26.75  ? 43  LEU F CG  1 
ATOM   15326 C CD1 . LEU F  1 43  ? 125.384 72.318  21.154  1.00   23.64  ? 43  LEU F CD1 1 
ATOM   15327 C CD2 . LEU F  1 43  ? 125.362 70.699  23.087  1.00   27.98  ? 43  LEU F CD2 1 
ATOM   15328 N N   . LEU F  1 44  ? 129.842 69.055  21.576  1.00   34.21  ? 44  LEU F N   1 
ATOM   15329 C CA  . LEU F  1 44  ? 130.897 68.488  20.731  1.00   32.32  ? 44  LEU F CA  1 
ATOM   15330 C C   . LEU F  1 44  ? 130.833 68.992  19.301  1.00   30.68  ? 44  LEU F C   1 
ATOM   15331 O O   . LEU F  1 44  ? 129.753 69.075  18.710  1.00   29.85  ? 44  LEU F O   1 
ATOM   15332 C CB  . LEU F  1 44  ? 130.813 66.965  20.715  1.00   33.27  ? 44  LEU F CB  1 
ATOM   15333 C CG  . LEU F  1 44  ? 131.830 66.187  19.864  1.00   33.53  ? 44  LEU F CG  1 
ATOM   15334 C CD1 . LEU F  1 44  ? 133.157 66.019  20.542  1.00   33.75  ? 44  LEU F CD1 1 
ATOM   15335 C CD2 . LEU F  1 44  ? 131.275 64.833  19.461  1.00   34.31  ? 44  LEU F CD2 1 
ATOM   15336 N N   . LEU F  1 45  ? 132.001 69.295  18.744  1.00   28.83  ? 45  LEU F N   1 
ATOM   15337 C CA  . LEU F  1 45  ? 132.125 69.648  17.334  1.00   26.82  ? 45  LEU F CA  1 
ATOM   15338 C C   . LEU F  1 45  ? 132.106 68.402  16.448  1.00   30.51  ? 45  LEU F C   1 
ATOM   15339 O O   . LEU F  1 45  ? 133.025 67.565  16.489  1.00   33.14  ? 45  LEU F O   1 
ATOM   15340 C CB  . LEU F  1 45  ? 133.406 70.435  17.097  1.00   27.09  ? 45  LEU F CB  1 
ATOM   15341 C CG  . LEU F  1 45  ? 133.743 70.791  15.651  1.00   26.83  ? 45  LEU F CG  1 
ATOM   15342 C CD1 . LEU F  1 45  ? 132.733 71.806  15.078  1.00   27.50  ? 45  LEU F CD1 1 
ATOM   15343 C CD2 . LEU F  1 45  ? 135.154 71.306  15.523  1.00   25.68  ? 45  LEU F CD2 1 
ATOM   15344 N N   . ASP F  1 46  ? 131.041 68.275  15.659  1.00   30.11  ? 46  ASP F N   1 
ATOM   15345 C CA  . ASP F  1 46  ? 130.854 67.131  14.797  1.00   31.92  ? 46  ASP F CA  1 
ATOM   15346 C C   . ASP F  1 46  ? 130.700 67.612  13.366  1.00   30.80  ? 46  ASP F C   1 
ATOM   15347 O O   . ASP F  1 46  ? 129.618 67.994  12.950  1.00   29.04  ? 46  ASP F O   1 
ATOM   15348 C CB  . ASP F  1 46  ? 129.631 66.312  15.237  1.00   29.98  ? 46  ASP F CB  1 
ATOM   15349 C CG  . ASP F  1 46  ? 129.438 65.072  14.413  1.00   31.17  ? 46  ASP F CG  1 
ATOM   15350 O OD1 . ASP F  1 46  ? 130.312 64.737  13.582  1.00   34.42  ? 46  ASP F OD1 1 
ATOM   15351 O OD2 . ASP F  1 46  ? 128.390 64.426  14.582  1.00   33.97  1 46  ASP F OD2 1 
ATOM   15352 N N   . LEU F  1 47  ? 131.797 67.592  12.631  1.00   30.37  ? 47  LEU F N   1 
ATOM   15353 C CA  . LEU F  1 47  ? 131.826 68.118  11.288  1.00   28.41  ? 47  LEU F CA  1 
ATOM   15354 C C   . LEU F  1 47  ? 130.776 67.521  10.378  1.00   28.27  ? 47  LEU F C   1 
ATOM   15355 O O   . LEU F  1 47  ? 130.157 68.216  9.595   1.00   30.45  ? 47  LEU F O   1 
ATOM   15356 C CB  . LEU F  1 47  ? 133.214 67.907  10.673  1.00   27.20  ? 47  LEU F CB  1 
ATOM   15357 C CG  . LEU F  1 47  ? 133.361 68.329  9.204   1.00   27.33  ? 47  LEU F CG  1 
ATOM   15358 C CD1 . LEU F  1 47  ? 133.186 69.837  9.007   1.00   25.65  ? 47  LEU F CD1 1 
ATOM   15359 C CD2 . LEU F  1 47  ? 134.696 67.900  8.716   1.00   28.48  ? 47  LEU F CD2 1 
ATOM   15360 N N   . ASN F  1 48  ? 130.562 66.226  10.464  1.00   29.56  ? 48  ASN F N   1 
ATOM   15361 C CA  . ASN F  1 48  ? 129.651 65.576  9.533   1.00   25.44  ? 48  ASN F CA  1 
ATOM   15362 C C   . ASN F  1 48  ? 128.254 65.427  10.075  1.00   25.15  ? 48  ASN F C   1 
ATOM   15363 O O   . ASN F  1 48  ? 127.400 64.889  9.407   1.00   27.37  ? 48  ASN F O   1 
ATOM   15364 C CB  . ASN F  1 48  ? 130.220 64.218  9.115   1.00   26.72  ? 48  ASN F CB  1 
ATOM   15365 C CG  . ASN F  1 48  ? 131.474 64.359  8.262   1.00   29.20  ? 48  ASN F CG  1 
ATOM   15366 O OD1 . ASN F  1 48  ? 131.469 65.081  7.276   1.00   32.90  ? 48  ASN F OD1 1 
ATOM   15367 N ND2 . ASN F  1 48  ? 132.558 63.726  8.672   1.00   27.22  ? 48  ASN F ND2 1 
ATOM   15368 N N   . GLY F  1 49  ? 128.012 65.948  11.269  1.00   26.84  ? 49  GLY F N   1 
ATOM   15369 C CA  . GLY F  1 49  ? 126.716 65.806  11.912  1.00   25.65  ? 49  GLY F CA  1 
ATOM   15370 C C   . GLY F  1 49  ? 125.559 66.478  11.205  1.00   25.91  ? 49  GLY F C   1 
ATOM   15371 O O   . GLY F  1 49  ? 125.685 67.602  10.728  1.00   27.62  ? 49  GLY F O   1 
ATOM   15372 N N   . LYS F  1 50  ? 124.408 65.813  11.171  1.00   24.39  ? 50  LYS F N   1 
ATOM   15373 C CA  . LYS F  1 50  ? 123.285 66.310  10.391  1.00   24.27  ? 50  LYS F CA  1 
ATOM   15374 C C   . LYS F  1 50  ? 122.535 67.454  11.062  1.00   25.71  ? 50  LYS F C   1 
ATOM   15375 O O   . LYS F  1 50  ? 121.895 68.263  10.386  1.00   23.00  ? 50  LYS F O   1 
ATOM   15376 C CB  . LYS F  1 50  ? 122.319 65.180  10.088  1.00   22.43  ? 50  LYS F CB  1 
ATOM   15377 C CG  . LYS F  1 50  ? 122.832 64.177  9.104   1.00   22.79  ? 50  LYS F CG  1 
ATOM   15378 C CD  . LYS F  1 50  ? 121.762 63.192  8.851   1.00   29.20  ? 50  LYS F CD  1 
ATOM   15379 C CE  . LYS F  1 50  ? 122.228 62.034  8.037   1.00   37.47  ? 50  LYS F CE  1 
ATOM   15380 N NZ  . LYS F  1 50  ? 121.141 61.005  7.966   1.00   44.36  ? 50  LYS F NZ  1 
ATOM   15381 N N   . HIS F  1 51  ? 122.648 67.551  12.381  1.00   25.12  ? 51  HIS F N   1 
ATOM   15382 C CA  . HIS F  1 51  ? 121.975 68.619  13.112  1.00   27.53  ? 51  HIS F CA  1 
ATOM   15383 C C   . HIS F  1 51  ? 122.617 68.857  14.495  1.00   30.57  ? 51  HIS F C   1 
ATOM   15384 O O   . HIS F  1 51  ? 123.501 68.096  14.936  1.00   31.75  ? 51  HIS F O   1 
ATOM   15385 C CB  . HIS F  1 51  ? 120.467 68.312  13.269  1.00   25.71  ? 51  HIS F CB  1 
ATOM   15386 C CG  . HIS F  1 51  ? 120.178 67.050  14.027  1.00   25.98  ? 51  HIS F CG  1 
ATOM   15387 N ND1 . HIS F  1 51  ? 119.758 65.895  13.414  1.00   26.51  ? 51  HIS F ND1 1 
ATOM   15388 C CD2 . HIS F  1 51  ? 120.289 66.757  15.345  1.00   27.56  ? 51  HIS F CD2 1 
ATOM   15389 C CE1 . HIS F  1 51  ? 119.613 64.942  14.322  1.00   28.90  ? 51  HIS F CE1 1 
ATOM   15390 N NE2 . HIS F  1 51  ? 119.939 65.436  15.499  1.00   28.18  ? 51  HIS F NE2 1 
ATOM   15391 N N   . LEU F  1 52  ? 122.187 69.938  15.149  1.00   27.76  ? 52  LEU F N   1 
ATOM   15392 C CA  . LEU F  1 52  ? 122.562 70.204  16.528  1.00   25.12  ? 52  LEU F CA  1 
ATOM   15393 C C   . LEU F  1 52  ? 121.576 69.494  17.441  1.00   25.60  ? 52  LEU F C   1 
ATOM   15394 O O   . LEU F  1 52  ? 120.367 69.553  17.202  1.00   26.07  ? 52  LEU F O   1 
ATOM   15395 C CB  . LEU F  1 52  ? 122.570 71.706  16.798  1.00   23.85  ? 52  LEU F CB  1 
ATOM   15396 C CG  . LEU F  1 52  ? 123.091 72.261  18.128  1.00   24.90  ? 52  LEU F CG  1 
ATOM   15397 C CD1 . LEU F  1 52  ? 123.625 73.652  17.846  1.00   23.26  ? 52  LEU F CD1 1 
ATOM   15398 C CD2 . LEU F  1 52  ? 122.050 72.336  19.202  1.00   25.98  ? 52  LEU F CD2 1 
ATOM   15399 N N   . TRP F  1 53  ? 122.083 68.804  18.454  1.00   26.30  ? 53  TRP F N   1 
ATOM   15400 C CA  . TRP F  1 53  ? 121.213 68.205  19.441  1.00   26.55  ? 53  TRP F CA  1 
ATOM   15401 C C   . TRP F  1 53  ? 121.727 68.457  20.849  1.00   28.43  ? 53  TRP F C   1 
ATOM   15402 O O   . TRP F  1 53  ? 122.915 68.650  21.068  1.00   29.05  ? 53  TRP F O   1 
ATOM   15403 C CB  . TRP F  1 53  ? 121.025 66.698  19.204  1.00   27.15  ? 53  TRP F CB  1 
ATOM   15404 C CG  . TRP F  1 53  ? 122.237 65.814  19.274  1.00   30.03  ? 53  TRP F CG  1 
ATOM   15405 C CD1 . TRP F  1 53  ? 123.040 65.444  18.227  1.00   27.89  ? 53  TRP F CD1 1 
ATOM   15406 C CD2 . TRP F  1 53  ? 122.758 65.131  20.439  1.00   34.71  ? 53  TRP F CD2 1 
ATOM   15407 N NE1 . TRP F  1 53  ? 124.034 64.602  18.669  1.00   31.11  ? 53  TRP F NE1 1 
ATOM   15408 C CE2 . TRP F  1 53  ? 123.887 64.396  20.020  1.00   32.72  ? 53  TRP F CE2 1 
ATOM   15409 C CE3 . TRP F  1 53  ? 122.396 65.092  21.791  1.00   27.34  ? 53  TRP F CE3 1 
ATOM   15410 C CZ2 . TRP F  1 53  ? 124.645 63.627  20.903  1.00   32.28  ? 53  TRP F CZ2 1 
ATOM   15411 C CZ3 . TRP F  1 53  ? 123.143 64.333  22.655  1.00   29.21  ? 53  TRP F CZ3 1 
ATOM   15412 C CH2 . TRP F  1 53  ? 124.256 63.608  22.216  1.00   33.48  ? 53  TRP F CH2 1 
ATOM   15413 N N   . VAL F  1 54  ? 120.795 68.473  21.792  1.00   30.90  ? 54  VAL F N   1 
ATOM   15414 C CA  . VAL F  1 54  ? 121.076 68.724  23.189  1.00   32.23  ? 54  VAL F CA  1 
ATOM   15415 C C   . VAL F  1 54  ? 120.281 67.727  23.962  1.00   28.22  ? 54  VAL F C   1 
ATOM   15416 O O   . VAL F  1 54  ? 119.191 67.380  23.554  1.00   31.40  ? 54  VAL F O   1 
ATOM   15417 C CB  . VAL F  1 54  ? 120.595 70.127  23.680  1.00   29.52  ? 54  VAL F CB  1 
ATOM   15418 C CG1 . VAL F  1 54  ? 121.297 70.508  24.976  1.00   33.30  ? 54  VAL F CG1 1 
ATOM   15419 C CG2 . VAL F  1 54  ? 120.802 71.154  22.681  1.00   28.04  ? 54  VAL F CG2 1 
ATOM   15420 N N   . THR F  1 55  ? 120.792 67.283  25.093  1.00   40.62  ? 55  THR F N   1 
ATOM   15421 C CA  . THR F  1 55  ? 119.959 66.511  25.975  1.00   45.98  ? 55  THR F CA  1 
ATOM   15422 C C   . THR F  1 55  ? 119.102 67.594  26.603  1.00   51.64  ? 55  THR F C   1 
ATOM   15423 O O   . THR F  1 55  ? 119.629 68.533  27.178  1.00   61.06  ? 55  THR F O   1 
ATOM   15424 C CB  . THR F  1 55  ? 120.786 65.696  27.008  1.00   47.86  ? 55  THR F CB  1 
ATOM   15425 O OG1 . THR F  1 55  ? 121.722 66.566  27.642  1.00   45.72  ? 55  THR F OG1 1 
ATOM   15426 C CG2 . THR F  1 55  ? 121.581 64.572  26.334  1.00   34.54  ? 55  THR F CG2 1 
ATOM   15427 N N   . CYS F  1 56  ? 117.788 67.487  26.518  1.00   50.00  ? 56  CYS F N   1 
ATOM   15428 C CA  . CYS F  1 56  ? 116.934 68.544  27.067  1.00   47.70  ? 56  CYS F CA  1 
ATOM   15429 C C   . CYS F  1 56  ? 116.327 67.999  28.330  1.00   48.85  ? 56  CYS F C   1 
ATOM   15430 O O   . CYS F  1 56  ? 115.799 66.889  28.353  1.00   49.59  ? 56  CYS F O   1 
ATOM   15431 C CB  . CYS F  1 56  ? 115.840 68.988  26.101  1.00   42.90  ? 56  CYS F CB  1 
ATOM   15432 S SG  . CYS F  1 56  ? 116.393 69.846  24.627  1.00   40.81  ? 56  CYS F SG  1 
ATOM   15433 N N   . SER F  1 57  ? 116.444 68.760  29.402  1.00   48.45  ? 57  SER F N   1 
ATOM   15434 C CA  . SER F  1 57  ? 116.012 68.243  30.674  1.00   48.70  ? 57  SER F CA  1 
ATOM   15435 C C   . SER F  1 57  ? 114.771 68.909  31.235  1.00   48.43  ? 57  SER F C   1 
ATOM   15436 O O   . SER F  1 57  ? 114.152 69.798  30.625  1.00   43.41  ? 57  SER F O   1 
ATOM   15437 C CB  . SER F  1 57  ? 117.170 68.334  31.674  1.00   47.93  ? 57  SER F CB  1 
ATOM   15438 O OG  . SER F  1 57  ? 117.508 69.675  31.966  1.00   46.62  ? 57  SER F OG  1 
ATOM   15439 N N   . GLN F  1 58  ? 114.421 68.443  32.422  1.00   54.80  ? 58  GLN F N   1 
ATOM   15440 C CA  . GLN F  1 58  ? 113.345 69.022  33.186  1.00   60.80  ? 58  GLN F CA  1 
ATOM   15441 C C   . GLN F  1 58  ? 113.636 70.480  33.524  1.00   57.79  ? 58  GLN F C   1 
ATOM   15442 O O   . GLN F  1 58  ? 112.727 71.311  33.552  1.00   55.40  ? 58  GLN F O   1 
ATOM   15443 C CB  . GLN F  1 58  ? 113.166 68.208  34.466  1.00   71.42  ? 58  GLN F CB  1 
ATOM   15444 C CG  . GLN F  1 58  ? 111.998 68.616  35.308  1.00   80.28  ? 58  GLN F CG  1 
ATOM   15445 C CD  . GLN F  1 58  ? 110.707 68.359  34.589  1.00   85.74  ? 58  GLN F CD  1 
ATOM   15446 O OE1 . GLN F  1 58  ? 110.407 67.218  34.225  1.00   89.10  ? 58  GLN F OE1 1 
ATOM   15447 N NE2 . GLN F  1 58  ? 109.939 69.416  34.353  1.00   86.35  ? 58  GLN F NE2 1 
ATOM   15448 N N   . HIS F  1 59  ? 114.921 70.787  33.697  1.00   57.32  ? 59  HIS F N   1 
ATOM   15449 C CA  . HIS F  1 59  ? 115.364 72.116  34.103  1.00   46.27  ? 59  HIS F CA  1 
ATOM   15450 C C   . HIS F  1 59  ? 115.815 73.020  32.961  1.00   48.32  ? 59  HIS F C   1 
ATOM   15451 O O   . HIS F  1 59  ? 116.606 73.933  33.169  1.00   49.38  ? 59  HIS F O   1 
ATOM   15452 C CB  . HIS F  1 59  ? 116.481 71.944  35.128  1.00   48.45  ? 59  HIS F CB  1 
ATOM   15453 C CG  . HIS F  1 59  ? 116.074 71.103  36.299  1.00   53.66  ? 59  HIS F CG  1 
ATOM   15454 N ND1 . HIS F  1 59  ? 115.102 71.499  37.192  1.00   57.29  ? 59  HIS F ND1 1 
ATOM   15455 C CD2 . HIS F  1 59  ? 116.429 69.852  36.669  1.00   53.85  ? 59  HIS F CD2 1 
ATOM   15456 C CE1 . HIS F  1 59  ? 114.919 70.553  38.094  1.00   57.96  ? 59  HIS F CE1 1 
ATOM   15457 N NE2 . HIS F  1 59  ? 115.707 69.538  37.793  1.00   58.72  ? 59  HIS F NE2 1 
ATOM   15458 N N   . TYR F  1 60  ? 115.287 72.764  31.768  1.00   46.68  ? 60  TYR F N   1 
ATOM   15459 C CA  . TYR F  1 60  ? 115.442 73.624  30.582  1.00   43.72  ? 60  TYR F CA  1 
ATOM   15460 C C   . TYR F  1 60  ? 114.613 74.899  30.751  1.00   43.93  ? 60  TYR F C   1 
ATOM   15461 O O   . TYR F  1 60  ? 113.390 74.832  30.822  1.00   43.00  ? 60  TYR F O   1 
ATOM   15462 C CB  . TYR F  1 60  ? 115.015 72.850  29.336  1.00   38.74  ? 60  TYR F CB  1 
ATOM   15463 C CG  . TYR F  1 60  ? 115.256 73.492  27.977  1.00   35.82  ? 60  TYR F CG  1 
ATOM   15464 C CD1 . TYR F  1 60  ? 114.627 74.678  27.601  1.00   33.74  ? 60  TYR F CD1 1 
ATOM   15465 C CD2 . TYR F  1 60  ? 116.053 72.853  27.036  1.00   37.01  ? 60  TYR F CD2 1 
ATOM   15466 C CE1 . TYR F  1 60  ? 114.821 75.226  26.352  1.00   29.80  ? 60  TYR F CE1 1 
ATOM   15467 C CE2 . TYR F  1 60  ? 116.257 73.395  25.787  1.00   35.18  ? 60  TYR F CE2 1 
ATOM   15468 C CZ  . TYR F  1 60  ? 115.638 74.575  25.450  1.00   34.85  ? 60  TYR F CZ  1 
ATOM   15469 O OH  . TYR F  1 60  ? 115.854 75.087  24.196  1.00   35.75  ? 60  TYR F OH  1 
ATOM   15470 N N   . SER F  1 61  ? 115.266 76.055  30.829  1.00   46.74  ? 61  SER F N   1 
ATOM   15471 C CA  . SER F  1 61  ? 114.540 77.312  31.042  1.00   50.70  ? 61  SER F CA  1 
ATOM   15472 C C   . SER F  1 61  ? 114.696 78.290  29.860  1.00   44.66  ? 61  SER F C   1 
ATOM   15473 O O   . SER F  1 61  ? 115.805 78.689  29.515  1.00   41.55  ? 61  SER F O   1 
ATOM   15474 C CB  . SER F  1 61  ? 115.009 77.966  32.350  1.00   58.36  ? 61  SER F CB  1 
ATOM   15475 O OG  . SER F  1 61  ? 114.348 79.197  32.600  1.00   61.22  ? 61  SER F OG  1 
ATOM   15476 N N   . SER F  1 62  ? 113.571 78.635  29.231  1.00   43.63  ? 62  SER F N   1 
ATOM   15477 C CA  . SER F  1 62  ? 113.542 79.549  28.089  1.00   40.92  ? 62  SER F CA  1 
ATOM   15478 C C   . SER F  1 62  ? 112.124 80.068  27.760  1.00   40.97  ? 62  SER F C   1 
ATOM   15479 O O   . SER F  1 62  ? 111.160 79.304  27.697  1.00   42.32  ? 62  SER F O   1 
ATOM   15480 C CB  . SER F  1 62  ? 114.142 78.856  26.865  1.00   37.60  ? 62  SER F CB  1 
ATOM   15481 O OG  . SER F  1 62  ? 114.115 79.700  25.732  1.00   38.10  ? 62  SER F OG  1 
ATOM   15482 N N   . SER F  1 63  ? 112.000 81.370  27.549  1.00   38.27  ? 63  SER F N   1 
ATOM   15483 C CA  . SER F  1 63  ? 110.729 81.936  27.165  1.00   37.37  ? 63  SER F CA  1 
ATOM   15484 C C   . SER F  1 63  ? 110.545 81.924  25.652  1.00   38.15  ? 63  SER F C   1 
ATOM   15485 O O   . SER F  1 63  ? 109.496 82.330  25.145  1.00   41.02  ? 63  SER F O   1 
ATOM   15486 C CB  . SER F  1 63  ? 110.582 83.359  27.722  1.00   40.52  ? 63  SER F CB  1 
ATOM   15487 O OG  . SER F  1 63  ? 111.521 84.251  27.154  1.00   39.96  ? 63  SER F OG  1 
ATOM   15488 N N   . THR F  1 64  ? 111.534 81.434  24.920  1.00   34.47  ? 64  THR F N   1 
ATOM   15489 C CA  . THR F  1 64  ? 111.413 81.421  23.465  1.00   32.71  ? 64  THR F CA  1 
ATOM   15490 C C   . THR F  1 64  ? 111.429 80.002  22.885  1.00   34.71  ? 64  THR F C   1 
ATOM   15491 O O   . THR F  1 64  ? 111.542 79.811  21.658  1.00   31.10  ? 64  THR F O   1 
ATOM   15492 C CB  . THR F  1 64  ? 112.529 82.232  22.821  1.00   30.54  ? 64  THR F CB  1 
ATOM   15493 O OG1 . THR F  1 64  ? 113.742 81.968  23.516  1.00   32.52  ? 64  THR F OG1 1 
ATOM   15494 C CG2 . THR F  1 64  ? 112.232 83.701  22.940  1.00   30.77  ? 64  THR F CG2 1 
ATOM   15495 N N   . TYR F  1 65  ? 111.339 79.009  23.772  1.00   35.55  ? 65  TYR F N   1 
ATOM   15496 C CA  . TYR F  1 65  ? 111.333 77.607  23.363  1.00   33.10  ? 65  TYR F CA  1 
ATOM   15497 C C   . TYR F  1 65  ? 109.985 77.176  22.848  1.00   33.63  ? 65  TYR F C   1 
ATOM   15498 O O   . TYR F  1 65  ? 108.971 77.537  23.427  1.00   33.76  ? 65  TYR F O   1 
ATOM   15499 C CB  . TYR F  1 65  ? 111.741 76.686  24.509  1.00   34.02  ? 65  TYR F CB  1 
ATOM   15500 C CG  . TYR F  1 65  ? 111.449 75.223  24.208  1.00   33.56  ? 65  TYR F CG  1 
ATOM   15501 C CD1 . TYR F  1 65  ? 112.311 74.465  23.425  1.00   32.17  ? 65  TYR F CD1 1 
ATOM   15502 C CD2 . TYR F  1 65  ? 110.324 74.599  24.728  1.00   33.76  ? 65  TYR F CD2 1 
ATOM   15503 C CE1 . TYR F  1 65  ? 112.046 73.141  23.159  1.00   31.21  ? 65  TYR F CE1 1 
ATOM   15504 C CE2 . TYR F  1 65  ? 110.058 73.287  24.462  1.00   33.89  ? 65  TYR F CE2 1 
ATOM   15505 C CZ  . TYR F  1 65  ? 110.920 72.561  23.678  1.00   32.16  ? 65  TYR F CZ  1 
ATOM   15506 O OH  . TYR F  1 65  ? 110.646 71.239  23.437  1.00   32.66  ? 65  TYR F OH  1 
ATOM   15507 N N   . GLN F  1 66  ? 109.999 76.377  21.777  1.00   34.56  ? 66  GLN F N   1 
ATOM   15508 C CA  . GLN F  1 66  ? 108.810 75.758  21.190  1.00   34.49  ? 66  GLN F CA  1 
ATOM   15509 C C   . GLN F  1 66  ? 109.112 74.371  20.643  1.00   30.64  ? 66  GLN F C   1 
ATOM   15510 O O   . GLN F  1 66  ? 110.198 74.126  20.159  1.00   28.08  ? 66  GLN F O   1 
ATOM   15511 C CB  . GLN F  1 66  ? 108.278 76.650  20.080  1.00   39.17  ? 66  GLN F CB  1 
ATOM   15512 C CG  . GLN F  1 66  ? 107.666 77.892  20.630  1.00   50.10  ? 66  GLN F CG  1 
ATOM   15513 C CD  . GLN F  1 66  ? 107.342 78.881  19.579  1.00   57.26  ? 66  GLN F CD  1 
ATOM   15514 O OE1 . GLN F  1 66  ? 106.805 78.528  18.533  1.00   60.56  ? 66  GLN F OE1 1 
ATOM   15515 N NE2 . GLN F  1 66  ? 107.647 80.148  19.847  1.00   60.32  ? 66  GLN F NE2 1 
ATOM   15516 N N   . ALA F  1 67  ? 108.147 73.465  20.712  1.00   31.25  ? 67  ALA F N   1 
ATOM   15517 C CA  . ALA F  1 67  ? 108.263 72.187  20.025  1.00   29.83  ? 67  ALA F CA  1 
ATOM   15518 C C   . ALA F  1 67  ? 107.322 72.166  18.812  1.00   31.72  ? 67  ALA F C   1 
ATOM   15519 O O   . ALA F  1 67  ? 106.112 72.093  18.981  1.00   35.13  ? 67  ALA F O   1 
ATOM   15520 C CB  . ALA F  1 67  ? 107.945 71.029  20.978  1.00   28.02  ? 67  ALA F CB  1 
ATOM   15521 N N   . PRO F  1 68  ? 107.871 72.236  17.582  1.00   29.61  ? 68  PRO F N   1 
ATOM   15522 C CA  . PRO F  1 68  ? 106.966 72.249  16.421  1.00   27.33  ? 68  PRO F CA  1 
ATOM   15523 C C   . PRO F  1 68  ? 105.995 71.072  16.384  1.00   26.49  ? 68  PRO F C   1 
ATOM   15524 O O   . PRO F  1 68  ? 106.304 69.991  16.862  1.00   30.87  ? 68  PRO F O   1 
ATOM   15525 C CB  . PRO F  1 68  ? 107.935 72.222  15.237  1.00   23.97  ? 68  PRO F CB  1 
ATOM   15526 C CG  . PRO F  1 68  ? 109.174 72.920  15.770  1.00   21.08  ? 68  PRO F CG  1 
ATOM   15527 C CD  . PRO F  1 68  ? 109.275 72.505  17.200  1.00   24.61  ? 68  PRO F CD  1 
ATOM   15528 N N   . PHE F  1 69  ? 104.801 71.297  15.864  1.00   26.90  ? 69  PHE F N   1 
ATOM   15529 C CA  . PHE F  1 69  ? 103.822 70.222  15.792  1.00   25.98  ? 69  PHE F CA  1 
ATOM   15530 C C   . PHE F  1 69  ? 104.061 69.348  14.594  1.00   26.82  ? 69  PHE F C   1 
ATOM   15531 O O   . PHE F  1 69  ? 104.617 69.793  13.606  1.00   31.91  ? 69  PHE F O   1 
ATOM   15532 C CB  . PHE F  1 69  ? 102.365 70.757  15.769  1.00   34.11  ? 69  PHE F CB  1 
ATOM   15533 C CG  . PHE F  1 69  ? 102.035 71.719  14.627  1.00   33.55  ? 69  PHE F CG  1 
ATOM   15534 C CD1 . PHE F  1 69  ? 101.734 71.248  13.352  1.00   30.16  ? 69  PHE F CD1 1 
ATOM   15535 C CD2 . PHE F  1 69  ? 101.908 73.090  14.866  1.00   37.01  ? 69  PHE F CD2 1 
ATOM   15536 C CE1 . PHE F  1 69  ? 101.381 72.120  12.325  1.00   29.39  ? 69  PHE F CE1 1 
ATOM   15537 C CE2 . PHE F  1 69  ? 101.563 73.977  13.833  1.00   36.58  ? 69  PHE F CE2 1 
ATOM   15538 C CZ  . PHE F  1 69  ? 101.300 73.485  12.562  1.00   32.22  ? 69  PHE F CZ  1 
ATOM   15539 N N   . CYS F  1 70  ? 103.594 68.112  14.662  1.00   28.00  ? 70  CYS F N   1 
ATOM   15540 C CA  . CYS F  1 70  ? 103.782 67.180  13.570  1.00   27.96  ? 70  CYS F CA  1 
ATOM   15541 C C   . CYS F  1 70  ? 103.115 67.687  12.289  1.00   28.31  ? 70  CYS F C   1 
ATOM   15542 O O   . CYS F  1 70  ? 101.997 68.185  12.324  1.00   28.48  ? 70  CYS F O   1 
ATOM   15543 C CB  . CYS F  1 70  ? 103.240 65.804  13.949  1.00   29.41  ? 70  CYS F CB  1 
ATOM   15544 S SG  . CYS F  1 70  ? 103.969 64.471  12.970  1.00   37.82  ? 70  CYS F SG  1 
ATOM   15545 N N   . HIS F  1 71  ? 103.824 67.524  11.170  1.00   27.44  ? 71  HIS F N   1 
ATOM   15546 C CA  . HIS F  1 71  ? 103.424 67.999  9.840   1.00   27.33  ? 71  HIS F CA  1 
ATOM   15547 C C   . HIS F  1 71  ? 103.514 69.510  9.682   1.00   27.79  ? 71  HIS F C   1 
ATOM   15548 O O   . HIS F  1 71  ? 103.022 70.043  8.702   1.00   30.06  ? 71  HIS F O   1 
ATOM   15549 C CB  . HIS F  1 71  ? 102.022 67.561  9.489   1.00   27.54  ? 71  HIS F CB  1 
ATOM   15550 C CG  . HIS F  1 71  ? 101.781 66.114  9.728   1.00   29.44  ? 71  HIS F CG  1 
ATOM   15551 N ND1 . HIS F  1 71  ? 102.441 65.128  9.031   1.00   33.38  ? 71  HIS F ND1 1 
ATOM   15552 C CD2 . HIS F  1 71  ? 100.968 65.481  10.601  1.00   30.40  ? 71  HIS F CD2 1 
ATOM   15553 C CE1 . HIS F  1 71  ? 102.027 63.945  9.449   1.00   32.63  ? 71  HIS F CE1 1 
ATOM   15554 N NE2 . HIS F  1 71  ? 101.133 64.133  10.402  1.00   33.34  ? 71  HIS F NE2 1 
ATOM   15555 N N   . SER F  1 72  ? 104.165 70.189  10.620  1.00   26.53  ? 72  SER F N   1 
ATOM   15556 C CA  . SER F  1 72  ? 104.416 71.610  10.487  1.00   25.17  ? 72  SER F CA  1 
ATOM   15557 C C   . SER F  1 72  ? 105.494 71.885  9.443   1.00   24.67  ? 72  SER F C   1 
ATOM   15558 O O   . SER F  1 72  ? 106.203 70.984  9.013   1.00   24.21  ? 72  SER F O   1 
ATOM   15559 C CB  . SER F  1 72  ? 104.851 72.184  11.818  1.00   24.60  ? 72  SER F CB  1 
ATOM   15560 O OG  . SER F  1 72  ? 106.053 71.561  12.207  1.00   25.06  ? 72  SER F OG  1 
ATOM   15561 N N   . THR F  1 73  ? 105.621 73.151  9.058   1.00   25.51  ? 73  THR F N   1 
ATOM   15562 C CA  . THR F  1 73  ? 106.693 73.606  8.162   1.00   26.08  ? 73  THR F CA  1 
ATOM   15563 C C   . THR F  1 73  ? 108.087 73.404  8.757   1.00   25.87  ? 73  THR F C   1 
ATOM   15564 O O   . THR F  1 73  ? 109.050 73.183  8.035   1.00   25.74  ? 73  THR F O   1 
ATOM   15565 C CB  . THR F  1 73  ? 106.518 75.073  7.826   1.00   25.10  ? 73  THR F CB  1 
ATOM   15566 O OG1 . THR F  1 73  ? 106.395 75.819  9.049   1.00   24.33  ? 73  THR F OG1 1 
ATOM   15567 C CG2 . THR F  1 73  ? 105.253 75.257  6.975   1.00   23.54  ? 73  THR F CG2 1 
ATOM   15568 N N   . GLN F  1 74  ? 108.202 73.510  10.076  1.00   25.01  ? 74  GLN F N   1 
ATOM   15569 C CA  . GLN F  1 74  ? 109.460 73.204  10.729  1.00   24.30  ? 74  GLN F CA  1 
ATOM   15570 C C   . GLN F  1 74  ? 109.869 71.731  10.578  1.00   24.50  ? 74  GLN F C   1 
ATOM   15571 O O   . GLN F  1 74  ? 111.034 71.399  10.322  1.00   24.39  ? 74  GLN F O   1 
ATOM   15572 C CB  . GLN F  1 74  ? 109.381 73.552  12.215  1.00   24.18  ? 74  GLN F CB  1 
ATOM   15573 C CG  . GLN F  1 74  ? 109.249 75.030  12.484  1.00   23.51  ? 74  GLN F CG  1 
ATOM   15574 C CD  . GLN F  1 74  ? 107.867 75.390  12.809  1.00   25.74  ? 74  GLN F CD  1 
ATOM   15575 O OE1 . GLN F  1 74  ? 106.946 74.743  12.353  1.00   29.56  ? 74  GLN F OE1 1 
ATOM   15576 N NE2 . GLN F  1 74  ? 107.693 76.397  13.635  1.00   30.02  ? 74  GLN F NE2 1 
ATOM   15577 N N   . CYS F  1 75  ? 108.900 70.846  10.734  1.00   25.13  ? 75  CYS F N   1 
ATOM   15578 C CA  . CYS F  1 75  ? 109.163 69.434  10.569  1.00   24.62  ? 75  CYS F CA  1 
ATOM   15579 C C   . CYS F  1 75  ? 109.492 69.127  9.122   1.00   23.77  ? 75  CYS F C   1 
ATOM   15580 O O   . CYS F  1 75  ? 110.334 68.287  8.841   1.00   27.71  ? 75  CYS F O   1 
ATOM   15581 C CB  . CYS F  1 75  ? 107.975 68.612  11.073  1.00   27.84  ? 75  CYS F CB  1 
ATOM   15582 S SG  . CYS F  1 75  ? 107.773 68.846  12.863  1.00   33.00  ? 75  CYS F SG  1 
ATOM   15583 N N   . SER F  1 76  ? 108.846 69.815  8.198   1.00   24.01  ? 76  SER F N   1 
ATOM   15584 C CA  . SER F  1 76  ? 109.199 69.672  6.782   1.00   25.88  ? 76  SER F CA  1 
ATOM   15585 C C   . SER F  1 76  ? 110.637 70.088  6.480   1.00   26.78  ? 76  SER F C   1 
ATOM   15586 O O   . SER F  1 76  ? 111.365 69.367  5.813   1.00   29.29  ? 76  SER F O   1 
ATOM   15587 C CB  . SER F  1 76  ? 108.266 70.486  5.891   1.00   25.99  ? 76  SER F CB  1 
ATOM   15588 O OG  . SER F  1 76  ? 108.648 70.312  4.540   1.00   28.92  ? 76  SER F OG  1 
ATOM   15589 N N   . ARG F  1 77  ? 111.044 71.249  6.972   1.00   26.11  ? 77  ARG F N   1 
ATOM   15590 C CA  . ARG F  1 77  ? 112.389 71.724  6.743   1.00   24.65  ? 77  ARG F CA  1 
ATOM   15591 C C   . ARG F  1 77  ? 113.426 70.770  7.317   1.00   26.75  ? 77  ARG F C   1 
ATOM   15592 O O   . ARG F  1 77  ? 114.462 70.509  6.693   1.00   27.85  ? 77  ARG F O   1 
ATOM   15593 C CB  . ARG F  1 77  ? 112.561 73.108  7.342   1.00   26.02  ? 77  ARG F CB  1 
ATOM   15594 C CG  . ARG F  1 77  ? 113.862 73.724  6.926   1.00   28.49  ? 77  ARG F CG  1 
ATOM   15595 C CD  . ARG F  1 77  ? 114.071 75.137  7.447   1.00   29.25  ? 77  ARG F CD  1 
ATOM   15596 N NE  . ARG F  1 77  ? 115.378 75.631  7.004   1.00   29.45  ? 77  ARG F NE  1 
ATOM   15597 C CZ  . ARG F  1 77  ? 116.008 76.675  7.533   1.00   31.47  ? 77  ARG F CZ  1 
ATOM   15598 N NH1 . ARG F  1 77  ? 117.195 77.030  7.063   1.00   34.35  ? 77  ARG F NH1 1 
ATOM   15599 N NH2 . ARG F  1 77  ? 115.448 77.362  8.519   1.00   31.66  ? 77  ARG F NH2 1 
ATOM   15600 N N   . ALA F  1 78  ? 113.125 70.207  8.485   1.00   25.93  ? 78  ALA F N   1 
ATOM   15601 C CA  . ALA F  1 78  ? 114.051 69.296  9.144   1.00   25.27  ? 78  ALA F CA  1 
ATOM   15602 C C   . ALA F  1 78  ? 114.066 67.955  8.479   1.00   28.74  ? 78  ALA F C   1 
ATOM   15603 O O   . ALA F  1 78  ? 114.892 67.129  8.808   1.00   30.12  ? 78  ALA F O   1 
ATOM   15604 C CB  . ALA F  1 78  ? 113.702 69.123  10.608  1.00   23.80  ? 78  ALA F CB  1 
ATOM   15605 N N   . ASN F  1 79  ? 113.156 67.758  7.538   1.00   33.32  ? 79  ASN F N   1 
ATOM   15606 C CA  . ASN F  1 79  ? 113.022 66.508  6.806   1.00   39.31  ? 79  ASN F CA  1 
ATOM   15607 C C   . ASN F  1 79  ? 112.579 65.346  7.710   1.00   39.41  ? 79  ASN F C   1 
ATOM   15608 O O   . ASN F  1 79  ? 113.077 64.235  7.602   1.00   37.43  ? 79  ASN F O   1 
ATOM   15609 C CB  . ASN F  1 79  ? 114.343 66.176  6.100   1.00   45.25  ? 79  ASN F CB  1 
ATOM   15610 C CG  . ASN F  1 79  ? 114.191 65.102  5.058   1.00   48.31  ? 79  ASN F CG  1 
ATOM   15611 O OD1 . ASN F  1 79  ? 113.116 64.932  4.479   1.00   49.90  ? 79  ASN F OD1 1 
ATOM   15612 N ND2 . ASN F  1 79  ? 115.260 64.344  4.830   1.00   48.88  ? 79  ASN F ND2 1 
ATOM   15613 N N   . THR F  1 80  ? 111.640 65.604  8.610   1.00   41.49  ? 80  THR F N   1 
ATOM   15614 C CA  . THR F  1 80  ? 111.068 64.520  9.389   1.00   45.81  ? 80  THR F CA  1 
ATOM   15615 C C   . THR F  1 80  ? 109.556 64.536  9.336   1.00   51.29  ? 80  THR F C   1 
ATOM   15616 O O   . THR F  1 80  ? 108.938 65.557  9.615   1.00   53.47  ? 80  THR F O   1 
ATOM   15617 C CB  . THR F  1 80  ? 111.484 64.565  10.853  1.00   43.61  ? 80  THR F CB  1 
ATOM   15618 O OG1 . THR F  1 80  ? 110.744 63.564  11.562  1.00   51.09  ? 80  THR F OG1 1 
ATOM   15619 C CG2 . THR F  1 80  ? 111.252 65.934  11.466  1.00   34.63  ? 80  THR F CG2 1 
ATOM   15620 N N   . HIS F  1 81  ? 108.945 63.420  8.965   1.00   52.73  ? 81  HIS F N   1 
ATOM   15621 C CA  . HIS F  1 81  ? 107.488 63.387  8.948   1.00   54.56  ? 81  HIS F CA  1 
ATOM   15622 C C   . HIS F  1 81  ? 106.941 62.282  9.834   1.00   57.40  ? 81  HIS F C   1 
ATOM   15623 O O   . HIS F  1 81  ? 105.749 61.936  9.757   1.00   58.86  ? 81  HIS F O   1 
ATOM   15624 C CB  . HIS F  1 81  ? 106.987 63.245  7.520   1.00   55.23  ? 81  HIS F CB  1 
ATOM   15625 C CG  . HIS F  1 81  ? 107.254 64.450  6.676   1.00   57.27  ? 81  HIS F CG  1 
ATOM   15626 N ND1 . HIS F  1 81  ? 106.349 65.481  6.538   1.00   56.58  ? 81  HIS F ND1 1 
ATOM   15627 C CD2 . HIS F  1 81  ? 108.345 64.806  5.954   1.00   59.39  ? 81  HIS F CD2 1 
ATOM   15628 C CE1 . HIS F  1 81  ? 106.859 66.406  5.744   1.00   58.09  ? 81  HIS F CE1 1 
ATOM   15629 N NE2 . HIS F  1 81  ? 108.070 66.024  5.381   1.00   59.78  ? 81  HIS F NE2 1 
ATOM   15630 N N   . GLN F  1 82  ? 107.819 61.800  10.718  1.00   55.31  ? 82  GLN F N   1 
ATOM   15631 C CA  . GLN F  1 82  ? 107.498 60.809  11.731  1.00   52.82  ? 82  GLN F CA  1 
ATOM   15632 C C   . GLN F  1 82  ? 107.091 61.527  13.020  1.00   46.97  ? 82  GLN F C   1 
ATOM   15633 O O   . GLN F  1 82  ? 107.819 62.386  13.509  1.00   45.40  ? 82  GLN F O   1 
ATOM   15634 C CB  . GLN F  1 82  ? 108.701 59.914  11.989  1.00   57.95  ? 82  GLN F CB  1 
ATOM   15635 C CG  . GLN F  1 82  ? 108.681 59.272  13.363  1.00   67.61  ? 82  GLN F CG  1 
ATOM   15636 C CD  . GLN F  1 82  ? 109.874 58.370  13.627  1.00   76.62  ? 82  GLN F CD  1 
ATOM   15637 O OE1 . GLN F  1 82  ? 110.722 58.160  12.758  1.00   80.48  ? 82  GLN F OE1 1 
ATOM   15638 N NE2 . GLN F  1 82  ? 109.939 57.823  14.834  1.00   79.59  ? 82  GLN F NE2 1 
ATOM   15639 N N   . CYS F  1 83  ? 105.895 61.236  13.524  1.00   44.98  ? 83  CYS F N   1 
ATOM   15640 C CA  . CYS F  1 83  ? 105.373 61.914  14.717  1.00   43.86  ? 83  CYS F CA  1 
ATOM   15641 C C   . CYS F  1 83  ? 105.950 61.332  16.012  1.00   43.62  ? 83  CYS F C   1 
ATOM   15642 O O   . CYS F  1 83  ? 106.242 60.152  16.095  1.00   44.95  ? 83  CYS F O   1 
ATOM   15643 C CB  . CYS F  1 83  ? 103.841 61.847  14.754  1.00   46.35  ? 83  CYS F CB  1 
ATOM   15644 S SG  . CYS F  1 83  ? 102.988 62.773  13.412  1.00   44.11  ? 83  CYS F SG  1 
ATOM   15645 N N   . PHE F  1 84  ? 106.041 62.171  17.033  1.00   39.46  ? 84  PHE F N   1 
ATOM   15646 C CA  . PHE F  1 84  ? 106.683 61.839  18.288  1.00   34.71  ? 84  PHE F CA  1 
ATOM   15647 C C   . PHE F  1 84  ? 105.664 61.628  19.377  1.00   40.19  ? 84  PHE F C   1 
ATOM   15648 O O   . PHE F  1 84  ? 104.716 62.412  19.529  1.00   39.91  ? 84  PHE F O   1 
ATOM   15649 C CB  . PHE F  1 84  ? 107.623 62.968  18.684  1.00   34.49  ? 84  PHE F CB  1 
ATOM   15650 C CG  . PHE F  1 84  ? 108.438 62.699  19.909  1.00   34.66  ? 84  PHE F CG  1 
ATOM   15651 C CD1 . PHE F  1 84  ? 109.678 62.091  19.809  1.00   34.37  ? 84  PHE F CD1 1 
ATOM   15652 C CD2 . PHE F  1 84  ? 107.975 63.076  21.165  1.00   36.20  ? 84  PHE F CD2 1 
ATOM   15653 C CE1 . PHE F  1 84  ? 110.435 61.852  20.944  1.00   36.51  ? 84  PHE F CE1 1 
ATOM   15654 C CE2 . PHE F  1 84  ? 108.721 62.843  22.296  1.00   34.29  ? 84  PHE F CE2 1 
ATOM   15655 C CZ  . PHE F  1 84  ? 109.951 62.234  22.191  1.00   40.91  ? 84  PHE F CZ  1 
ATOM   15656 N N   . THR F  1 85  ? 105.879 60.577  20.156  1.00   41.94  ? 85  THR F N   1 
ATOM   15657 C CA  . THR F  1 85  ? 105.058 60.306  21.311  1.00   47.91  ? 85  THR F CA  1 
ATOM   15658 C C   . THR F  1 85  ? 105.970 60.154  22.513  1.00   51.08  ? 85  THR F C   1 
ATOM   15659 O O   . THR F  1 85  ? 106.927 59.384  22.481  1.00   53.16  ? 85  THR F O   1 
ATOM   15660 C CB  . THR F  1 85  ? 104.193 59.067  21.104  1.00   50.82  ? 85  THR F CB  1 
ATOM   15661 O OG1 . THR F  1 85  ? 103.302 59.313  20.006  1.00   51.37  ? 85  THR F OG1 1 
ATOM   15662 C CG2 . THR F  1 85  ? 103.380 58.783  22.342  1.00   54.07  ? 85  THR F CG2 1 
ATOM   15663 N N   . CYS F  1 86  ? 105.702 60.933  23.554  1.00   51.96  ? 86  CYS F N   1 
ATOM   15664 C CA  . CYS F  1 86  ? 106.525 60.872  24.742  1.00   59.16  ? 86  CYS F CA  1 
ATOM   15665 C C   . CYS F  1 86  ? 106.051 59.668  25.542  1.00   67.65  ? 86  CYS F C   1 
ATOM   15666 O O   . CYS F  1 86  ? 104.928 59.630  26.056  1.00   71.45  ? 86  CYS F O   1 
ATOM   15667 C CB  . CYS F  1 86  ? 106.425 62.157  25.563  1.00   59.43  ? 86  CYS F CB  1 
ATOM   15668 S SG  . CYS F  1 86  ? 107.701 62.298  26.849  1.00   63.07  ? 86  CYS F SG  1 
ATOM   15669 N N   . THR F  1 87  ? 106.960 58.714  25.688  1.00   70.76  ? 87  THR F N   1 
ATOM   15670 C CA  . THR F  1 87  ? 106.686 57.441  26.326  1.00   76.25  ? 87  THR F CA  1 
ATOM   15671 C C   . THR F  1 87  ? 107.368 57.450  27.658  1.00   80.11  ? 87  THR F C   1 
ATOM   15672 O O   . THR F  1 87  ? 107.480 56.434  28.336  1.00   84.92  ? 87  THR F O   1 
ATOM   15673 C CB  . THR F  1 87  ? 107.253 56.281  25.493  1.00   76.45  ? 87  THR F CB  1 
ATOM   15674 O OG1 . THR F  1 87  ? 108.660 56.505  25.301  1.00   76.29  ? 87  THR F OG1 1 
ATOM   15675 C CG2 . THR F  1 87  ? 106.581 56.203  24.126  1.00   73.03  ? 87  THR F CG2 1 
ATOM   15676 N N   . ASP F  1 88  ? 107.800 58.639  28.035  1.00   79.56  ? 88  ASP F N   1 
ATOM   15677 C CA  . ASP F  1 88  ? 108.494 58.839  29.279  1.00   83.45  ? 88  ASP F CA  1 
ATOM   15678 C C   . ASP F  1 88  ? 107.630 59.453  30.398  1.00   86.36  ? 88  ASP F C   1 
ATOM   15679 O O   . ASP F  1 88  ? 106.835 58.756  31.047  1.00   91.56  ? 88  ASP F O   1 
ATOM   15680 C CB  . ASP F  1 88  ? 109.733 59.690  28.952  1.00   83.47  ? 88  ASP F CB  1 
ATOM   15681 C CG  . ASP F  1 88  ? 110.459 60.196  30.171  1.00   89.44  ? 88  ASP F CG  1 
ATOM   15682 O OD1 . ASP F  1 88  ? 110.237 59.667  31.282  1.00   94.82  ? 88  ASP F OD1 1 
ATOM   15683 O OD2 . ASP F  1 88  ? 111.248 61.148  30.007  1.00   88.79  ? 88  ASP F OD2 1 
ATOM   15684 N N   . SER F  1 89  ? 107.749 60.764  30.573  1.00   83.32  ? 89  SER F N   1 
ATOM   15685 C CA  . SER F  1 89  ? 107.122 61.504  31.661  1.00   85.01  ? 89  SER F CA  1 
ATOM   15686 C C   . SER F  1 89  ? 105.598 61.455  31.586  1.00   83.65  ? 89  SER F C   1 
ATOM   15687 O O   . SER F  1 89  ? 105.017 61.094  30.552  1.00   83.91  ? 89  SER F O   1 
ATOM   15688 C CB  . SER F  1 89  ? 107.656 62.953  31.643  1.00   84.54  ? 89  SER F CB  1 
ATOM   15689 O OG  . SER F  1 89  ? 106.811 63.884  32.292  1.00   87.46  ? 89  SER F OG  1 
ATOM   15690 N N   . THR F  1 90  ? 104.958 61.799  32.696  1.00   82.20  ? 90  THR F N   1 
ATOM   15691 C CA  . THR F  1 90  ? 103.516 61.892  32.706  1.00   81.26  ? 90  THR F CA  1 
ATOM   15692 C C   . THR F  1 90  ? 103.090 63.337  32.545  1.00   76.37  ? 90  THR F C   1 
ATOM   15693 O O   . THR F  1 90  ? 101.914 63.635  32.350  1.00   76.72  ? 90  THR F O   1 
ATOM   15694 C CB  . THR F  1 90  ? 102.949 61.360  34.034  1.00   86.39  ? 90  THR F CB  1 
ATOM   15695 O OG1 . THR F  1 90  ? 103.539 62.089  35.119  1.00   87.67  ? 90  THR F OG1 1 
ATOM   15696 C CG2 . THR F  1 90  ? 103.252 59.880  34.190  1.00   88.85  ? 90  THR F CG2 1 
ATOM   15697 N N   . THR F  1 91  ? 104.081 64.217  32.535  1.00   72.34  ? 91  THR F N   1 
ATOM   15698 C CA  . THR F  1 91  ? 103.894 65.618  32.213  1.00   70.49  ? 91  THR F CA  1 
ATOM   15699 C C   . THR F  1 91  ? 104.836 66.069  31.102  1.00   67.99  ? 91  THR F C   1 
ATOM   15700 O O   . THR F  1 91  ? 105.899 65.483  30.899  1.00   66.52  ? 91  THR F O   1 
ATOM   15701 C CB  . THR F  1 91  ? 104.161 66.496  33.439  1.00   73.08  ? 91  THR F CB  1 
ATOM   15702 O OG1 . THR F  1 91  ? 105.477 66.213  33.943  1.00   75.04  ? 91  THR F OG1 1 
ATOM   15703 C CG2 . THR F  1 91  ? 103.099 66.268  34.517  1.00   76.01  ? 91  THR F CG2 1 
ATOM   15704 N N   . THR F  1 92  ? 104.485 67.157  30.432  1.00   65.99  ? 92  THR F N   1 
ATOM   15705 C CA  . THR F  1 92  ? 105.305 67.636  29.337  1.00   62.45  ? 92  THR F CA  1 
ATOM   15706 C C   . THR F  1 92  ? 106.468 68.480  29.880  1.00   59.88  ? 92  THR F C   1 
ATOM   15707 O O   . THR F  1 92  ? 106.437 68.965  31.011  1.00   61.29  ? 92  THR F O   1 
ATOM   15708 C CB  . THR F  1 92  ? 104.507 68.468  28.309  1.00   61.77  ? 92  THR F CB  1 
ATOM   15709 O OG1 . THR F  1 92  ? 104.138 69.715  28.893  1.00   64.18  ? 92  THR F OG1 1 
ATOM   15710 C CG2 . THR F  1 92  ? 103.259 67.738  27.854  1.00   62.35  ? 92  THR F CG2 1 
ATOM   15711 N N   . ARG F  1 93  ? 107.525 68.566  29.084  1.00   54.23  ? 93  ARG F N   1 
ATOM   15712 C CA  . ARG F  1 93  ? 108.722 69.334  29.380  1.00   50.28  ? 93  ARG F CA  1 
ATOM   15713 C C   . ARG F  1 93  ? 109.406 69.440  28.021  1.00   45.13  ? 93  ARG F C   1 
ATOM   15714 O O   . ARG F  1 93  ? 109.021 68.727  27.094  1.00   44.82  ? 93  ARG F O   1 
ATOM   15715 C CB  . ARG F  1 93  ? 109.612 68.641  30.421  1.00   51.06  ? 93  ARG F CB  1 
ATOM   15716 C CG  . ARG F  1 93  ? 110.036 67.274  29.968  1.00   51.80  ? 93  ARG F CG  1 
ATOM   15717 C CD  . ARG F  1 93  ? 111.027 66.590  30.854  1.00   57.64  ? 93  ARG F CD  1 
ATOM   15718 N NE  . ARG F  1 93  ? 111.311 65.278  30.284  1.00   62.25  ? 93  ARG F NE  1 
ATOM   15719 C CZ  . ARG F  1 93  ? 112.255 65.045  29.377  1.00   63.67  ? 93  ARG F CZ  1 
ATOM   15720 N NH1 . ARG F  1 93  ? 113.006 66.034  28.923  1.00   61.90  ? 93  ARG F NH1 1 
ATOM   15721 N NH2 . ARG F  1 93  ? 112.434 63.824  28.903  1.00   65.21  ? 93  ARG F NH2 1 
ATOM   15722 N N   . PRO F  1 94  ? 110.392 70.334  27.875  1.00   41.82  ? 94  PRO F N   1 
ATOM   15723 C CA  . PRO F  1 94  ? 111.129 70.335  26.615  1.00   39.18  ? 94  PRO F CA  1 
ATOM   15724 C C   . PRO F  1 94  ? 111.660 68.943  26.337  1.00   41.44  ? 94  PRO F C   1 
ATOM   15725 O O   . PRO F  1 94  ? 112.243 68.331  27.235  1.00   42.36  ? 94  PRO F O   1 
ATOM   15726 C CB  . PRO F  1 94  ? 112.274 71.317  26.873  1.00   37.18  ? 94  PRO F CB  1 
ATOM   15727 C CG  . PRO F  1 94  ? 111.758 72.217  27.877  1.00   39.46  ? 94  PRO F CG  1 
ATOM   15728 C CD  . PRO F  1 94  ? 110.910 71.360  28.791  1.00   43.56  ? 94  PRO F CD  1 
ATOM   15729 N N   . GLY F  1 95  ? 111.414 68.426  25.140  1.00   40.41  ? 95  GLY F N   1 
ATOM   15730 C CA  . GLY F  1 95  ? 111.887 67.103  24.795  1.00   42.36  ? 95  GLY F CA  1 
ATOM   15731 C C   . GLY F  1 95  ? 110.838 66.045  25.035  1.00   45.60  ? 95  GLY F C   1 
ATOM   15732 O O   . GLY F  1 95  ? 111.015 64.888  24.642  1.00   47.55  ? 95  GLY F O   1 
ATOM   15733 N N   . CYS F  1 96  ? 109.753 66.432  25.700  1.00   46.57  ? 96  CYS F N   1 
ATOM   15734 C CA  . CYS F  1 96  ? 108.681 65.493  26.002  1.00   49.17  ? 96  CYS F CA  1 
ATOM   15735 C C   . CYS F  1 96  ? 107.287 66.071  25.761  1.00   47.64  ? 96  CYS F C   1 
ATOM   15736 O O   . CYS F  1 96  ? 106.681 66.665  26.655  1.00   47.67  ? 96  CYS F O   1 
ATOM   15737 C CB  . CYS F  1 96  ? 108.801 65.020  27.449  1.00   54.58  ? 96  CYS F CB  1 
ATOM   15738 S SG  . CYS F  1 96  ? 107.450 63.943  27.999  1.00   86.02  ? 96  CYS F SG  1 
ATOM   15739 N N   . HIS F  1 97  ? 106.771 65.857  24.556  1.00   46.90  ? 97  HIS F N   1 
ATOM   15740 C CA  . HIS F  1 97  ? 105.391 66.191  24.242  1.00   47.00  ? 97  HIS F CA  1 
ATOM   15741 C C   . HIS F  1 97  ? 104.799 65.093  23.379  1.00   49.09  ? 97  HIS F C   1 
ATOM   15742 O O   . HIS F  1 97  ? 105.513 64.211  22.899  1.00   46.97  ? 97  HIS F O   1 
ATOM   15743 C CB  . HIS F  1 97  ? 105.267 67.531  23.511  1.00   43.23  ? 97  HIS F CB  1 
ATOM   15744 C CG  . HIS F  1 97  ? 106.033 68.649  24.144  1.00   40.75  ? 97  HIS F CG  1 
ATOM   15745 N ND1 . HIS F  1 97  ? 107.360 68.885  23.869  1.00   35.75  ? 97  HIS F ND1 1 
ATOM   15746 C CD2 . HIS F  1 97  ? 105.669 69.582  25.055  1.00   43.03  ? 97  HIS F CD2 1 
ATOM   15747 C CE1 . HIS F  1 97  ? 107.776 69.924  24.571  1.00   33.72  ? 97  HIS F CE1 1 
ATOM   15748 N NE2 . HIS F  1 97  ? 106.769 70.363  25.301  1.00   34.13  ? 97  HIS F NE2 1 
ATOM   15749 N N   . ASN F  1 98  ? 103.494 65.191  23.153  1.00   49.50  ? 98  ASN F N   1 
ATOM   15750 C CA  . ASN F  1 98  ? 102.813 64.352  22.200  1.00   49.79  ? 98  ASN F CA  1 
ATOM   15751 C C   . ASN F  1 98  ? 102.491 65.184  20.962  1.00   41.95  ? 98  ASN F C   1 
ATOM   15752 O O   . ASN F  1 98  ? 102.450 66.402  21.031  1.00   39.26  ? 98  ASN F O   1 
ATOM   15753 C CB  . ASN F  1 98  ? 101.541 63.782  22.838  1.00   60.21  ? 98  ASN F CB  1 
ATOM   15754 C CG  . ASN F  1 98  ? 101.836 62.667  23.816  1.00   67.71  ? 98  ASN F CG  1 
ATOM   15755 O OD1 . ASN F  1 98  ? 102.868 62.024  23.715  1.00   61.18  ? 98  ASN F OD1 1 
ATOM   15756 N ND2 . ASN F  1 98  ? 100.964 62.466  24.793  1.00   84.35  ? 98  ASN F ND2 1 
ATOM   15757 N N   . ASN F  1 99  ? 102.291 64.534  19.830  1.00   41.18  ? 99  ASN F N   1 
ATOM   15758 C CA  . ASN F  1 99  ? 101.991 65.236  18.582  1.00   39.97  ? 99  ASN F CA  1 
ATOM   15759 C C   . ASN F  1 99  ? 103.065 66.225  18.097  1.00   36.20  ? 99  ASN F C   1 
ATOM   15760 O O   . ASN F  1 99  ? 102.744 67.218  17.460  1.00   37.01  ? 99  ASN F O   1 
ATOM   15761 C CB  . ASN F  1 99  ? 100.652 65.995  18.733  1.00   41.45  ? 99  ASN F CB  1 
ATOM   15762 C CG  . ASN F  1 99  ? 99.485  65.078  19.184  1.00   74.42  ? 99  ASN F CG  1 
ATOM   15763 O OD1 . ASN F  1 99  ? 99.276  64.000  18.618  1.00   74.86  ? 99  ASN F OD1 1 
ATOM   15764 N ND2 . ASN F  1 99  ? 98.734  65.510  20.211  1.00   74.10  ? 99  ASN F ND2 1 
ATOM   15765 N N   . THR F  1 100 ? 104.335 65.932  18.363  1.00   34.91  ? 100 THR F N   1 
ATOM   15766 C CA  . THR F  1 100 ? 105.478 66.655  17.819  1.00   30.36  ? 100 THR F CA  1 
ATOM   15767 C C   . THR F  1 100 ? 106.122 65.747  16.780  1.00   31.28  ? 100 THR F C   1 
ATOM   15768 O O   . THR F  1 100 ? 105.492 64.785  16.359  1.00   31.57  ? 100 THR F O   1 
ATOM   15769 C CB  . THR F  1 100 ? 106.464 67.016  18.911  1.00   31.68  ? 100 THR F CB  1 
ATOM   15770 O OG1 . THR F  1 100 ? 106.565 65.916  19.810  1.00   34.86  ? 100 THR F OG1 1 
ATOM   15771 C CG2 . THR F  1 100 ? 105.967 68.182  19.706  1.00   33.32  ? 100 THR F CG2 1 
ATOM   15772 N N   . CYS F  1 101 ? 107.344 66.038  16.340  1.00   32.66  ? 101 CYS F N   1 
ATOM   15773 C CA  . CYS F  1 101 ? 108.010 65.126  15.396  1.00   35.63  ? 101 CYS F CA  1 
ATOM   15774 C C   . CYS F  1 101 ? 109.354 64.575  15.874  1.00   32.75  ? 101 CYS F C   1 
ATOM   15775 O O   . CYS F  1 101 ? 110.126 65.247  16.551  1.00   30.73  ? 101 CYS F O   1 
ATOM   15776 C CB  A CYS F  1 101 ? 108.239 65.842  14.077  0.50   35.04  ? 101 CYS F CB  1 
ATOM   15777 C CB  B CYS F  1 101 ? 108.177 65.779  14.010  0.50   35.16  ? 101 CYS F CB  1 
ATOM   15778 S SG  A CYS F  1 101 ? 107.260 67.302  13.994  0.50   33.95  ? 101 CYS F SG  1 
ATOM   15779 S SG  B CYS F  1 101 ? 108.803 67.455  13.922  0.50   28.54  ? 101 CYS F SG  1 
ATOM   15780 N N   . GLY F  1 102 ? 109.618 63.339  15.466  1.00   33.71  ? 102 GLY F N   1 
ATOM   15781 C CA  . GLY F  1 102 ? 110.759 62.600  15.942  1.00   35.22  ? 102 GLY F CA  1 
ATOM   15782 C C   . GLY F  1 102 ? 111.903 62.726  14.980  1.00   36.32  ? 102 GLY F C   1 
ATOM   15783 O O   . GLY F  1 102 ? 111.740 62.717  13.761  1.00   35.57  ? 102 GLY F O   1 
ATOM   15784 N N   . LEU F  1 103 ? 113.083 62.832  15.561  1.00   39.79  ? 103 LEU F N   1 
ATOM   15785 C CA  . LEU F  1 103 ? 114.326 63.050  14.843  1.00   38.77  ? 103 LEU F CA  1 
ATOM   15786 C C   . LEU F  1 103 ? 115.387 62.168  15.445  1.00   34.79  ? 103 LEU F C   1 
ATOM   15787 O O   . LEU F  1 103 ? 115.571 62.176  16.653  1.00   32.69  ? 103 LEU F O   1 
ATOM   15788 C CB  . LEU F  1 103 ? 114.724 64.516  14.927  1.00   43.78  ? 103 LEU F CB  1 
ATOM   15789 C CG  . LEU F  1 103 ? 115.795 64.937  13.952  1.00   48.20  ? 103 LEU F CG  1 
ATOM   15790 C CD1 . LEU F  1 103 ? 115.406 64.457  12.572  1.00   53.26  ? 103 LEU F CD1 1 
ATOM   15791 C CD2 . LEU F  1 103 ? 115.886 66.440  13.994  1.00   47.62  ? 103 LEU F CD2 1 
ATOM   15792 N N   . LEU F  1 104 ? 116.069 61.387  14.621  1.00   34.60  ? 104 LEU F N   1 
ATOM   15793 C CA  . LEU F  1 104 ? 117.084 60.484  15.129  1.00   37.24  ? 104 LEU F CA  1 
ATOM   15794 C C   . LEU F  1 104 ? 118.440 61.174  15.298  1.00   34.92  ? 104 LEU F C   1 
ATOM   15795 O O   . LEU F  1 104 ? 118.961 61.713  14.328  1.00   33.79  ? 104 LEU F O   1 
ATOM   15796 C CB  . LEU F  1 104 ? 117.187 59.300  14.184  1.00   42.02  ? 104 LEU F CB  1 
ATOM   15797 C CG  . LEU F  1 104 ? 117.729 57.996  14.717  1.00   47.45  ? 104 LEU F CG  1 
ATOM   15798 C CD1 . LEU F  1 104 ? 116.768 57.479  15.759  1.00   51.01  ? 104 LEU F CD1 1 
ATOM   15799 C CD2 . LEU F  1 104 ? 117.766 57.036  13.556  1.00   50.41  ? 104 LEU F CD2 1 
ATOM   15800 N N   . SER F  1 105 ? 118.987 61.185  16.520  1.00   34.02  ? 105 SER F N   1 
ATOM   15801 C CA  . SER F  1 105 ? 120.292 61.806  16.804  1.00   31.52  ? 105 SER F CA  1 
ATOM   15802 C C   . SER F  1 105 ? 121.335 60.737  17.093  1.00   32.71  ? 105 SER F C   1 
ATOM   15803 O O   . SER F  1 105 ? 121.002 59.687  17.624  1.00   36.22  ? 105 SER F O   1 
ATOM   15804 C CB  . SER F  1 105 ? 120.226 62.798  17.986  1.00   28.13  ? 105 SER F CB  1 
ATOM   15805 O OG  . SER F  1 105 ? 119.356 63.890  17.756  1.00   27.91  ? 105 SER F OG  1 
ATOM   15806 N N   . SER F  1 106 ? 122.587 61.015  16.740  1.00   33.54  ? 106 SER F N   1 
ATOM   15807 C CA  . SER F  1 106 ? 123.691 60.067  16.921  1.00   37.94  ? 106 SER F CA  1 
ATOM   15808 C C   . SER F  1 106 ? 124.805 60.605  17.790  1.00   37.16  ? 106 SER F C   1 
ATOM   15809 O O   . SER F  1 106 ? 125.179 61.767  17.657  1.00   39.14  ? 106 SER F O   1 
ATOM   15810 C CB  . SER F  1 106 ? 124.315 59.686  15.580  1.00   38.45  ? 106 SER F CB  1 
ATOM   15811 O OG  . SER F  1 106 ? 123.505 58.784  14.861  1.00   43.14  ? 106 SER F OG  1 
ATOM   15812 N N   . ASN F  1 107 ? 125.302 59.770  18.693  1.00   34.30  ? 107 ASN F N   1 
ATOM   15813 C CA  . ASN F  1 107 ? 126.581 60.000  19.364  1.00   33.77  ? 107 ASN F CA  1 
ATOM   15814 C C   . ASN F  1 107 ? 127.675 59.470  18.436  1.00   33.60  ? 107 ASN F C   1 
ATOM   15815 O O   . ASN F  1 107 ? 127.798 58.272  18.268  1.00   33.22  ? 107 ASN F O   1 
ATOM   15816 C CB  . ASN F  1 107 ? 126.593 59.302  20.731  1.00   34.70  ? 107 ASN F CB  1 
ATOM   15817 C CG  . ASN F  1 107 ? 127.899 59.461  21.484  1.00   37.11  ? 107 ASN F CG  1 
ATOM   15818 O OD1 . ASN F  1 107 ? 128.968 59.496  20.891  1.00   38.08  ? 107 ASN F OD1 1 
ATOM   15819 N ND2 . ASN F  1 107 ? 127.821 59.476  22.814  1.00   37.48  ? 107 ASN F ND2 1 
ATOM   15820 N N   . PRO F  1 108 ? 128.481 60.360  17.827  1.00   37.06  ? 108 PRO F N   1 
ATOM   15821 C CA  . PRO F  1 108 ? 129.423 59.947  16.773  1.00   39.61  ? 108 PRO F CA  1 
ATOM   15822 C C   . PRO F  1 108 ? 130.633 59.193  17.324  1.00   41.83  ? 108 PRO F C   1 
ATOM   15823 O O   . PRO F  1 108 ? 131.361 58.507  16.595  1.00   43.27  ? 108 PRO F O   1 
ATOM   15824 C CB  . PRO F  1 108 ? 129.838 61.283  16.149  1.00   37.47  ? 108 PRO F CB  1 
ATOM   15825 C CG  . PRO F  1 108 ? 129.743 62.245  17.269  1.00   34.44  ? 108 PRO F CG  1 
ATOM   15826 C CD  . PRO F  1 108 ? 128.571 61.803  18.098  1.00   33.09  ? 108 PRO F CD  1 
ATOM   15827 N N   . VAL F  1 109 ? 130.836 59.311  18.631  1.00   42.02  ? 109 VAL F N   1 
ATOM   15828 C CA  . VAL F  1 109 ? 131.919 58.616  19.285  1.00   40.25  ? 109 VAL F CA  1 
ATOM   15829 C C   . VAL F  1 109 ? 131.473 57.202  19.572  1.00   40.75  ? 109 VAL F C   1 
ATOM   15830 O O   . VAL F  1 109 ? 132.171 56.260  19.230  1.00   43.97  ? 109 VAL F O   1 
ATOM   15831 C CB  . VAL F  1 109 ? 132.347 59.306  20.579  1.00   40.40  ? 109 VAL F CB  1 
ATOM   15832 C CG1 . VAL F  1 109 ? 133.373 58.455  21.308  1.00   42.66  ? 109 VAL F CG1 1 
ATOM   15833 C CG2 . VAL F  1 109 ? 132.928 60.680  20.275  1.00   39.87  ? 109 VAL F CG2 1 
ATOM   15834 N N   . THR F  1 110 ? 130.310 57.044  20.195  1.00   38.81  ? 110 THR F N   1 
ATOM   15835 C CA  . THR F  1 110 ? 129.843 55.713  20.545  1.00   43.13  ? 110 THR F CA  1 
ATOM   15836 C C   . THR F  1 110 ? 128.989 55.076  19.452  1.00   46.07  ? 110 THR F C   1 
ATOM   15837 O O   . THR F  1 110 ? 128.755 53.876  19.498  1.00   48.74  ? 110 THR F O   1 
ATOM   15838 C CB  . THR F  1 110 ? 129.020 55.707  21.849  1.00   42.78  ? 110 THR F CB  1 
ATOM   15839 O OG1 . THR F  1 110 ? 127.777 56.371  21.640  1.00   42.59  ? 110 THR F OG1 1 
ATOM   15840 C CG2 . THR F  1 110 ? 129.763 56.396  22.959  1.00   44.14  ? 110 THR F CG2 1 
ATOM   15841 N N   . GLN F  1 111 ? 128.524 55.872  18.491  1.00   45.38  ? 111 GLN F N   1 
ATOM   15842 C CA  . GLN F  1 111 ? 127.650 55.410  17.402  1.00   47.80  ? 111 GLN F CA  1 
ATOM   15843 C C   . GLN F  1 111 ? 126.288 54.952  17.899  1.00   47.90  ? 111 GLN F C   1 
ATOM   15844 O O   . GLN F  1 111 ? 125.539 54.320  17.170  1.00   50.73  ? 111 GLN F O   1 
ATOM   15845 C CB  . GLN F  1 111 ? 128.317 54.326  16.571  1.00   53.32  ? 111 GLN F CB  1 
ATOM   15846 C CG  . GLN F  1 111 ? 129.455 54.874  15.711  1.00   61.47  ? 111 GLN F CG  1 
ATOM   15847 C CD  . GLN F  1 111 ? 130.312 53.781  15.084  1.00   73.58  ? 111 GLN F CD  1 
ATOM   15848 O OE1 . GLN F  1 111 ? 131.296 53.323  15.676  1.00   76.78  ? 111 GLN F OE1 1 
ATOM   15849 N NE2 . GLN F  1 111 ? 129.946 53.366  13.869  1.00   79.26  ? 111 GLN F NE2 1 
ATOM   15850 N N   . GLU F  1 112 ? 125.987 55.270  19.151  1.00   46.81  ? 112 GLU F N   1 
ATOM   15851 C CA  . GLU F  1 112 ? 124.643 55.140  19.695  1.00   46.76  ? 112 GLU F CA  1 
ATOM   15852 C C   . GLU F  1 112 ? 123.748 56.112  18.965  1.00   41.69  ? 112 GLU F C   1 
ATOM   15853 O O   . GLU F  1 112 ? 124.186 57.195  18.599  1.00   35.38  ? 112 GLU F O   1 
ATOM   15854 C CB  . GLU F  1 112 ? 124.618 55.500  21.177  1.00   51.78  ? 112 GLU F CB  1 
ATOM   15855 C CG  . GLU F  1 112 ? 125.190 54.509  22.166  1.00   58.19  ? 112 GLU F CG  1 
ATOM   15856 C CD  . GLU F  1 112 ? 125.467 55.183  23.509  1.00   62.15  ? 112 GLU F CD  1 
ATOM   15857 O OE1 . GLU F  1 112 ? 125.181 54.572  24.556  1.00   65.27  ? 112 GLU F OE1 1 
ATOM   15858 O OE2 . GLU F  1 112 ? 125.918 56.355  23.515  1.00   61.82  1 112 GLU F OE2 1 
ATOM   15859 N N   . SER F  1 113 ? 122.483 55.762  18.795  1.00   44.70  ? 113 SER F N   1 
ATOM   15860 C CA  . SER F  1 113 ? 121.526 56.742  18.307  1.00   45.14  ? 113 SER F CA  1 
ATOM   15861 C C   . SER F  1 113 ? 120.283 56.703  19.174  1.00   41.17  ? 113 SER F C   1 
ATOM   15862 O O   . SER F  1 113 ? 120.025 55.722  19.863  1.00   41.72  ? 113 SER F O   1 
ATOM   15863 C CB  . SER F  1 113 ? 121.157 56.490  16.844  1.00   49.99  ? 113 SER F CB  1 
ATOM   15864 O OG  . SER F  1 113 ? 120.462 55.266  16.702  1.00   55.39  ? 113 SER F OG  1 
ATOM   15865 N N   . GLY F  1 114 ? 119.522 57.783  19.155  1.00   38.10  ? 114 GLY F N   1 
ATOM   15866 C CA  . GLY F  1 114 ? 118.305 57.828  19.941  1.00   39.65  ? 114 GLY F CA  1 
ATOM   15867 C C   . GLY F  1 114 ? 117.294 58.752  19.301  1.00   35.00  ? 114 GLY F C   1 
ATOM   15868 O O   . GLY F  1 114 ? 117.683 59.683  18.606  1.00   31.76  ? 114 GLY F O   1 
ATOM   15869 N N   . LEU F  1 115 ? 116.005 58.502  19.518  1.00   35.27  ? 115 LEU F N   1 
ATOM   15870 C CA  . LEU F  1 115 ? 114.977 59.355  18.922  1.00   36.18  ? 115 LEU F CA  1 
ATOM   15871 C C   . LEU F  1 115 ? 114.638 60.550  19.820  1.00   36.33  ? 115 LEU F C   1 
ATOM   15872 O O   . LEU F  1 115 ? 114.133 60.408  20.944  1.00   39.68  ? 115 LEU F O   1 
ATOM   15873 C CB  . LEU F  1 115 ? 113.719 58.555  18.588  1.00   37.54  ? 115 LEU F CB  1 
ATOM   15874 C CG  . LEU F  1 115 ? 112.713 59.268  17.679  1.00   33.43  ? 115 LEU F CG  1 
ATOM   15875 C CD1 . LEU F  1 115 ? 113.167 59.213  16.248  1.00   29.74  ? 115 LEU F CD1 1 
ATOM   15876 C CD2 . LEU F  1 115 ? 111.383 58.559  17.827  1.00   39.81  ? 115 LEU F CD2 1 
ATOM   15877 N N   . GLY F  1 116 ? 114.939 61.729  19.302  1.00   36.37  ? 116 GLY F N   1 
ATOM   15878 C CA  . GLY F  1 116 ? 114.659 62.954  20.001  1.00   37.21  ? 116 GLY F CA  1 
ATOM   15879 C C   . GLY F  1 116 ? 113.458 63.634  19.398  1.00   33.86  ? 116 GLY F C   1 
ATOM   15880 O O   . GLY F  1 116 ? 112.866 63.152  18.444  1.00   33.98  ? 116 GLY F O   1 
ATOM   15881 N N   . GLU F  1 117 ? 113.126 64.777  19.968  1.00   33.40  ? 117 GLU F N   1 
ATOM   15882 C CA  . GLU F  1 117 ? 112.006 65.581  19.536  1.00   28.79  ? 117 GLU F CA  1 
ATOM   15883 C C   . GLU F  1 117 ? 112.532 66.865  18.870  1.00   27.77  ? 117 GLU F C   1 
ATOM   15884 O O   . GLU F  1 117 ? 113.460 67.497  19.365  1.00   27.21  ? 117 GLU F O   1 
ATOM   15885 C CB  . GLU F  1 117 ? 111.125 65.894  20.749  1.00   27.12  ? 117 GLU F CB  1 
ATOM   15886 C CG  . GLU F  1 117 ? 109.778 66.531  20.446  1.00   27.62  ? 117 GLU F CG  1 
ATOM   15887 C CD  . GLU F  1 117 ? 109.034 66.988  21.694  1.00   30.67  ? 117 GLU F CD  1 
ATOM   15888 O OE1 . GLU F  1 117 ? 109.624 67.732  22.490  1.00   34.56  ? 117 GLU F OE1 1 
ATOM   15889 O OE2 . GLU F  1 117 ? 107.866 66.617  21.885  1.00   32.08  1 117 GLU F OE2 1 
ATOM   15890 N N   . LEU F  1 118 ? 111.983 67.235  17.720  1.00   29.17  ? 118 LEU F N   1 
ATOM   15891 C CA  . LEU F  1 118 ? 112.370 68.504  17.103  1.00   27.29  ? 118 LEU F CA  1 
ATOM   15892 C C   . LEU F  1 118 ? 112.019 69.686  18.039  1.00   27.81  ? 118 LEU F C   1 
ATOM   15893 O O   . LEU F  1 118 ? 110.929 69.739  18.615  1.00   29.72  ? 118 LEU F O   1 
ATOM   15894 C CB  . LEU F  1 118 ? 111.693 68.673  15.733  1.00   25.96  ? 118 LEU F CB  1 
ATOM   15895 C CG  . LEU F  1 118 ? 112.119 69.907  14.910  1.00   25.40  ? 118 LEU F CG  1 
ATOM   15896 C CD1 . LEU F  1 118 ? 113.568 69.817  14.495  1.00   25.46  ? 118 LEU F CD1 1 
ATOM   15897 C CD2 . LEU F  1 118 ? 111.233 70.154  13.716  1.00   24.02  ? 118 LEU F CD2 1 
ATOM   15898 N N   . ALA F  1 119 ? 112.956 70.631  18.165  1.00   26.52  ? 119 ALA F N   1 
ATOM   15899 C CA  . ALA F  1 119 ? 112.835 71.775  19.057  1.00   24.51  ? 119 ALA F CA  1 
ATOM   15900 C C   . ALA F  1 119 ? 113.177 73.059  18.331  1.00   25.99  ? 119 ALA F C   1 
ATOM   15901 O O   . ALA F  1 119 ? 113.840 73.029  17.314  1.00   26.70  ? 119 ALA F O   1 
ATOM   15902 C CB  . ALA F  1 119 ? 113.729 71.620  20.227  1.00   24.18  ? 119 ALA F CB  1 
ATOM   15903 N N   . GLN F  1 120 ? 112.738 74.184  18.882  1.00   25.82  ? 120 GLN F N   1 
ATOM   15904 C CA  . GLN F  1 120 ? 112.990 75.500  18.303  1.00   26.35  ? 120 GLN F CA  1 
ATOM   15905 C C   . GLN F  1 120 ? 113.317 76.459  19.426  1.00   27.84  ? 120 GLN F C   1 
ATOM   15906 O O   . GLN F  1 120 ? 112.586 76.503  20.393  1.00   28.83  ? 120 GLN F O   1 
ATOM   15907 C CB  . GLN F  1 120 ? 111.762 75.982  17.537  1.00   28.36  ? 120 GLN F CB  1 
ATOM   15908 C CG  . GLN F  1 120 ? 111.891 77.342  16.933  1.00   29.77  ? 120 GLN F CG  1 
ATOM   15909 C CD  . GLN F  1 120 ? 110.606 77.807  16.308  1.00   31.01  ? 120 GLN F CD  1 
ATOM   15910 O OE1 . GLN F  1 120 ? 110.208 77.299  15.269  1.00   32.03  ? 120 GLN F OE1 1 
ATOM   15911 N NE2 . GLN F  1 120 ? 109.953 78.780  16.925  1.00   31.19  ? 120 GLN F NE2 1 
ATOM   15912 N N   . ASP F  1 121 ? 114.405 77.215  19.324  1.00   29.09  ? 121 ASP F N   1 
ATOM   15913 C CA  . ASP F  1 121 ? 114.732 78.202  20.363  1.00   31.21  ? 121 ASP F CA  1 
ATOM   15914 C C   . ASP F  1 121 ? 115.709 79.208  19.787  1.00   30.40  ? 121 ASP F C   1 
ATOM   15915 O O   . ASP F  1 121 ? 116.029 79.131  18.615  1.00   28.11  ? 121 ASP F O   1 
ATOM   15916 C CB  . ASP F  1 121 ? 115.317 77.535  21.611  1.00   30.27  ? 121 ASP F CB  1 
ATOM   15917 C CG  . ASP F  1 121 ? 115.000 78.298  22.884  1.00   30.85  ? 121 ASP F CG  1 
ATOM   15918 O OD1 . ASP F  1 121 ? 114.813 79.524  22.849  1.00   31.03  ? 121 ASP F OD1 1 
ATOM   15919 O OD2 . ASP F  1 121 ? 114.905 77.669  23.946  1.00   33.89  1 121 ASP F OD2 1 
ATOM   15920 N N   . VAL F  1 122 ? 116.131 80.177  20.594  1.00   32.18  ? 122 VAL F N   1 
ATOM   15921 C CA  . VAL F  1 122 ? 117.164 81.137  20.202  1.00   30.74  ? 122 VAL F CA  1 
ATOM   15922 C C   . VAL F  1 122 ? 118.550 80.519  20.187  1.00   32.44  ? 122 VAL F C   1 
ATOM   15923 O O   . VAL F  1 122 ? 118.921 79.825  21.126  1.00   32.53  ? 122 VAL F O   1 
ATOM   15924 C CB  . VAL F  1 122 ? 117.224 82.338  21.161  1.00   31.95  ? 122 VAL F CB  1 
ATOM   15925 C CG1 . VAL F  1 122 ? 118.453 83.204  20.891  1.00   31.03  ? 122 VAL F CG1 1 
ATOM   15926 C CG2 . VAL F  1 122 ? 115.958 83.144  21.077  1.00   30.51  ? 122 VAL F CG2 1 
ATOM   15927 N N   . LEU F  1 123 ? 119.303 80.776  19.116  1.00   30.34  ? 123 LEU F N   1 
ATOM   15928 C CA  . LEU F  1 123 ? 120.735 80.580  19.114  1.00   29.06  ? 123 LEU F CA  1 
ATOM   15929 C C   . LEU F  1 123 ? 121.401 81.941  18.839  1.00   32.14  ? 123 LEU F C   1 
ATOM   15930 O O   . LEU F  1 123 ? 120.912 82.702  18.004  1.00   32.74  ? 123 LEU F O   1 
ATOM   15931 C CB  . LEU F  1 123 ? 121.140 79.556  18.060  1.00   24.80  ? 123 LEU F CB  1 
ATOM   15932 C CG  . LEU F  1 123 ? 122.628 79.260  17.923  1.00   24.61  ? 123 LEU F CG  1 
ATOM   15933 C CD1 . LEU F  1 123 ? 122.779 77.810  17.573  1.00   24.49  ? 123 LEU F CD1 1 
ATOM   15934 C CD2 . LEU F  1 123 ? 123.306 80.108  16.866  1.00   25.41  ? 123 LEU F CD2 1 
ATOM   15935 N N   . ALA F  1 124 ? 122.500 82.237  19.545  1.00   32.28  ? 124 ALA F N   1 
ATOM   15936 C CA  . ALA F  1 124 ? 123.307 83.437  19.325  1.00   28.05  ? 124 ALA F CA  1 
ATOM   15937 C C   . ALA F  1 124 ? 124.773 83.068  19.041  1.00   29.25  ? 124 ALA F C   1 
ATOM   15938 O O   . ALA F  1 124 ? 125.270 82.039  19.476  1.00   27.61  ? 124 ALA F O   1 
ATOM   15939 C CB  . ALA F  1 124 ? 123.204 84.368  20.520  1.00   30.44  ? 124 ALA F CB  1 
ATOM   15940 N N   . ILE F  1 125 ? 125.461 83.914  18.294  1.00   29.06  ? 125 ILE F N   1 
ATOM   15941 C CA  . ILE F  1 125 ? 126.830 83.655  17.900  1.00   28.13  ? 125 ILE F CA  1 
ATOM   15942 C C   . ILE F  1 125 ? 127.553 84.996  17.656  1.00   30.61  ? 125 ILE F C   1 
ATOM   15943 O O   . ILE F  1 125 ? 126.922 85.994  17.354  1.00   30.96  ? 125 ILE F O   1 
ATOM   15944 C CB  . ILE F  1 125 ? 126.865 82.753  16.652  1.00   24.88  ? 125 ILE F CB  1 
ATOM   15945 C CG1 . ILE F  1 125 ? 128.289 82.381  16.276  1.00   23.30  ? 125 ILE F CG1 1 
ATOM   15946 C CG2 . ILE F  1 125 ? 126.190 83.420  15.489  1.00   25.31  ? 125 ILE F CG2 1 
ATOM   15947 C CD1 . ILE F  1 125 ? 128.373 81.494  15.065  1.00   23.79  ? 125 ILE F CD1 1 
ATOM   15948 N N   . HIS F  1 126 ? 128.863 85.055  17.832  1.00   29.54  ? 126 HIS F N   1 
ATOM   15949 C CA  . HIS F  1 126 ? 129.549 86.323  17.594  1.00   31.24  ? 126 HIS F CA  1 
ATOM   15950 C C   . HIS F  1 126 ? 129.540 86.764  16.149  1.00   29.18  ? 126 HIS F C   1 
ATOM   15951 O O   . HIS F  1 126 ? 129.795 85.967  15.255  1.00   30.22  ? 126 HIS F O   1 
ATOM   15952 C CB  . HIS F  1 126 ? 131.002 86.227  18.025  1.00   33.38  ? 126 HIS F CB  1 
ATOM   15953 C CG  . HIS F  1 126 ? 131.200 86.374  19.489  1.00   35.59  ? 126 HIS F CG  1 
ATOM   15954 N ND1 . HIS F  1 126 ? 131.138 87.590  20.124  1.00   41.22  ? 126 HIS F ND1 1 
ATOM   15955 C CD2 . HIS F  1 126 ? 131.437 85.456  20.450  1.00   37.36  ? 126 HIS F CD2 1 
ATOM   15956 C CE1 . HIS F  1 126 ? 131.363 87.422  21.415  1.00   41.88  ? 126 HIS F CE1 1 
ATOM   15957 N NE2 . HIS F  1 126 ? 131.547 86.135  21.639  1.00   39.58  ? 126 HIS F NE2 1 
ATOM   15958 N N   . SER F  1 127 ? 129.293 88.046  15.918  1.00   31.37  ? 127 SER F N   1 
ATOM   15959 C CA  . SER F  1 127 ? 129.605 88.640  14.635  1.00   32.14  ? 127 SER F CA  1 
ATOM   15960 C C   . SER F  1 127 ? 130.999 89.203  14.743  1.00   33.36  ? 127 SER F C   1 
ATOM   15961 O O   . SER F  1 127 ? 131.694 88.934  15.707  1.00   35.07  ? 127 SER F O   1 
ATOM   15962 C CB  . SER F  1 127 ? 128.598 89.722  14.258  1.00   35.61  ? 127 SER F CB  1 
ATOM   15963 O OG  . SER F  1 127 ? 128.470 90.708  15.269  1.00   38.41  ? 127 SER F OG  1 
ATOM   15964 N N   . THR F  1 128 ? 131.420 90.003  13.774  1.00   37.19  ? 128 THR F N   1 
ATOM   15965 C CA  . THR F  1 128 ? 132.712 90.676  13.897  1.00   37.08  ? 128 THR F CA  1 
ATOM   15966 C C   . THR F  1 128 ? 132.542 92.206  13.833  1.00   37.21  ? 128 THR F C   1 
ATOM   15967 O O   . THR F  1 128 ? 131.578 92.721  13.253  1.00   33.61  ? 128 THR F O   1 
ATOM   15968 C CB  . THR F  1 128 ? 133.723 90.184  12.817  1.00   36.73  ? 128 THR F CB  1 
ATOM   15969 O OG1 . THR F  1 128 ? 133.246 90.518  11.516  1.00   39.46  ? 128 THR F OG1 1 
ATOM   15970 C CG2 . THR F  1 128 ? 133.867 88.692  12.863  1.00   32.08  ? 128 THR F CG2 1 
ATOM   15971 N N   . HIS F  1 129 ? 133.488 92.916  14.451  1.00   37.63  ? 129 HIS F N   1 
ATOM   15972 C CA  . HIS F  1 129 ? 133.491 94.368  14.526  1.00   41.82  ? 129 HIS F CA  1 
ATOM   15973 C C   . HIS F  1 129 ? 134.870 94.897  14.220  1.00   44.45  ? 129 HIS F C   1 
ATOM   15974 O O   . HIS F  1 129 ? 135.747 94.841  15.074  1.00   45.90  ? 129 HIS F O   1 
ATOM   15975 C CB  . HIS F  1 129 ? 133.064 94.851  15.918  1.00   44.34  ? 129 HIS F CB  1 
ATOM   15976 C CG  . HIS F  1 129 ? 132.967 96.341  16.038  1.00   47.79  ? 129 HIS F CG  1 
ATOM   15977 N ND1 . HIS F  1 129 ? 133.837 97.083  16.810  1.00   51.31  ? 129 HIS F ND1 1 
ATOM   15978 C CD2 . HIS F  1 129 ? 132.111 97.229  15.482  1.00   49.07  ? 129 HIS F CD2 1 
ATOM   15979 C CE1 . HIS F  1 129 ? 133.524 98.362  16.721  1.00   54.55  ? 129 HIS F CE1 1 
ATOM   15980 N NE2 . HIS F  1 129 ? 132.477 98.477  15.926  1.00   54.10  ? 129 HIS F NE2 1 
ATOM   15981 N N   . GLY F  1 130 ? 135.064 95.419  13.012  1.00   44.97  ? 130 GLY F N   1 
ATOM   15982 C CA  . GLY F  1 130 ? 136.392 95.811  12.572  1.00   44.59  ? 130 GLY F CA  1 
ATOM   15983 C C   . GLY F  1 130 ? 137.257 94.566  12.519  1.00   43.10  ? 130 GLY F C   1 
ATOM   15984 O O   . GLY F  1 130 ? 136.925 93.599  11.835  1.00   40.88  ? 130 GLY F O   1 
ATOM   15985 N N   . SER F  1 131 ? 138.374 94.599  13.239  1.00   45.06  ? 131 SER F N   1 
ATOM   15986 C CA  . SER F  1 131 ? 139.275 93.452  13.323  1.00   46.86  ? 131 SER F CA  1 
ATOM   15987 C C   . SER F  1 131 ? 138.996 92.554  14.535  1.00   46.07  ? 131 SER F C   1 
ATOM   15988 O O   . SER F  1 131 ? 139.695 91.572  14.738  1.00   45.44  ? 131 SER F O   1 
ATOM   15989 C CB  . SER F  1 131 ? 140.731 93.923  13.379  1.00   50.31  ? 131 SER F CB  1 
ATOM   15990 O OG  . SER F  1 131 ? 141.078 94.412  14.668  1.00   50.01  ? 131 SER F OG  1 
ATOM   15991 N N   . LYS F  1 132 ? 137.985 92.898  15.332  1.00   47.15  ? 132 LYS F N   1 
ATOM   15992 C CA  . LYS F  1 132 ? 137.695 92.194  16.582  1.00   45.36  ? 132 LYS F CA  1 
ATOM   15993 C C   . LYS F  1 132 ? 136.411 91.378  16.510  1.00   39.69  ? 132 LYS F C   1 
ATOM   15994 O O   . LYS F  1 132 ? 135.676 91.471  15.538  1.00   36.82  ? 132 LYS F O   1 
ATOM   15995 C CB  . LYS F  1 132 ? 137.595 93.203  17.737  1.00   46.63  ? 132 LYS F CB  1 
ATOM   15996 C CG  . LYS F  1 132 ? 138.853 93.991  17.998  1.00   50.20  ? 132 LYS F CG  1 
ATOM   15997 C CD  . LYS F  1 132 ? 138.968 94.347  19.473  1.00   56.78  ? 132 LYS F CD  1 
ATOM   15998 C CE  . LYS F  1 132 ? 140.056 95.381  19.700  1.00   65.46  ? 132 LYS F CE  1 
ATOM   15999 N NZ  . LYS F  1 132 ? 139.754 96.344  20.808  1.00   70.02  ? 132 LYS F NZ  1 
ATOM   16000 N N   . LEU F  1 133 ? 136.158 90.571  17.539  1.00   38.32  ? 133 LEU F N   1 
ATOM   16001 C CA  . LEU F  1 133 ? 134.841 89.973  17.719  1.00   36.15  ? 133 LEU F CA  1 
ATOM   16002 C C   . LEU F  1 133 ? 133.830 91.062  18.004  1.00   38.16  ? 133 LEU F C   1 
ATOM   16003 O O   . LEU F  1 133 ? 134.102 92.002  18.753  1.00   41.25  ? 133 LEU F O   1 
ATOM   16004 C CB  . LEU F  1 133 ? 134.816 88.974  18.873  1.00   35.83  ? 133 LEU F CB  1 
ATOM   16005 C CG  . LEU F  1 133 ? 135.555 87.649  18.743  1.00   35.42  ? 133 LEU F CG  1 
ATOM   16006 C CD1 . LEU F  1 133 ? 135.351 86.885  20.017  1.00   37.43  ? 133 LEU F CD1 1 
ATOM   16007 C CD2 . LEU F  1 133 ? 135.066 86.857  17.565  1.00   31.44  ? 133 LEU F CD2 1 
ATOM   16008 N N   . GLY F  1 134 ? 132.656 90.931  17.413  1.00   36.85  ? 134 GLY F N   1 
ATOM   16009 C CA  . GLY F  1 134 ? 131.599 91.895  17.630  1.00   38.36  ? 134 GLY F CA  1 
ATOM   16010 C C   . GLY F  1 134 ? 130.467 91.347  18.478  1.00   41.01  ? 134 GLY F C   1 
ATOM   16011 O O   . GLY F  1 134 ? 130.594 90.288  19.091  1.00   40.49  ? 134 GLY F O   1 
ATOM   16012 N N   . PRO F  1 135 ? 129.343 92.073  18.519  1.00   44.25  ? 135 PRO F N   1 
ATOM   16013 C CA  . PRO F  1 135 ? 128.221 91.619  19.336  1.00   43.37  ? 135 PRO F CA  1 
ATOM   16014 C C   . PRO F  1 135 ? 127.634 90.315  18.850  1.00   36.91  ? 135 PRO F C   1 
ATOM   16015 O O   . PRO F  1 135 ? 127.732 89.982  17.681  1.00   33.11  ? 135 PRO F O   1 
ATOM   16016 C CB  . PRO F  1 135 ? 127.199 92.755  19.202  1.00   45.47  ? 135 PRO F CB  1 
ATOM   16017 C CG  . PRO F  1 135 ? 127.590 93.482  17.961  1.00   45.59  ? 135 PRO F CG  1 
ATOM   16018 C CD  . PRO F  1 135 ? 129.073 93.367  17.868  1.00   44.91  ? 135 PRO F CD  1 
ATOM   16019 N N   . MET F  1 136 ? 127.026 89.589  19.774  1.00   37.22  ? 136 MET F N   1 
ATOM   16020 C CA  . MET F  1 136 ? 126.283 88.388  19.465  1.00   35.99  ? 136 MET F CA  1 
ATOM   16021 C C   . MET F  1 136 ? 125.107 88.722  18.602  1.00   31.95  ? 136 MET F C   1 
ATOM   16022 O O   . MET F  1 136 ? 124.414 89.703  18.850  1.00   35.73  ? 136 MET F O   1 
ATOM   16023 C CB  . MET F  1 136 ? 125.780 87.745  20.745  1.00   40.97  ? 136 MET F CB  1 
ATOM   16024 C CG  . MET F  1 136 ? 126.850 87.561  21.776  1.00   44.61  ? 136 MET F CG  1 
ATOM   16025 S SD  . MET F  1 136 ? 127.772 86.087  21.398  1.00   46.56  ? 136 MET F SD  1 
ATOM   16026 C CE  . MET F  1 136 ? 126.540 84.906  21.840  1.00   40.53  ? 136 MET F CE  1 
ATOM   16027 N N   . VAL F  1 137 ? 124.855 87.901  17.605  1.00   28.98  ? 137 VAL F N   1 
ATOM   16028 C CA  . VAL F  1 137 ? 123.635 88.050  16.834  1.00   30.30  ? 137 VAL F CA  1 
ATOM   16029 C C   . VAL F  1 137 ? 122.829 86.748  16.938  1.00   32.31  ? 137 VAL F C   1 
ATOM   16030 O O   . VAL F  1 137 ? 123.389 85.674  17.173  1.00   31.59  ? 137 VAL F O   1 
ATOM   16031 C CB  . VAL F  1 137 ? 123.927 88.440  15.372  1.00   28.01  ? 137 VAL F CB  1 
ATOM   16032 C CG1 . VAL F  1 137 ? 124.406 89.905  15.312  1.00   27.71  ? 137 VAL F CG1 1 
ATOM   16033 C CG2 . VAL F  1 137 ? 124.944 87.502  14.756  1.00   26.67  ? 137 VAL F CG2 1 
ATOM   16034 N N   . LYS F  1 138 ? 121.518 86.860  16.785  1.00   33.52  ? 138 LYS F N   1 
ATOM   16035 C CA  . LYS F  1 138 ? 120.620 85.757  17.082  1.00   34.64  ? 138 LYS F CA  1 
ATOM   16036 C C   . LYS F  1 138 ? 119.925 85.155  15.878  1.00   33.85  ? 138 LYS F C   1 
ATOM   16037 O O   . LYS F  1 138 ? 119.611 85.836  14.916  1.00   34.60  ? 138 LYS F O   1 
ATOM   16038 C CB  . LYS F  1 138 ? 119.543 86.214  18.083  1.00   37.63  ? 138 LYS F CB  1 
ATOM   16039 C CG  . LYS F  1 138 ? 120.068 86.709  19.433  1.00   41.73  ? 138 LYS F CG  1 
ATOM   16040 C CD  . LYS F  1 138 ? 118.918 87.115  20.340  1.00   47.61  ? 138 LYS F CD  1 
ATOM   16041 C CE  . LYS F  1 138 ? 119.384 87.636  21.689  1.00   56.82  ? 138 LYS F CE  1 
ATOM   16042 N NZ  . LYS F  1 138 ? 119.761 89.078  21.634  1.00   65.03  ? 138 LYS F NZ  1 
ATOM   16043 N N   . VAL F  1 139 ? 119.704 83.850  15.944  1.00   33.40  ? 139 VAL F N   1 
ATOM   16044 C CA  . VAL F  1 139 ? 118.717 83.174  15.116  1.00   29.20  ? 139 VAL F CA  1 
ATOM   16045 C C   . VAL F  1 139 ? 117.557 82.865  16.045  1.00   28.44  ? 139 VAL F C   1 
ATOM   16046 O O   . VAL F  1 139 ? 117.684 81.999  16.883  1.00   29.19  ? 139 VAL F O   1 
ATOM   16047 C CB  . VAL F  1 139 ? 119.286 81.899  14.469  1.00   26.10  ? 139 VAL F CB  1 
ATOM   16048 C CG1 . VAL F  1 139 ? 118.246 81.190  13.603  1.00   25.31  ? 139 VAL F CG1 1 
ATOM   16049 C CG2 . VAL F  1 139 ? 120.524 82.231  13.666  1.00   24.96  ? 139 VAL F CG2 1 
ATOM   16050 N N   . PRO F  1 140 ? 116.446 83.625  15.951  1.00   29.73  ? 140 PRO F N   1 
ATOM   16051 C CA  . PRO F  1 140 ? 115.408 83.502  16.987  1.00   30.66  ? 140 PRO F CA  1 
ATOM   16052 C C   . PRO F  1 140 ? 114.637 82.175  16.970  1.00   29.02  ? 140 PRO F C   1 
ATOM   16053 O O   . PRO F  1 140 ? 114.168 81.735  18.017  1.00   30.66  ? 140 PRO F O   1 
ATOM   16054 C CB  . PRO F  1 140 ? 114.462 84.689  16.679  1.00   29.68  ? 140 PRO F CB  1 
ATOM   16055 C CG  . PRO F  1 140 ? 115.222 85.593  15.751  1.00   29.40  ? 140 PRO F CG  1 
ATOM   16056 C CD  . PRO F  1 140 ? 116.120 84.684  14.974  1.00   28.18  ? 140 PRO F CD  1 
ATOM   16057 N N   . GLN F  1 141 ? 114.528 81.552  15.799  1.00   29.48  ? 141 GLN F N   1 
ATOM   16058 C CA  . GLN F  1 141 ? 113.872 80.251  15.634  1.00   29.26  ? 141 GLN F CA  1 
ATOM   16059 C C   . GLN F  1 141 ? 114.835 79.188  15.108  1.00   26.57  ? 141 GLN F C   1 
ATOM   16060 O O   . GLN F  1 141 ? 114.627 78.647  14.029  1.00   27.49  ? 141 GLN F O   1 
ATOM   16061 C CB  . GLN F  1 141 ? 112.653 80.329  14.682  1.00   34.88  ? 141 GLN F CB  1 
ATOM   16062 C CG  . GLN F  1 141 ? 111.433 81.133  15.183  1.00   40.98  ? 141 GLN F CG  1 
ATOM   16063 C CD  . GLN F  1 141 ? 111.426 82.597  14.770  1.00   46.62  ? 141 GLN F CD  1 
ATOM   16064 O OE1 . GLN F  1 141 ? 112.070 82.998  13.803  1.00   44.95  ? 141 GLN F OE1 1 
ATOM   16065 N NE2 . GLN F  1 141 ? 110.711 83.409  15.533  1.00   52.63  ? 141 GLN F NE2 1 
ATOM   16066 N N   . PHE F  1 142 ? 115.910 78.931  15.844  1.00   26.74  ? 142 PHE F N   1 
ATOM   16067 C CA  . PHE F  1 142 ? 116.876 77.895  15.463  1.00   26.07  ? 142 PHE F CA  1 
ATOM   16068 C C   . PHE F  1 142 ? 116.288 76.495  15.721  1.00   23.78  ? 142 PHE F C   1 
ATOM   16069 O O   . PHE F  1 142 ? 115.779 76.221  16.806  1.00   23.28  ? 142 PHE F O   1 
ATOM   16070 C CB  . PHE F  1 142 ? 118.210 78.078  16.217  1.00   26.56  ? 142 PHE F CB  1 
ATOM   16071 C CG  . PHE F  1 142 ? 119.303 77.135  15.765  1.00   29.84  ? 142 PHE F CG  1 
ATOM   16072 C CD1 . PHE F  1 142 ? 120.041 77.401  14.609  1.00   28.19  ? 142 PHE F CD1 1 
ATOM   16073 C CD2 . PHE F  1 142 ? 119.611 75.989  16.500  1.00   29.12  ? 142 PHE F CD2 1 
ATOM   16074 C CE1 . PHE F  1 142 ? 121.057 76.535  14.191  1.00   26.02  ? 142 PHE F CE1 1 
ATOM   16075 C CE2 . PHE F  1 142 ? 120.634 75.121  16.081  1.00   24.63  ? 142 PHE F CE2 1 
ATOM   16076 C CZ  . PHE F  1 142 ? 121.346 75.399  14.921  1.00   24.56  ? 142 PHE F CZ  1 
ATOM   16077 N N   . LEU F  1 143 ? 116.345 75.627  14.714  1.00   21.67  ? 143 LEU F N   1 
ATOM   16078 C CA  . LEU F  1 143 ? 115.820 74.272  14.829  1.00   23.16  ? 143 LEU F CA  1 
ATOM   16079 C C   . LEU F  1 143 ? 116.892 73.266  15.215  1.00   23.87  ? 143 LEU F C   1 
ATOM   16080 O O   . LEU F  1 143 ? 117.990 73.232  14.641  1.00   25.18  ? 143 LEU F O   1 
ATOM   16081 C CB  . LEU F  1 143 ? 115.148 73.832  13.520  1.00   23.58  ? 143 LEU F CB  1 
ATOM   16082 C CG  . LEU F  1 143 ? 113.948 74.627  13.009  1.00   25.20  ? 143 LEU F CG  1 
ATOM   16083 C CD1 . LEU F  1 143 ? 113.565 74.115  11.634  1.00   23.92  ? 143 LEU F CD1 1 
ATOM   16084 C CD2 . LEU F  1 143 ? 112.774 74.503  13.957  1.00   26.41  ? 143 LEU F CD2 1 
ATOM   16085 N N   . PHE F  1 144 ? 116.549 72.407  16.160  1.00   24.21  ? 144 PHE F N   1 
ATOM   16086 C CA  . PHE F  1 144 ? 117.497 71.455  16.666  1.00   23.94  ? 144 PHE F CA  1 
ATOM   16087 C C   . PHE F  1 144 ? 116.778 70.267  17.253  1.00   26.14  ? 144 PHE F C   1 
ATOM   16088 O O   . PHE F  1 144 ? 115.567 70.180  17.196  1.00   28.42  ? 144 PHE F O   1 
ATOM   16089 C CB  . PHE F  1 144 ? 118.418 72.109  17.710  1.00   24.42  ? 144 PHE F CB  1 
ATOM   16090 C CG  . PHE F  1 144 ? 117.719 72.557  18.978  1.00   24.09  ? 144 PHE F CG  1 
ATOM   16091 C CD1 . PHE F  1 144 ? 117.078 73.779  19.035  1.00   24.40  ? 144 PHE F CD1 1 
ATOM   16092 C CD2 . PHE F  1 144 ? 117.741 71.766  20.119  1.00   22.48  ? 144 PHE F CD2 1 
ATOM   16093 C CE1 . PHE F  1 144 ? 116.466 74.185  20.191  1.00   24.38  ? 144 PHE F CE1 1 
ATOM   16094 C CE2 . PHE F  1 144 ? 117.128 72.163  21.261  1.00   22.94  ? 144 PHE F CE2 1 
ATOM   16095 C CZ  . PHE F  1 144 ? 116.486 73.378  21.305  1.00   24.12  ? 144 PHE F CZ  1 
ATOM   16096 N N   . SER F  1 145 ? 117.528 69.329  17.808  1.00   26.61  ? 145 SER F N   1 
ATOM   16097 C CA  . SER F  1 145 ? 116.904 68.154  18.385  1.00   27.66  ? 145 SER F CA  1 
ATOM   16098 C C   . SER F  1 145 ? 117.060 68.121  19.909  1.00   27.63  ? 145 SER F C   1 
ATOM   16099 O O   . SER F  1 145 ? 118.162 68.334  20.427  1.00   27.36  ? 145 SER F O   1 
ATOM   16100 C CB  . SER F  1 145 ? 117.510 66.892  17.754  1.00   26.64  ? 145 SER F CB  1 
ATOM   16101 O OG  . SER F  1 145 ? 117.012 65.725  18.376  1.00   29.81  ? 145 SER F OG  1 
ATOM   16102 N N   . CYS F  1 146 ? 115.957 67.868  20.618  1.00   27.89  ? 146 CYS F N   1 
ATOM   16103 C CA  . CYS F  1 146 ? 116.021 67.509  22.035  1.00   29.33  ? 146 CYS F CA  1 
ATOM   16104 C C   . CYS F  1 146 ? 116.216 66.011  22.175  1.00   29.55  ? 146 CYS F C   1 
ATOM   16105 O O   . CYS F  1 146 ? 115.273 65.252  22.037  1.00   32.76  ? 146 CYS F O   1 
ATOM   16106 C CB  . CYS F  1 146 ? 114.764 67.948  22.797  1.00   29.42  ? 146 CYS F CB  1 
ATOM   16107 S SG  . CYS F  1 146 ? 114.801 69.681  23.338  1.00   37.05  ? 146 CYS F SG  1 
ATOM   16108 N N   . ALA F  1 147 ? 117.440 65.604  22.475  1.00   27.20  ? 147 ALA F N   1 
ATOM   16109 C CA  . ALA F  1 147 ? 117.788 64.204  22.458  1.00   27.26  ? 147 ALA F CA  1 
ATOM   16110 C C   . ALA F  1 147 ? 117.610 63.542  23.810  1.00   33.07  ? 147 ALA F C   1 
ATOM   16111 O O   . ALA F  1 147 ? 117.661 64.210  24.845  1.00   36.09  ? 147 ALA F O   1 
ATOM   16112 C CB  . ALA F  1 147 ? 119.198 64.046  21.980  1.00   27.73  ? 147 ALA F CB  1 
ATOM   16113 N N   . PRO F  1 148 ? 117.405 62.205  23.806  1.00   37.29  ? 148 PRO F N   1 
ATOM   16114 C CA  . PRO F  1 148 ? 117.327 61.425  25.047  1.00   37.99  ? 148 PRO F CA  1 
ATOM   16115 C C   . PRO F  1 148 ? 118.620 61.505  25.833  1.00   38.70  ? 148 PRO F C   1 
ATOM   16116 O O   . PRO F  1 148 ? 119.703 61.449  25.249  1.00   38.11  ? 148 PRO F O   1 
ATOM   16117 C CB  . PRO F  1 148 ? 117.071 59.993  24.557  1.00   38.25  ? 148 PRO F CB  1 
ATOM   16118 C CG  . PRO F  1 148 ? 117.408 59.998  23.074  1.00   35.45  ? 148 PRO F CG  1 
ATOM   16119 C CD  . PRO F  1 148 ? 117.137 61.378  22.609  1.00   34.98  ? 148 PRO F CD  1 
ATOM   16120 N N   . SER F  1 149 ? 118.492 61.606  27.148  1.00   40.44  ? 149 SER F N   1 
ATOM   16121 C CA  . SER F  1 149 ? 119.623 61.846  28.033  1.00   44.46  ? 149 SER F CA  1 
ATOM   16122 C C   . SER F  1 149 ? 120.805 60.848  27.959  1.00   45.15  ? 149 SER F C   1 
ATOM   16123 O O   . SER F  1 149 ? 121.965 61.246  28.086  1.00   43.37  ? 149 SER F O   1 
ATOM   16124 C CB  . SER F  1 149 ? 119.087 61.922  29.450  1.00   51.90  ? 149 SER F CB  1 
ATOM   16125 O OG  . SER F  1 149 ? 118.544 60.667  29.825  1.00   58.56  ? 149 SER F OG  1 
ATOM   16126 N N   . PHE F  1 150 ? 120.531 59.571  27.735  1.00   38.26  ? 150 PHE F N   1 
ATOM   16127 C CA  . PHE F  1 150 ? 121.592 58.569  27.744  1.00   39.79  ? 150 PHE F CA  1 
ATOM   16128 C C   . PHE F  1 150 ? 122.599 58.855  26.634  1.00   41.78  ? 150 PHE F C   1 
ATOM   16129 O O   . PHE F  1 150 ? 123.713 58.323  26.632  1.00   44.98  ? 150 PHE F O   1 
ATOM   16130 C CB  . PHE F  1 150 ? 121.026 57.149  27.577  1.00   41.51  ? 150 PHE F CB  1 
ATOM   16131 C CG  . PHE F  1 150 ? 120.715 56.798  26.149  1.00   47.89  ? 150 PHE F CG  1 
ATOM   16132 C CD1 . PHE F  1 150 ? 121.695 56.296  25.305  1.00   45.43  ? 150 PHE F CD1 1 
ATOM   16133 C CD2 . PHE F  1 150 ? 119.450 57.011  25.631  1.00   45.11  ? 150 PHE F CD2 1 
ATOM   16134 C CE1 . PHE F  1 150 ? 121.408 56.010  23.971  1.00   42.61  ? 150 PHE F CE1 1 
ATOM   16135 C CE2 . PHE F  1 150 ? 119.157 56.711  24.304  1.00   41.77  ? 150 PHE F CE2 1 
ATOM   16136 C CZ  . PHE F  1 150 ? 120.137 56.216  23.474  1.00   40.59  ? 150 PHE F CZ  1 
ATOM   16137 N N   . LEU F  1 151 ? 122.179 59.616  25.639  1.00   34.98  ? 151 LEU F N   1 
ATOM   16138 C CA  . LEU F  1 151 ? 122.963 59.734  24.419  1.00   38.46  ? 151 LEU F CA  1 
ATOM   16139 C C   . LEU F  1 151 ? 124.269 60.510  24.661  1.00   40.74  ? 151 LEU F C   1 
ATOM   16140 O O   . LEU F  1 151 ? 125.218 60.383  23.900  1.00   41.38  ? 151 LEU F O   1 
ATOM   16141 C CB  . LEU F  1 151 ? 122.126 60.364  23.313  1.00   34.56  ? 151 LEU F CB  1 
ATOM   16142 C CG  . LEU F  1 151 ? 122.624 60.151  21.887  1.00   31.97  ? 151 LEU F CG  1 
ATOM   16143 C CD1 . LEU F  1 151 ? 122.770 58.694  21.584  1.00   31.02  ? 151 LEU F CD1 1 
ATOM   16144 C CD2 . LEU F  1 151 ? 121.627 60.767  20.935  1.00   31.15  ? 151 LEU F CD2 1 
ATOM   16145 N N   . ALA F  1 152 ? 124.299 61.368  25.675  1.00   40.67  ? 152 ALA F N   1 
ATOM   16146 C CA  . ALA F  1 152 ? 125.515 62.122  25.970  1.00   40.53  ? 152 ALA F CA  1 
ATOM   16147 C C   . ALA F  1 152 ? 126.327 61.556  27.138  1.00   48.05  ? 152 ALA F C   1 
ATOM   16148 O O   . ALA F  1 152 ? 127.336 62.144  27.536  1.00   52.28  ? 152 ALA F O   1 
ATOM   16149 C CB  . ALA F  1 152 ? 125.174 63.553  26.251  1.00   38.24  ? 152 ALA F CB  1 
ATOM   16150 N N   . GLN F  1 153 ? 125.916 60.411  27.672  1.00   49.43  ? 153 GLN F N   1 
ATOM   16151 C CA  . GLN F  1 153 ? 126.496 59.922  28.914  1.00   50.45  ? 153 GLN F CA  1 
ATOM   16152 C C   . GLN F  1 153 ? 127.836 59.292  28.680  1.00   47.51  ? 153 GLN F C   1 
ATOM   16153 O O   . GLN F  1 153 ? 128.602 59.098  29.600  1.00   45.69  ? 153 GLN F O   1 
ATOM   16154 C CB  . GLN F  1 153 ? 125.572 58.902  29.562  1.00   58.73  ? 153 GLN F CB  1 
ATOM   16155 C CG  . GLN F  1 153 ? 124.416 59.521  30.315  1.00   67.91  ? 153 GLN F CG  1 
ATOM   16156 C CD  . GLN F  1 153 ? 123.441 58.477  30.820  1.00   77.64  ? 153 GLN F CD  1 
ATOM   16157 O OE1 . GLN F  1 153 ? 123.567 57.292  30.495  1.00   82.44  ? 153 GLN F OE1 1 
ATOM   16158 N NE2 . GLN F  1 153 ? 122.423 58.917  31.561  1.00   79.65  ? 153 GLN F NE2 1 
ATOM   16159 N N   . LYS F  1 154 ? 128.143 59.027  27.427  1.00   46.62  ? 154 LYS F N   1 
ATOM   16160 C CA  . LYS F  1 154 ? 129.372 58.340  27.108  1.00   50.03  ? 154 LYS F CA  1 
ATOM   16161 C C   . LYS F  1 154 ? 130.144 58.883  25.917  1.00   48.70  ? 154 LYS F C   1 
ATOM   16162 O O   . LYS F  1 154 ? 129.569 59.207  24.881  1.00   44.42  ? 154 LYS F O   1 
ATOM   16163 C CB  . LYS F  1 154 ? 129.080 56.864  26.859  1.00   55.44  ? 154 LYS F CB  1 
ATOM   16164 C CG  . LYS F  1 154 ? 129.650 55.968  27.914  1.00   64.93  ? 154 LYS F CG  1 
ATOM   16165 C CD  . LYS F  1 154 ? 129.538 54.490  27.527  1.00   71.55  ? 154 LYS F CD  1 
ATOM   16166 C CE  . LYS F  1 154 ? 128.160 54.078  27.032  1.00   72.11  ? 154 LYS F CE  1 
ATOM   16167 N NZ  . LYS F  1 154 ? 127.256 53.771  28.195  1.00   75.21  ? 154 LYS F NZ  1 
ATOM   16168 N N   . GLY F  1 155 ? 131.459 58.970  26.089  1.00   50.63  ? 155 GLY F N   1 
ATOM   16169 C CA  . GLY F  1 155 ? 132.376 59.192  24.995  1.00   50.46  ? 155 GLY F CA  1 
ATOM   16170 C C   . GLY F  1 155 ? 132.723 60.642  24.804  1.00   50.23  ? 155 GLY F C   1 
ATOM   16171 O O   . GLY F  1 155 ? 133.666 60.974  24.099  1.00   51.32  ? 155 GLY F O   1 
ATOM   16172 N N   . LEU F  1 156 ? 131.958 61.520  25.432  1.00   48.90  ? 156 LEU F N   1 
ATOM   16173 C CA  . LEU F  1 156 ? 132.116 62.941  25.179  1.00   42.91  ? 156 LEU F CA  1 
ATOM   16174 C C   . LEU F  1 156 ? 133.008 63.619  26.208  1.00   43.03  ? 156 LEU F C   1 
ATOM   16175 O O   . LEU F  1 156 ? 133.225 63.079  27.286  1.00   44.70  ? 156 LEU F O   1 
ATOM   16176 C CB  . LEU F  1 156 ? 130.744 63.603  25.130  1.00   40.58  ? 156 LEU F CB  1 
ATOM   16177 C CG  . LEU F  1 156 ? 129.811 62.845  24.192  1.00   42.49  ? 156 LEU F CG  1 
ATOM   16178 C CD1 . LEU F  1 156 ? 128.473 63.554  24.046  1.00   40.96  ? 156 LEU F CD1 1 
ATOM   16179 C CD2 . LEU F  1 156 ? 130.471 62.651  22.832  1.00   39.75  ? 156 LEU F CD2 1 
ATOM   16180 N N   . PRO F  1 157 ? 133.539 64.809  25.870  1.00   42.44  ? 157 PRO F N   1 
ATOM   16181 C CA  . PRO F  1 157 ? 134.288 65.563  26.878  1.00   45.11  ? 157 PRO F CA  1 
ATOM   16182 C C   . PRO F  1 157 ? 133.447 65.821  28.126  1.00   46.62  ? 157 PRO F C   1 
ATOM   16183 O O   . PRO F  1 157 ? 132.227 65.706  28.104  1.00   47.46  ? 157 PRO F O   1 
ATOM   16184 C CB  . PRO F  1 157 ? 134.642 66.856  26.156  1.00   43.76  ? 157 PRO F CB  1 
ATOM   16185 C CG  . PRO F  1 157 ? 134.651 66.478  24.693  1.00   40.73  ? 157 PRO F CG  1 
ATOM   16186 C CD  . PRO F  1 157 ? 133.579 65.461  24.543  1.00   39.32  ? 157 PRO F CD  1 
ATOM   16187 N N   . ASN F  1 158 ? 134.105 66.130  29.224  1.00   47.04  ? 158 ASN F N   1 
ATOM   16188 C CA  . ASN F  1 158 ? 133.403 66.219  30.473  1.00   48.58  ? 158 ASN F CA  1 
ATOM   16189 C C   . ASN F  1 158 ? 132.407 67.366  30.406  1.00   44.80  ? 158 ASN F C   1 
ATOM   16190 O O   . ASN F  1 158 ? 132.714 68.433  29.873  1.00   41.38  ? 158 ASN F O   1 
ATOM   16191 C CB  . ASN F  1 158 ? 134.402 66.395  31.604  1.00   57.93  ? 158 ASN F CB  1 
ATOM   16192 C CG  . ASN F  1 158 ? 133.811 66.071  32.940  1.00   67.69  ? 158 ASN F CG  1 
ATOM   16193 O OD1 . ASN F  1 158 ? 133.171 66.909  33.561  1.00   70.96  ? 158 ASN F OD1 1 
ATOM   16194 N ND2 . ASN F  1 158 ? 134.015 64.835  33.395  1.00   72.88  ? 158 ASN F ND2 1 
ATOM   16195 N N   . ASN F  1 159 ? 131.199 67.107  30.898  1.00   50.53  ? 159 ASN F N   1 
ATOM   16196 C CA  . ASN F  1 159 ? 130.087 68.070  30.921  1.00   56.32  ? 159 ASN F CA  1 
ATOM   16197 C C   . ASN F  1 159 ? 129.476 68.440  29.567  1.00   48.79  ? 159 ASN F C   1 
ATOM   16198 O O   . ASN F  1 159 ? 128.604 69.302  29.495  1.00   46.33  ? 159 ASN F O   1 
ATOM   16199 C CB  . ASN F  1 159 ? 130.466 69.373  31.613  1.00   68.96  ? 159 ASN F CB  1 
ATOM   16200 C CG  . ASN F  1 159 ? 129.228 70.148  32.090  1.00   78.28  ? 159 ASN F CG  1 
ATOM   16201 O OD1 . ASN F  1 159 ? 128.211 69.550  32.473  1.00   80.43  ? 159 ASN F OD1 1 
ATOM   16202 N ND2 . ASN F  1 159 ? 129.287 71.476  32.000  1.00   81.49  ? 159 ASN F ND2 1 
ATOM   16203 N N   . VAL F  1 160 ? 129.937 67.822  28.494  1.00   44.16  ? 160 VAL F N   1 
ATOM   16204 C CA  . VAL F  1 160 ? 129.377 68.096  27.183  1.00   39.43  ? 160 VAL F CA  1 
ATOM   16205 C C   . VAL F  1 160 ? 128.005 67.395  27.049  1.00   41.94  ? 160 VAL F C   1 
ATOM   16206 O O   . VAL F  1 160 ? 127.831 66.239  27.463  1.00   43.43  ? 160 VAL F O   1 
ATOM   16207 C CB  . VAL F  1 160 ? 130.372 67.678  26.087  1.00   35.82  ? 160 VAL F CB  1 
ATOM   16208 C CG1 . VAL F  1 160 ? 129.695 67.505  24.771  1.00   31.62  ? 160 VAL F CG1 1 
ATOM   16209 C CG2 . VAL F  1 160 ? 131.484 68.712  25.974  1.00   35.86  ? 160 VAL F CG2 1 
ATOM   16210 N N   . GLN F  1 161 ? 127.028 68.128  26.508  1.00   40.46  ? 161 GLN F N   1 
ATOM   16211 C CA  . GLN F  1 161 ? 125.613 67.746  26.570  1.00   39.46  ? 161 GLN F CA  1 
ATOM   16212 C C   . GLN F  1 161 ? 124.968 67.557  25.197  1.00   37.38  ? 161 GLN F C   1 
ATOM   16213 O O   . GLN F  1 161 ? 123.745 67.610  25.060  1.00   37.27  ? 161 GLN F O   1 
ATOM   16214 C CB  . GLN F  1 161 ? 124.857 68.821  27.345  1.00   42.14  ? 161 GLN F CB  1 
ATOM   16215 C CG  . GLN F  1 161 ? 125.131 68.795  28.857  1.00   49.59  ? 161 GLN F CG  1 
ATOM   16216 C CD  . GLN F  1 161 ? 124.830 70.132  29.532  1.00   55.61  ? 161 GLN F CD  1 
ATOM   16217 O OE1 . GLN F  1 161 ? 123.717 70.650  29.433  1.00   58.20  ? 161 GLN F OE1 1 
ATOM   16218 N NE2 . GLN F  1 161 ? 125.837 70.711  30.197  1.00   57.62  ? 161 GLN F NE2 1 
ATOM   16219 N N   . GLY F  1 162 ? 125.783 67.387  24.169  1.00   32.01  ? 162 GLY F N   1 
ATOM   16220 C CA  . GLY F  1 162 ? 125.243 67.213  22.846  1.00   28.58  ? 162 GLY F CA  1 
ATOM   16221 C C   . GLY F  1 162 ? 126.293 67.484  21.817  1.00   26.31  ? 162 GLY F C   1 
ATOM   16222 O O   . GLY F  1 162 ? 127.466 67.465  22.122  1.00   28.59  ? 162 GLY F O   1 
ATOM   16223 N N   . ALA F  1 163 ? 125.879 67.728  20.587  1.00   25.73  ? 163 ALA F N   1 
ATOM   16224 C CA  . ALA F  1 163 ? 126.839 67.995  19.531  1.00   28.17  ? 163 ALA F CA  1 
ATOM   16225 C C   . ALA F  1 163 ? 126.270 69.001  18.571  1.00   28.90  ? 163 ALA F C   1 
ATOM   16226 O O   . ALA F  1 163 ? 125.078 69.070  18.370  1.00   27.36  ? 163 ALA F O   1 
ATOM   16227 C CB  . ALA F  1 163 ? 127.217 66.714  18.803  1.00   27.79  ? 163 ALA F CB  1 
ATOM   16228 N N   . LEU F  1 164 ? 127.141 69.782  17.963  1.00   30.47  ? 164 LEU F N   1 
ATOM   16229 C CA  . LEU F  1 164 ? 126.719 70.643  16.882  1.00   27.20  ? 164 LEU F CA  1 
ATOM   16230 C C   . LEU F  1 164 ? 127.215 70.067  15.545  1.00   26.61  ? 164 LEU F C   1 
ATOM   16231 O O   . LEU F  1 164 ? 128.384 69.761  15.385  1.00   29.61  ? 164 LEU F O   1 
ATOM   16232 C CB  . LEU F  1 164 ? 127.227 72.059  17.151  1.00   28.22  ? 164 LEU F CB  1 
ATOM   16233 C CG  . LEU F  1 164 ? 128.739 72.289  17.260  1.00   32.02  ? 164 LEU F CG  1 
ATOM   16234 C CD1 . LEU F  1 164 ? 129.249 73.159  16.123  1.00   32.24  ? 164 LEU F CD1 1 
ATOM   16235 C CD2 . LEU F  1 164 ? 129.195 72.805  18.623  1.00   32.00  ? 164 LEU F CD2 1 
ATOM   16236 N N   . GLY F  1 165 ? 126.308 69.896  14.593  1.00   25.50  ? 165 GLY F N   1 
ATOM   16237 C CA  . GLY F  1 165 ? 126.657 69.284  13.332  1.00   25.56  ? 165 GLY F CA  1 
ATOM   16238 C C   . GLY F  1 165 ? 126.786 70.307  12.212  1.00   24.49  ? 165 GLY F C   1 
ATOM   16239 O O   . GLY F  1 165 ? 125.958 71.208  12.095  1.00   25.87  ? 165 GLY F O   1 
ATOM   16240 N N   . LEU F  1 166 ? 127.828 70.143  11.394  1.00   21.76  ? 166 LEU F N   1 
ATOM   16241 C CA  . LEU F  1 166 ? 128.150 71.003  10.248  1.00   22.89  ? 166 LEU F CA  1 
ATOM   16242 C C   . LEU F  1 166 ? 128.092 70.250  8.924   1.00   22.71  ? 166 LEU F C   1 
ATOM   16243 O O   . LEU F  1 166 ? 128.766 70.630  7.956   1.00   23.83  ? 166 LEU F O   1 
ATOM   16244 C CB  . LEU F  1 166 ? 129.537 71.631  10.405  1.00   25.76  ? 166 LEU F CB  1 
ATOM   16245 C CG  . LEU F  1 166 ? 129.670 72.579  11.590  1.00   28.68  ? 166 LEU F CG  1 
ATOM   16246 C CD1 . LEU F  1 166 ? 131.084 73.015  11.748  1.00   29.08  ? 166 LEU F CD1 1 
ATOM   16247 C CD2 . LEU F  1 166 ? 128.820 73.768  11.355  1.00   30.34  ? 166 LEU F CD2 1 
ATOM   16248 N N   . GLY F  1 167 ? 127.303 69.170  8.906   1.00   23.64  ? 167 GLY F N   1 
ATOM   16249 C CA  . GLY F  1 167 ? 127.167 68.296  7.752   1.00   23.18  ? 167 GLY F CA  1 
ATOM   16250 C C   . GLY F  1 167 ? 126.279 68.877  6.673   1.00   23.60  ? 167 GLY F C   1 
ATOM   16251 O O   . GLY F  1 167 ? 125.604 69.884  6.860   1.00   23.47  ? 167 GLY F O   1 
ATOM   16252 N N   . GLN F  1 168 ? 126.275 68.211  5.531   1.00   25.49  ? 168 GLN F N   1 
ATOM   16253 C CA  . GLN F  1 168 ? 125.444 68.615  4.421   1.00   24.99  ? 168 GLN F CA  1 
ATOM   16254 C C   . GLN F  1 168 ? 124.043 68.090  4.585   1.00   23.63  ? 168 GLN F C   1 
ATOM   16255 O O   . GLN F  1 168 ? 123.706 67.044  4.067   1.00   25.08  ? 168 GLN F O   1 
ATOM   16256 C CB  . GLN F  1 168 ? 126.061 68.129  3.136   1.00   28.03  ? 168 GLN F CB  1 
ATOM   16257 C CG  . GLN F  1 168 ? 127.257 68.938  2.761   1.00   27.74  ? 168 GLN F CG  1 
ATOM   16258 C CD  . GLN F  1 168 ? 126.831 70.326  2.460   1.00   29.44  ? 168 GLN F CD  1 
ATOM   16259 O OE1 . GLN F  1 168 ? 126.097 70.557  1.502   1.00   32.17  ? 168 GLN F OE1 1 
ATOM   16260 N NE2 . GLN F  1 168 ? 127.235 71.263  3.295   1.00   27.84  ? 168 GLN F NE2 1 
ATOM   16261 N N   . ALA F  1 169 ? 123.233 68.841  5.326   1.00   24.68  ? 169 ALA F N   1 
ATOM   16262 C CA  . ALA F  1 169 ? 121.873 68.441  5.682   1.00   24.83  ? 169 ALA F CA  1 
ATOM   16263 C C   . ALA F  1 169 ? 121.042 69.707  6.003   1.00   25.30  ? 169 ALA F C   1 
ATOM   16264 O O   . ALA F  1 169 ? 121.612 70.706  6.452   1.00   27.25  ? 169 ALA F O   1 
ATOM   16265 C CB  . ALA F  1 169 ? 121.896 67.479  6.863   1.00   22.93  ? 169 ALA F CB  1 
ATOM   16266 N N   . PRO F  1 170 ? 119.703 69.664  5.779   1.00   25.47  ? 170 PRO F N   1 
ATOM   16267 C CA  . PRO F  1 170 ? 118.876 70.875  5.755   1.00   22.55  ? 170 PRO F CA  1 
ATOM   16268 C C   . PRO F  1 170 ? 118.838 71.635  7.056   1.00   26.14  ? 170 PRO F C   1 
ATOM   16269 O O   . PRO F  1 170 ? 118.678 72.829  6.990   1.00   28.15  ? 170 PRO F O   1 
ATOM   16270 C CB  . PRO F  1 170 ? 117.492 70.356  5.405   1.00   24.65  ? 170 PRO F CB  1 
ATOM   16271 C CG  . PRO F  1 170 ? 117.522 68.913  5.694   1.00   25.34  ? 170 PRO F CG  1 
ATOM   16272 C CD  . PRO F  1 170 ? 118.912 68.488  5.388   1.00   27.34  ? 170 PRO F CD  1 
ATOM   16273 N N   . ILE F  1 171 ? 118.969 71.017  8.223   1.00   28.17  ? 171 ILE F N   1 
ATOM   16274 C CA  . ILE F  1 171 ? 119.052 71.880  9.391   1.00   21.66  ? 171 ILE F CA  1 
ATOM   16275 C C   . ILE F  1 171 ? 120.387 71.801  10.139  1.00   22.28  ? 171 ILE F C   1 
ATOM   16276 O O   . ILE F  1 171 ? 120.450 71.985  11.352  1.00   22.67  ? 171 ILE F O   1 
ATOM   16277 C CB  . ILE F  1 171 ? 117.889 71.627  10.355  1.00   23.33  ? 171 ILE F CB  1 
ATOM   16278 C CG1 . ILE F  1 171 ? 117.880 70.189  10.888  1.00   23.19  ? 171 ILE F CG1 1 
ATOM   16279 C CG2 . ILE F  1 171 ? 116.585 72.003  9.653   1.00   23.91  ? 171 ILE F CG2 1 
ATOM   16280 C CD1 . ILE F  1 171 ? 117.141 70.056  12.173  1.00   22.38  ? 171 ILE F CD1 1 
ATOM   16281 N N   . SER F  1 172 ? 121.470 71.599  9.391   1.00   27.18  ? 172 SER F N   1 
ATOM   16282 C CA  . SER F  1 172 ? 122.809 71.718  9.953   1.00   26.17  ? 172 SER F CA  1 
ATOM   16283 C C   . SER F  1 172 ? 123.020 73.129  10.452  1.00   26.81  ? 172 SER F C   1 
ATOM   16284 O O   . SER F  1 172 ? 122.291 74.030  10.074  1.00   27.44  ? 172 SER F O   1 
ATOM   16285 C CB  . SER F  1 172 ? 123.867 71.370  8.925   1.00   25.02  ? 172 SER F CB  1 
ATOM   16286 O OG  . SER F  1 172 ? 123.812 72.261  7.843   1.00   26.21  ? 172 SER F OG  1 
ATOM   16287 N N   . LEU F  1 173 ? 124.013 73.320  11.315  1.00   27.97  ? 173 LEU F N   1 
ATOM   16288 C CA  . LEU F  1 173 ? 124.252 74.628  11.898  1.00   25.88  ? 173 LEU F CA  1 
ATOM   16289 C C   . LEU F  1 173 ? 124.589 75.657  10.850  1.00   25.25  ? 173 LEU F C   1 
ATOM   16290 O O   . LEU F  1 173 ? 123.977 76.685  10.823  1.00   26.19  ? 173 LEU F O   1 
ATOM   16291 C CB  . LEU F  1 173 ? 125.370 74.572  12.928  1.00   25.30  ? 173 LEU F CB  1 
ATOM   16292 C CG  . LEU F  1 173 ? 125.858 75.931  13.405  1.00   25.32  ? 173 LEU F CG  1 
ATOM   16293 C CD1 . LEU F  1 173 ? 124.763 76.694  14.115  1.00   25.02  ? 173 LEU F CD1 1 
ATOM   16294 C CD2 . LEU F  1 173 ? 127.023 75.763  14.328  1.00   24.58  ? 173 LEU F CD2 1 
ATOM   16295 N N   . GLN F  1 174 ? 125.523 75.382  9.955   1.00   26.35  ? 174 GLN F N   1 
ATOM   16296 C CA  . GLN F  1 174 ? 125.929 76.398  8.988   1.00   24.14  ? 174 GLN F CA  1 
ATOM   16297 C C   . GLN F  1 174 ? 124.796 76.722  8.017   1.00   26.94  ? 174 GLN F C   1 
ATOM   16298 O O   . GLN F  1 174 ? 124.630 77.858  7.604   1.00   29.30  ? 174 GLN F O   1 
ATOM   16299 C CB  . GLN F  1 174 ? 127.184 75.959  8.224   1.00   25.35  ? 174 GLN F CB  1 
ATOM   16300 C CG  . GLN F  1 174 ? 126.975 75.026  7.023   1.00   22.83  ? 174 GLN F CG  1 
ATOM   16301 C CD  . GLN F  1 174 ? 126.786 73.585  7.420   1.00   25.15  ? 174 GLN F CD  1 
ATOM   16302 O OE1 . GLN F  1 174 ? 126.837 73.256  8.595   1.00   26.27  ? 174 GLN F OE1 1 
ATOM   16303 N NE2 . GLN F  1 174 ? 126.590 72.715  6.444   1.00   25.40  ? 174 GLN F NE2 1 
ATOM   16304 N N   . ASN F  1 175 ? 124.013 75.717  7.659   1.00   28.51  ? 175 ASN F N   1 
ATOM   16305 C CA  . ASN F  1 175 ? 122.931 75.860  6.705   1.00   29.13  ? 175 ASN F CA  1 
ATOM   16306 C C   . ASN F  1 175 ? 121.910 76.865  7.254   1.00   25.45  ? 175 ASN F C   1 
ATOM   16307 O O   . ASN F  1 175 ? 121.425 77.727  6.517   1.00   24.82  ? 175 ASN F O   1 
ATOM   16308 C CB  . ASN F  1 175 ? 122.344 74.456  6.457   1.00   38.46  ? 175 ASN F CB  1 
ATOM   16309 C CG  . ASN F  1 175 ? 121.239 74.411  5.425   1.00   49.81  ? 175 ASN F CG  1 
ATOM   16310 O OD1 . ASN F  1 175 ? 120.088 74.734  5.715   1.00   53.02  ? 175 ASN F OD1 1 
ATOM   16311 N ND2 . ASN F  1 175 ? 121.571 73.933  4.223   1.00   54.92  ? 175 ASN F ND2 1 
ATOM   16312 N N   . GLN F  1 176 ? 121.620 76.795  8.551   1.00   22.99  ? 176 GLN F N   1 
ATOM   16313 C CA  . GLN F  1 176 ? 120.674 77.724  9.178   1.00   24.33  ? 176 GLN F CA  1 
ATOM   16314 C C   . GLN F  1 176 ? 121.270 79.143  9.375   1.00   25.71  ? 176 GLN F C   1 
ATOM   16315 O O   . GLN F  1 176 ? 120.578 80.146  9.275   1.00   28.26  ? 176 GLN F O   1 
ATOM   16316 C CB  . GLN F  1 176 ? 120.190 77.167  10.517  1.00   22.87  ? 176 GLN F CB  1 
ATOM   16317 C CG  . GLN F  1 176 ? 119.254 75.998  10.397  1.00   21.77  ? 176 GLN F CG  1 
ATOM   16318 C CD  . GLN F  1 176 ? 118.588 75.652  11.707  1.00   22.20  ? 176 GLN F CD  1 
ATOM   16319 O OE1 . GLN F  1 176 ? 117.691 76.350  12.160  1.00   22.65  ? 176 GLN F OE1 1 
ATOM   16320 N NE2 . GLN F  1 176 ? 119.037 74.574  12.335  1.00   22.08  ? 176 GLN F NE2 1 
ATOM   16321 N N   . LEU F  1 177 ? 122.552 79.222  9.675   1.00   24.62  ? 177 LEU F N   1 
ATOM   16322 C CA  . LEU F  1 177 ? 123.214 80.498  9.759   1.00   22.40  ? 177 LEU F CA  1 
ATOM   16323 C C   . LEU F  1 177 ? 123.348 81.157  8.391   1.00   21.30  ? 177 LEU F C   1 
ATOM   16324 O O   . LEU F  1 177 ? 123.154 82.359  8.264   1.00   23.19  ? 177 LEU F O   1 
ATOM   16325 C CB  . LEU F  1 177 ? 124.579 80.322  10.394  1.00   24.31  ? 177 LEU F CB  1 
ATOM   16326 C CG  . LEU F  1 177 ? 124.739 79.868  11.848  1.00   21.56  ? 177 LEU F CG  1 
ATOM   16327 C CD1 . LEU F  1 177 ? 126.214 79.686  12.100  1.00   22.87  ? 177 LEU F CD1 1 
ATOM   16328 C CD2 . LEU F  1 177 ? 124.167 80.841  12.847  1.00   22.04  ? 177 LEU F CD2 1 
ATOM   16329 N N   . PHE F  1 178 ? 123.722 80.387  7.378   1.00   20.96  ? 178 PHE F N   1 
ATOM   16330 C CA  . PHE F  1 178 ? 123.812 80.928  6.023   1.00   23.10  ? 178 PHE F CA  1 
ATOM   16331 C C   . PHE F  1 178 ? 122.496 81.581  5.634   1.00   26.19  ? 178 PHE F C   1 
ATOM   16332 O O   . PHE F  1 178 ? 122.471 82.702  5.145   1.00   32.37  ? 178 PHE F O   1 
ATOM   16333 C CB  . PHE F  1 178 ? 124.133 79.853  4.968   1.00   21.40  ? 178 PHE F CB  1 
ATOM   16334 C CG  . PHE F  1 178 ? 125.514 79.234  5.066   1.00   23.15  ? 178 PHE F CG  1 
ATOM   16335 C CD1 . PHE F  1 178 ? 126.554 79.861  5.708   1.00   21.77  ? 178 PHE F CD1 1 
ATOM   16336 C CD2 . PHE F  1 178 ? 125.761 78.000  4.466   1.00   22.31  ? 178 PHE F CD2 1 
ATOM   16337 C CE1 . PHE F  1 178 ? 127.793 79.266  5.775   1.00   23.00  ? 178 PHE F CE1 1 
ATOM   16338 C CE2 . PHE F  1 178 ? 127.011 77.408  4.529   1.00   23.63  ? 178 PHE F CE2 1 
ATOM   16339 C CZ  . PHE F  1 178 ? 128.025 78.040  5.186   1.00   22.93  ? 178 PHE F CZ  1 
ATOM   16340 N N   . SER F  1 179 ? 121.395 80.865  5.826   1.00   25.42  ? 179 SER F N   1 
ATOM   16341 C CA  . SER F  1 179 ? 120.109 81.315  5.306   1.00   27.50  ? 179 SER F CA  1 
ATOM   16342 C C   . SER F  1 179 ? 119.491 82.423  6.162   1.00   25.68  ? 179 SER F C   1 
ATOM   16343 O O   . SER F  1 179 ? 118.815 83.279  5.645   1.00   27.71  ? 179 SER F O   1 
ATOM   16344 C CB  . SER F  1 179 ? 119.140 80.138  5.163   1.00   31.69  ? 179 SER F CB  1 
ATOM   16345 O OG  . SER F  1 179 ? 118.616 79.746  6.409   1.00   37.61  ? 179 SER F OG  1 
ATOM   16346 N N   . HIS F  1 180 ? 119.719 82.422  7.465   1.00   22.19  ? 180 HIS F N   1 
ATOM   16347 C CA  . HIS F  1 180 ? 119.151 83.468  8.269   1.00   22.63  ? 180 HIS F CA  1 
ATOM   16348 C C   . HIS F  1 180 ? 119.763 84.793  7.970   1.00   26.98  ? 180 HIS F C   1 
ATOM   16349 O O   . HIS F  1 180 ? 119.066 85.794  7.931   1.00   31.41  ? 180 HIS F O   1 
ATOM   16350 C CB  . HIS F  1 180 ? 119.333 83.214  9.756   1.00   24.82  ? 180 HIS F CB  1 
ATOM   16351 C CG  . HIS F  1 180 ? 118.605 84.204  10.617  1.00   27.01  ? 180 HIS F CG  1 
ATOM   16352 N ND1 . HIS F  1 180 ? 117.234 84.201  10.773  1.00   30.72  ? 180 HIS F ND1 1 
ATOM   16353 C CD2 . HIS F  1 180 ? 119.054 85.262  11.330  1.00   27.75  ? 180 HIS F CD2 1 
ATOM   16354 C CE1 . HIS F  1 180 ? 116.877 85.190  11.569  1.00   29.71  ? 180 HIS F CE1 1 
ATOM   16355 N NE2 . HIS F  1 180 ? 117.965 85.856  11.915  1.00   29.95  ? 180 HIS F NE2 1 
ATOM   16356 N N   . PHE F  1 181 ? 121.067 84.819  7.768   1.00   24.19  ? 181 PHE F N   1 
ATOM   16357 C CA  . PHE F  1 181 ? 121.757 86.086  7.641   1.00   24.47  ? 181 PHE F CA  1 
ATOM   16358 C C   . PHE F  1 181 ? 122.116 86.364  6.222   1.00   27.34  ? 181 PHE F C   1 
ATOM   16359 O O   . PHE F  1 181 ? 122.675 87.388  5.946   1.00   32.58  ? 181 PHE F O   1 
ATOM   16360 C CB  . PHE F  1 181 ? 123.032 86.117  8.495   1.00   22.75  ? 181 PHE F CB  1 
ATOM   16361 C CG  . PHE F  1 181 ? 122.787 86.088  9.982   1.00   23.54  ? 181 PHE F CG  1 
ATOM   16362 C CD1 . PHE F  1 181 ? 122.358 87.217  10.647  1.00   26.19  ? 181 PHE F CD1 1 
ATOM   16363 C CD2 . PHE F  1 181 ? 122.999 84.937  10.711  1.00   25.00  ? 181 PHE F CD2 1 
ATOM   16364 C CE1 . PHE F  1 181 ? 122.147 87.207  12.015  1.00   27.01  ? 181 PHE F CE1 1 
ATOM   16365 C CE2 . PHE F  1 181 ? 122.777 84.910  12.082  1.00   24.75  ? 181 PHE F CE2 1 
ATOM   16366 C CZ  . PHE F  1 181 ? 122.360 86.056  12.734  1.00   25.72  ? 181 PHE F CZ  1 
ATOM   16367 N N   . GLY F  1 182 ? 121.822 85.440  5.323   1.00   27.68  ? 182 GLY F N   1 
ATOM   16368 C CA  . GLY F  1 182 ? 122.168 85.611  3.925   1.00   26.33  ? 182 GLY F CA  1 
ATOM   16369 C C   . GLY F  1 182 ? 123.669 85.561  3.665   1.00   26.52  ? 182 GLY F C   1 
ATOM   16370 O O   . GLY F  1 182 ? 124.167 86.310  2.839   1.00   28.43  ? 182 GLY F O   1 
ATOM   16371 N N   . LEU F  1 183 ? 124.388 84.680  4.353   1.00   25.91  ? 183 LEU F N   1 
ATOM   16372 C CA  . LEU F  1 183 ? 125.847 84.580  4.220   1.00   27.37  ? 183 LEU F CA  1 
ATOM   16373 C C   . LEU F  1 183 ? 126.293 83.847  2.960   1.00   32.83  ? 183 LEU F C   1 
ATOM   16374 O O   . LEU F  1 183 ? 125.531 83.038  2.404   1.00   36.70  ? 183 LEU F O   1 
ATOM   16375 C CB  . LEU F  1 183 ? 126.451 83.863  5.439   1.00   23.69  ? 183 LEU F CB  1 
ATOM   16376 C CG  . LEU F  1 183 ? 126.190 84.421  6.833   1.00   24.69  ? 183 LEU F CG  1 
ATOM   16377 C CD1 . LEU F  1 183 ? 126.689 83.471  7.897   1.00   23.18  ? 183 LEU F CD1 1 
ATOM   16378 C CD2 . LEU F  1 183 ? 126.900 85.750  6.970   1.00   27.26  ? 183 LEU F CD2 1 
ATOM   16379 N N   . LYS F  1 184 ? 127.536 84.095  2.528   1.00   31.07  ? 184 LYS F N   1 
ATOM   16380 C CA  . LYS F  1 184 ? 128.148 83.278  1.477   1.00   28.89  ? 184 LYS F CA  1 
ATOM   16381 C C   . LYS F  1 184 ? 128.229 81.848  2.015   1.00   26.78  ? 184 LYS F C   1 
ATOM   16382 O O   . LYS F  1 184 ? 128.569 81.661  3.178   1.00   27.13  ? 184 LYS F O   1 
ATOM   16383 C CB  . LYS F  1 184 ? 129.533 83.822  1.089   1.00   29.33  ? 184 LYS F CB  1 
ATOM   16384 C CG  . LYS F  1 184 ? 130.318 82.939  0.077   1.00   57.73  ? 184 LYS F CG  1 
ATOM   16385 C CD  . LYS F  1 184 ? 131.501 83.684  -0.598  1.00   62.35  ? 184 LYS F CD  1 
ATOM   16386 C CE  . LYS F  1 184 ? 132.264 82.812  -1.611  1.00   64.17  ? 184 LYS F CE  1 
ATOM   16387 N NZ  . LYS F  1 184 ? 132.614 81.429  -1.151  1.00   64.03  ? 184 LYS F NZ  1 
ATOM   16388 N N   . ARG F  1 185 ? 127.939 80.850  1.172   1.00   26.14  ? 185 ARG F N   1 
ATOM   16389 C CA  . ARG F  1 185 ? 127.913 79.452  1.593   1.00   22.72  ? 185 ARG F CA  1 
ATOM   16390 C C   . ARG F  1 185 ? 129.316 78.868  1.650   1.00   23.61  ? 185 ARG F C   1 
ATOM   16391 O O   . ARG F  1 185 ? 129.802 78.244  0.735   1.00   24.74  ? 185 ARG F O   1 
ATOM   16392 C CB  . ARG F  1 185 ? 127.018 78.644  0.664   1.00   24.88  ? 185 ARG F CB  1 
ATOM   16393 C CG  . ARG F  1 185 ? 125.600 79.230  0.593   1.00   26.20  ? 185 ARG F CG  1 
ATOM   16394 C CD  . ARG F  1 185 ? 124.579 78.379  -0.166  1.00   28.73  ? 185 ARG F CD  1 
ATOM   16395 N NE  . ARG F  1 185 ? 124.176 77.201  0.595   1.00   28.42  ? 185 ARG F NE  1 
ATOM   16396 C CZ  . ARG F  1 185 ? 123.200 77.173  1.494   1.00   27.13  ? 185 ARG F CZ  1 
ATOM   16397 N NH1 . ARG F  1 185 ? 122.949 76.043  2.127   1.00   27.53  ? 185 ARG F NH1 1 
ATOM   16398 N NH2 . ARG F  1 185 ? 122.484 78.265  1.771   1.00   29.03  ? 185 ARG F NH2 1 
ATOM   16399 N N   . GLN F  1 186 ? 129.956 79.114  2.768   1.00   22.93  ? 186 GLN F N   1 
ATOM   16400 C CA  . GLN F  1 186 ? 131.323 78.748  2.962   1.00   24.20  ? 186 GLN F CA  1 
ATOM   16401 C C   . GLN F  1 186 ? 131.565 78.772  4.455   1.00   24.00  ? 186 GLN F C   1 
ATOM   16402 O O   . GLN F  1 186 ? 131.102 79.688  5.131   1.00   24.29  ? 186 GLN F O   1 
ATOM   16403 C CB  . GLN F  1 186 ? 132.221 79.740  2.230   1.00   26.13  ? 186 GLN F CB  1 
ATOM   16404 C CG  . GLN F  1 186 ? 133.706 79.490  2.314   1.00   31.71  ? 186 GLN F CG  1 
ATOM   16405 C CD  . GLN F  1 186 ? 134.464 80.720  1.860   1.00   37.35  ? 186 GLN F CD  1 
ATOM   16406 O OE1 . GLN F  1 186 ? 134.506 81.031  0.684   1.00   42.40  ? 186 GLN F OE1 1 
ATOM   16407 N NE2 . GLN F  1 186 ? 135.021 81.450  2.801   1.00   37.30  ? 186 GLN F NE2 1 
ATOM   16408 N N   . PHE F  1 187 ? 132.260 77.781  4.989   1.00   25.83  ? 187 PHE F N   1 
ATOM   16409 C CA  . PHE F  1 187 ? 132.742 77.925  6.361   1.00   27.28  ? 187 PHE F CA  1 
ATOM   16410 C C   . PHE F  1 187 ? 134.190 77.445  6.446   1.00   25.28  ? 187 PHE F C   1 
ATOM   16411 O O   . PHE F  1 187 ? 134.678 76.714  5.577   1.00   22.73  ? 187 PHE F O   1 
ATOM   16412 C CB  . PHE F  1 187 ? 131.845 77.197  7.390   1.00   27.73  ? 187 PHE F CB  1 
ATOM   16413 C CG  . PHE F  1 187 ? 131.855 75.698  7.283   1.00   26.91  ? 187 PHE F CG  1 
ATOM   16414 C CD1 . PHE F  1 187 ? 130.972 75.041  6.454   1.00   28.46  ? 187 PHE F CD1 1 
ATOM   16415 C CD2 . PHE F  1 187 ? 132.744 74.952  8.023   1.00   24.87  ? 187 PHE F CD2 1 
ATOM   16416 C CE1 . PHE F  1 187 ? 130.990 73.658  6.367   1.00   29.15  ? 187 PHE F CE1 1 
ATOM   16417 C CE2 . PHE F  1 187 ? 132.773 73.575  7.936   1.00   23.29  ? 187 PHE F CE2 1 
ATOM   16418 C CZ  . PHE F  1 187 ? 131.903 72.924  7.117   1.00   25.96  ? 187 PHE F CZ  1 
ATOM   16419 N N   . SER F  1 188 ? 134.892 77.949  7.455   1.00   24.28  ? 188 SER F N   1 
ATOM   16420 C CA  . SER F  1 188 ? 136.306 77.682  7.608   1.00   27.39  ? 188 SER F CA  1 
ATOM   16421 C C   . SER F  1 188 ? 136.644 77.178  9.001   1.00   29.60  ? 188 SER F C   1 
ATOM   16422 O O   . SER F  1 188 ? 136.174 77.702  10.002  1.00   29.64  ? 188 SER F O   1 
ATOM   16423 C CB  . SER F  1 188 ? 137.113 78.932  7.317   1.00   31.29  ? 188 SER F CB  1 
ATOM   16424 O OG  . SER F  1 188 ? 136.831 79.370  6.004   1.00   36.67  ? 188 SER F OG  1 
ATOM   16425 N N   . VAL F  1 189 ? 137.509 76.181  9.046   1.00   29.83  ? 189 VAL F N   1 
ATOM   16426 C CA  . VAL F  1 189 ? 137.890 75.547  10.285  1.00   29.98  ? 189 VAL F CA  1 
ATOM   16427 C C   . VAL F  1 189 ? 139.367 75.741  10.649  1.00   30.19  ? 189 VAL F C   1 
ATOM   16428 O O   . VAL F  1 189 ? 140.262 75.405  9.883   1.00   33.93  ? 189 VAL F O   1 
ATOM   16429 C CB  . VAL F  1 189 ? 137.579 74.062  10.193  1.00   30.85  ? 189 VAL F CB  1 
ATOM   16430 C CG1 . VAL F  1 189 ? 137.912 73.367  11.487  1.00   31.11  ? 189 VAL F CG1 1 
ATOM   16431 C CG2 . VAL F  1 189 ? 136.114 73.875  9.812   1.00   30.18  ? 189 VAL F CG2 1 
ATOM   16432 N N   . CYS F  1 190 ? 139.625 76.301  11.820  1.00   28.37  ? 190 CYS F N   1 
ATOM   16433 C CA  . CYS F  1 190 ? 140.991 76.378  12.294  1.00   31.26  ? 190 CYS F CA  1 
ATOM   16434 C C   . CYS F  1 190 ? 141.079 75.857  13.720  1.00   34.34  ? 190 CYS F C   1 
ATOM   16435 O O   . CYS F  1 190 ? 141.022 76.618  14.679  1.00   33.85  ? 190 CYS F O   1 
ATOM   16436 C CB  . CYS F  1 190 ? 141.503 77.810  12.206  1.00   32.67  ? 190 CYS F CB  1 
ATOM   16437 S SG  . CYS F  1 190 ? 143.309 77.989  12.005  1.00   40.95  ? 190 CYS F SG  1 
ATOM   16438 N N   . LEU F  1 191 ? 141.265 74.552  13.861  1.00   38.13  ? 191 LEU F N   1 
ATOM   16439 C CA  . LEU F  1 191 ? 141.326 73.945  15.179  1.00   34.18  ? 191 LEU F CA  1 
ATOM   16440 C C   . LEU F  1 191 ? 142.643 74.176  15.845  1.00   34.24  ? 191 LEU F C   1 
ATOM   16441 O O   . LEU F  1 191 ? 143.684 74.139  15.201  1.00   36.68  ? 191 LEU F O   1 
ATOM   16442 C CB  . LEU F  1 191 ? 141.094 72.462  15.083  1.00   28.86  ? 191 LEU F CB  1 
ATOM   16443 C CG  . LEU F  1 191 ? 139.822 72.043  14.396  1.00   26.84  ? 191 LEU F CG  1 
ATOM   16444 C CD1 . LEU F  1 191 ? 139.713 70.514  14.467  1.00   28.91  ? 191 LEU F CD1 1 
ATOM   16445 C CD2 . LEU F  1 191 ? 138.676 72.738  15.087  1.00   29.44  ? 191 LEU F CD2 1 
ATOM   16446 N N   . SER F  1 192 ? 142.598 74.401  17.147  1.00   35.74  ? 192 SER F N   1 
ATOM   16447 C CA  . SER F  1 192 ? 143.811 74.575  17.913  1.00   37.08  ? 192 SER F CA  1 
ATOM   16448 C C   . SER F  1 192 ? 144.256 73.276  18.578  1.00   40.93  ? 192 SER F C   1 
ATOM   16449 O O   . SER F  1 192 ? 143.448 72.550  19.145  1.00   40.79  ? 192 SER F O   1 
ATOM   16450 C CB  . SER F  1 192 ? 143.611 75.672  18.936  1.00   35.03  ? 192 SER F CB  1 
ATOM   16451 O OG  . SER F  1 192 ? 144.746 75.818  19.737  1.00   37.80  ? 192 SER F OG  1 
ATOM   16452 N N   . ARG F  1 193 ? 145.548 72.977  18.471  1.00   45.09  ? 193 ARG F N   1 
ATOM   16453 C CA  . ARG F  1 193 ? 146.177 71.805  19.096  1.00   48.30  ? 193 ARG F CA  1 
ATOM   16454 C C   . ARG F  1 193 ? 146.188 71.761  20.617  1.00   48.52  ? 193 ARG F C   1 
ATOM   16455 O O   . ARG F  1 193 ? 146.310 70.695  21.220  1.00   48.33  ? 193 ARG F O   1 
ATOM   16456 C CB  . ARG F  1 193 ? 147.626 71.729  18.665  1.00   56.62  ? 193 ARG F CB  1 
ATOM   16457 C CG  . ARG F  1 193 ? 148.045 70.393  18.233  1.00   67.02  ? 193 ARG F CG  1 
ATOM   16458 C CD  . ARG F  1 193 ? 149.510 70.419  17.999  1.00   79.47  ? 193 ARG F CD  1 
ATOM   16459 N NE  . ARG F  1 193 ? 149.811 69.743  16.756  1.00   89.36  ? 193 ARG F NE  1 
ATOM   16460 C CZ  . ARG F  1 193 ? 150.887 69.998  16.030  1.00   99.20  ? 193 ARG F CZ  1 
ATOM   16461 N NH1 . ARG F  1 193 ? 151.764 70.909  16.441  1.00   102.44 ? 193 ARG F NH1 1 
ATOM   16462 N NH2 . ARG F  1 193 ? 151.080 69.345  14.895  1.00   103.58 ? 193 ARG F NH2 1 
ATOM   16463 N N   . TYR F  1 194 ? 146.099 72.941  21.217  1.00   49.56  ? 194 TYR F N   1 
ATOM   16464 C CA  . TYR F  1 194 ? 146.277 73.134  22.647  1.00   53.82  ? 194 TYR F CA  1 
ATOM   16465 C C   . TYR F  1 194 ? 144.974 73.298  23.397  1.00   49.42  ? 194 TYR F C   1 
ATOM   16466 O O   . TYR F  1 194 ? 144.124 74.082  23.007  1.00   45.97  ? 194 TYR F O   1 
ATOM   16467 C CB  . TYR F  1 194 ? 147.125 74.377  22.894  1.00   62.27  ? 194 TYR F CB  1 
ATOM   16468 C CG  . TYR F  1 194 ? 148.281 74.507  21.944  1.00   68.56  ? 194 TYR F CG  1 
ATOM   16469 C CD1 . TYR F  1 194 ? 149.433 73.753  22.119  1.00   72.99  ? 194 TYR F CD1 1 
ATOM   16470 C CD2 . TYR F  1 194 ? 148.215 75.379  20.861  1.00   70.02  ? 194 TYR F CD2 1 
ATOM   16471 C CE1 . TYR F  1 194 ? 150.496 73.865  21.243  1.00   77.67  ? 194 TYR F CE1 1 
ATOM   16472 C CE2 . TYR F  1 194 ? 149.272 75.501  19.976  1.00   73.80  ? 194 TYR F CE2 1 
ATOM   16473 C CZ  . TYR F  1 194 ? 150.414 74.740  20.172  1.00   78.76  ? 194 TYR F CZ  1 
ATOM   16474 O OH  . TYR F  1 194 ? 151.485 74.847  19.302  1.00   83.08  ? 194 TYR F OH  1 
ATOM   16475 N N   . SER F  1 195 ? 144.839 72.612  24.519  1.00   52.67  ? 195 SER F N   1 
ATOM   16476 C CA  . SER F  1 195 ? 143.635 72.755  25.323  1.00   53.27  ? 195 SER F CA  1 
ATOM   16477 C C   . SER F  1 195 ? 143.560 74.142  25.972  1.00   52.78  ? 195 SER F C   1 
ATOM   16478 O O   . SER F  1 195 ? 142.488 74.563  26.397  1.00   52.78  ? 195 SER F O   1 
ATOM   16479 C CB  . SER F  1 195 ? 143.579 71.652  26.389  1.00   57.74  ? 195 SER F CB  1 
ATOM   16480 O OG  . SER F  1 195 ? 144.735 71.660  27.216  1.00   62.70  ? 195 SER F OG  1 
ATOM   16481 N N   . THR F  1 196 ? 144.697 74.842  26.015  1.00   51.51  ? 196 THR F N   1 
ATOM   16482 C CA  . THR F  1 196 ? 144.843 76.122  26.707  1.00   50.85  ? 196 THR F CA  1 
ATOM   16483 C C   . THR F  1 196 ? 144.562 77.375  25.878  1.00   51.20  ? 196 THR F C   1 
ATOM   16484 O O   . THR F  1 196 ? 144.640 78.485  26.394  1.00   51.19  ? 196 THR F O   1 
ATOM   16485 C CB  . THR F  1 196 ? 146.255 76.271  27.248  1.00   53.01  ? 196 THR F CB  1 
ATOM   16486 O OG1 . THR F  1 196 ? 147.177 76.315  26.150  1.00   53.60  ? 196 THR F OG1 1 
ATOM   16487 C CG2 . THR F  1 196 ? 146.594 75.110  28.176  1.00   55.06  ? 196 THR F CG2 1 
ATOM   16488 N N   . SER F  1 197 ? 144.276 77.206  24.593  1.00   50.55  ? 197 SER F N   1 
ATOM   16489 C CA  . SER F  1 197 ? 143.883 78.323  23.737  1.00   51.51  ? 197 SER F CA  1 
ATOM   16490 C C   . SER F  1 197 ? 142.874 77.865  22.670  1.00   53.51  ? 197 SER F C   1 
ATOM   16491 O O   . SER F  1 197 ? 142.853 76.699  22.275  1.00   56.56  ? 197 SER F O   1 
ATOM   16492 C CB  . SER F  1 197 ? 145.108 78.982  23.097  1.00   53.08  ? 197 SER F CB  1 
ATOM   16493 O OG  . SER F  1 197 ? 145.855 78.085  22.307  1.00   54.82  ? 197 SER F OG  1 
ATOM   16494 N N   . ASN F  1 198 ? 141.993 78.769  22.254  1.00   49.16  ? 198 ASN F N   1 
ATOM   16495 C CA  . ASN F  1 198 ? 140.927 78.411  21.330  1.00   43.31  ? 198 ASN F CA  1 
ATOM   16496 C C   . ASN F  1 198 ? 141.315 78.433  19.863  1.00   38.35  ? 198 ASN F C   1 
ATOM   16497 O O   . ASN F  1 198 ? 142.238 79.131  19.460  1.00   39.48  ? 198 ASN F O   1 
ATOM   16498 C CB  . ASN F  1 198 ? 139.726 79.331  21.531  1.00   45.11  ? 198 ASN F CB  1 
ATOM   16499 C CG  . ASN F  1 198 ? 138.995 79.062  22.834  1.00   47.25  ? 198 ASN F CG  1 
ATOM   16500 O OD1 . ASN F  1 198 ? 139.189 78.030  23.482  1.00   49.66  ? 198 ASN F OD1 1 
ATOM   16501 N ND2 . ASN F  1 198 ? 138.129 79.978  23.210  1.00   47.12  ? 198 ASN F ND2 1 
ATOM   16502 N N   . GLY F  1 199 ? 140.595 77.633  19.083  1.00   35.92  ? 199 GLY F N   1 
ATOM   16503 C CA  . GLY F  1 199 ? 140.592 77.708  17.636  1.00   32.64  ? 199 GLY F CA  1 
ATOM   16504 C C   . GLY F  1 199 ? 139.236 78.281  17.300  1.00   29.88  ? 199 GLY F C   1 
ATOM   16505 O O   . GLY F  1 199 ? 138.556 78.756  18.184  1.00   31.04  ? 199 GLY F O   1 
ATOM   16506 N N   . ALA F  1 200 ? 138.827 78.244  16.042  1.00   28.25  ? 200 ALA F N   1 
ATOM   16507 C CA  . ALA F  1 200 ? 137.549 78.837  15.690  1.00   30.29  ? 200 ALA F CA  1 
ATOM   16508 C C   . ALA F  1 200 ? 136.895 78.217  14.483  1.00   28.45  ? 200 ALA F C   1 
ATOM   16509 O O   . ALA F  1 200 ? 137.554 77.612  13.655  1.00   30.76  ? 200 ALA F O   1 
ATOM   16510 C CB  . ALA F  1 200 ? 137.724 80.323  15.446  1.00   33.42  ? 200 ALA F CB  1 
ATOM   16511 N N   . ILE F  1 201 ? 135.591 78.410  14.377  1.00   27.28  ? 201 ILE F N   1 
ATOM   16512 C CA  . ILE F  1 201 ? 134.908 78.195  13.121  1.00   27.69  ? 201 ILE F CA  1 
ATOM   16513 C C   . ILE F  1 201 ? 134.363 79.520  12.603  1.00   29.56  ? 201 ILE F C   1 
ATOM   16514 O O   . ILE F  1 201 ? 133.749 80.289  13.350  1.00   29.95  ? 201 ILE F O   1 
ATOM   16515 C CB  . ILE F  1 201 ? 133.750 77.230  13.263  1.00   28.27  ? 201 ILE F CB  1 
ATOM   16516 C CG1 . ILE F  1 201 ? 134.152 76.072  14.171  1.00   29.71  ? 201 ILE F CG1 1 
ATOM   16517 C CG2 . ILE F  1 201 ? 133.205 76.825  11.881  1.00   26.20  ? 201 ILE F CG2 1 
ATOM   16518 C CD1 . ILE F  1 201 ? 135.111 75.156  13.585  1.00   31.13  ? 201 ILE F CD1 1 
ATOM   16519 N N   . LEU F  1 202 ? 134.593 79.776  11.318  1.00   28.86  ? 202 LEU F N   1 
ATOM   16520 C CA  . LEU F  1 202 ? 134.129 80.995  10.658  1.00   29.42  ? 202 LEU F CA  1 
ATOM   16521 C C   . LEU F  1 202 ? 133.085 80.711  9.604   1.00   29.17  ? 202 LEU F C   1 
ATOM   16522 O O   . LEU F  1 202 ? 133.271 79.825  8.775   1.00   31.67  ? 202 LEU F O   1 
ATOM   16523 C CB  . LEU F  1 202 ? 135.279 81.745  10.013  1.00   29.84  ? 202 LEU F CB  1 
ATOM   16524 C CG  . LEU F  1 202 ? 135.965 82.802  10.854  1.00   34.24  ? 202 LEU F CG  1 
ATOM   16525 C CD1 . LEU F  1 202 ? 136.628 82.224  12.034  1.00   37.14  ? 202 LEU F CD1 1 
ATOM   16526 C CD2 . LEU F  1 202 ? 136.982 83.461  9.986   1.00   38.71  ? 202 LEU F CD2 1 
ATOM   16527 N N   . PHE F  1 203 ? 132.008 81.495  9.627   1.00   27.00  ? 203 PHE F N   1 
ATOM   16528 C CA  . PHE F  1 203 ? 130.888 81.308  8.714   1.00   25.41  ? 203 PHE F CA  1 
ATOM   16529 C C   . PHE F  1 203 ? 130.738 82.511  7.825   1.00   24.33  ? 203 PHE F C   1 
ATOM   16530 O O   . PHE F  1 203 ? 130.539 83.597  8.312   1.00   24.63  ? 203 PHE F O   1 
ATOM   16531 C CB  . PHE F  1 203 ? 129.582 81.053  9.483   1.00   24.46  ? 203 PHE F CB  1 
ATOM   16532 C CG  . PHE F  1 203 ? 129.635 79.852  10.401  1.00   28.27  ? 203 PHE F CG  1 
ATOM   16533 C CD1 . PHE F  1 203 ? 130.067 79.983  11.721  1.00   27.07  ? 203 PHE F CD1 1 
ATOM   16534 C CD2 . PHE F  1 203 ? 129.263 78.598  9.941   1.00   27.61  ? 203 PHE F CD2 1 
ATOM   16535 C CE1 . PHE F  1 203 ? 130.103 78.909  12.554  1.00   25.24  ? 203 PHE F CE1 1 
ATOM   16536 C CE2 . PHE F  1 203 ? 129.303 77.510  10.780  1.00   26.83  ? 203 PHE F CE2 1 
ATOM   16537 C CZ  . PHE F  1 203 ? 129.729 77.663  12.084  1.00   27.20  ? 203 PHE F CZ  1 
ATOM   16538 N N   . GLY F  1 204 ? 130.815 82.303  6.516   1.00   24.47  ? 204 GLY F N   1 
ATOM   16539 C CA  . GLY F  1 204 ? 130.777 83.400  5.578   1.00   23.62  ? 204 GLY F CA  1 
ATOM   16540 C C   . GLY F  1 204 ? 132.040 83.523  4.757   1.00   26.25  ? 204 GLY F C   1 
ATOM   16541 O O   . GLY F  1 204 ? 132.946 82.733  4.890   1.00   29.74  ? 204 GLY F O   1 
ATOM   16542 N N   . ASP F  1 205 ? 132.097 84.552  3.926   1.00   30.51  ? 205 ASP F N   1 
ATOM   16543 C CA  . ASP F  1 205 ? 133.181 84.796  2.995   1.00   36.90  ? 205 ASP F CA  1 
ATOM   16544 C C   . ASP F  1 205 ? 134.409 85.301  3.725   1.00   39.27  ? 205 ASP F C   1 
ATOM   16545 O O   . ASP F  1 205 ? 134.366 86.318  4.416   1.00   40.54  ? 205 ASP F O   1 
ATOM   16546 C CB  . ASP F  1 205 ? 132.736 85.833  1.955   1.00   45.33  ? 205 ASP F CB  1 
ATOM   16547 C CG  . ASP F  1 205 ? 133.719 86.012  0.825   1.00   52.90  ? 205 ASP F CG  1 
ATOM   16548 O OD1 . ASP F  1 205 ? 134.666 85.204  0.668   1.00   55.77  ? 205 ASP F OD1 1 
ATOM   16549 O OD2 . ASP F  1 205 ? 133.511 86.974  0.068   1.00   57.59  1 205 ASP F OD2 1 
ATOM   16550 N N   . ILE F  1 206 ? 135.506 84.579  3.601   1.00   40.22  ? 206 ILE F N   1 
ATOM   16551 C CA  . ILE F  1 206 ? 136.727 85.042  4.210   1.00   41.13  ? 206 ILE F CA  1 
ATOM   16552 C C   . ILE F  1 206 ? 137.557 85.791  3.192   1.00   42.87  ? 206 ILE F C   1 
ATOM   16553 O O   . ILE F  1 206 ? 138.641 86.252  3.503   1.00   46.18  ? 206 ILE F O   1 
ATOM   16554 C CB  . ILE F  1 206 ? 137.583 83.901  4.725   1.00   40.71  ? 206 ILE F CB  1 
ATOM   16555 C CG1 . ILE F  1 206 ? 137.825 82.910  3.590   1.00   41.04  ? 206 ILE F CG1 1 
ATOM   16556 C CG2 . ILE F  1 206 ? 136.959 83.244  5.917   1.00   38.27  ? 206 ILE F CG2 1 
ATOM   16557 C CD1 . ILE F  1 206 ? 138.711 81.811  3.980   1.00   43.33  ? 206 ILE F CD1 1 
ATOM   16558 N N   . ASN F  1 207 ? 137.092 85.907  1.965   1.00   44.95  ? 207 ASN F N   1 
ATOM   16559 C CA  . ASN F  1 207 ? 137.987 86.510  1.011   1.00   54.15  ? 207 ASN F CA  1 
ATOM   16560 C C   . ASN F  1 207 ? 137.562 87.857  0.465   1.00   53.84  ? 207 ASN F C   1 
ATOM   16561 O O   . ASN F  1 207 ? 137.797 88.131  -0.707  1.00   53.36  ? 207 ASN F O   1 
ATOM   16562 C CB  . ASN F  1 207 ? 138.291 85.537  -0.130  1.00   63.92  ? 207 ASN F CB  1 
ATOM   16563 C CG  . ASN F  1 207 ? 139.792 85.481  -0.445  1.00   73.51  ? 207 ASN F CG  1 
ATOM   16564 O OD1 . ASN F  1 207 ? 140.582 86.301  0.052   1.00   77.38  ? 207 ASN F OD1 1 
ATOM   16565 N ND2 . ASN F  1 207 ? 140.188 84.515  -1.257  1.00   76.79  ? 207 ASN F ND2 1 
ATOM   16566 N N   . ASP F  1 208 ? 136.868 88.671  1.254   1.00   53.67  ? 208 ASP F N   1 
ATOM   16567 C CA  . ASP F  1 208 ? 136.575 90.013  0.766   1.00   56.77  ? 208 ASP F CA  1 
ATOM   16568 C C   . ASP F  1 208 ? 137.314 91.068  1.608   1.00   55.66  ? 208 ASP F C   1 
ATOM   16569 O O   . ASP F  1 208 ? 136.657 91.859  2.277   1.00   53.05  ? 208 ASP F O   1 
ATOM   16570 C CB  . ASP F  1 208 ? 135.074 90.254  0.770   1.00   57.69  ? 208 ASP F CB  1 
ATOM   16571 C CG  . ASP F  1 208 ? 134.702 91.567  0.130   1.00   61.93  ? 208 ASP F CG  1 
ATOM   16572 O OD1 . ASP F  1 208 ? 135.588 92.179  -0.511  1.00   60.20  ? 208 ASP F OD1 1 
ATOM   16573 O OD2 . ASP F  1 208 ? 133.518 91.958  0.243   1.00   65.48  1 208 ASP F OD2 1 
ATOM   16574 N N   . PRO F  1 209 ? 138.678 91.084  1.568   1.00   56.49  ? 209 PRO F N   1 
ATOM   16575 C CA  . PRO F  1 209 ? 139.512 91.977  2.399   1.00   60.37  ? 209 PRO F CA  1 
ATOM   16576 C C   . PRO F  1 209 ? 139.067 93.413  2.370   1.00   67.76  ? 209 PRO F C   1 
ATOM   16577 O O   . PRO F  1 209 ? 139.202 94.136  3.350   1.00   71.11  ? 209 PRO F O   1 
ATOM   16578 C CB  . PRO F  1 209 ? 140.906 91.868  1.765   1.00   57.64  ? 209 PRO F CB  1 
ATOM   16579 C CG  . PRO F  1 209 ? 140.675 91.322  0.422   1.00   55.56  ? 209 PRO F CG  1 
ATOM   16580 C CD  . PRO F  1 209 ? 139.500 90.425  0.535   1.00   52.93  ? 209 PRO F CD  1 
ATOM   16581 N N   . ASN F  1 210 ? 138.551 93.829  1.228   1.00   69.37  ? 210 ASN F N   1 
ATOM   16582 C CA  . ASN F  1 210 ? 138.104 95.200  1.124   1.00   69.41  ? 210 ASN F CA  1 
ATOM   16583 C C   . ASN F  1 210 ? 136.903 95.534  2.014   1.00   65.72  ? 210 ASN F C   1 
ATOM   16584 O O   . ASN F  1 210 ? 136.798 96.690  2.447   1.00   62.82  ? 210 ASN F O   1 
ATOM   16585 C CB  . ASN F  1 210 ? 137.826 95.557  -0.335  1.00   68.55  ? 210 ASN F CB  1 
ATOM   16586 C CG  . ASN F  1 210 ? 139.107 95.777  -1.147  1.00   67.57  ? 210 ASN F CG  1 
ATOM   16587 O OD1 . ASN F  1 210 ? 140.207 95.844  -0.590  1.00   67.99  ? 210 ASN F OD1 1 
ATOM   16588 N ND2 . ASN F  1 210 ? 138.963 95.897  -2.466  1.00   67.68  ? 210 ASN F ND2 1 
ATOM   16589 N N   . ASN F  1 211 ? 135.991 94.588  2.296   1.00   62.93  ? 211 ASN F N   1 
ATOM   16590 C CA  . ASN F  1 211 ? 134.953 94.997  3.246   1.00   62.34  ? 211 ASN F CA  1 
ATOM   16591 C C   . ASN F  1 211 ? 134.974 93.982  4.346   1.00   54.76  ? 211 ASN F C   1 
ATOM   16592 O O   . ASN F  1 211 ? 133.935 93.454  4.751   1.00   50.30  ? 211 ASN F O   1 
ATOM   16593 C CB  . ASN F  1 211 ? 133.512 95.078  2.716   1.00   64.66  ? 211 ASN F CB  1 
ATOM   16594 C CG  . ASN F  1 211 ? 133.385 95.486  1.225   1.00   68.58  ? 211 ASN F CG  1 
ATOM   16595 O OD1 . ASN F  1 211 ? 132.637 94.776  0.553   1.00   70.20  ? 211 ASN F OD1 1 
ATOM   16596 N ND2 . ASN F  1 211 ? 134.262 96.378  0.670   1.00   69.46  ? 211 ASN F ND2 1 
ATOM   16597 N N   . ASN F  1 212 ? 136.174 93.619  4.758   1.00   53.82  ? 212 ASN F N   1 
ATOM   16598 C CA  . ASN F  1 212 ? 136.320 92.594  5.769   1.00   51.77  ? 212 ASN F CA  1 
ATOM   16599 C C   . ASN F  1 212 ? 137.681 92.753  6.431   1.00   51.23  ? 212 ASN F C   1 
ATOM   16600 O O   . ASN F  1 212 ? 138.663 92.186  5.968   1.00   51.11  ? 212 ASN F O   1 
ATOM   16601 C CB  . ASN F  1 212 ? 136.185 91.198  5.166   1.00   50.51  ? 212 ASN F CB  1 
ATOM   16602 C CG  . ASN F  1 212 ? 135.761 90.178  6.184   1.00   50.41  ? 212 ASN F CG  1 
ATOM   16603 O OD1 . ASN F  1 212 ? 135.888 90.405  7.393   1.00   50.53  ? 212 ASN F OD1 1 
ATOM   16604 N ND2 . ASN F  1 212 ? 135.342 89.006  5.708   1.00   48.72  ? 212 ASN F ND2 1 
ATOM   16605 N N   . ASN F  1 213 ? 137.738 93.596  7.460   1.00   50.37  ? 213 ASN F N   1 
ATOM   16606 C CA  . ASN F  1 213 ? 138.988 93.870  8.191   1.00   46.18  ? 213 ASN F CA  1 
ATOM   16607 C C   . ASN F  1 213 ? 139.377 92.756  9.140   1.00   40.05  ? 213 ASN F C   1 
ATOM   16608 O O   . ASN F  1 213 ? 140.532 92.689  9.551   1.00   38.62  ? 213 ASN F O   1 
ATOM   16609 C CB  . ASN F  1 213 ? 138.940 95.191  8.967   1.00   45.67  ? 213 ASN F CB  1 
ATOM   16610 C CG  . ASN F  1 213 ? 139.077 96.411  8.069   1.00   46.92  ? 213 ASN F CG  1 
ATOM   16611 O OD1 . ASN F  1 213 ? 139.849 96.419  7.112   1.00   47.78  ? 213 ASN F OD1 1 
ATOM   16612 N ND2 . ASN F  1 213 ? 138.370 97.470  8.417   1.00   42.59  ? 213 ASN F ND2 1 
ATOM   16613 N N   . TYR F  1 214 ? 138.403 91.917  9.500   1.00   36.53  ? 214 TYR F N   1 
ATOM   16614 C CA  . TYR F  1 214 ? 138.607 90.825  10.457  1.00   38.62  ? 214 TYR F CA  1 
ATOM   16615 C C   . TYR F  1 214 ? 139.632 89.802  9.913   1.00   39.98  ? 214 TYR F C   1 
ATOM   16616 O O   . TYR F  1 214 ? 140.384 89.178  10.680  1.00   41.09  ? 214 TYR F O   1 
ATOM   16617 C CB  . TYR F  1 214 ? 137.271 90.140  10.801  1.00   38.21  ? 214 TYR F CB  1 
ATOM   16618 C CG  . TYR F  1 214 ? 137.377 89.144  11.943  1.00   35.77  ? 214 TYR F CG  1 
ATOM   16619 C CD1 . TYR F  1 214 ? 137.460 89.577  13.260  1.00   37.98  ? 214 TYR F CD1 1 
ATOM   16620 C CD2 . TYR F  1 214 ? 137.402 87.781  11.706  1.00   35.06  ? 214 TYR F CD2 1 
ATOM   16621 C CE1 . TYR F  1 214 ? 137.579 88.682  14.312  1.00   36.07  ? 214 TYR F CE1 1 
ATOM   16622 C CE2 . TYR F  1 214 ? 137.517 86.864  12.764  1.00   33.43  ? 214 TYR F CE2 1 
ATOM   16623 C CZ  . TYR F  1 214 ? 137.607 87.333  14.057  1.00   34.85  ? 214 TYR F CZ  1 
ATOM   16624 O OH  . TYR F  1 214 ? 137.717 86.452  15.099  1.00   35.70  ? 214 TYR F OH  1 
ATOM   16625 N N   . ILE F  1 215 ? 139.686 89.652  8.595   1.00   37.82  ? 215 ILE F N   1 
ATOM   16626 C CA  . ILE F  1 215 ? 140.599 88.695  7.984   1.00   37.12  ? 215 ILE F CA  1 
ATOM   16627 C C   . ILE F  1 215 ? 141.937 89.283  7.489   1.00   39.90  ? 215 ILE F C   1 
ATOM   16628 O O   . ILE F  1 215 ? 142.737 88.560  6.897   1.00   40.52  ? 215 ILE F O   1 
ATOM   16629 C CB  . ILE F  1 215 ? 139.912 88.006  6.796   1.00   35.37  ? 215 ILE F CB  1 
ATOM   16630 C CG1 . ILE F  1 215 ? 139.391 89.055  5.809   1.00   37.30  ? 215 ILE F CG1 1 
ATOM   16631 C CG2 . ILE F  1 215 ? 138.727 87.154  7.270   1.00   32.45  ? 215 ILE F CG2 1 
ATOM   16632 C CD1 . ILE F  1 215 ? 140.251 89.255  4.599   1.00   41.42  ? 215 ILE F CD1 1 
ATOM   16633 N N   . HIS F  1 216 ? 142.192 90.568  7.737   1.00   44.36  ? 216 HIS F N   1 
ATOM   16634 C CA  . HIS F  1 216 ? 143.387 91.222  7.195   1.00   48.56  ? 216 HIS F CA  1 
ATOM   16635 C C   . HIS F  1 216 ? 144.645 90.535  7.710   1.00   47.76  ? 216 HIS F C   1 
ATOM   16636 O O   . HIS F  1 216 ? 145.593 90.378  6.964   1.00   49.59  ? 216 HIS F O   1 
ATOM   16637 C CB  . HIS F  1 216 ? 143.420 92.730  7.509   1.00   49.75  ? 216 HIS F CB  1 
ATOM   16638 C CG  . HIS F  1 216 ? 144.535 93.496  6.820   1.00   56.19  ? 216 HIS F CG  1 
ATOM   16639 N ND1 . HIS F  1 216 ? 145.761 93.752  7.409   1.00   57.81  ? 216 HIS F ND1 1 
ATOM   16640 C CD2 . HIS F  1 216 ? 144.582 94.102  5.604   1.00   56.44  ? 216 HIS F CD2 1 
ATOM   16641 C CE1 . HIS F  1 216 ? 146.518 94.454  6.583   1.00   55.50  ? 216 HIS F CE1 1 
ATOM   16642 N NE2 . HIS F  1 216 ? 145.826 94.681  5.481   1.00   57.25  ? 216 HIS F NE2 1 
ATOM   16643 N N   . ASN F  1 217 ? 144.660 90.114  8.970   1.00   44.34  ? 217 ASN F N   1 
ATOM   16644 C CA  . ASN F  1 217 ? 145.859 89.461  9.511   1.00   47.95  ? 217 ASN F CA  1 
ATOM   16645 C C   . ASN F  1 217 ? 146.166 88.084  8.903   1.00   45.14  ? 217 ASN F C   1 
ATOM   16646 O O   . ASN F  1 217 ? 147.286 87.599  9.026   1.00   47.18  ? 217 ASN F O   1 
ATOM   16647 C CB  . ASN F  1 217 ? 145.747 89.317  11.037  1.00   52.29  ? 217 ASN F CB  1 
ATOM   16648 C CG  . ASN F  1 217 ? 147.000 88.698  11.675  1.00   59.35  ? 217 ASN F CG  1 
ATOM   16649 O OD1 . ASN F  1 217 ? 148.085 89.294  11.667  1.00   67.26  ? 217 ASN F OD1 1 
ATOM   16650 N ND2 . ASN F  1 217 ? 146.847 87.505  12.244  1.00   56.90  ? 217 ASN F ND2 1 
ATOM   16651 N N   . SER F  1 218 ? 145.205 87.485  8.201   1.00   40.49  ? 218 SER F N   1 
ATOM   16652 C CA  . SER F  1 218 ? 145.384 86.142  7.636   1.00   36.78  ? 218 SER F CA  1 
ATOM   16653 C C   . SER F  1 218 ? 145.673 86.106  6.139   1.00   35.82  ? 218 SER F C   1 
ATOM   16654 O O   . SER F  1 218 ? 145.684 85.050  5.536   1.00   39.09  ? 218 SER F O   1 
ATOM   16655 C CB  . SER F  1 218 ? 144.130 85.312  7.867   1.00   35.54  ? 218 SER F CB  1 
ATOM   16656 O OG  . SER F  1 218 ? 143.174 85.643  6.878   1.00   36.25  ? 218 SER F OG  1 
ATOM   16657 N N   . LEU F  1 219 ? 145.864 87.264  5.534   1.00   39.31  ? 219 LEU F N   1 
ATOM   16658 C CA  . LEU F  1 219 ? 145.924 87.369  4.082   1.00   37.32  ? 219 LEU F CA  1 
ATOM   16659 C C   . LEU F  1 219 ? 147.113 86.650  3.459   1.00   38.88  ? 219 LEU F C   1 
ATOM   16660 O O   . LEU F  1 219 ? 147.024 86.262  2.312   1.00   41.27  ? 219 LEU F O   1 
ATOM   16661 C CB  . LEU F  1 219 ? 145.889 88.842  3.663   1.00   41.88  ? 219 LEU F CB  1 
ATOM   16662 C CG  . LEU F  1 219 ? 144.489 89.481  3.657   1.00   44.44  ? 219 LEU F CG  1 
ATOM   16663 C CD1 . LEU F  1 219 ? 144.550 90.973  3.406   1.00   49.26  ? 219 LEU F CD1 1 
ATOM   16664 C CD2 . LEU F  1 219 ? 143.583 88.813  2.617   1.00   44.73  ? 219 LEU F CD2 1 
ATOM   16665 N N   . ASP F  1 220 ? 148.237 86.524  4.170   1.00   42.92  ? 220 ASP F N   1 
ATOM   16666 C CA  . ASP F  1 220 ? 149.387 85.806  3.613   1.00   46.09  ? 220 ASP F CA  1 
ATOM   16667 C C   . ASP F  1 220 ? 149.074 84.335  3.535   1.00   41.06  ? 220 ASP F C   1 
ATOM   16668 O O   . ASP F  1 220 ? 149.436 83.656  2.587   1.00   41.05  ? 220 ASP F O   1 
ATOM   16669 C CB  . ASP F  1 220 ? 150.631 85.989  4.449   1.00   54.24  ? 220 ASP F CB  1 
ATOM   16670 C CG  . ASP F  1 220 ? 151.077 87.399  4.494   1.00   66.76  ? 220 ASP F CG  1 
ATOM   16671 O OD1 . ASP F  1 220 ? 151.021 88.077  3.438   1.00   69.94  ? 220 ASP F OD1 1 
ATOM   16672 O OD2 . ASP F  1 220 ? 151.481 87.829  5.594   1.00   72.42  ? 220 ASP F OD2 1 
ATOM   16673 N N   . VAL F  1 221 ? 148.406 83.841  4.557   1.00   39.19  ? 221 VAL F N   1 
ATOM   16674 C CA  . VAL F  1 221 ? 147.949 82.479  4.519   1.00   38.34  ? 221 VAL F CA  1 
ATOM   16675 C C   . VAL F  1 221 ? 146.907 82.283  3.404   1.00   37.26  ? 221 VAL F C   1 
ATOM   16676 O O   . VAL F  1 221 ? 147.021 81.339  2.627   1.00   39.29  ? 221 VAL F O   1 
ATOM   16677 C CB  . VAL F  1 221 ? 147.366 82.054  5.871   1.00   36.52  ? 221 VAL F CB  1 
ATOM   16678 C CG1 . VAL F  1 221 ? 146.930 80.620  5.802   1.00   33.18  ? 221 VAL F CG1 1 
ATOM   16679 C CG2 . VAL F  1 221 ? 148.390 82.235  6.962   1.00   35.40  ? 221 VAL F CG2 1 
ATOM   16680 N N   . LEU F  1 222 ? 145.929 83.192  3.299   1.00   34.49  ? 222 LEU F N   1 
ATOM   16681 C CA  . LEU F  1 222 ? 144.851 83.043  2.317   1.00   33.09  ? 222 LEU F CA  1 
ATOM   16682 C C   . LEU F  1 222 ? 145.340 83.058  0.875   1.00   36.94  ? 222 LEU F C   1 
ATOM   16683 O O   . LEU F  1 222 ? 144.775 82.414  0.001   1.00   37.60  ? 222 LEU F O   1 
ATOM   16684 C CB  . LEU F  1 222 ? 143.803 84.131  2.487   1.00   34.49  ? 222 LEU F CB  1 
ATOM   16685 C CG  . LEU F  1 222 ? 143.029 84.065  3.797   1.00   36.55  ? 222 LEU F CG  1 
ATOM   16686 C CD1 . LEU F  1 222 ? 141.923 85.115  3.797   1.00   37.66  ? 222 LEU F CD1 1 
ATOM   16687 C CD2 . LEU F  1 222 ? 142.468 82.675  3.973   1.00   32.96  ? 222 LEU F CD2 1 
ATOM   16688 N N   . HIS F  1 223 ? 146.380 83.830  0.637   1.00   40.31  ? 223 HIS F N   1 
ATOM   16689 C CA  . HIS F  1 223 ? 146.982 83.947  -0.676  1.00   46.77  ? 223 HIS F CA  1 
ATOM   16690 C C   . HIS F  1 223 ? 147.540 82.633  -1.235  1.00   46.81  ? 223 HIS F C   1 
ATOM   16691 O O   . HIS F  1 223 ? 147.497 82.404  -2.448  1.00   50.07  ? 223 HIS F O   1 
ATOM   16692 C CB  . HIS F  1 223 ? 148.082 85.007  -0.584  1.00   55.69  ? 223 HIS F CB  1 
ATOM   16693 C CG  . HIS F  1 223 ? 148.847 85.224  -1.852  1.00   67.15  ? 223 HIS F CG  1 
ATOM   16694 N ND1 . HIS F  1 223 ? 150.175 84.865  -1.983  1.00   73.59  ? 223 HIS F ND1 1 
ATOM   16695 C CD2 . HIS F  1 223 ? 148.488 85.777  -3.033  1.00   71.78  ? 223 HIS F CD2 1 
ATOM   16696 C CE1 . HIS F  1 223 ? 150.597 85.182  -3.194  1.00   77.93  ? 223 HIS F CE1 1 
ATOM   16697 N NE2 . HIS F  1 223 ? 149.594 85.737  -3.851  1.00   77.38  ? 223 HIS F NE2 1 
ATOM   16698 N N   . ASP F  1 224 ? 148.028 81.765  -0.349  1.00   43.85  ? 224 ASP F N   1 
ATOM   16699 C CA  . ASP F  1 224 ? 148.722 80.534  -0.748  1.00   40.48  ? 224 ASP F CA  1 
ATOM   16700 C C   . ASP F  1 224 ? 147.857 79.302  -0.594  1.00   38.44  ? 224 ASP F C   1 
ATOM   16701 O O   . ASP F  1 224 ? 148.364 78.189  -0.657  1.00   42.32  ? 224 ASP F O   1 
ATOM   16702 C CB  . ASP F  1 224 ? 149.980 80.344  0.081   1.00   40.79  ? 224 ASP F CB  1 
ATOM   16703 C CG  . ASP F  1 224 ? 150.976 81.432  -0.137  1.00   47.59  ? 224 ASP F CG  1 
ATOM   16704 O OD1 . ASP F  1 224 ? 150.963 82.022  -1.228  1.00   51.04  ? 224 ASP F OD1 1 
ATOM   16705 O OD2 . ASP F  1 224 ? 151.737 81.748  0.800   1.00   49.06  1 224 ASP F OD2 1 
ATOM   16706 N N   . LEU F  1 225 ? 146.560 79.493  -0.372  1.00   35.49  ? 225 LEU F N   1 
ATOM   16707 C CA  . LEU F  1 225 ? 145.645 78.364  -0.216  1.00   33.16  ? 225 LEU F CA  1 
ATOM   16708 C C   . LEU F  1 225 ? 145.691 77.528  -1.455  1.00   34.32  ? 225 LEU F C   1 
ATOM   16709 O O   . LEU F  1 225 ? 145.810 78.057  -2.565  1.00   37.03  ? 225 LEU F O   1 
ATOM   16710 C CB  . LEU F  1 225 ? 144.220 78.826  0.014   1.00   29.95  ? 225 LEU F CB  1 
ATOM   16711 C CG  . LEU F  1 225 ? 143.918 79.389  1.387   1.00   31.77  ? 225 LEU F CG  1 
ATOM   16712 C CD1 . LEU F  1 225 ? 142.436 79.541  1.531   1.00   31.66  ? 225 LEU F CD1 1 
ATOM   16713 C CD2 . LEU F  1 225 ? 144.447 78.513  2.450   1.00   31.23  ? 225 LEU F CD2 1 
ATOM   16714 N N   . VAL F  1 226 ? 145.645 76.220  -1.254  1.00   34.78  ? 226 VAL F N   1 
ATOM   16715 C CA  . VAL F  1 226 ? 145.576 75.273  -2.344  1.00   36.73  ? 226 VAL F CA  1 
ATOM   16716 C C   . VAL F  1 226 ? 144.252 74.526  -2.217  1.00   35.65  ? 226 VAL F C   1 
ATOM   16717 O O   . VAL F  1 226 ? 143.824 74.184  -1.108  1.00   32.78  ? 226 VAL F O   1 
ATOM   16718 C CB  . VAL F  1 226 ? 146.778 74.358  -2.325  1.00   41.39  ? 226 VAL F CB  1 
ATOM   16719 C CG1 . VAL F  1 226 ? 146.516 73.107  -3.120  1.00   43.77  ? 226 VAL F CG1 1 
ATOM   16720 C CG2 . VAL F  1 226 ? 147.983 75.110  -2.869  1.00   43.60  ? 226 VAL F CG2 1 
ATOM   16721 N N   . TYR F  1 227 ? 143.608 74.285  -3.358  1.00   36.97  ? 227 TYR F N   1 
ATOM   16722 C CA  . TYR F  1 227 ? 142.247 73.746  -3.398  1.00   33.92  ? 227 TYR F CA  1 
ATOM   16723 C C   . TYR F  1 227 ? 142.151 72.380  -4.040  1.00   34.20  ? 227 TYR F C   1 
ATOM   16724 O O   . TYR F  1 227 ? 142.938 72.049  -4.924  1.00   39.18  ? 227 TYR F O   1 
ATOM   16725 C CB  . TYR F  1 227 ? 141.337 74.706  -4.162  1.00   35.21  ? 227 TYR F CB  1 
ATOM   16726 C CG  . TYR F  1 227 ? 141.198 76.043  -3.488  1.00   39.90  ? 227 TYR F CG  1 
ATOM   16727 C CD1 . TYR F  1 227 ? 142.134 77.043  -3.709  1.00   45.63  ? 227 TYR F CD1 1 
ATOM   16728 C CD2 . TYR F  1 227 ? 140.153 76.299  -2.617  1.00   41.44  ? 227 TYR F CD2 1 
ATOM   16729 C CE1 . TYR F  1 227 ? 142.027 78.257  -3.091  1.00   51.24  ? 227 TYR F CE1 1 
ATOM   16730 C CE2 . TYR F  1 227 ? 140.037 77.518  -1.989  1.00   47.15  ? 227 TYR F CE2 1 
ATOM   16731 C CZ  . TYR F  1 227 ? 140.977 78.494  -2.232  1.00   52.30  ? 227 TYR F CZ  1 
ATOM   16732 O OH  . TYR F  1 227 ? 140.872 79.722  -1.622  1.00   56.82  ? 227 TYR F OH  1 
ATOM   16733 N N   . THR F  1 228 ? 141.158 71.611  -3.609  1.00   32.38  ? 228 THR F N   1 
ATOM   16734 C CA  . THR F  1 228 ? 140.861 70.292  -4.178  1.00   32.95  ? 228 THR F CA  1 
ATOM   16735 C C   . THR F  1 228 ? 139.331 70.078  -4.162  1.00   30.46  ? 228 THR F C   1 
ATOM   16736 O O   . THR F  1 228 ? 138.660 70.651  -3.334  1.00   32.81  ? 228 THR F O   1 
ATOM   16737 C CB  . THR F  1 228 ? 141.625 69.159  -3.394  1.00   37.35  ? 228 THR F CB  1 
ATOM   16738 O OG1 . THR F  1 228 ? 141.562 67.919  -4.108  1.00   36.91  ? 228 THR F OG1 1 
ATOM   16739 C CG2 . THR F  1 228 ? 141.069 68.960  -1.988  1.00   34.25  ? 228 THR F CG2 1 
ATOM   16740 N N   . PRO F  1 229 ? 138.767 69.309  -5.113  1.00   30.20  ? 229 PRO F N   1 
ATOM   16741 C CA  . PRO F  1 229 ? 137.310 69.165  -5.131  1.00   28.41  ? 229 PRO F CA  1 
ATOM   16742 C C   . PRO F  1 229 ? 136.740 68.473  -3.911  1.00   27.46  ? 229 PRO F C   1 
ATOM   16743 O O   . PRO F  1 229 ? 137.345 67.564  -3.365  1.00   28.94  ? 229 PRO F O   1 
ATOM   16744 C CB  . PRO F  1 229 ? 137.054 68.326  -6.371  1.00   28.55  ? 229 PRO F CB  1 
ATOM   16745 C CG  . PRO F  1 229 ? 138.218 68.597  -7.247  1.00   32.09  ? 229 PRO F CG  1 
ATOM   16746 C CD  . PRO F  1 229 ? 139.375 68.709  -6.316  1.00   32.17  ? 229 PRO F CD  1 
ATOM   16747 N N   . LEU F  1 230 ? 135.568 68.935  -3.508  1.00   27.25  ? 230 LEU F N   1 
ATOM   16748 C CA  . LEU F  1 230 ? 134.839 68.387  -2.391  1.00   29.73  ? 230 LEU F CA  1 
ATOM   16749 C C   . LEU F  1 230 ? 133.675 67.525  -2.893  1.00   28.84  ? 230 LEU F C   1 
ATOM   16750 O O   . LEU F  1 230 ? 132.901 67.966  -3.719  1.00   27.71  ? 230 LEU F O   1 
ATOM   16751 C CB  . LEU F  1 230 ? 134.322 69.524  -1.513  1.00   29.95  ? 230 LEU F CB  1 
ATOM   16752 C CG  . LEU F  1 230 ? 133.474 69.195  -0.287  1.00   30.22  ? 230 LEU F CG  1 
ATOM   16753 C CD1 . LEU F  1 230 ? 134.269 68.383  0.735   1.00   27.40  ? 230 LEU F CD1 1 
ATOM   16754 C CD2 . LEU F  1 230 ? 132.924 70.486  0.312   1.00   28.85  ? 230 LEU F CD2 1 
ATOM   16755 N N   . THR F  1 231 ? 133.560 66.290  -2.400  1.00   29.89  ? 231 THR F N   1 
ATOM   16756 C CA  . THR F  1 231 ? 132.396 65.469  -2.705  1.00   26.74  ? 231 THR F CA  1 
ATOM   16757 C C   . THR F  1 231 ? 131.702 65.118  -1.407  1.00   26.20  ? 231 THR F C   1 
ATOM   16758 O O   . THR F  1 231 ? 132.330 65.045  -0.346  1.00   24.54  ? 231 THR F O   1 
ATOM   16759 C CB  . THR F  1 231 ? 132.734 64.168  -3.453  1.00   26.51  ? 231 THR F CB  1 
ATOM   16760 O OG1 . THR F  1 231 ? 133.864 63.557  -2.837  1.00   30.38  ? 231 THR F OG1 1 
ATOM   16761 C CG2 . THR F  1 231 ? 133.030 64.435  -4.929  1.00   26.21  ? 231 THR F CG2 1 
ATOM   16762 N N   . ILE F  1 232 ? 130.397 64.889  -1.523  1.00   26.44  ? 232 ILE F N   1 
ATOM   16763 C CA  . ILE F  1 232 ? 129.512 64.722  -0.387  1.00   24.78  ? 232 ILE F CA  1 
ATOM   16764 C C   . ILE F  1 232 ? 128.812 63.372  -0.490  1.00   26.12  ? 232 ILE F C   1 
ATOM   16765 O O   . ILE F  1 232 ? 128.240 63.068  -1.517  1.00   28.05  ? 232 ILE F O   1 
ATOM   16766 C CB  . ILE F  1 232 ? 128.452 65.860  -0.349  1.00   24.01  ? 232 ILE F CB  1 
ATOM   16767 C CG1 . ILE F  1 232 ? 129.117 67.230  -0.343  1.00   20.84  ? 232 ILE F CG1 1 
ATOM   16768 C CG2 . ILE F  1 232 ? 127.576 65.735  0.862   1.00   26.69  ? 232 ILE F CG2 1 
ATOM   16769 C CD1 . ILE F  1 232 ? 129.973 67.455  0.882   1.00   20.55  ? 232 ILE F CD1 1 
ATOM   16770 N N   . SER F  1 233 ? 128.848 62.554  0.554   1.00   26.38  ? 233 SER F N   1 
ATOM   16771 C CA  . SER F  1 233 ? 128.166 61.261  0.498   1.00   28.50  ? 233 SER F CA  1 
ATOM   16772 C C   . SER F  1 233 ? 126.656 61.390  0.689   1.00   31.06  ? 233 SER F C   1 
ATOM   16773 O O   . SER F  1 233 ? 126.143 62.467  1.032   1.00   30.69  ? 233 SER F O   1 
ATOM   16774 C CB  . SER F  1 233 ? 128.738 60.303  1.529   1.00   27.16  ? 233 SER F CB  1 
ATOM   16775 O OG  . SER F  1 233 ? 128.326 60.677  2.812   1.00   27.55  ? 233 SER F OG  1 
ATOM   16776 N N   . LYS F  1 234 ? 125.938 60.284  0.493   1.00   34.01  ? 234 LYS F N   1 
ATOM   16777 C CA  . LYS F  1 234 ? 124.481 60.310  0.649   1.00   33.57  ? 234 LYS F CA  1 
ATOM   16778 C C   . LYS F  1 234 ? 124.097 60.633  2.093   1.00   32.68  ? 234 LYS F C   1 
ATOM   16779 O O   . LYS F  1 234 ? 122.965 61.027  2.344   1.00   32.25  ? 234 LYS F O   1 
ATOM   16780 C CB  . LYS F  1 234 ? 123.837 58.980  0.215   1.00   40.47  ? 234 LYS F CB  1 
ATOM   16781 C CG  . LYS F  1 234 ? 124.135 58.607  -1.237  1.00   48.20  ? 234 LYS F CG  1 
ATOM   16782 C CD  . LYS F  1 234 ? 123.563 57.249  -1.670  1.00   55.93  ? 234 LYS F CD  1 
ATOM   16783 C CE  . LYS F  1 234 ? 124.256 56.804  -2.963  1.00   61.98  ? 234 LYS F CE  1 
ATOM   16784 N NZ  . LYS F  1 234 ? 124.020 57.655  -4.159  1.00   64.29  ? 234 LYS F NZ  1 
ATOM   16785 N N   . GLN F  1 235 ? 125.037 60.512  3.036   1.00   32.23  ? 235 GLN F N   1 
ATOM   16786 C CA  . GLN F  1 235 ? 124.729 60.794  4.432   1.00   33.94  ? 235 GLN F CA  1 
ATOM   16787 C C   . GLN F  1 235 ? 125.154 62.191  4.828   1.00   33.37  ? 235 GLN F C   1 
ATOM   16788 O O   . GLN F  1 235 ? 124.978 62.573  5.976   1.00   36.22  ? 235 GLN F O   1 
ATOM   16789 C CB  . GLN F  1 235 ? 125.423 59.786  5.354   1.00   39.61  ? 235 GLN F CB  1 
ATOM   16790 C CG  . GLN F  1 235 ? 124.849 58.375  5.284   1.00   51.84  ? 235 GLN F CG  1 
ATOM   16791 C CD  . GLN F  1 235 ? 123.375 58.298  5.689   1.00   63.09  ? 235 GLN F CD  1 
ATOM   16792 O OE1 . GLN F  1 235 ? 122.939 58.958  6.630   1.00   65.88  ? 235 GLN F OE1 1 
ATOM   16793 N NE2 . GLN F  1 235 ? 122.599 57.495  4.959   1.00   69.20  ? 235 GLN F NE2 1 
ATOM   16794 N N   . GLY F  1 236 ? 125.669 62.961  3.874   1.00   30.96  ? 236 GLY F N   1 
ATOM   16795 C CA  . GLY F  1 236 ? 126.046 64.330  4.133   1.00   29.55  ? 236 GLY F CA  1 
ATOM   16796 C C   . GLY F  1 236 ? 127.462 64.533  4.665   1.00   28.12  ? 236 GLY F C   1 
ATOM   16797 O O   . GLY F  1 236 ? 127.752 65.578  5.251   1.00   25.98  ? 236 GLY F O   1 
ATOM   16798 N N   . GLU F  1 237 ? 128.334 63.541  4.480   1.00   25.56  ? 237 GLU F N   1 
ATOM   16799 C CA  . GLU F  1 237 ? 129.720 63.607  4.941   1.00   25.76  ? 237 GLU F CA  1 
ATOM   16800 C C   . GLU F  1 237 ? 130.650 64.229  3.898   1.00   25.99  ? 237 GLU F C   1 
ATOM   16801 O O   . GLU F  1 237 ? 130.389 64.124  2.706   1.00   23.46  ? 237 GLU F O   1 
ATOM   16802 C CB  . GLU F  1 237 ? 130.236 62.210  5.264   1.00   28.30  ? 237 GLU F CB  1 
ATOM   16803 C CG  . GLU F  1 237 ? 129.418 61.403  6.239   1.00   30.22  ? 237 GLU F CG  1 
ATOM   16804 C CD  . GLU F  1 237 ? 129.605 59.909  6.018   1.00   34.20  ? 237 GLU F CD  1 
ATOM   16805 O OE1 . GLU F  1 237 ? 129.268 59.423  4.925   1.00   34.48  ? 237 GLU F OE1 1 
ATOM   16806 O OE2 . GLU F  1 237 ? 130.086 59.221  6.932   1.00   35.56  1 237 GLU F OE2 1 
ATOM   16807 N N   . TYR F  1 238 ? 131.744 64.838  4.354   1.00   26.18  ? 238 TYR F N   1 
ATOM   16808 C CA  . TYR F  1 238 ? 132.700 65.516  3.488   1.00   24.34  ? 238 TYR F CA  1 
ATOM   16809 C C   . TYR F  1 238 ? 133.830 64.612  3.064   1.00   24.31  ? 238 TYR F C   1 
ATOM   16810 O O   . TYR F  1 238 ? 134.487 64.009  3.893   1.00   24.25  ? 238 TYR F O   1 
ATOM   16811 C CB  . TYR F  1 238 ? 133.290 66.765  4.187   1.00   26.68  ? 238 TYR F CB  1 
ATOM   16812 C CG  . TYR F  1 238 ? 132.266 67.820  4.541   1.00   26.04  ? 238 TYR F CG  1 
ATOM   16813 C CD1 . TYR F  1 238 ? 131.723 68.653  3.562   1.00   24.59  ? 238 TYR F CD1 1 
ATOM   16814 C CD2 . TYR F  1 238 ? 131.834 67.986  5.851   1.00   26.57  ? 238 TYR F CD2 1 
ATOM   16815 C CE1 . TYR F  1 238 ? 130.761 69.636  3.888   1.00   21.19  ? 238 TYR F CE1 1 
ATOM   16816 C CE2 . TYR F  1 238 ? 130.875 68.955  6.176   1.00   25.72  ? 238 TYR F CE2 1 
ATOM   16817 C CZ  . TYR F  1 238 ? 130.351 69.770  5.193   1.00   21.95  ? 238 TYR F CZ  1 
ATOM   16818 O OH  . TYR F  1 238 ? 129.418 70.705  5.540   1.00   23.62  ? 238 TYR F OH  1 
ATOM   16819 N N   . PHE F  1 239 ? 134.058 64.541  1.762   1.00   26.27  ? 239 PHE F N   1 
ATOM   16820 C CA  . PHE F  1 239 ? 135.106 63.704  1.204   1.00   26.94  ? 239 PHE F CA  1 
ATOM   16821 C C   . PHE F  1 239 ? 136.003 64.472  0.265   1.00   28.10  ? 239 PHE F C   1 
ATOM   16822 O O   . PHE F  1 239 ? 135.547 65.344  -0.462  1.00   23.96  ? 239 PHE F O   1 
ATOM   16823 C CB  . PHE F  1 239 ? 134.497 62.516  0.438   1.00   27.90  ? 239 PHE F CB  1 
ATOM   16824 C CG  . PHE F  1 239 ? 134.046 61.373  1.326   1.00   28.79  ? 239 PHE F CG  1 
ATOM   16825 C CD1 . PHE F  1 239 ? 132.803 61.381  1.921   1.00   27.91  ? 239 PHE F CD1 1 
ATOM   16826 C CD2 . PHE F  1 239 ? 134.874 60.299  1.555   1.00   27.58  ? 239 PHE F CD2 1 
ATOM   16827 C CE1 . PHE F  1 239 ? 132.407 60.349  2.744   1.00   25.52  ? 239 PHE F CE1 1 
ATOM   16828 C CE2 . PHE F  1 239 ? 134.486 59.271  2.358   1.00   28.80  ? 239 PHE F CE2 1 
ATOM   16829 C CZ  . PHE F  1 239 ? 133.236 59.298  2.954   1.00   29.44  ? 239 PHE F CZ  1 
ATOM   16830 N N   . ILE F  1 240 ? 137.282 64.117  0.268   1.00   32.87  ? 240 ILE F N   1 
ATOM   16831 C CA  . ILE F  1 240 ? 138.190 64.501  -0.812  1.00   35.70  ? 240 ILE F CA  1 
ATOM   16832 C C   . ILE F  1 240 ? 138.897 63.262  -1.377  1.00   36.10  ? 240 ILE F C   1 
ATOM   16833 O O   . ILE F  1 240 ? 138.864 62.182  -0.786  1.00   36.77  ? 240 ILE F O   1 
ATOM   16834 C CB  . ILE F  1 240 ? 139.270 65.521  -0.367  1.00   31.74  ? 240 ILE F CB  1 
ATOM   16835 C CG1 . ILE F  1 240 ? 140.080 64.960  0.799   1.00   33.94  ? 240 ILE F CG1 1 
ATOM   16836 C CG2 . ILE F  1 240 ? 138.649 66.872  -0.026  1.00   28.67  ? 240 ILE F CG2 1 
ATOM   16837 C CD1 . ILE F  1 240 ? 141.274 65.778  1.130   1.00   33.73  ? 240 ILE F CD1 1 
ATOM   16838 N N   . GLN F  1 241 ? 139.558 63.453  -2.516  1.00   35.76  ? 241 GLN F N   1 
ATOM   16839 C CA  . GLN F  1 241 ? 140.233 62.382  -3.221  1.00   35.98  ? 241 GLN F CA  1 
ATOM   16840 C C   . GLN F  1 241 ? 141.755 62.427  -3.005  1.00   36.60  ? 241 GLN F C   1 
ATOM   16841 O O   . GLN F  1 241 ? 142.438 63.348  -3.429  1.00   34.95  ? 241 GLN F O   1 
ATOM   16842 C CB  . GLN F  1 241 ? 139.889 62.470  -4.711  1.00   36.81  ? 241 GLN F CB  1 
ATOM   16843 C CG  . GLN F  1 241 ? 140.643 61.529  -5.617  1.00   43.31  ? 241 GLN F CG  1 
ATOM   16844 C CD  . GLN F  1 241 ? 140.419 60.050  -5.300  1.00   46.13  ? 241 GLN F CD  1 
ATOM   16845 O OE1 . GLN F  1 241 ? 139.376 59.658  -4.743  1.00   44.36  ? 241 GLN F OE1 1 
ATOM   16846 N NE2 . GLN F  1 241 ? 141.417 59.216  -5.647  1.00   40.09  ? 241 GLN F NE2 1 
ATOM   16847 N N   . VAL F  1 242 ? 142.265 61.386  -2.365  1.00   33.13  ? 242 VAL F N   1 
ATOM   16848 C CA  . VAL F  1 242 ? 143.684 61.195  -2.169  1.00   31.05  ? 242 VAL F CA  1 
ATOM   16849 C C   . VAL F  1 242 ? 144.125 60.125  -3.139  1.00   32.65  ? 242 VAL F C   1 
ATOM   16850 O O   . VAL F  1 242 ? 143.728 58.975  -3.004  1.00   33.66  ? 242 VAL F O   1 
ATOM   16851 C CB  . VAL F  1 242 ? 144.001 60.739  -0.739  1.00   29.86  ? 242 VAL F CB  1 
ATOM   16852 C CG1 . VAL F  1 242 ? 145.485 60.387  -0.601  1.00   32.10  ? 242 VAL F CG1 1 
ATOM   16853 C CG2 . VAL F  1 242 ? 143.605 61.797  0.241   1.00   31.00  ? 242 VAL F CG2 1 
ATOM   16854 N N   . ASN F  1 243 ? 144.933 60.499  -4.122  1.00   32.91  ? 243 ASN F N   1 
ATOM   16855 C CA  . ASN F  1 243 ? 145.399 59.540  -5.095  1.00   33.06  ? 243 ASN F CA  1 
ATOM   16856 C C   . ASN F  1 243 ? 146.484 58.653  -4.505  1.00   34.06  ? 243 ASN F C   1 
ATOM   16857 O O   . ASN F  1 243 ? 146.622 57.487  -4.878  1.00   37.03  ? 243 ASN F O   1 
ATOM   16858 C CB  . ASN F  1 243 ? 145.893 60.262  -6.341  1.00   34.77  ? 243 ASN F CB  1 
ATOM   16859 C CG  . ASN F  1 243 ? 144.759 60.639  -7.269  1.00   44.73  ? 243 ASN F CG  1 
ATOM   16860 O OD1 . ASN F  1 243 ? 143.588 60.394  -6.979  1.00   42.13  ? 243 ASN F OD1 1 
ATOM   16861 N ND2 . ASN F  1 243 ? 145.098 61.236  -8.397  1.00   48.59  ? 243 ASN F ND2 1 
ATOM   16862 N N   . ALA F  1 244 ? 147.248 59.196  -3.572  1.00   32.39  ? 244 ALA F N   1 
ATOM   16863 C CA  . ALA F  1 244 ? 148.312 58.438  -2.942  1.00   33.14  ? 244 ALA F CA  1 
ATOM   16864 C C   . ALA F  1 244 ? 148.799 59.099  -1.674  1.00   35.43  ? 244 ALA F C   1 
ATOM   16865 O O   . ALA F  1 244 ? 148.642 60.298  -1.477  1.00   38.60  ? 244 ALA F O   1 
ATOM   16866 C CB  . ALA F  1 244 ? 149.481 58.245  -3.900  1.00   35.34  ? 244 ALA F CB  1 
ATOM   16867 N N   . ILE F  1 245 ? 149.416 58.301  -0.821  1.00   36.92  ? 245 ILE F N   1 
ATOM   16868 C CA  . ILE F  1 245 ? 150.224 58.804  0.293   1.00   42.03  ? 245 ILE F CA  1 
ATOM   16869 C C   . ILE F  1 245 ? 151.717 58.663  -0.057  1.00   45.45  ? 245 ILE F C   1 
ATOM   16870 O O   . ILE F  1 245 ? 152.183 57.567  -0.372  1.00   45.19  ? 245 ILE F O   1 
ATOM   16871 C CB  . ILE F  1 245 ? 149.933 58.036  1.618   1.00   36.88  ? 245 ILE F CB  1 
ATOM   16872 C CG1 . ILE F  1 245 ? 148.434 58.016  1.920   1.00   33.86  ? 245 ILE F CG1 1 
ATOM   16873 C CG2 . ILE F  1 245 ? 150.755 58.620  2.784   1.00   36.68  ? 245 ILE F CG2 1 
ATOM   16874 C CD1 . ILE F  1 245 ? 148.061 57.003  2.964   1.00   33.86  ? 245 ILE F CD1 1 
ATOM   16875 N N   . ARG F  1 246 ? 152.456 59.769  -0.024  1.00   47.30  ? 246 ARG F N   1 
ATOM   16876 C CA  . ARG F  1 246 ? 153.873 59.764  -0.381  1.00   48.78  ? 246 ARG F CA  1 
ATOM   16877 C C   . ARG F  1 246 ? 154.741 59.677  0.861   1.00   49.89  ? 246 ARG F C   1 
ATOM   16878 O O   . ARG F  1 246 ? 154.562 60.463  1.795   1.00   47.06  ? 246 ARG F O   1 
ATOM   16879 C CB  . ARG F  1 246 ? 154.242 61.036  -1.165  1.00   50.80  ? 246 ARG F CB  1 
ATOM   16880 C CG  . ARG F  1 246 ? 155.704 61.165  -1.590  1.00   55.74  ? 246 ARG F CG  1 
ATOM   16881 C CD  . ARG F  1 246 ? 156.074 62.639  -1.829  1.00   61.87  ? 246 ARG F CD  1 
ATOM   16882 N NE  . ARG F  1 246 ? 155.570 63.225  -3.077  1.00   63.45  ? 246 ARG F NE  1 
ATOM   16883 C CZ  . ARG F  1 246 ? 155.250 64.514  -3.227  1.00   65.20  ? 246 ARG F CZ  1 
ATOM   16884 N NH1 . ARG F  1 246 ? 155.356 65.363  -2.208  1.00   65.37  ? 246 ARG F NH1 1 
ATOM   16885 N NH2 . ARG F  1 246 ? 154.817 64.962  -4.398  1.00   66.73  ? 246 ARG F NH2 1 
ATOM   16886 N N   . VAL F  1 247 ? 155.661 58.708  0.877   1.00   50.06  ? 247 VAL F N   1 
ATOM   16887 C CA  . VAL F  1 247 ? 156.732 58.667  1.882   1.00   53.92  ? 247 VAL F CA  1 
ATOM   16888 C C   . VAL F  1 247 ? 158.094 58.611  1.185   1.00   56.97  ? 247 VAL F C   1 
ATOM   16889 O O   . VAL F  1 247 ? 158.443 57.583  0.603   1.00   56.10  ? 247 VAL F O   1 
ATOM   16890 C CB  . VAL F  1 247 ? 156.585 57.475  2.831   1.00   53.17  ? 247 VAL F CB  1 
ATOM   16891 C CG1 . VAL F  1 247 ? 157.682 57.497  3.883   1.00   55.23  ? 247 VAL F CG1 1 
ATOM   16892 C CG2 . VAL F  1 247 ? 155.213 57.494  3.486   1.00   50.81  ? 247 VAL F CG2 1 
ATOM   16893 N N   . ASN F  1 248 ? 158.843 59.714  1.247   1.00   61.46  ? 248 ASN F N   1 
ATOM   16894 C CA  . ASN F  1 248 ? 160.064 59.895  0.456   1.00   65.18  ? 248 ASN F CA  1 
ATOM   16895 C C   . ASN F  1 248 ? 159.811 59.585  -1.026  1.00   62.89  ? 248 ASN F C   1 
ATOM   16896 O O   . ASN F  1 248 ? 158.987 60.264  -1.645  1.00   61.43  ? 248 ASN F O   1 
ATOM   16897 C CB  . ASN F  1 248 ? 161.226 59.070  1.025   1.00   69.30  ? 248 ASN F CB  1 
ATOM   16898 C CG  . ASN F  1 248 ? 161.799 59.673  2.311   1.00   70.72  ? 248 ASN F CG  1 
ATOM   16899 O OD1 . ASN F  1 248 ? 161.592 60.845  2.598   1.00   71.97  ? 248 ASN F OD1 1 
ATOM   16900 N ND2 . ASN F  1 248 ? 162.514 58.869  3.084   1.00   70.78  ? 248 ASN F ND2 1 
ATOM   16901 N N   . LYS F  1 249 ? 160.395 58.527  -1.583  1.00   62.05  ? 249 LYS F N   1 
ATOM   16902 C CA  . LYS F  1 249 ? 160.125 58.245  -2.992  1.00   62.78  ? 249 LYS F CA  1 
ATOM   16903 C C   . LYS F  1 249 ? 159.199 57.044  -3.138  1.00   62.66  ? 249 LYS F C   1 
ATOM   16904 O O   . LYS F  1 249 ? 159.099 56.435  -4.201  1.00   62.93  ? 249 LYS F O   1 
ATOM   16905 C CB  . LYS F  1 249 ? 161.419 57.947  -3.730  1.00   63.04  ? 249 LYS F CB  1 
ATOM   16906 C CG  . LYS F  1 249 ? 162.497 58.974  -3.563  1.00   67.43  ? 249 LYS F CG  1 
ATOM   16907 C CD  . LYS F  1 249 ? 163.707 58.633  -4.402  1.00   72.00  ? 249 LYS F CD  1 
ATOM   16908 C CE  . LYS F  1 249 ? 164.912 59.493  -4.051  1.00   77.62  ? 249 LYS F CE  1 
ATOM   16909 N NZ  . LYS F  1 249 ? 166.093 59.195  -4.921  1.00   82.39  ? 249 LYS F NZ  1 
ATOM   16910 N N   . HIS F  1 250 ? 158.515 56.727  -2.051  1.00   49.41  ? 250 HIS F N   1 
ATOM   16911 C CA  . HIS F  1 250 ? 157.534 55.654  -2.019  1.00   52.64  ? 250 HIS F CA  1 
ATOM   16912 C C   . HIS F  1 250 ? 156.116 56.146  -2.011  1.00   49.98  ? 250 HIS F C   1 
ATOM   16913 O O   . HIS F  1 250 ? 155.775 57.065  -1.267  1.00   51.69  ? 250 HIS F O   1 
ATOM   16914 C CB  . HIS F  1 250 ? 157.724 54.768  -0.798  1.00   55.15  ? 250 HIS F CB  1 
ATOM   16915 C CG  . HIS F  1 250 ? 158.897 53.860  -0.892  1.00   60.18  ? 250 HIS F CG  1 
ATOM   16916 N ND1 . HIS F  1 250 ? 158.826 52.641  -1.527  1.00   61.03  ? 250 HIS F ND1 1 
ATOM   16917 C CD2 . HIS F  1 250 ? 160.156 53.967  -0.413  1.00   64.37  ? 250 HIS F CD2 1 
ATOM   16918 C CE1 . HIS F  1 250 ? 159.999 52.043  -1.460  1.00   66.04  ? 250 HIS F CE1 1 
ATOM   16919 N NE2 . HIS F  1 250 ? 160.823 52.827  -0.786  1.00   69.05  ? 250 HIS F NE2 1 
ATOM   16920 N N   . LEU F  1 251 ? 155.300 55.544  -2.870  1.00   48.14  ? 251 LEU F N   1 
ATOM   16921 C CA  . LEU F  1 251 ? 153.879 55.866  -2.982  1.00   43.81  ? 251 LEU F CA  1 
ATOM   16922 C C   . LEU F  1 251 ? 152.978 54.701  -2.560  1.00   42.54  ? 251 LEU F C   1 
ATOM   16923 O O   . LEU F  1 251 ? 153.165 53.594  -3.037  1.00   42.03  ? 251 LEU F O   1 
ATOM   16924 C CB  . LEU F  1 251 ? 153.538 56.245  -4.410  1.00   44.73  ? 251 LEU F CB  1 
ATOM   16925 C CG  . LEU F  1 251 ? 154.183 57.536  -4.865  1.00   49.04  ? 251 LEU F CG  1 
ATOM   16926 C CD1 . LEU F  1 251 ? 153.697 57.872  -6.246  1.00   51.05  ? 251 LEU F CD1 1 
ATOM   16927 C CD2 . LEU F  1 251 ? 153.879 58.643  -3.899  1.00   50.69  ? 251 LEU F CD2 1 
ATOM   16928 N N   . VAL F  1 252 ? 152.060 54.933  -1.622  1.00   41.96  ? 252 VAL F N   1 
ATOM   16929 C CA  . VAL F  1 252 ? 151.029 53.960  -1.301  1.00   41.33  ? 252 VAL F CA  1 
ATOM   16930 C C   . VAL F  1 252 ? 149.786 54.389  -2.084  1.00   39.77  ? 252 VAL F C   1 
ATOM   16931 O O   . VAL F  1 252 ? 149.213 55.431  -1.806  1.00   41.51  ? 252 VAL F O   1 
ATOM   16932 C CB  . VAL F  1 252 ? 150.737 53.913  0.200   1.00   39.39  ? 252 VAL F CB  1 
ATOM   16933 C CG1 . VAL F  1 252 ? 149.689 52.889  0.494   1.00   37.55  ? 252 VAL F CG1 1 
ATOM   16934 C CG2 . VAL F  1 252 ? 151.991 53.587  0.962   1.00   41.52  ? 252 VAL F CG2 1 
ATOM   16935 N N   . ILE F  1 253 ? 149.391 53.617  -3.090  1.00   39.76  ? 253 ILE F N   1 
ATOM   16936 C CA  . ILE F  1 253 ? 148.306 54.027  -3.992  1.00   37.23  ? 253 ILE F CA  1 
ATOM   16937 C C   . ILE F  1 253 ? 147.000 53.221  -3.867  1.00   35.93  ? 253 ILE F C   1 
ATOM   16938 O O   . ILE F  1 253 ? 146.893 52.125  -4.404  1.00   37.94  ? 253 ILE F O   1 
ATOM   16939 C CB  . ILE F  1 253 ? 148.799 53.947  -5.442  1.00   38.59  ? 253 ILE F CB  1 
ATOM   16940 C CG1 . ILE F  1 253 ? 150.104 54.734  -5.573  1.00   39.39  ? 253 ILE F CG1 1 
ATOM   16941 C CG2 . ILE F  1 253 ? 147.748 54.487  -6.372  1.00   38.05  ? 253 ILE F CG2 1 
ATOM   16942 C CD1 . ILE F  1 253 ? 150.992 54.318  -6.728  1.00   42.79  ? 253 ILE F CD1 1 
ATOM   16943 N N   . PRO F  1 254 ? 145.977 53.804  -3.231  1.00   35.82  ? 254 PRO F N   1 
ATOM   16944 C CA  . PRO F  1 254 ? 144.645 53.223  -2.985  1.00   35.30  ? 254 PRO F CA  1 
ATOM   16945 C C   . PRO F  1 254 ? 143.854 52.969  -4.290  1.00   36.49  ? 254 PRO F C   1 
ATOM   16946 O O   . PRO F  1 254 ? 144.069 53.686  -5.260  1.00   38.07  ? 254 PRO F O   1 
ATOM   16947 C CB  . PRO F  1 254 ? 143.967 54.281  -2.121  1.00   35.22  ? 254 PRO F CB  1 
ATOM   16948 C CG  . PRO F  1 254 ? 145.108 55.187  -1.617  1.00   34.24  ? 254 PRO F CG  1 
ATOM   16949 C CD  . PRO F  1 254 ? 146.083 55.177  -2.703  1.00   33.99  ? 254 PRO F CD  1 
ATOM   16950 N N   . THR F  1 255 ? 143.036 51.923  -4.359  1.00   39.01  ? 255 THR F N   1 
ATOM   16951 C CA  . THR F  1 255 ? 142.189 51.725  -5.545  1.00   41.15  ? 255 THR F CA  1 
ATOM   16952 C C   . THR F  1 255 ? 140.674 51.832  -5.283  1.00   42.61  ? 255 THR F C   1 
ATOM   16953 O O   . THR F  1 255 ? 140.216 51.787  -4.141  1.00   42.08  ? 255 THR F O   1 
ATOM   16954 C CB  . THR F  1 255 ? 142.459 50.370  -6.190  1.00   44.44  ? 255 THR F CB  1 
ATOM   16955 O OG1 . THR F  1 255 ? 142.193 49.341  -5.234  1.00   48.57  ? 255 THR F OG1 1 
ATOM   16956 C CG2 . THR F  1 255 ? 143.892 50.258  -6.613  1.00   40.16  ? 255 THR F CG2 1 
ATOM   16957 N N   . GLY F  1 271 ? 135.128 60.235  -11.612 1.00   74.87  ? 271 GLY F N   1 
ATOM   16958 C CA  . GLY F  1 271 ? 134.127 61.175  -11.136 1.00   78.47  ? 271 GLY F CA  1 
ATOM   16959 C C   . GLY F  1 271 ? 133.122 60.570  -10.169 1.00   80.25  ? 271 GLY F C   1 
ATOM   16960 O O   . GLY F  1 271 ? 131.926 60.450  -10.476 1.00   83.05  ? 271 GLY F O   1 
ATOM   16961 N N   . GLU F  1 272 ? 133.605 60.225  -8.979  1.00   76.93  ? 272 GLU F N   1 
ATOM   16962 C CA  . GLU F  1 272 ? 132.779 59.613  -7.949  1.00   74.97  ? 272 GLU F CA  1 
ATOM   16963 C C   . GLU F  1 272 ? 133.173 60.300  -6.639  1.00   64.59  ? 272 GLU F C   1 
ATOM   16964 O O   . GLU F  1 272 ? 133.927 61.259  -6.674  1.00   65.00  ? 272 GLU F O   1 
ATOM   16965 C CB  . GLU F  1 272 ? 133.004 58.089  -7.968  1.00   81.26  ? 272 GLU F CB  1 
ATOM   16966 C CG  . GLU F  1 272 ? 131.834 57.237  -7.477  1.00   88.50  ? 272 GLU F CG  1 
ATOM   16967 C CD  . GLU F  1 272 ? 131.721 57.038  -5.964  1.00   91.74  ? 272 GLU F CD  1 
ATOM   16968 O OE1 . GLU F  1 272 ? 132.626 57.451  -5.205  1.00   92.93  ? 272 GLU F OE1 1 
ATOM   16969 O OE2 . GLU F  1 272 ? 130.693 56.446  -5.531  1.00   93.74  ? 272 GLU F OE2 1 
ATOM   16970 N N   . ILE F  1 273 ? 132.686 59.833  -5.495  1.00   57.34  ? 273 ILE F N   1 
ATOM   16971 C CA  . ILE F  1 273 ? 133.004 60.445  -4.192  1.00   51.81  ? 273 ILE F CA  1 
ATOM   16972 C C   . ILE F  1 273 ? 134.490 60.212  -3.832  1.00   48.85  ? 273 ILE F C   1 
ATOM   16973 O O   . ILE F  1 273 ? 135.045 59.144  -4.111  1.00   49.11  ? 273 ILE F O   1 
ATOM   16974 C CB  . ILE F  1 273 ? 132.096 59.864  -3.049  1.00   54.08  ? 273 ILE F CB  1 
ATOM   16975 C CG1 . ILE F  1 273 ? 130.624 59.959  -3.394  1.00   53.42  ? 273 ILE F CG1 1 
ATOM   16976 C CG2 . ILE F  1 273 ? 132.304 60.618  -1.747  1.00   52.20  ? 273 ILE F CG2 1 
ATOM   16977 C CD1 . ILE F  1 273 ? 129.760 59.540  -2.235  1.00   53.36  ? 273 ILE F CD1 1 
ATOM   16978 N N   . GLY F  1 274 ? 135.129 61.189  -3.191  1.00   42.99  ? 274 GLY F N   1 
ATOM   16979 C CA  . GLY F  1 274 ? 136.515 61.032  -2.792  1.00   37.90  ? 274 GLY F CA  1 
ATOM   16980 C C   . GLY F  1 274 ? 136.655 59.829  -1.888  1.00   38.86  ? 274 GLY F C   1 
ATOM   16981 O O   . GLY F  1 274 ? 135.656 59.314  -1.394  1.00   41.28  ? 274 GLY F O   1 
ATOM   16982 N N   . GLY F  1 275 ? 137.878 59.346  -1.704  1.00   37.25  ? 275 GLY F N   1 
ATOM   16983 C CA  . GLY F  1 275 ? 138.081 58.161  -0.904  1.00   34.51  ? 275 GLY F CA  1 
ATOM   16984 C C   . GLY F  1 275 ? 138.462 58.496  0.509   1.00   33.86  ? 275 GLY F C   1 
ATOM   16985 O O   . GLY F  1 275 ? 138.480 57.619  1.360   1.00   37.08  ? 275 GLY F O   1 
ATOM   16986 N N   . ALA F  1 276 ? 138.759 59.767  0.765   1.00   31.87  ? 276 ALA F N   1 
ATOM   16987 C CA  . ALA F  1 276 ? 139.178 60.180  2.106   1.00   29.38  ? 276 ALA F CA  1 
ATOM   16988 C C   . ALA F  1 276 ? 138.148 61.033  2.834   1.00   29.39  ? 276 ALA F C   1 
ATOM   16989 O O   . ALA F  1 276 ? 137.858 62.150  2.448   1.00   31.38  ? 276 ALA F O   1 
ATOM   16990 C CB  . ALA F  1 276 ? 140.479 60.918  2.044   1.00   25.90  ? 276 ALA F CB  1 
ATOM   16991 N N   . LEU F  1 277 ? 137.639 60.496  3.929   1.00   27.76  ? 277 LEU F N   1 
ATOM   16992 C CA  . LEU F  1 277 ? 136.717 61.200  4.774   1.00   24.81  ? 277 LEU F CA  1 
ATOM   16993 C C   . LEU F  1 277 ? 137.417 62.247  5.619   1.00   28.76  ? 277 LEU F C   1 
ATOM   16994 O O   . LEU F  1 277 ? 138.537 62.031  6.101   1.00   28.11  ? 277 LEU F O   1 
ATOM   16995 C CB  . LEU F  1 277 ? 136.028 60.210  5.685   1.00   26.76  ? 277 LEU F CB  1 
ATOM   16996 C CG  . LEU F  1 277 ? 135.132 60.806  6.758   1.00   25.06  ? 277 LEU F CG  1 
ATOM   16997 C CD1 . LEU F  1 277 ? 133.836 61.326  6.127   1.00   25.05  ? 277 LEU F CD1 1 
ATOM   16998 C CD2 . LEU F  1 277 ? 134.892 59.744  7.801   1.00   25.43  ? 277 LEU F CD2 1 
ATOM   16999 N N   . ILE F  1 278 ? 136.758 63.390  5.811   1.00   30.66  ? 278 ILE F N   1 
ATOM   17000 C CA  . ILE F  1 278 ? 137.223 64.363  6.791   1.00   27.65  ? 278 ILE F CA  1 
ATOM   17001 C C   . ILE F  1 278 ? 136.274 64.389  7.951   1.00   28.18  ? 278 ILE F C   1 
ATOM   17002 O O   . ILE F  1 278 ? 135.075 64.530  7.754   1.00   29.83  ? 278 ILE F O   1 
ATOM   17003 C CB  . ILE F  1 278 ? 137.328 65.750  6.215   1.00   24.88  ? 278 ILE F CB  1 
ATOM   17004 C CG1 . ILE F  1 278 ? 138.168 65.715  4.936   1.00   23.90  ? 278 ILE F CG1 1 
ATOM   17005 C CG2 . ILE F  1 278 ? 137.941 66.673  7.239   1.00   25.36  ? 278 ILE F CG2 1 
ATOM   17006 C CD1 . ILE F  1 278 ? 138.153 66.996  4.173   1.00   25.06  ? 278 ILE F CD1 1 
ATOM   17007 N N   . THR F  1 279 ? 136.806 64.253  9.159   1.00   27.35  ? 279 THR F N   1 
ATOM   17008 C CA  . THR F  1 279 ? 135.960 64.163  10.341  1.00   27.71  ? 279 THR F CA  1 
ATOM   17009 C C   . THR F  1 279 ? 136.619 64.849  11.538  1.00   29.33  ? 279 THR F C   1 
ATOM   17010 O O   . THR F  1 279 ? 137.815 65.088  11.530  1.00   33.99  ? 279 THR F O   1 
ATOM   17011 C CB  . THR F  1 279 ? 135.660 62.700  10.690  1.00   27.42  ? 279 THR F CB  1 
ATOM   17012 O OG1 . THR F  1 279 ? 134.821 62.635  11.848  1.00   28.96  ? 279 THR F OG1 1 
ATOM   17013 C CG2 . THR F  1 279 ? 136.932 61.972  10.978  1.00   30.10  ? 279 THR F CG2 1 
ATOM   17014 N N   . THR F  1 280 ? 135.829 65.238  12.534  1.00   28.41  ? 280 THR F N   1 
ATOM   17015 C CA  . THR F  1 280 ? 136.399 65.805  13.749  1.00   28.22  ? 280 THR F CA  1 
ATOM   17016 C C   . THR F  1 280 ? 136.108 64.917  14.932  1.00   29.37  ? 280 THR F C   1 
ATOM   17017 O O   . THR F  1 280 ? 136.408 65.290  16.063  1.00   33.89  ? 280 THR F O   1 
ATOM   17018 C CB  . THR F  1 280 ? 135.858 67.236  14.092  1.00   27.18  ? 280 THR F CB  1 
ATOM   17019 O OG1 . THR F  1 280 ? 134.426 67.237  14.231  1.00   28.06  ? 280 THR F OG1 1 
ATOM   17020 C CG2 . THR F  1 280 ? 136.250 68.222  13.053  1.00   29.10  ? 280 THR F CG2 1 
ATOM   17021 N N   . THR F  1 281 ? 135.503 63.760  14.702  1.00   29.03  ? 281 THR F N   1 
ATOM   17022 C CA  . THR F  1 281 ? 135.007 62.982  15.837  1.00   32.32  ? 281 THR F CA  1 
ATOM   17023 C C   . THR F  1 281 ? 135.913 61.805  16.228  1.00   34.90  ? 281 THR F C   1 
ATOM   17024 O O   . THR F  1 281 ? 135.560 60.992  17.076  1.00   34.38  ? 281 THR F O   1 
ATOM   17025 C CB  . THR F  1 281 ? 133.581 62.504  15.572  1.00   31.41  ? 281 THR F CB  1 
ATOM   17026 O OG1 . THR F  1 281 ? 133.512 61.880  14.285  1.00   30.66  ? 281 THR F OG1 1 
ATOM   17027 C CG2 . THR F  1 281 ? 132.645 63.711  15.560  1.00   30.71  ? 281 THR F CG2 1 
ATOM   17028 N N   . HIS F  1 282 ? 137.100 61.744  15.634  1.00   36.12  ? 282 HIS F N   1 
ATOM   17029 C CA  . HIS F  1 282 ? 138.174 60.972  16.231  1.00   37.14  ? 282 HIS F CA  1 
ATOM   17030 C C   . HIS F  1 282 ? 139.469 61.730  15.985  1.00   36.26  ? 282 HIS F C   1 
ATOM   17031 O O   . HIS F  1 282 ? 139.612 62.376  14.950  1.00   35.87  ? 282 HIS F O   1 
ATOM   17032 C CB  . HIS F  1 282 ? 138.236 59.534  15.675  1.00   38.23  ? 282 HIS F CB  1 
ATOM   17033 C CG  . HIS F  1 282 ? 138.377 59.428  14.183  1.00   37.68  ? 282 HIS F CG  1 
ATOM   17034 N ND1 . HIS F  1 282 ? 139.517 59.811  13.508  1.00   39.64  ? 282 HIS F ND1 1 
ATOM   17035 C CD2 . HIS F  1 282 ? 137.544 58.921  13.245  1.00   35.76  ? 282 HIS F CD2 1 
ATOM   17036 C CE1 . HIS F  1 282 ? 139.372 59.564  12.218  1.00   36.61  ? 282 HIS F CE1 1 
ATOM   17037 N NE2 . HIS F  1 282 ? 138.182 59.027  12.033  1.00   35.27  ? 282 HIS F NE2 1 
ATOM   17038 N N   . PRO F  1 283 ? 140.404 61.688  16.953  1.00   37.09  ? 283 PRO F N   1 
ATOM   17039 C CA  . PRO F  1 283 ? 141.631 62.466  16.819  1.00   36.72  ? 283 PRO F CA  1 
ATOM   17040 C C   . PRO F  1 283 ? 142.578 61.938  15.757  1.00   38.28  ? 283 PRO F C   1 
ATOM   17041 O O   . PRO F  1 283 ? 143.090 62.716  14.960  1.00   40.33  ? 283 PRO F O   1 
ATOM   17042 C CB  . PRO F  1 283 ? 142.264 62.375  18.215  1.00   40.20  ? 283 PRO F CB  1 
ATOM   17043 C CG  . PRO F  1 283 ? 141.656 61.219  18.857  1.00   40.25  ? 283 PRO F CG  1 
ATOM   17044 C CD  . PRO F  1 283 ? 140.266 61.139  18.314  1.00   38.26  ? 283 PRO F CD  1 
ATOM   17045 N N   . TYR F  1 284 ? 142.836 60.643  15.728  1.00   37.89  ? 284 TYR F N   1 
ATOM   17046 C CA  . TYR F  1 284 ? 143.883 60.181  14.831  1.00   36.78  ? 284 TYR F CA  1 
ATOM   17047 C C   . TYR F  1 284 ? 143.332 59.800  13.497  1.00   35.78  ? 284 TYR F C   1 
ATOM   17048 O O   . TYR F  1 284 ? 142.156 59.551  13.364  1.00   38.39  ? 284 TYR F O   1 
ATOM   17049 C CB  . TYR F  1 284 ? 144.639 59.016  15.448  1.00   37.92  ? 284 TYR F CB  1 
ATOM   17050 C CG  . TYR F  1 284 ? 145.148 59.364  16.810  1.00   41.39  ? 284 TYR F CG  1 
ATOM   17051 C CD1 . TYR F  1 284 ? 146.011 60.421  16.986  1.00   43.93  ? 284 TYR F CD1 1 
ATOM   17052 C CD2 . TYR F  1 284 ? 144.729 58.669  17.929  1.00   45.71  ? 284 TYR F CD2 1 
ATOM   17053 C CE1 . TYR F  1 284 ? 146.468 60.752  18.230  1.00   48.63  ? 284 TYR F CE1 1 
ATOM   17054 C CE2 . TYR F  1 284 ? 145.176 59.000  19.178  1.00   48.89  ? 284 TYR F CE2 1 
ATOM   17055 C CZ  . TYR F  1 284 ? 146.049 60.039  19.321  1.00   52.19  ? 284 TYR F CZ  1 
ATOM   17056 O OH  . TYR F  1 284 ? 146.512 60.376  20.571  1.00   61.48  ? 284 TYR F OH  1 
ATOM   17057 N N   . THR F  1 285 ? 144.198 59.788  12.499  1.00   35.37  ? 285 THR F N   1 
ATOM   17058 C CA  . THR F  1 285 ? 143.813 59.396  11.162  1.00   35.04  ? 285 THR F CA  1 
ATOM   17059 C C   . THR F  1 285 ? 143.670 57.895  11.096  1.00   36.99  ? 285 THR F C   1 
ATOM   17060 O O   . THR F  1 285 ? 144.534 57.161  11.578  1.00   39.61  ? 285 THR F O   1 
ATOM   17061 C CB  . THR F  1 285 ? 144.832 59.876  10.133  1.00   35.32  ? 285 THR F CB  1 
ATOM   17062 O OG1 . THR F  1 285 ? 144.803 61.303  10.121  1.00   36.24  ? 285 THR F OG1 1 
ATOM   17063 C CG2 . THR F  1 285 ? 144.491 59.380  8.740   1.00   27.83  ? 285 THR F CG2 1 
ATOM   17064 N N   . VAL F  1 286 ? 142.555 57.455  10.523  1.00   34.88  ? 286 VAL F N   1 
ATOM   17065 C CA  . VAL F  1 286 ? 142.214 56.056  10.462  1.00   33.05  ? 286 VAL F CA  1 
ATOM   17066 C C   . VAL F  1 286 ? 142.318 55.527  9.045   1.00   32.79  ? 286 VAL F C   1 
ATOM   17067 O O   . VAL F  1 286 ? 141.757 56.082  8.109   1.00   30.12  ? 286 VAL F O   1 
ATOM   17068 C CB  . VAL F  1 286 ? 140.819 55.811  11.003  1.00   34.03  ? 286 VAL F CB  1 
ATOM   17069 C CG1 . VAL F  1 286 ? 140.429 54.371  10.816  1.00   33.75  ? 286 VAL F CG1 1 
ATOM   17070 C CG2 . VAL F  1 286 ? 140.770 56.189  12.468  1.00   35.55  ? 286 VAL F CG2 1 
ATOM   17071 N N   . LEU F  1 287 ? 143.045 54.427  8.919   1.00   34.96  ? 287 LEU F N   1 
ATOM   17072 C CA  . LEU F  1 287 ? 143.272 53.767  7.659   1.00   32.81  ? 287 LEU F CA  1 
ATOM   17073 C C   . LEU F  1 287 ? 142.631 52.382  7.665   1.00   37.19  ? 287 LEU F C   1 
ATOM   17074 O O   . LEU F  1 287 ? 142.675 51.653  8.677   1.00   38.78  ? 287 LEU F O   1 
ATOM   17075 C CB  . LEU F  1 287 ? 144.774 53.647  7.393   1.00   31.94  ? 287 LEU F CB  1 
ATOM   17076 C CG  . LEU F  1 287 ? 145.676 54.879  7.480   1.00   30.71  ? 287 LEU F CG  1 
ATOM   17077 C CD1 . LEU F  1 287 ? 147.120 54.455  7.373   1.00   35.34  ? 287 LEU F CD1 1 
ATOM   17078 C CD2 . LEU F  1 287 ? 145.342 55.904  6.401   1.00   28.90  ? 287 LEU F CD2 1 
ATOM   17079 N N   . SER F  1 288 ? 142.028 52.016  6.539   1.00   37.30  ? 288 SER F N   1 
ATOM   17080 C CA  . SER F  1 288 ? 141.490 50.680  6.421   1.00   40.36  ? 288 SER F CA  1 
ATOM   17081 C C   . SER F  1 288 ? 142.665 49.723  6.472   1.00   44.53  ? 288 SER F C   1 
ATOM   17082 O O   . SER F  1 288 ? 143.788 50.083  6.107   1.00   43.62  ? 288 SER F O   1 
ATOM   17083 C CB  . SER F  1 288 ? 140.678 50.502  5.139   1.00   39.72  ? 288 SER F CB  1 
ATOM   17084 O OG  . SER F  1 288 ? 141.494 50.655  3.995   1.00   38.55  ? 288 SER F OG  1 
ATOM   17085 N N   . HIS F  1 289 ? 142.380 48.500  6.896   1.00   46.16  ? 289 HIS F N   1 
ATOM   17086 C CA  . HIS F  1 289 ? 143.396 47.529  7.198   1.00   40.74  ? 289 HIS F CA  1 
ATOM   17087 C C   . HIS F  1 289 ? 144.407 47.303  6.106   1.00   44.00  ? 289 HIS F C   1 
ATOM   17088 O O   . HIS F  1 289 ? 145.596 47.242  6.368   1.00   41.86  ? 289 HIS F O   1 
ATOM   17089 C CB  . HIS F  1 289 ? 142.756 46.198  7.510   1.00   44.06  ? 289 HIS F CB  1 
ATOM   17090 C CG  . HIS F  1 289 ? 143.759 45.126  7.738   1.00   54.93  ? 289 HIS F CG  1 
ATOM   17091 N ND1 . HIS F  1 289 ? 144.587 45.108  8.839   1.00   56.34  ? 289 HIS F ND1 1 
ATOM   17092 C CD2 . HIS F  1 289 ? 144.129 44.077  6.968   1.00   57.11  ? 289 HIS F CD2 1 
ATOM   17093 C CE1 . HIS F  1 289 ? 145.399 44.068  8.755   1.00   59.38  ? 289 HIS F CE1 1 
ATOM   17094 N NE2 . HIS F  1 289 ? 145.143 43.428  7.629   1.00   59.94  ? 289 HIS F NE2 1 
ATOM   17095 N N   . SER F  1 290 ? 143.936 47.163  4.882   1.00   44.51  ? 290 SER F N   1 
ATOM   17096 C CA  . SER F  1 290 ? 144.829 46.885  3.771   1.00   48.27  ? 290 SER F CA  1 
ATOM   17097 C C   . SER F  1 290 ? 145.796 48.042  3.517   1.00   42.91  ? 290 SER F C   1 
ATOM   17098 O O   . SER F  1 290 ? 146.957 47.830  3.184   1.00   43.67  ? 290 SER F O   1 
ATOM   17099 C CB  . SER F  1 290 ? 144.012 46.574  2.522   1.00   56.33  ? 290 SER F CB  1 
ATOM   17100 O OG  . SER F  1 290 ? 143.209 47.698  2.190   1.00   57.62  ? 290 SER F OG  1 
ATOM   17101 N N   . ILE F  1 291 ? 145.296 49.266  3.631   1.00   39.65  ? 291 ILE F N   1 
ATOM   17102 C CA  . ILE F  1 291 ? 146.137 50.449  3.512   1.00   38.91  ? 291 ILE F CA  1 
ATOM   17103 C C   . ILE F  1 291 ? 147.017 50.611  4.739   1.00   38.57  ? 291 ILE F C   1 
ATOM   17104 O O   . ILE F  1 291 ? 148.198 50.944  4.645   1.00   39.85  ? 291 ILE F O   1 
ATOM   17105 C CB  . ILE F  1 291 ? 145.296 51.714  3.305   1.00   37.34  ? 291 ILE F CB  1 
ATOM   17106 C CG1 . ILE F  1 291 ? 144.583 51.630  1.970   1.00   36.40  ? 291 ILE F CG1 1 
ATOM   17107 C CG2 . ILE F  1 291 ? 146.161 52.975  3.317   1.00   34.82  ? 291 ILE F CG2 1 
ATOM   17108 C CD1 . ILE F  1 291 ? 143.721 52.805  1.708   1.00   33.73  ? 291 ILE F CD1 1 
ATOM   17109 N N   . PHE F  1 292 ? 146.426 50.381  5.898   1.00   37.88  ? 292 PHE F N   1 
ATOM   17110 C CA  . PHE F  1 292 ? 147.170 50.463  7.127   1.00   37.51  ? 292 PHE F CA  1 
ATOM   17111 C C   . PHE F  1 292 ? 148.364 49.525  7.130   1.00   44.50  ? 292 PHE F C   1 
ATOM   17112 O O   . PHE F  1 292 ? 149.475 49.926  7.442   1.00   46.98  ? 292 PHE F O   1 
ATOM   17113 C CB  . PHE F  1 292 ? 146.276 50.128  8.295   1.00   38.24  ? 292 PHE F CB  1 
ATOM   17114 C CG  . PHE F  1 292 ? 146.996 50.061  9.595   1.00   40.48  ? 292 PHE F CG  1 
ATOM   17115 C CD1 . PHE F  1 292 ? 147.263 51.216  10.309  1.00   42.25  ? 292 PHE F CD1 1 
ATOM   17116 C CD2 . PHE F  1 292 ? 147.421 48.850  10.099  1.00   45.02  ? 292 PHE F CD2 1 
ATOM   17117 C CE1 . PHE F  1 292 ? 147.920 51.160  11.512  1.00   44.14  ? 292 PHE F CE1 1 
ATOM   17118 C CE2 . PHE F  1 292 ? 148.086 48.790  11.292  1.00   48.32  ? 292 PHE F CE2 1 
ATOM   17119 C CZ  . PHE F  1 292 ? 148.340 49.949  11.998  1.00   47.71  ? 292 PHE F CZ  1 
ATOM   17120 N N   . GLU F  1 293 ? 148.148 48.274  6.752   1.00   45.56  ? 293 GLU F N   1 
ATOM   17121 C CA  . GLU F  1 293 ? 149.208 47.282  6.845   1.00   46.93  ? 293 GLU F CA  1 
ATOM   17122 C C   . GLU F  1 293 ? 150.405 47.589  5.923   1.00   45.79  ? 293 GLU F C   1 
ATOM   17123 O O   . GLU F  1 293 ? 151.562 47.381  6.304   1.00   47.49  ? 293 GLU F O   1 
ATOM   17124 C CB  . GLU F  1 293 ? 148.634 45.890  6.574   1.00   51.52  ? 293 GLU F CB  1 
ATOM   17125 C CG  . GLU F  1 293 ? 149.143 44.869  7.561   1.00   60.55  ? 293 GLU F CG  1 
ATOM   17126 C CD  . GLU F  1 293 ? 148.492 43.522  7.410   1.00   71.85  ? 293 GLU F CD  1 
ATOM   17127 O OE1 . GLU F  1 293 ? 148.249 43.112  6.259   1.00   76.01  ? 293 GLU F OE1 1 
ATOM   17128 O OE2 . GLU F  1 293 ? 148.238 42.860  8.440   1.00   77.00  1 293 GLU F OE2 1 
ATOM   17129 N N   . VAL F  1 294 ? 150.132 48.041  4.704   1.00   45.31  ? 294 VAL F N   1 
ATOM   17130 C CA  . VAL F  1 294 ? 151.184 48.405  3.745   1.00   47.93  ? 294 VAL F CA  1 
ATOM   17131 C C   . VAL F  1 294 ? 151.878 49.719  4.106   1.00   49.61  ? 294 VAL F C   1 
ATOM   17132 O O   . VAL F  1 294 ? 153.096 49.837  4.007   1.00   52.97  ? 294 VAL F O   1 
ATOM   17133 C CB  . VAL F  1 294 ? 150.638 48.504  2.313   1.00   46.69  ? 294 VAL F CB  1 
ATOM   17134 C CG1 . VAL F  1 294 ? 151.680 49.106  1.376   1.00   41.65  ? 294 VAL F CG1 1 
ATOM   17135 C CG2 . VAL F  1 294 ? 150.204 47.130  1.835   1.00   48.33  ? 294 VAL F CG2 1 
ATOM   17136 N N   . PHE F  1 295 ? 151.090 50.715  4.487   1.00   47.21  ? 295 PHE F N   1 
ATOM   17137 C CA  . PHE F  1 295 ? 151.624 52.011  4.866   1.00   46.40  ? 295 PHE F CA  1 
ATOM   17138 C C   . PHE F  1 295 ? 152.537 51.965  6.089   1.00   51.13  ? 295 PHE F C   1 
ATOM   17139 O O   . PHE F  1 295 ? 153.596 52.570  6.089   1.00   52.01  ? 295 PHE F O   1 
ATOM   17140 C CB  . PHE F  1 295 ? 150.483 52.985  5.131   1.00   44.19  ? 295 PHE F CB  1 
ATOM   17141 C CG  . PHE F  1 295 ? 150.919 54.247  5.799   1.00   42.93  ? 295 PHE F CG  1 
ATOM   17142 C CD1 . PHE F  1 295 ? 151.539 55.248  5.080   1.00   41.80  ? 295 PHE F CD1 1 
ATOM   17143 C CD2 . PHE F  1 295 ? 150.716 54.432  7.149   1.00   43.44  ? 295 PHE F CD2 1 
ATOM   17144 C CE1 . PHE F  1 295 ? 151.944 56.399  5.689   1.00   37.80  ? 295 PHE F CE1 1 
ATOM   17145 C CE2 . PHE F  1 295 ? 151.123 55.592  7.764   1.00   42.85  ? 295 PHE F CE2 1 
ATOM   17146 C CZ  . PHE F  1 295 ? 151.739 56.570  7.035   1.00   40.67  ? 295 PHE F CZ  1 
ATOM   17147 N N   . THR F  1 296 ? 152.141 51.253  7.133   1.00   54.60  ? 296 THR F N   1 
ATOM   17148 C CA  . THR F  1 296 ? 152.935 51.244  8.352   1.00   46.11  ? 296 THR F CA  1 
ATOM   17149 C C   . THR F  1 296 ? 154.285 50.613  8.069   1.00   53.44  ? 296 THR F C   1 
ATOM   17150 O O   . THR F  1 296 ? 155.294 50.981  8.659   1.00   57.69  ? 296 THR F O   1 
ATOM   17151 C CB  . THR F  1 296 ? 152.224 50.495  9.475   1.00   47.88  ? 296 THR F CB  1 
ATOM   17152 O OG1 . THR F  1 296 ? 150.994 51.153  9.776   1.00   51.61  ? 296 THR F OG1 1 
ATOM   17153 C CG2 . THR F  1 296 ? 153.072 50.466  10.709  1.00   50.86  ? 296 THR F CG2 1 
ATOM   17154 N N   . GLN F  1 297 ? 154.296 49.656  7.152   1.00   53.04  ? 297 GLN F N   1 
ATOM   17155 C CA  . GLN F  1 297 ? 155.517 48.979  6.773   1.00   56.78  ? 297 GLN F CA  1 
ATOM   17156 C C   . GLN F  1 297 ? 156.424 49.873  5.950   1.00   51.94  ? 297 GLN F C   1 
ATOM   17157 O O   . GLN F  1 297 ? 157.626 49.909  6.185   1.00   54.91  ? 297 GLN F O   1 
ATOM   17158 C CB  . GLN F  1 297 ? 155.207 47.698  5.989   1.00   60.62  ? 297 GLN F CB  1 
ATOM   17159 C CG  . GLN F  1 297 ? 155.280 46.411  6.814   1.00   66.50  ? 297 GLN F CG  1 
ATOM   17160 C CD  . GLN F  1 297 ? 156.597 46.244  7.553   1.00   68.53  ? 297 GLN F CD  1 
ATOM   17161 O OE1 . GLN F  1 297 ? 156.619 46.038  8.767   1.00   70.54  ? 297 GLN F OE1 1 
ATOM   17162 N NE2 . GLN F  1 297 ? 157.701 46.318  6.819   1.00   67.85  ? 297 GLN F NE2 1 
ATOM   17163 N N   . VAL F  1 298 ? 155.867 50.563  4.965   1.00   48.93  ? 298 VAL F N   1 
ATOM   17164 C CA  . VAL F  1 298 ? 156.652 51.507  4.165   1.00   50.53  ? 298 VAL F CA  1 
ATOM   17165 C C   . VAL F  1 298 ? 157.305 52.587  5.048   1.00   50.47  ? 298 VAL F C   1 
ATOM   17166 O O   . VAL F  1 298 ? 158.469 52.940  4.852   1.00   52.94  ? 298 VAL F O   1 
ATOM   17167 C CB  . VAL F  1 298 ? 155.792 52.186  3.078   1.00   48.61  ? 298 VAL F CB  1 
ATOM   17168 C CG1 . VAL F  1 298 ? 156.518 53.381  2.494   1.00   49.77  ? 298 VAL F CG1 1 
ATOM   17169 C CG2 . VAL F  1 298 ? 155.453 51.207  1.974   1.00   46.94  ? 298 VAL F CG2 1 
ATOM   17170 N N   . PHE F  1 299 ? 156.558 53.099  6.027   1.00   49.39  ? 299 PHE F N   1 
ATOM   17171 C CA  . PHE F  1 299 ? 157.097 54.084  6.965   1.00   54.09  ? 299 PHE F CA  1 
ATOM   17172 C C   . PHE F  1 299 ? 158.219 53.484  7.792   1.00   60.42  ? 299 PHE F C   1 
ATOM   17173 O O   . PHE F  1 299 ? 159.257 54.112  7.982   1.00   66.14  ? 299 PHE F O   1 
ATOM   17174 C CB  . PHE F  1 299 ? 156.014 54.620  7.889   1.00   49.51  ? 299 PHE F CB  1 
ATOM   17175 C CG  . PHE F  1 299 ? 156.470 55.747  8.761   1.00   51.84  ? 299 PHE F CG  1 
ATOM   17176 C CD1 . PHE F  1 299 ? 157.053 55.489  9.993   1.00   55.04  ? 299 PHE F CD1 1 
ATOM   17177 C CD2 . PHE F  1 299 ? 156.301 57.062  8.368   1.00   52.42  ? 299 PHE F CD2 1 
ATOM   17178 C CE1 . PHE F  1 299 ? 157.471 56.520  10.815  1.00   60.31  ? 299 PHE F CE1 1 
ATOM   17179 C CE2 . PHE F  1 299 ? 156.713 58.108  9.189   1.00   56.31  ? 299 PHE F CE2 1 
ATOM   17180 C CZ  . PHE F  1 299 ? 157.302 57.836  10.414  1.00   59.49  ? 299 PHE F CZ  1 
ATOM   17181 N N   . ALA F  1 300 ? 157.996 52.275  8.294   1.00   61.53  ? 300 ALA F N   1 
ATOM   17182 C CA  . ALA F  1 300 ? 158.991 51.586  9.105   1.00   61.06  ? 300 ALA F CA  1 
ATOM   17183 C C   . ALA F  1 300 ? 160.299 51.424  8.326   1.00   63.59  ? 300 ALA F C   1 
ATOM   17184 O O   . ALA F  1 300 ? 161.394 51.496  8.901   1.00   67.82  ? 300 ALA F O   1 
ATOM   17185 C CB  . ALA F  1 300 ? 158.462 50.241  9.551   1.00   61.71  ? 300 ALA F CB  1 
ATOM   17186 N N   . ASN F  1 301 ? 160.164 51.245  7.013   1.00   61.29  ? 301 ASN F N   1 
ATOM   17187 C CA  . ASN F  1 301 ? 161.294 51.135  6.096   1.00   63.30  ? 301 ASN F CA  1 
ATOM   17188 C C   . ASN F  1 301 ? 162.063 52.452  5.887   1.00   68.34  ? 301 ASN F C   1 
ATOM   17189 O O   . ASN F  1 301 ? 163.219 52.436  5.464   1.00   67.58  ? 301 ASN F O   1 
ATOM   17190 C CB  . ASN F  1 301 ? 160.813 50.618  4.729   1.00   60.57  ? 301 ASN F CB  1 
ATOM   17191 C CG  . ASN F  1 301 ? 160.383 49.150  4.752   1.00   66.51  ? 301 ASN F CG  1 
ATOM   17192 O OD1 . ASN F  1 301 ? 160.606 48.422  5.724   1.00   63.54  ? 301 ASN F OD1 1 
ATOM   17193 N ND2 . ASN F  1 301 ? 159.725 48.724  3.678   1.00   64.09  ? 301 ASN F ND2 1 
ATOM   17194 N N   . ASN F  1 302 ? 161.438 53.589  6.176   1.00   66.70  ? 302 ASN F N   1 
ATOM   17195 C CA  . ASN F  1 302 ? 162.130 54.876  6.051   1.00   69.00  ? 302 ASN F CA  1 
ATOM   17196 C C   . ASN F  1 302 ? 162.552 55.404  7.423   1.00   74.13  ? 302 ASN F C   1 
ATOM   17197 O O   . ASN F  1 302 ? 162.751 56.603  7.605   1.00   75.93  ? 302 ASN F O   1 
ATOM   17198 C CB  . ASN F  1 302 ? 161.263 55.909  5.291   1.00   60.77  ? 302 ASN F CB  1 
ATOM   17199 C CG  . ASN F  1 302 ? 161.281 55.691  3.767   1.00   59.19  ? 302 ASN F CG  1 
ATOM   17200 O OD1 . ASN F  1 302 ? 162.075 56.297  3.052   1.00   61.11  ? 302 ASN F OD1 1 
ATOM   17201 N ND2 . ASN F  1 302 ? 160.427 54.806  3.281   1.00   56.21  ? 302 ASN F ND2 1 
ATOM   17202 N N   . MET F  1 303 ? 162.709 54.493  8.381   1.00   67.73  ? 303 MET F N   1 
ATOM   17203 C CA  . MET F  1 303 ? 163.120 54.860  9.730   1.00   80.17  ? 303 MET F CA  1 
ATOM   17204 C C   . MET F  1 303 ? 164.156 53.846  10.211  1.00   83.56  ? 303 MET F C   1 
ATOM   17205 O O   . MET F  1 303 ? 164.231 52.749  9.673   1.00   87.65  ? 303 MET F O   1 
ATOM   17206 C CB  . MET F  1 303 ? 161.916 54.884  10.671  1.00   65.90  ? 303 MET F CB  1 
ATOM   17207 C CG  . MET F  1 303 ? 160.903 55.948  10.324  1.00   63.93  ? 303 MET F CG  1 
ATOM   17208 S SD  . MET F  1 303 ? 161.532 57.613  10.595  1.00   81.88  ? 303 MET F SD  1 
ATOM   17209 C CE  . MET F  1 303 ? 161.430 57.744  12.371  1.00   67.25  ? 303 MET F CE  1 
ATOM   17210 N N   . PRO F  1 304 ? 164.982 54.210  11.204  1.00   82.55  ? 304 PRO F N   1 
ATOM   17211 C CA  . PRO F  1 304 ? 165.882 53.228  11.828  1.00   82.80  ? 304 PRO F CA  1 
ATOM   17212 C C   . PRO F  1 304 ? 165.131 52.190  12.664  1.00   81.27  ? 304 PRO F C   1 
ATOM   17213 O O   . PRO F  1 304 ? 164.585 52.511  13.714  1.00   80.87  ? 304 PRO F O   1 
ATOM   17214 C CB  . PRO F  1 304 ? 166.783 54.089  12.705  1.00   84.94  ? 304 PRO F CB  1 
ATOM   17215 C CG  . PRO F  1 304 ? 166.002 55.347  12.933  1.00   83.97  ? 304 PRO F CG  1 
ATOM   17216 C CD  . PRO F  1 304 ? 165.246 55.579  11.675  1.00   82.67  ? 304 PRO F CD  1 
ATOM   17217 N N   . LYS F  1 305 ? 165.140 50.943  12.213  1.00   81.20  ? 305 LYS F N   1 
ATOM   17218 C CA  . LYS F  1 305 ? 164.365 49.877  12.846  1.00   72.26  ? 305 LYS F CA  1 
ATOM   17219 C C   . LYS F  1 305 ? 164.826 49.541  14.265  1.00   73.68  ? 305 LYS F C   1 
ATOM   17220 O O   . LYS F  1 305 ? 164.050 49.028  15.070  1.00   72.44  ? 305 LYS F O   1 
ATOM   17221 C CB  . LYS F  1 305 ? 164.438 48.617  11.985  0.0000 73.23  ? 305 LYS F CB  1 
ATOM   17222 C CG  . LYS F  1 305 ? 163.955 47.344  12.656  0.0000 73.28  ? 305 LYS F CG  1 
ATOM   17223 C CD  . LYS F  1 305 ? 164.764 46.171  12.189  0.0000 76.42  ? 305 LYS F CD  1 
ATOM   17224 C CE  . LYS F  1 305 ? 164.094 44.869  12.530  0.0000 76.69  ? 305 LYS F CE  1 
ATOM   17225 N NZ  . LYS F  1 305 ? 164.833 43.730  11.933  0.0000 80.22  ? 305 LYS F NZ  1 
ATOM   17226 N N   . GLN F  1 306 ? 166.066 49.879  14.607  1.00   79.29  ? 306 GLN F N   1 
ATOM   17227 C CA  . GLN F  1 306 ? 166.610 49.408  15.874  1.00   81.43  ? 306 GLN F CA  1 
ATOM   17228 C C   . GLN F  1 306 ? 166.290 50.428  16.924  1.00   77.77  ? 306 GLN F C   1 
ATOM   17229 O O   . GLN F  1 306 ? 166.738 50.342  18.069  1.00   79.42  ? 306 GLN F O   1 
ATOM   17230 C CB  . GLN F  1 306 ? 168.136 49.252  15.792  0.0000 85.16  ? 306 GLN F CB  1 
ATOM   17231 C CG  . GLN F  1 306 ? 168.965 50.552  15.497  0.0000 84.68  ? 306 GLN F CG  1 
ATOM   17232 C CD  . GLN F  1 306 ? 168.657 51.284  14.182  0.0000 83.73  ? 306 GLN F CD  1 
ATOM   17233 O OE1 . GLN F  1 306 ? 167.759 50.906  13.430  0.0000 81.02  ? 306 GLN F OE1 1 
ATOM   17234 N NE2 . GLN F  1 306 ? 169.426 52.340  13.904  0.0000 86.44  ? 306 GLN F NE2 1 
ATOM   17235 N N   . ALA F  1 307 ? 165.428 51.350  16.522  1.00   75.49  ? 307 ALA F N   1 
ATOM   17236 C CA  . ALA F  1 307 ? 164.963 52.416  17.376  1.00   75.24  ? 307 ALA F CA  1 
ATOM   17237 C C   . ALA F  1 307 ? 163.523 52.238  17.794  1.00   72.23  ? 307 ALA F C   1 
ATOM   17238 O O   . ALA F  1 307 ? 163.014 52.971  18.638  1.00   72.17  ? 307 ALA F O   1 
ATOM   17239 C CB  . ALA F  1 307 ? 165.130 53.718  16.665  1.00   76.03  ? 307 ALA F CB  1 
ATOM   17240 N N   . GLN F  1 308 ? 162.877 51.242  17.207  1.00   74.56  ? 308 GLN F N   1 
ATOM   17241 C CA  . GLN F  1 308 ? 161.477 50.969  17.481  1.00   71.66  ? 308 GLN F CA  1 
ATOM   17242 C C   . GLN F  1 308 ? 161.344 50.390  18.885  1.00   73.75  ? 308 GLN F C   1 
ATOM   17243 O O   . GLN F  1 308 ? 162.276 49.760  19.384  1.00   77.75  ? 308 GLN F O   1 
ATOM   17244 C CB  . GLN F  1 308 ? 160.919 50.015  16.433  1.00   70.76  ? 308 GLN F CB  1 
ATOM   17245 C CG  . GLN F  1 308 ? 161.217 50.491  15.035  1.00   71.73  ? 308 GLN F CG  1 
ATOM   17246 C CD  . GLN F  1 308 ? 160.584 49.640  13.972  1.00   70.44  ? 308 GLN F CD  1 
ATOM   17247 O OE1 . GLN F  1 308 ? 159.847 48.703  14.267  1.00   64.98  ? 308 GLN F OE1 1 
ATOM   17248 N NE2 . GLN F  1 308 ? 160.859 49.970  12.719  1.00   70.47  ? 308 GLN F NE2 1 
ATOM   17249 N N   . VAL F  1 309 ? 160.203 50.616  19.527  1.00   70.50  ? 309 VAL F N   1 
ATOM   17250 C CA  . VAL F  1 309 ? 159.939 50.070  20.860  1.00   72.68  ? 309 VAL F CA  1 
ATOM   17251 C C   . VAL F  1 309 ? 158.595 49.358  20.832  1.00   74.66  ? 309 VAL F C   1 
ATOM   17252 O O   . VAL F  1 309 ? 157.901 49.401  19.812  1.00   76.55  ? 309 VAL F O   1 
ATOM   17253 C CB  . VAL F  1 309 ? 159.986 51.148  21.965  1.00   72.28  ? 309 VAL F CB  1 
ATOM   17254 C CG1 . VAL F  1 309 ? 161.370 51.777  22.022  1.00   73.30  ? 309 VAL F CG1 1 
ATOM   17255 C CG2 . VAL F  1 309 ? 158.924 52.190  21.753  1.00   70.19  ? 309 VAL F CG2 1 
ATOM   17256 N N   . LYS F  1 310 ? 158.261 48.630  21.895  1.00   74.84  ? 310 LYS F N   1 
ATOM   17257 C CA  . LYS F  1 310 ? 156.959 47.975  21.927  1.00   75.10  ? 310 LYS F CA  1 
ATOM   17258 C C   . LYS F  1 310 ? 155.845 48.951  21.592  1.00   70.99  ? 310 LYS F C   1 
ATOM   17259 O O   . LYS F  1 310 ? 155.653 49.948  22.273  1.00   69.77  ? 310 LYS F O   1 
ATOM   17260 C CB  . LYS F  1 310 ? 156.669 47.357  23.285  1.00   81.39  ? 310 LYS F CB  1 
ATOM   17261 C CG  . LYS F  1 310 ? 155.439 46.463  23.242  1.00   86.56  ? 310 LYS F CG  1 
ATOM   17262 C CD  . LYS F  1 310 ? 155.180 45.798  24.582  1.00   94.33  ? 310 LYS F CD  1 
ATOM   17263 C CE  . LYS F  1 310 ? 154.640 46.798  25.613  1.00   98.34  ? 310 LYS F CE  1 
ATOM   17264 N NZ  . LYS F  1 310 ? 153.935 46.102  26.731  1.00   103.57 ? 310 LYS F NZ  1 
ATOM   17265 N N   . ALA F  1 311 ? 155.085 48.615  20.562  1.00   68.65  ? 311 ALA F N   1 
ATOM   17266 C CA  . ALA F  1 311 ? 154.003 49.455  20.089  1.00   69.23  ? 311 ALA F CA  1 
ATOM   17267 C C   . ALA F  1 311 ? 153.040 49.765  21.225  1.00   74.49  ? 311 ALA F C   1 
ATOM   17268 O O   . ALA F  1 311 ? 152.843 48.949  22.119  1.00   77.85  ? 311 ALA F O   1 
ATOM   17269 C CB  . ALA F  1 311 ? 153.284 48.780  18.946  1.00   67.70  ? 311 ALA F CB  1 
ATOM   17270 N N   . VAL F  1 312 ? 152.488 50.972  21.219  1.00   75.21  ? 312 VAL F N   1 
ATOM   17271 C CA  . VAL F  1 312 ? 151.667 51.434  22.331  1.00   77.48  ? 312 VAL F CA  1 
ATOM   17272 C C   . VAL F  1 312 ? 150.375 52.127  21.915  1.00   76.70  ? 312 VAL F C   1 
ATOM   17273 O O   . VAL F  1 312 ? 150.308 52.774  20.866  1.00   74.36  ? 312 VAL F O   1 
ATOM   17274 C CB  . VAL F  1 312 ? 152.509 52.389  23.224  1.00   87.78  ? 312 VAL F CB  1 
ATOM   17275 C CG1 . VAL F  1 312 ? 151.654 53.314  24.079  1.00   89.26  ? 312 VAL F CG1 1 
ATOM   17276 C CG2 . VAL F  1 312 ? 153.499 51.591  24.064  1.00   91.74  ? 312 VAL F CG2 1 
ATOM   17277 N N   . GLY F  1 313 ? 149.341 51.962  22.739  1.00   78.22  ? 313 GLY F N   1 
ATOM   17278 C CA  . GLY F  1 313 ? 148.090 52.658  22.533  1.00   77.52  ? 313 GLY F CA  1 
ATOM   17279 C C   . GLY F  1 313 ? 147.334 52.063  21.379  1.00   75.35  ? 313 GLY F C   1 
ATOM   17280 O O   . GLY F  1 313 ? 147.280 50.845  21.217  1.00   76.17  ? 313 GLY F O   1 
ATOM   17281 N N   . PRO F  1 314 ? 146.718 52.934  20.582  1.00   72.66  ? 314 PRO F N   1 
ATOM   17282 C CA  . PRO F  1 314 ? 145.987 52.578  19.370  1.00   71.91  ? 314 PRO F CA  1 
ATOM   17283 C C   . PRO F  1 314 ? 146.953 52.418  18.208  1.00   63.66  ? 314 PRO F C   1 
ATOM   17284 O O   . PRO F  1 314 ? 146.545 52.038  17.110  1.00   62.20  ? 314 PRO F O   1 
ATOM   17285 C CB  . PRO F  1 314 ? 145.070 53.782  19.159  1.00   73.47  ? 314 PRO F CB  1 
ATOM   17286 C CG  . PRO F  1 314 ? 145.890 54.946  19.697  1.00   72.97  ? 314 PRO F CG  1 
ATOM   17287 C CD  . PRO F  1 314 ? 146.671 54.381  20.864  1.00   73.41  ? 314 PRO F CD  1 
ATOM   17288 N N   . PHE F  1 315 ? 148.229 52.707  18.470  1.00   62.98  ? 315 PHE F N   1 
ATOM   17289 C CA  . PHE F  1 315 ? 149.240 52.780  17.426  1.00   60.46  ? 315 PHE F CA  1 
ATOM   17290 C C   . PHE F  1 315 ? 149.909 51.467  17.173  1.00   62.77  ? 315 PHE F C   1 
ATOM   17291 O O   . PHE F  1 315 ? 150.065 50.642  18.071  1.00   65.03  ? 315 PHE F O   1 
ATOM   17292 C CB  . PHE F  1 315 ? 150.286 53.797  17.803  1.00   60.39  ? 315 PHE F CB  1 
ATOM   17293 C CG  . PHE F  1 315 ? 149.713 55.114  18.103  1.00   62.91  ? 315 PHE F CG  1 
ATOM   17294 C CD1 . PHE F  1 315 ? 149.078 55.836  17.111  1.00   59.28  ? 315 PHE F CD1 1 
ATOM   17295 C CD2 . PHE F  1 315 ? 149.743 55.615  19.387  1.00   65.35  ? 315 PHE F CD2 1 
ATOM   17296 C CE1 . PHE F  1 315 ? 148.523 57.047  17.380  1.00   60.19  ? 315 PHE F CE1 1 
ATOM   17297 C CE2 . PHE F  1 315 ? 149.187 56.834  19.666  1.00   64.62  ? 315 PHE F CE2 1 
ATOM   17298 C CZ  . PHE F  1 315 ? 148.574 57.553  18.658  1.00   63.27  ? 315 PHE F CZ  1 
ATOM   17299 N N   . GLY F  1 316 ? 150.385 51.304  15.953  1.00   58.73  ? 316 GLY F N   1 
ATOM   17300 C CA  . GLY F  1 316 ? 150.981 50.046  15.584  1.00   59.29  ? 316 GLY F CA  1 
ATOM   17301 C C   . GLY F  1 316 ? 152.490 50.137  15.509  1.00   76.51  ? 316 GLY F C   1 
ATOM   17302 O O   . GLY F  1 316 ? 153.185 49.124  15.624  1.00   82.43  ? 316 GLY F O   1 
ATOM   17303 N N   . LEU F  1 317 ? 153.011 51.349  15.376  1.00   71.15  ? 317 LEU F N   1 
ATOM   17304 C CA  . LEU F  1 317 ? 154.439 51.531  15.194  1.00   58.31  ? 317 LEU F CA  1 
ATOM   17305 C C   . LEU F  1 317 ? 154.935 52.615  16.093  1.00   59.16  ? 317 LEU F C   1 
ATOM   17306 O O   . LEU F  1 317 ? 154.631 53.791  15.884  1.00   64.04  ? 317 LEU F O   1 
ATOM   17307 C CB  . LEU F  1 317 ? 154.757 51.872  13.738  1.00   56.87  ? 317 LEU F CB  1 
ATOM   17308 C CG  . LEU F  1 317 ? 156.205 52.107  13.319  1.00   57.67  ? 317 LEU F CG  1 
ATOM   17309 C CD1 . LEU F  1 317 ? 157.069 50.901  13.626  1.00   59.45  ? 317 LEU F CD1 1 
ATOM   17310 C CD2 . LEU F  1 317 ? 156.272 52.461  11.838  1.00   56.57  ? 317 LEU F CD2 1 
ATOM   17311 N N   . CYS F  1 318 ? 155.674 52.216  17.116  1.00   61.02  ? 318 CYS F N   1 
ATOM   17312 C CA  . CYS F  1 318 ? 156.219 53.179  18.054  1.00   69.40  ? 318 CYS F CA  1 
ATOM   17313 C C   . CYS F  1 318 ? 157.744 53.092  18.132  1.00   73.05  ? 318 CYS F C   1 
ATOM   17314 O O   . CYS F  1 318 ? 158.327 52.027  17.938  1.00   76.65  ? 318 CYS F O   1 
ATOM   17315 C CB  . CYS F  1 318 ? 155.594 52.990  19.431  1.00   69.24  ? 318 CYS F CB  1 
ATOM   17316 S SG  . CYS F  1 318 ? 153.844 53.408  19.467  1.00   63.42  ? 318 CYS F SG  1 
ATOM   17317 N N   . TYR F  1 319 ? 158.374 54.224  18.439  1.00   71.81  ? 319 TYR F N   1 
ATOM   17318 C CA  . TYR F  1 319 ? 159.828 54.342  18.482  1.00   70.63  ? 319 TYR F CA  1 
ATOM   17319 C C   . TYR F  1 319 ? 160.321 54.908  19.813  1.00   73.72  ? 319 TYR F C   1 
ATOM   17320 O O   . TYR F  1 319 ? 159.546 55.505  20.568  1.00   72.95  ? 319 TYR F O   1 
ATOM   17321 C CB  . TYR F  1 319 ? 160.323 55.253  17.359  1.00   69.06  ? 319 TYR F CB  1 
ATOM   17322 C CG  . TYR F  1 319 ? 160.116 54.728  15.961  1.00   68.47  ? 319 TYR F CG  1 
ATOM   17323 C CD1 . TYR F  1 319 ? 158.907 54.908  15.309  1.00   67.09  ? 319 TYR F CD1 1 
ATOM   17324 C CD2 . TYR F  1 319 ? 161.145 54.093  15.274  1.00   71.40  ? 319 TYR F CD2 1 
ATOM   17325 C CE1 . TYR F  1 319 ? 158.714 54.447  14.027  1.00   67.75  ? 319 TYR F CE1 1 
ATOM   17326 C CE2 . TYR F  1 319 ? 160.963 53.636  13.982  1.00   72.52  ? 319 TYR F CE2 1 
ATOM   17327 C CZ  . TYR F  1 319 ? 159.740 53.811  13.369  1.00   71.58  ? 319 TYR F CZ  1 
ATOM   17328 O OH  . TYR F  1 319 ? 159.529 53.355  12.091  1.00   73.45  ? 319 TYR F OH  1 
ATOM   17329 N N   . ASP F  1 320 ? 161.624 54.757  20.064  1.00   76.44  ? 320 ASP F N   1 
ATOM   17330 C CA  . ASP F  1 320 ? 162.273 55.407  21.191  1.00   77.63  ? 320 ASP F CA  1 
ATOM   17331 C C   . ASP F  1 320 ? 162.248 56.897  20.876  1.00   76.64  ? 320 ASP F C   1 
ATOM   17332 O O   . ASP F  1 320 ? 162.667 57.299  19.790  1.00   76.17  ? 320 ASP F O   1 
ATOM   17333 C CB  . ASP F  1 320 ? 163.717 54.887  21.335  0.0000 80.69  ? 320 ASP F CB  1 
ATOM   17334 C CG  . ASP F  1 320 ? 164.580 55.750  22.247  0.0000 84.83  ? 320 ASP F CG  1 
ATOM   17335 O OD1 . ASP F  1 320 ? 164.047 56.619  22.972  0.0000 85.36  ? 320 ASP F OD1 1 
ATOM   17336 O OD2 . ASP F  1 320 ? 165.815 55.571  22.219  0.0000 87.87  ? 320 ASP F OD2 1 
ATOM   17337 N N   . SER F  1 321 ? 161.802 57.731  21.811  1.00   78.15  ? 321 SER F N   1 
ATOM   17338 C CA  . SER F  1 321 ? 161.720 59.138  21.447  1.00   81.21  ? 321 SER F CA  1 
ATOM   17339 C C   . SER F  1 321 ? 163.144 59.672  21.332  1.00   85.91  ? 321 SER F C   1 
ATOM   17340 O O   . SER F  1 321 ? 163.613 59.922  20.273  1.00   86.52  ? 321 SER F O   1 
ATOM   17341 C CB  . SER F  1 321 ? 160.900 59.975  22.432  1.00   83.22  ? 321 SER F CB  1 
ATOM   17342 O OG  . SER F  1 321 ? 159.697 59.330  22.753  0.0000 80.76  ? 321 SER F OG  1 
ATOM   17343 N N   . ARG F  1 322 ? 163.894 59.699  22.426  0.0000 88.83  ? 322 ARG F N   1 
ATOM   17344 C CA  . ARG F  1 322 ? 165.261 60.228  22.362  0.0000 92.96  ? 322 ARG F CA  1 
ATOM   17345 C C   . ARG F  1 322 ? 166.116 59.231  21.614  0.0000 91.98  ? 322 ARG F C   1 
ATOM   17346 O O   . ARG F  1 322 ? 166.866 58.434  22.185  0.0000 93.39  ? 322 ARG F O   1 
ATOM   17347 C CB  . ARG F  1 322 ? 165.875 60.555  23.735  0.0000 97.71  ? 322 ARG F CB  1 
ATOM   17348 C CG  . ARG F  1 322 ? 166.887 61.696  23.631  0.0000 102.81 ? 322 ARG F CG  1 
ATOM   17349 C CD  . ARG F  1 322 ? 167.255 62.132  25.013  0.0000 107.16 ? 322 ARG F CD  1 
ATOM   17350 N NE  . ARG F  1 322 ? 166.263 61.684  25.987  0.0000 105.09 ? 322 ARG F NE  1 
ATOM   17351 C CZ  . ARG F  1 322 ? 166.527 61.515  27.275  0.0000 107.03 ? 322 ARG F CZ  1 
ATOM   17352 N NH1 . ARG F  1 322 ? 165.583 61.084  28.098  0.0000 104.26 ? 322 ARG F NH1 1 
ATOM   17353 N NH2 . ARG F  1 322 ? 167.750 61.758  27.727  0.0000 112.18 ? 322 ARG F NH2 1 
ATOM   17354 N N   . LYS F  1 323 ? 165.988 59.375  20.294  0.0000 89.84  ? 323 LYS F N   1 
ATOM   17355 C CA  . LYS F  1 323 ? 166.657 58.610  19.252  0.0000 88.76  ? 323 LYS F CA  1 
ATOM   17356 C C   . LYS F  1 323 ? 165.943 58.958  17.916  0.0000 98.04  ? 323 LYS F C   1 
ATOM   17357 O O   . LYS F  1 323 ? 166.415 58.553  16.853  0.0000 98.77  ? 323 LYS F O   1 
ATOM   17358 C CB  . LYS F  1 323 ? 166.677 57.091  19.555  0.0000 86.12  ? 323 LYS F CB  1 
ATOM   17359 C CG  . LYS F  1 323 ? 166.895 56.163  18.379  0.0000 83.87  ? 323 LYS F CG  1 
ATOM   17360 C CD  . LYS F  1 323 ? 167.701 54.932  18.756  0.0000 84.74  ? 323 LYS F CD  1 
ATOM   17361 C CE  . LYS F  1 323 ? 169.098 55.323  19.202  0.0000 89.45  ? 323 LYS F CE  1 
ATOM   17362 N NZ  . LYS F  1 323 ? 169.880 55.837  18.031  0.0000 91.78  ? 323 LYS F NZ  1 
ATOM   17363 N N   . ILE F  1 324 ? 164.887 59.795  17.930  0.0000 96.25  ? 324 ILE F N   1 
ATOM   17364 C CA  . ILE F  1 324 ? 164.165 60.193  16.678  0.0000 94.74  ? 324 ILE F CA  1 
ATOM   17365 C C   . ILE F  1 324 ? 165.118 60.565  15.545  0.0000 99.31  ? 324 ILE F C   1 
ATOM   17366 O O   . ILE F  1 324 ? 164.723 60.731  14.393  0.0000 97.21  ? 324 ILE F O   1 
ATOM   17367 C CB  . ILE F  1 324 ? 163.219 61.455  16.851  0.0000 96.85  ? 324 ILE F CB  1 
ATOM   17368 C CG1 . ILE F  1 324 ? 162.569 61.579  18.231  0.0000 97.57  ? 324 ILE F CG1 1 
ATOM   17369 C CG2 . ILE F  1 324 ? 162.076 61.402  15.851  0.0000 93.24  ? 324 ILE F CG2 1 
ATOM   17370 C CD1 . ILE F  1 324 ? 163.189 62.694  19.125  0.0000 97.24  ? 324 ILE F CD1 1 
ATOM   17371 N N   . SER F  1 325 ? 166.371 60.766  15.931  1.00   107.06 ? 325 SER F N   1 
ATOM   17372 C CA  . SER F  1 325 ? 167.437 61.193  15.047  1.00   112.06 ? 325 SER F CA  1 
ATOM   17373 C C   . SER F  1 325 ? 166.994 62.556  14.579  1.00   111.08 ? 325 SER F C   1 
ATOM   17374 O O   . SER F  1 325 ? 167.410 63.028  13.527  1.00   112.12 ? 325 SER F O   1 
ATOM   17375 C CB  . SER F  1 325 ? 167.642 60.219  13.876  1.00   111.38 ? 325 SER F CB  1 
ATOM   17376 O OG  . SER F  1 325 ? 167.831 58.903  14.350  1.00   109.27 ? 325 SER F OG  1 
ATOM   17377 N N   . GLY F  1 326 ? 166.187 63.200  15.420  1.00   108.55 ? 326 GLY F N   1 
ATOM   17378 C CA  . GLY F  1 326 ? 165.720 64.539  15.167  1.00   109.14 ? 326 GLY F CA  1 
ATOM   17379 C C   . GLY F  1 326 ? 165.190 64.589  13.745  1.00   106.01 ? 326 GLY F C   1 
ATOM   17380 O O   . GLY F  1 326 ? 165.410 65.578  13.066  1.00   110.53 ? 326 GLY F O   1 
ATOM   17381 N N   . GLY F  1 327 ? 164.525 63.530  13.271  1.00   98.06  ? 327 GLY F N   1 
ATOM   17382 C CA  . GLY F  1 327 ? 164.275 63.408  11.840  1.00   94.44  ? 327 GLY F CA  1 
ATOM   17383 C C   . GLY F  1 327 ? 163.444 62.236  11.332  1.00   88.43  ? 327 GLY F C   1 
ATOM   17384 O O   . GLY F  1 327 ? 163.852 61.069  11.409  1.00   88.22  ? 327 GLY F O   1 
ATOM   17385 N N   . ALA F  1 328 ? 162.277 62.591  10.785  1.00   83.33  ? 328 ALA F N   1 
ATOM   17386 C CA  . ALA F  1 328 ? 161.303 61.689  10.146  1.00   77.74  ? 328 ALA F CA  1 
ATOM   17387 C C   . ALA F  1 328 ? 161.101 61.980  8.646   1.00   78.03  ? 328 ALA F C   1 
ATOM   17388 O O   . ALA F  1 328 ? 161.378 63.089  8.205   1.00   83.05  ? 328 ALA F O   1 
ATOM   17389 C CB  . ALA F  1 328 ? 159.991 61.778  10.867  1.00   75.24  ? 328 ALA F CB  1 
ATOM   17390 N N   . PRO F  1 329 ? 160.598 61.001  7.853   1.00   74.27  ? 329 PRO F N   1 
ATOM   17391 C CA  . PRO F  1 329 ? 160.533 61.291  6.407   1.00   73.28  ? 329 PRO F CA  1 
ATOM   17392 C C   . PRO F  1 329 ? 159.408 62.257  5.996   1.00   69.36  ? 329 PRO F C   1 
ATOM   17393 O O   . PRO F  1 329 ? 158.510 62.518  6.787   1.00   64.92  ? 329 PRO F O   1 
ATOM   17394 C CB  . PRO F  1 329 ? 160.288 59.905  5.782   1.00   70.77  ? 329 PRO F CB  1 
ATOM   17395 C CG  . PRO F  1 329 ? 159.642 59.117  6.839   1.00   62.67  ? 329 PRO F CG  1 
ATOM   17396 C CD  . PRO F  1 329 ? 160.155 59.626  8.161   1.00   69.78  ? 329 PRO F CD  1 
ATOM   17397 N N   . SER F  1 330 ? 159.494 62.790  4.775   1.00   72.10  ? 330 SER F N   1 
ATOM   17398 C CA  . SER F  1 330 ? 158.419 63.566  4.144   1.00   71.99  ? 330 SER F CA  1 
ATOM   17399 C C   . SER F  1 330 ? 157.121 62.764  3.995   1.00   67.59  ? 330 SER F C   1 
ATOM   17400 O O   . SER F  1 330 ? 157.129 61.731  3.340   1.00   64.88  ? 330 SER F O   1 
ATOM   17401 C CB  . SER F  1 330 ? 158.887 64.065  2.767   1.00   76.46  ? 330 SER F CB  1 
ATOM   17402 O OG  . SER F  1 330 ? 158.451 63.206  1.720   1.00   76.48  ? 330 SER F OG  1 
ATOM   17403 N N   . VAL F  1 331 ? 156.018 63.239  4.587   1.00   59.15  ? 331 VAL F N   1 
ATOM   17404 C CA  . VAL F  1 331 ? 154.689 62.620  4.388   1.00   58.03  ? 331 VAL F CA  1 
ATOM   17405 C C   . VAL F  1 331 ? 153.630 63.561  3.771   1.00   57.43  ? 331 VAL F C   1 
ATOM   17406 O O   . VAL F  1 331 ? 153.165 64.502  4.417   1.00   61.01  ? 331 VAL F O   1 
ATOM   17407 C CB  . VAL F  1 331 ? 154.121 62.096  5.706   1.00   58.04  ? 331 VAL F CB  1 
ATOM   17408 C CG1 . VAL F  1 331 ? 152.810 61.390  5.449   1.00   55.27  ? 331 VAL F CG1 1 
ATOM   17409 C CG2 . VAL F  1 331 ? 155.077 61.124  6.335   1.00   62.72  ? 331 VAL F CG2 1 
ATOM   17410 N N   . ASP F  1 332 ? 153.232 63.276  2.534   1.00   52.21  ? 332 ASP F N   1 
ATOM   17411 C CA  . ASP F  1 332 ? 152.368 64.160  1.762   1.00   48.06  ? 332 ASP F CA  1 
ATOM   17412 C C   . ASP F  1 332 ? 151.168 63.391  1.230   1.00   45.59  ? 332 ASP F C   1 
ATOM   17413 O O   . ASP F  1 332 ? 151.293 62.217  0.900   1.00   46.70  ? 332 ASP F O   1 
ATOM   17414 C CB  . ASP F  1 332 ? 153.123 64.770  0.578   1.00   53.40  ? 332 ASP F CB  1 
ATOM   17415 C CG  . ASP F  1 332 ? 154.422 65.445  0.984   1.00   59.20  ? 332 ASP F CG  1 
ATOM   17416 O OD1 . ASP F  1 332 ? 154.526 65.898  2.140   1.00   60.66  ? 332 ASP F OD1 1 
ATOM   17417 O OD2 . ASP F  1 332 ? 155.348 65.504  0.148   1.00   53.41  ? 332 ASP F OD2 1 
ATOM   17418 N N   . LEU F  1 333 ? 149.998 64.023  1.204   1.00   40.54  ? 333 LEU F N   1 
ATOM   17419 C CA  . LEU F  1 333 ? 148.855 63.474  0.475   1.00   39.00  ? 333 LEU F CA  1 
ATOM   17420 C C   . LEU F  1 333 ? 148.824 64.002  -0.939  1.00   41.57  ? 333 LEU F C   1 
ATOM   17421 O O   . LEU F  1 333 ? 148.744 65.197  -1.140  1.00   42.94  ? 333 LEU F O   1 
ATOM   17422 C CB  . LEU F  1 333 ? 147.526 63.816  1.136   1.00   35.65  ? 333 LEU F CB  1 
ATOM   17423 C CG  . LEU F  1 333 ? 147.307 63.537  2.616   1.00   34.97  ? 333 LEU F CG  1 
ATOM   17424 C CD1 . LEU F  1 333 ? 145.882 63.893  3.020   1.00   30.91  ? 333 LEU F CD1 1 
ATOM   17425 C CD2 . LEU F  1 333 ? 147.619 62.109  2.894   1.00   33.86  ? 333 LEU F CD2 1 
ATOM   17426 N N   . ILE F  1 334 ? 148.884 63.121  -1.918  1.00   39.26  ? 334 ILE F N   1 
ATOM   17427 C CA  . ILE F  1 334 ? 148.726 63.535  -3.294  1.00   41.02  ? 334 ILE F CA  1 
ATOM   17428 C C   . ILE F  1 334 ? 147.240 63.503  -3.603  1.00   43.40  ? 334 ILE F C   1 
ATOM   17429 O O   . ILE F  1 334 ? 146.592 62.456  -3.525  1.00   44.96  ? 334 ILE F O   1 
ATOM   17430 C CB  . ILE F  1 334 ? 149.489 62.630  -4.254  1.00   44.59  ? 334 ILE F CB  1 
ATOM   17431 C CG1 . ILE F  1 334 ? 150.893 62.350  -3.713  1.00   52.82  ? 334 ILE F CG1 1 
ATOM   17432 C CG2 . ILE F  1 334 ? 149.526 63.225  -5.635  1.00   47.52  ? 334 ILE F CG2 1 
ATOM   17433 C CD1 . ILE F  1 334 ? 151.730 63.580  -3.486  1.00   55.87  ? 334 ILE F CD1 1 
ATOM   17434 N N   . LEU F  1 335 ? 146.710 64.650  -3.984  1.00   40.29  ? 335 LEU F N   1 
ATOM   17435 C CA  . LEU F  1 335 ? 145.279 64.852  -4.059  1.00   38.34  ? 335 LEU F CA  1 
ATOM   17436 C C   . LEU F  1 335 ? 144.750 64.663  -5.460  1.00   43.23  ? 335 LEU F C   1 
ATOM   17437 O O   . LEU F  1 335 ? 145.486 64.319  -6.370  1.00   45.99  ? 335 LEU F O   1 
ATOM   17438 C CB  . LEU F  1 335 ? 144.922 66.243  -3.558  1.00   37.89  ? 335 LEU F CB  1 
ATOM   17439 C CG  . LEU F  1 335 ? 145.435 66.516  -2.150  1.00   39.57  ? 335 LEU F CG  1 
ATOM   17440 C CD1 . LEU F  1 335 ? 145.047 67.908  -1.690  1.00   40.31  ? 335 LEU F CD1 1 
ATOM   17441 C CD2 . LEU F  1 335 ? 144.916 65.461  -1.224  1.00   38.71  ? 335 LEU F CD2 1 
ATOM   17442 N N   . ASP F  1 336 ? 143.451 64.874  -5.600  1.00   46.64  ? 336 ASP F N   1 
ATOM   17443 C CA  . ASP F  1 336 ? 142.701 64.629  -6.818  1.00   52.48  ? 336 ASP F CA  1 
ATOM   17444 C C   . ASP F  1 336 ? 143.437 65.077  -8.080  1.00   53.54  ? 336 ASP F C   1 
ATOM   17445 O O   . ASP F  1 336 ? 143.959 66.188  -8.148  1.00   52.91  ? 336 ASP F O   1 
ATOM   17446 C CB  . ASP F  1 336 ? 141.342 65.339  -6.720  1.00   57.36  ? 336 ASP F CB  1 
ATOM   17447 C CG  . ASP F  1 336 ? 140.392 64.970  -7.859  1.00   63.11  ? 336 ASP F CG  1 
ATOM   17448 O OD1 . ASP F  1 336 ? 139.666 63.961  -7.726  1.00   63.41  ? 336 ASP F OD1 1 
ATOM   17449 O OD2 . ASP F  1 336 ? 140.357 65.697  -8.875  1.00   67.38  ? 336 ASP F OD2 1 
ATOM   17450 N N   . LYS F  1 337 ? 143.509 64.157  -9.037  1.00   56.51  ? 337 LYS F N   1 
ATOM   17451 C CA  . LYS F  1 337 ? 144.056 64.369  -10.370 1.00   65.90  ? 337 LYS F CA  1 
ATOM   17452 C C   . LYS F  1 337 ? 145.547 64.659  -10.322 1.00   68.60  ? 337 LYS F C   1 
ATOM   17453 O O   . LYS F  1 337 ? 146.116 65.150  -11.298 1.00   70.51  ? 337 LYS F O   1 
ATOM   17454 C CB  . LYS F  1 337 ? 143.341 65.534  -11.066 1.00   72.08  ? 337 LYS F CB  1 
ATOM   17455 C CG  . LYS F  1 337 ? 141.999 65.189  -11.716 1.00   76.61  ? 337 LYS F CG  1 
ATOM   17456 C CD  . LYS F  1 337 ? 141.909 63.749  -12.181 1.00   83.05  ? 337 LYS F CD  1 
ATOM   17457 C CE  . LYS F  1 337 ? 140.540 63.460  -12.794 1.00   87.45  ? 337 LYS F CE  1 
ATOM   17458 N NZ  . LYS F  1 337 ? 140.248 61.990  -12.870 1.00   90.08  ? 337 LYS F NZ  1 
ATOM   17459 N N   . ASN F  1 338 ? 146.163 64.328  -9.188  1.00   68.44  ? 338 ASN F N   1 
ATOM   17460 C CA  . ASN F  1 338 ? 147.553 64.676  -8.870  1.00   70.55  ? 338 ASN F CA  1 
ATOM   17461 C C   . ASN F  1 338 ? 147.863 66.172  -8.999  1.00   71.93  ? 338 ASN F C   1 
ATOM   17462 O O   . ASN F  1 338 ? 149.028 66.569  -9.039  1.00   76.16  ? 338 ASN F O   1 
ATOM   17463 C CB  . ASN F  1 338 ? 148.527 63.862  -9.737  1.00   75.01  ? 338 ASN F CB  1 
ATOM   17464 C CG  . ASN F  1 338 ? 148.262 62.364  -9.679  1.00   73.91  ? 338 ASN F CG  1 
ATOM   17465 O OD1 . ASN F  1 338 ? 148.060 61.802  -8.600  1.00   70.78  ? 338 ASN F OD1 1 
ATOM   17466 N ND2 . ASN F  1 338 ? 148.298 61.704  -10.838 1.00   76.47  ? 338 ASN F ND2 1 
ATOM   17467 N N   . ASP F  1 339 ? 146.822 67.001  -8.990  1.00   68.70  ? 339 ASP F N   1 
ATOM   17468 C CA  . ASP F  1 339 ? 147.001 68.437  -9.122  1.00   70.72  ? 339 ASP F CA  1 
ATOM   17469 C C   . ASP F  1 339 ? 147.470 69.109  -7.841  1.00   66.84  ? 339 ASP F C   1 
ATOM   17470 O O   . ASP F  1 339 ? 148.029 70.197  -7.892  1.00   72.35  ? 339 ASP F O   1 
ATOM   17471 C CB  . ASP F  1 339 ? 145.697 69.084  -9.597  1.00   73.89  ? 339 ASP F CB  1 
ATOM   17472 C CG  . ASP F  1 339 ? 145.373 68.743  -11.041 1.00   82.24  ? 339 ASP F CG  1 
ATOM   17473 O OD1 . ASP F  1 339 ? 146.300 68.352  -11.778 1.00   90.38  1 339 ASP F OD1 1 
ATOM   17474 O OD2 . ASP F  1 339 ? 144.195 68.847  -11.442 1.00   81.04  ? 339 ASP F OD2 1 
ATOM   17475 N N   . ALA F  1 340 ? 147.269 68.475  -6.693  1.00   58.72  ? 340 ALA F N   1 
ATOM   17476 C CA  . ALA F  1 340 ? 147.568 69.158  -5.443  1.00   53.49  ? 340 ALA F CA  1 
ATOM   17477 C C   . ALA F  1 340 ? 148.216 68.239  -4.410  1.00   47.48  ? 340 ALA F C   1 
ATOM   17478 O O   . ALA F  1 340 ? 148.067 67.030  -4.483  1.00   46.15  ? 340 ALA F O   1 
ATOM   17479 C CB  . ALA F  1 340 ? 146.280 69.776  -4.874  1.00   50.79  ? 340 ALA F CB  1 
ATOM   17480 N N   . VAL F  1 341 ? 148.892 68.824  -3.423  1.00   45.77  ? 341 VAL F N   1 
ATOM   17481 C CA  . VAL F  1 341 ? 149.617 68.045  -2.422  1.00   45.27  ? 341 VAL F CA  1 
ATOM   17482 C C   . VAL F  1 341 ? 149.323 68.645  -1.048  1.00   43.79  ? 341 VAL F C   1 
ATOM   17483 O O   . VAL F  1 341 ? 149.419 69.863  -0.865  1.00   43.72  ? 341 VAL F O   1 
ATOM   17484 C CB  . VAL F  1 341 ? 151.143 68.041  -2.649  1.00   47.66  ? 341 VAL F CB  1 
ATOM   17485 C CG1 . VAL F  1 341 ? 151.850 67.478  -1.436  1.00   47.75  ? 341 VAL F CG1 1 
ATOM   17486 C CG2 . VAL F  1 341 ? 151.513 67.225  -3.867  1.00   49.89  ? 341 VAL F CG2 1 
ATOM   17487 N N   . TRP F  1 342 ? 148.950 67.788  -0.099  1.00   39.20  ? 342 TRP F N   1 
ATOM   17488 C CA  . TRP F  1 342 ? 148.814 68.179  1.289   1.00   37.79  ? 342 TRP F CA  1 
ATOM   17489 C C   . TRP F  1 342 ? 149.967 67.607  2.098   1.00   42.26  ? 342 TRP F C   1 
ATOM   17490 O O   . TRP F  1 342 ? 149.941 66.462  2.518   1.00   42.09  ? 342 TRP F O   1 
ATOM   17491 C CB  . TRP F  1 342 ? 147.477 67.721  1.875   1.00   35.80  ? 342 TRP F CB  1 
ATOM   17492 C CG  . TRP F  1 342 ? 147.086 68.537  3.067   1.00   36.30  ? 342 TRP F CG  1 
ATOM   17493 C CD1 . TRP F  1 342 ? 147.904 69.330  3.802   1.00   41.69  ? 342 TRP F CD1 1 
ATOM   17494 C CD2 . TRP F  1 342 ? 145.774 68.711  3.607   1.00   37.97  ? 342 TRP F CD2 1 
ATOM   17495 N NE1 . TRP F  1 342 ? 147.199 69.970  4.786   1.00   42.98  ? 342 TRP F NE1 1 
ATOM   17496 C CE2 . TRP F  1 342 ? 145.884 69.604  4.693   1.00   40.84  ? 342 TRP F CE2 1 
ATOM   17497 C CE3 . TRP F  1 342 ? 144.517 68.192  3.289   1.00   39.53  ? 342 TRP F CE3 1 
ATOM   17498 C CZ2 . TRP F  1 342 ? 144.787 69.992  5.464   1.00   40.95  ? 342 TRP F CZ2 1 
ATOM   17499 C CZ3 . TRP F  1 342 ? 143.423 68.569  4.065   1.00   39.48  ? 342 TRP F CZ3 1 
ATOM   17500 C CH2 . TRP F  1 342 ? 143.566 69.469  5.131   1.00   41.06  ? 342 TRP F CH2 1 
ATOM   17501 N N   . ARG F  1 343 ? 150.964 68.438  2.330   1.00   46.41  ? 343 ARG F N   1 
ATOM   17502 C CA  . ARG F  1 343 ? 152.158 68.058  3.043   1.00   51.59  ? 343 ARG F CA  1 
ATOM   17503 C C   . ARG F  1 343 ? 151.818 67.928  4.525   1.00   48.82  ? 343 ARG F C   1 
ATOM   17504 O O   . ARG F  1 343 ? 151.196 68.829  5.081   1.00   49.53  ? 343 ARG F O   1 
ATOM   17505 C CB  . ARG F  1 343 ? 153.207 69.142  2.805   1.00   60.07  ? 343 ARG F CB  1 
ATOM   17506 C CG  . ARG F  1 343 ? 153.609 69.241  1.332   1.00   66.60  ? 343 ARG F CG  1 
ATOM   17507 C CD  . ARG F  1 343 ? 154.102 70.658  0.951   1.00   77.30  ? 343 ARG F CD  1 
ATOM   17508 N NE  . ARG F  1 343 ? 154.074 70.903  -0.498  1.00   82.36  ? 343 ARG F NE  1 
ATOM   17509 C CZ  . ARG F  1 343 ? 154.817 70.266  -1.406  1.00   88.96  ? 343 ARG F CZ  1 
ATOM   17510 N NH1 . ARG F  1 343 ? 154.694 70.573  -2.695  1.00   90.94  ? 343 ARG F NH1 1 
ATOM   17511 N NH2 . ARG F  1 343 ? 155.689 69.330  -1.040  1.00   92.62  ? 343 ARG F NH2 1 
ATOM   17512 N N   . ILE F  1 344 ? 152.211 66.829  5.170   1.00   46.66  ? 344 ILE F N   1 
ATOM   17513 C CA  . ILE F  1 344 ? 151.959 66.674  6.607   1.00   44.32  ? 344 ILE F CA  1 
ATOM   17514 C C   . ILE F  1 344 ? 153.219 66.680  7.466   1.00   51.54  ? 344 ILE F C   1 
ATOM   17515 O O   . ILE F  1 344 ? 154.124 65.866  7.273   1.00   47.53  ? 344 ILE F O   1 
ATOM   17516 C CB  . ILE F  1 344 ? 151.218 65.387  6.931   1.00   41.66  ? 344 ILE F CB  1 
ATOM   17517 C CG1 . ILE F  1 344 ? 149.954 65.259  6.103   1.00   38.72  ? 344 ILE F CG1 1 
ATOM   17518 C CG2 . ILE F  1 344 ? 150.855 65.344  8.405   1.00   41.13  ? 344 ILE F CG2 1 
ATOM   17519 C CD1 . ILE F  1 344 ? 149.285 63.942  6.343   1.00   38.90  ? 344 ILE F CD1 1 
ATOM   17520 N N   . SER F  1 345 ? 153.258 67.609  8.420   1.00   57.06  ? 345 SER F N   1 
ATOM   17521 C CA  . SER F  1 345 ? 154.394 67.787  9.325   1.00   62.52  ? 345 SER F CA  1 
ATOM   17522 C C   . SER F  1 345 ? 154.541 66.685  10.357  1.00   61.78  ? 345 SER F C   1 
ATOM   17523 O O   . SER F  1 345 ? 153.558 66.146  10.845  1.00   58.22  ? 345 SER F O   1 
ATOM   17524 C CB  . SER F  1 345 ? 154.300 69.111  10.071  1.00   67.54  ? 345 SER F CB  1 
ATOM   17525 O OG  . SER F  1 345 ? 155.195 69.093  11.178  1.00   74.28  ? 345 SER F OG  1 
ATOM   17526 N N   . SER F  1 346 ? 155.784 66.375  10.695  1.00   66.16  ? 346 SER F N   1 
ATOM   17527 C CA  . SER F  1 346 ? 156.092 65.355  11.683  1.00   68.18  ? 346 SER F CA  1 
ATOM   17528 C C   . SER F  1 346 ? 155.713 65.785  13.093  1.00   67.60  ? 346 SER F C   1 
ATOM   17529 O O   . SER F  1 346 ? 155.700 64.974  14.003  1.00   66.08  ? 346 SER F O   1 
ATOM   17530 C CB  . SER F  1 346 ? 157.562 65.032  11.639  1.00   75.45  ? 346 SER F CB  1 
ATOM   17531 O OG  . SER F  1 346 ? 158.278 66.100  12.233  1.00   82.14  ? 346 SER F OG  1 
ATOM   17532 N N   . GLU F  1 347 ? 155.367 67.053  13.276  1.00   69.97  ? 347 GLU F N   1 
ATOM   17533 C CA  . GLU F  1 347 ? 154.936 67.493  14.594  1.00   74.72  ? 347 GLU F CA  1 
ATOM   17534 C C   . GLU F  1 347 ? 153.474 67.163  14.703  1.00   71.58  ? 347 GLU F C   1 
ATOM   17535 O O   . GLU F  1 347 ? 152.912 67.093  15.791  1.00   74.03  ? 347 GLU F O   1 
ATOM   17536 C CB  . GLU F  1 347 ? 155.087 69.008  14.783  1.00   79.09  ? 347 GLU F CB  1 
ATOM   17537 C CG  . GLU F  1 347 ? 156.456 69.639  14.587  1.00   87.56  ? 347 GLU F CG  1 
ATOM   17538 C CD  . GLU F  1 347 ? 156.460 71.081  15.091  1.00   98.33  ? 347 GLU F CD  1 
ATOM   17539 O OE1 . GLU F  1 347 ? 155.600 71.413  15.938  1.00   101.42 ? 347 GLU F OE1 1 
ATOM   17540 O OE2 . GLU F  1 347 ? 157.306 71.881  14.636  1.00   103.98 ? 347 GLU F OE2 1 
ATOM   17541 N N   . ASN F  1 348 ? 152.867 66.902  13.555  1.00   67.90  ? 348 ASN F N   1 
ATOM   17542 C CA  . ASN F  1 348 ? 151.461 66.533  13.509  1.00   66.51  ? 348 ASN F CA  1 
ATOM   17543 C C   . ASN F  1 348 ? 151.252 65.020  13.595  1.00   62.36  ? 348 ASN F C   1 
ATOM   17544 O O   . ASN F  1 348 ? 150.491 64.546  14.432  1.00   63.80  ? 348 ASN F O   1 
ATOM   17545 C CB  . ASN F  1 348 ? 150.840 67.137  12.233  1.00   68.61  ? 348 ASN F CB  1 
ATOM   17546 C CG  . ASN F  1 348 ? 149.340 66.906  12.107  1.00   69.10  ? 348 ASN F CG  1 
ATOM   17547 O OD1 . ASN F  1 348 ? 148.778 65.956  12.651  1.00   69.14  ? 348 ASN F OD1 1 
ATOM   17548 N ND2 . ASN F  1 348 ? 148.680 67.816  11.394  1.00   69.58  ? 348 ASN F ND2 1 
ATOM   17549 N N   . PHE F  1 349 ? 151.961 64.242  12.788  1.00   58.17  ? 349 PHE F N   1 
ATOM   17550 C CA  . PHE F  1 349 ? 151.639 62.817  12.741  1.00   55.72  ? 349 PHE F CA  1 
ATOM   17551 C C   . PHE F  1 349 ? 152.452 61.962  13.706  1.00   58.95  ? 349 PHE F C   1 
ATOM   17552 O O   . PHE F  1 349 ? 152.119 60.811  13.925  1.00   56.46  ? 349 PHE F O   1 
ATOM   17553 C CB  . PHE F  1 349 ? 151.775 62.288  11.302  1.00   52.26  ? 349 PHE F CB  1 
ATOM   17554 C CG  . PHE F  1 349 ? 153.165 62.322  10.752  1.00   55.33  ? 349 PHE F CG  1 
ATOM   17555 C CD1 . PHE F  1 349 ? 154.118 61.413  11.173  1.00   59.27  ? 349 PHE F CD1 1 
ATOM   17556 C CD2 . PHE F  1 349 ? 153.508 63.245  9.785   1.00   56.41  ? 349 PHE F CD2 1 
ATOM   17557 C CE1 . PHE F  1 349 ? 155.403 61.450  10.658  1.00   62.42  ? 349 PHE F CE1 1 
ATOM   17558 C CE2 . PHE F  1 349 ? 154.778 63.284  9.261   1.00   58.86  ? 349 PHE F CE2 1 
ATOM   17559 C CZ  . PHE F  1 349 ? 155.730 62.387  9.695   1.00   62.43  ? 349 PHE F CZ  1 
ATOM   17560 N N   . MET F  1 350 ? 153.486 62.527  14.319  1.00   57.57  ? 350 MET F N   1 
ATOM   17561 C CA  . MET F  1 350 ? 154.169 61.808  15.381  1.00   64.25  ? 350 MET F CA  1 
ATOM   17562 C C   . MET F  1 350 ? 153.547 62.227  16.685  1.00   69.06  ? 350 MET F C   1 
ATOM   17563 O O   . MET F  1 350 ? 153.509 63.410  17.043  1.00   71.85  ? 350 MET F O   1 
ATOM   17564 C CB  . MET F  1 350 ? 155.675 62.065  15.398  1.00   67.83  ? 350 MET F CB  1 
ATOM   17565 C CG  . MET F  1 350 ? 156.419 61.490  14.215  1.00   67.03  ? 350 MET F CG  1 
ATOM   17566 S SD  . MET F  1 350 ? 156.118 59.724  13.979  1.00   59.88  ? 350 MET F SD  1 
ATOM   17567 C CE  . MET F  1 350 ? 156.667 59.049  15.541  1.00   53.72  ? 350 MET F CE  1 
ATOM   17568 N N   . VAL F  1 351 ? 153.080 61.227  17.410  1.00   69.95  ? 351 VAL F N   1 
ATOM   17569 C CA  . VAL F  1 351 ? 152.374 61.465  18.644  1.00   70.28  ? 351 VAL F CA  1 
ATOM   17570 C C   . VAL F  1 351 ? 153.306 61.023  19.757  1.00   72.73  ? 351 VAL F C   1 
ATOM   17571 O O   . VAL F  1 351 ? 154.019 60.045  19.611  1.00   75.10  ? 351 VAL F O   1 
ATOM   17572 C CB  . VAL F  1 351 ? 151.029 60.677  18.661  1.00   56.99  ? 351 VAL F CB  1 
ATOM   17573 C CG1 . VAL F  1 351 ? 150.193 61.054  19.856  1.00   60.36  ? 351 VAL F CG1 1 
ATOM   17574 C CG2 . VAL F  1 351 ? 150.230 60.958  17.398  1.00   50.45  ? 351 VAL F CG2 1 
ATOM   17575 N N   . GLN F  1 352 ? 153.335 61.757  20.856  1.00   73.29  ? 352 GLN F N   1 
ATOM   17576 C CA  . GLN F  1 352 ? 154.216 61.402  21.945  1.00   79.00  ? 352 GLN F CA  1 
ATOM   17577 C C   . GLN F  1 352 ? 153.400 60.604  22.946  1.00   81.62  ? 352 GLN F C   1 
ATOM   17578 O O   . GLN F  1 352 ? 153.303 60.969  24.120  1.00   88.58  ? 352 GLN F O   1 
ATOM   17579 C CB  . GLN F  1 352 ? 154.866 62.629  22.582  1.00   82.43  ? 352 GLN F CB  1 
ATOM   17580 C CG  . GLN F  1 352 ? 156.364 62.765  22.284  1.00   86.59  ? 352 GLN F CG  1 
ATOM   17581 C CD  . GLN F  1 352 ? 157.243 61.790  23.093  1.00   92.47  ? 352 GLN F CD  1 
ATOM   17582 O OE1 . GLN F  1 352 ? 157.459 61.957  24.301  1.00   94.51  ? 352 GLN F OE1 1 
ATOM   17583 N NE2 . GLN F  1 352 ? 157.761 60.773  22.414  1.00   95.49  ? 352 GLN F NE2 1 
ATOM   17584 N N   . ALA F  1 353 ? 152.826 59.509  22.448  1.00   77.17  ? 353 ALA F N   1 
ATOM   17585 C CA  . ALA F  1 353 ? 151.988 58.571  23.209  1.00   75.31  ? 353 ALA F CA  1 
ATOM   17586 C C   . ALA F  1 353 ? 152.353 58.436  24.671  1.00   75.88  ? 353 ALA F C   1 
ATOM   17587 O O   . ALA F  1 353 ? 151.494 58.481  25.551  1.00   76.38  ? 353 ALA F O   1 
ATOM   17588 C CB  . ALA F  1 353 ? 152.028 57.201  22.556  1.00   75.34  ? 353 ALA F CB  1 
ATOM   17589 N N   . GLN F  1 354 ? 153.633 58.276  24.938  1.00   76.59  ? 354 GLN F N   1 
ATOM   17590 C CA  . GLN F  1 354 ? 154.048 58.094  26.302  1.00   78.58  ? 354 GLN F CA  1 
ATOM   17591 C C   . GLN F  1 354 ? 155.314 58.870  26.562  1.00   84.41  ? 354 GLN F C   1 
ATOM   17592 O O   . GLN F  1 354 ? 155.988 59.337  25.639  1.00   84.41  ? 354 GLN F O   1 
ATOM   17593 C CB  . GLN F  1 354 ? 154.211 56.603  26.604  1.00   77.64  ? 354 GLN F CB  1 
ATOM   17594 C CG  . GLN F  1 354 ? 153.204 56.108  27.635  1.00   77.12  ? 354 GLN F CG  1 
ATOM   17595 C CD  . GLN F  1 354 ? 152.947 54.616  27.577  0.0000 75.62  ? 354 GLN F CD  1 
ATOM   17596 O OE1 . GLN F  1 354 ? 153.695 53.859  26.960  0.0000 75.60  ? 354 GLN F OE1 1 
ATOM   17597 N NE2 . GLN F  1 354 ? 151.868 54.186  28.224  0.0000 74.69  ? 354 GLN F NE2 1 
ATOM   17598 N N   . ASP F  1 355 ? 155.590 59.036  27.846  1.00   90.19  ? 355 ASP F N   1 
ATOM   17599 C CA  . ASP F  1 355 ? 156.851 59.574  28.342  1.00   94.28  ? 355 ASP F CA  1 
ATOM   17600 C C   . ASP F  1 355 ? 158.082 58.853  27.813  1.00   90.82  ? 355 ASP F C   1 
ATOM   17601 O O   . ASP F  1 355 ? 158.620 57.974  28.475  1.00   94.15  ? 355 ASP F O   1 
ATOM   17602 C CB  . ASP F  1 355 ? 156.854 59.538  29.874  1.00   102.30 ? 355 ASP F CB  1 
ATOM   17603 C CG  . ASP F  1 355 ? 155.773 60.419  30.485  1.00   103.86 ? 355 ASP F CG  1 
ATOM   17604 O OD1 . ASP F  1 355 ? 154.674 60.542  29.892  1.00   99.60  ? 355 ASP F OD1 1 
ATOM   17605 O OD2 . ASP F  1 355 ? 156.024 60.969  31.579  1.00   109.28 ? 355 ASP F OD2 1 
ATOM   17606 N N   . GLY F  1 356 ? 158.484 59.199  26.598  1.00   85.69  ? 356 GLY F N   1 
ATOM   17607 C CA  . GLY F  1 356 ? 159.663 58.631  25.977  1.00   88.71  ? 356 GLY F CA  1 
ATOM   17608 C C   . GLY F  1 356 ? 159.286 57.621  24.919  1.00   86.87  ? 356 GLY F C   1 
ATOM   17609 O O   . GLY F  1 356 ? 160.091 56.761  24.546  1.00   91.48  ? 356 GLY F O   1 
ATOM   17610 N N   . VAL F  1 357 ? 158.059 57.749  24.421  1.00   80.39  ? 357 VAL F N   1 
ATOM   17611 C CA  . VAL F  1 357 ? 157.568 56.950  23.307  1.00   75.28  ? 357 VAL F CA  1 
ATOM   17612 C C   . VAL F  1 357 ? 157.005 57.870  22.238  1.00   69.01  ? 357 VAL F C   1 
ATOM   17613 O O   . VAL F  1 357 ? 156.125 58.680  22.521  1.00   64.90  ? 357 VAL F O   1 
ATOM   17614 C CB  . VAL F  1 357 ? 156.487 55.960  23.743  1.00   74.98  ? 357 VAL F CB  1 
ATOM   17615 C CG1 . VAL F  1 357 ? 155.967 55.195  22.538  1.00   72.43  ? 357 VAL F CG1 1 
ATOM   17616 C CG2 . VAL F  1 357 ? 157.030 55.009  24.780  1.00   78.69  ? 357 VAL F CG2 1 
ATOM   17617 N N   . SER F  1 358 ? 157.510 57.777  21.020  1.00   67.88  ? 358 SER F N   1 
ATOM   17618 C CA  . SER F  1 358 ? 156.984 58.622  19.966  1.00   65.53  ? 358 SER F CA  1 
ATOM   17619 C C   . SER F  1 358 ? 156.350 57.734  18.885  1.00   63.91  ? 358 SER F C   1 
ATOM   17620 O O   . SER F  1 358 ? 157.046 56.940  18.252  1.00   65.83  ? 358 SER F O   1 
ATOM   17621 C CB  . SER F  1 358 ? 158.095 59.486  19.395  1.00   67.43  ? 358 SER F CB  1 
ATOM   17622 O OG  . SER F  1 358 ? 157.601 60.317  18.368  1.00   65.64  ? 358 SER F OG  1 
ATOM   17623 N N   . CYS F  1 359 ? 155.044 57.900  18.649  1.00   62.00  ? 359 CYS F N   1 
ATOM   17624 C CA  . CYS F  1 359 ? 154.270 56.981  17.791  1.00   58.49  ? 359 CYS F CA  1 
ATOM   17625 C C   . CYS F  1 359 ? 153.787 57.519  16.459  1.00   52.51  ? 359 CYS F C   1 
ATOM   17626 O O   . CYS F  1 359 ? 153.469 58.695  16.316  1.00   46.99  ? 359 CYS F O   1 
ATOM   17627 C CB  . CYS F  1 359 ? 153.034 56.470  18.539  1.00   57.94  ? 359 CYS F CB  1 
ATOM   17628 S SG  . CYS F  1 359 ? 153.352 55.346  19.905  1.00   76.20  ? 359 CYS F SG  1 
ATOM   17629 N N   . LEU F  1 360 ? 153.734 56.616  15.488  1.00   52.10  ? 360 LEU F N   1 
ATOM   17630 C CA  . LEU F  1 360 ? 153.162 56.909  14.190  1.00   49.81  ? 360 LEU F CA  1 
ATOM   17631 C C   . LEU F  1 360 ? 151.653 56.991  14.372  1.00   49.62  ? 360 LEU F C   1 
ATOM   17632 O O   . LEU F  1 360 ? 151.016 56.007  14.734  1.00   52.01  ? 360 LEU F O   1 
ATOM   17633 C CB  . LEU F  1 360 ? 153.542 55.844  13.165  1.00   49.50  ? 360 LEU F CB  1 
ATOM   17634 C CG  . LEU F  1 360 ? 152.958 56.100  11.777  1.00   45.50  ? 360 LEU F CG  1 
ATOM   17635 C CD1 . LEU F  1 360 ? 153.490 57.401  11.225  1.00   42.43  ? 360 LEU F CD1 1 
ATOM   17636 C CD2 . LEU F  1 360 ? 153.294 54.970  10.858  1.00   43.97  ? 360 LEU F CD2 1 
ATOM   17637 N N   . GLY F  1 361 ? 151.097 58.177  14.152  1.00   49.79  ? 361 GLY F N   1 
ATOM   17638 C CA  . GLY F  1 361 ? 149.714 58.478  14.492  1.00   47.68  ? 361 GLY F CA  1 
ATOM   17639 C C   . GLY F  1 361 ? 148.663 58.074  13.488  1.00   43.92  ? 361 GLY F C   1 
ATOM   17640 O O   . GLY F  1 361 ? 147.787 58.848  13.132  1.00   43.00  ? 361 GLY F O   1 
ATOM   17641 N N   . PHE F  1 362 ? 148.756 56.855  13.009  1.00   44.82  ? 362 PHE F N   1 
ATOM   17642 C CA  . PHE F  1 362 ? 147.724 56.323  12.155  1.00   42.15  ? 362 PHE F CA  1 
ATOM   17643 C C   . PHE F  1 362 ? 147.230 55.032  12.766  1.00   47.26  ? 362 PHE F C   1 
ATOM   17644 O O   . PHE F  1 362 ? 148.030 54.195  13.196  1.00   50.91  ? 362 PHE F O   1 
ATOM   17645 C CB  . PHE F  1 362 ? 148.250 56.088  10.750  1.00   39.34  ? 362 PHE F CB  1 
ATOM   17646 C CG  . PHE F  1 362 ? 148.686 57.331  10.056  1.00   37.91  ? 362 PHE F CG  1 
ATOM   17647 C CD1 . PHE F  1 362 ? 149.860 57.955  10.394  1.00   38.93  ? 362 PHE F CD1 1 
ATOM   17648 C CD2 . PHE F  1 362 ? 147.923 57.868  9.041   1.00   37.32  ? 362 PHE F CD2 1 
ATOM   17649 C CE1 . PHE F  1 362 ? 150.261 59.082  9.740   1.00   34.18  ? 362 PHE F CE1 1 
ATOM   17650 C CE2 . PHE F  1 362 ? 148.322 59.015  8.389   1.00   35.62  ? 362 PHE F CE2 1 
ATOM   17651 C CZ  . PHE F  1 362 ? 149.490 59.616  8.742   1.00   35.65  ? 362 PHE F CZ  1 
ATOM   17652 N N   . VAL F  1 363 ? 145.919 54.836  12.733  1.00   47.45  ? 363 VAL F N   1 
ATOM   17653 C CA  . VAL F  1 363 ? 145.310 53.710  13.414  1.00   46.25  ? 363 VAL F CA  1 
ATOM   17654 C C   . VAL F  1 363 ? 144.593 52.817  12.404  1.00   42.14  ? 363 VAL F C   1 
ATOM   17655 O O   . VAL F  1 363 ? 144.136 53.274  11.365  1.00   39.22  ? 363 VAL F O   1 
ATOM   17656 C CB  . VAL F  1 363 ? 144.330 54.210  14.499  1.00   45.62  ? 363 VAL F CB  1 
ATOM   17657 C CG1 . VAL F  1 363 ? 143.739 53.042  15.259  1.00   50.93  ? 363 VAL F CG1 1 
ATOM   17658 C CG2 . VAL F  1 363 ? 145.069 55.106  15.473  1.00   44.50  ? 363 VAL F CG2 1 
ATOM   17659 N N   . ASP F  1 364 ? 144.537 51.532  12.704  1.00   43.18  ? 364 ASP F N   1 
ATOM   17660 C CA  . ASP F  1 364 ? 143.934 50.551  11.831  1.00   44.02  ? 364 ASP F CA  1 
ATOM   17661 C C   . ASP F  1 364 ? 142.421 50.619  11.951  1.00   44.88  ? 364 ASP F C   1 
ATOM   17662 O O   . ASP F  1 364 ? 141.865 50.399  13.025  1.00   47.56  ? 364 ASP F O   1 
ATOM   17663 C CB  . ASP F  1 364 ? 144.455 49.171  12.203  1.00   48.92  ? 364 ASP F CB  1 
ATOM   17664 C CG  . ASP F  1 364 ? 144.155 48.129  11.165  1.00   52.46  ? 364 ASP F CG  1 
ATOM   17665 O OD1 . ASP F  1 364 ? 143.298 48.381  10.292  1.00   53.02  ? 364 ASP F OD1 1 
ATOM   17666 O OD2 . ASP F  1 364 ? 144.804 47.060  11.218  1.00   55.80  1 364 ASP F OD2 1 
ATOM   17667 N N   . GLY F  1 365 ? 141.738 50.917  10.857  1.00   40.43  ? 365 GLY F N   1 
ATOM   17668 C CA  . GLY F  1 365 ? 140.295 50.967  10.931  1.00   40.84  ? 365 GLY F CA  1 
ATOM   17669 C C   . GLY F  1 365 ? 139.581 49.641  10.806  1.00   43.08  ? 365 GLY F C   1 
ATOM   17670 O O   . GLY F  1 365 ? 138.362 49.575  10.903  1.00   46.65  ? 365 GLY F O   1 
ATOM   17671 N N   . GLY F  1 366 ? 140.333 48.575  10.617  1.00   43.09  ? 366 GLY F N   1 
ATOM   17672 C CA  . GLY F  1 366 ? 139.738 47.266  10.450  1.00   47.78  ? 366 GLY F CA  1 
ATOM   17673 C C   . GLY F  1 366 ? 139.328 47.063  9.006   1.00   51.64  ? 366 GLY F C   1 
ATOM   17674 O O   . GLY F  1 366 ? 139.601 47.903  8.153   1.00   49.53  ? 366 GLY F O   1 
ATOM   17675 N N   . VAL F  1 367 ? 138.634 45.968  8.727   1.00   59.37  ? 367 VAL F N   1 
ATOM   17676 C CA  . VAL F  1 367 ? 138.363 45.611  7.341   1.00   64.00  ? 367 VAL F CA  1 
ATOM   17677 C C   . VAL F  1 367 ? 137.039 46.160  6.833   1.00   66.65  ? 367 VAL F C   1 
ATOM   17678 O O   . VAL F  1 367 ? 136.802 46.171  5.632   1.00   68.91  ? 367 VAL F O   1 
ATOM   17679 C CB  . VAL F  1 367 ? 138.396 44.069  7.138   1.00   59.90  ? 367 VAL F CB  1 
ATOM   17680 C CG1 . VAL F  1 367 ? 139.773 43.540  7.412   1.00   59.84  ? 367 VAL F CG1 1 
ATOM   17681 C CG2 . VAL F  1 367 ? 137.398 43.374  8.036   1.00   61.97  ? 367 VAL F CG2 1 
ATOM   17682 N N   . HIS F  1 368 ? 136.177 46.619  7.736   1.00   66.56  ? 368 HIS F N   1 
ATOM   17683 C CA  . HIS F  1 368 ? 134.922 47.239  7.322   1.00   65.22  ? 368 HIS F CA  1 
ATOM   17684 C C   . HIS F  1 368 ? 134.868 48.680  7.776   1.00   60.92  ? 368 HIS F C   1 
ATOM   17685 O O   . HIS F  1 368 ? 133.864 49.157  8.303   1.00   61.97  ? 368 HIS F O   1 
ATOM   17686 C CB  . HIS F  1 368 ? 133.746 46.430  7.834   1.00   67.61  ? 368 HIS F CB  1 
ATOM   17687 C CG  . HIS F  1 368 ? 133.751 45.024  7.322   1.00   71.75  ? 368 HIS F CG  1 
ATOM   17688 N ND1 . HIS F  1 368 ? 134.149 43.952  8.093   1.00   74.18  ? 368 HIS F ND1 1 
ATOM   17689 C CD2 . HIS F  1 368 ? 133.468 44.520  6.096   1.00   73.70  ? 368 HIS F CD2 1 
ATOM   17690 C CE1 . HIS F  1 368 ? 134.076 42.844  7.376   1.00   77.52  ? 368 HIS F CE1 1 
ATOM   17691 N NE2 . HIS F  1 368 ? 133.668 43.162  6.160   1.00   77.52  ? 368 HIS F NE2 1 
ATOM   17692 N N   . ALA F  1 369 ? 136.001 49.346  7.599   1.00   56.61  ? 369 ALA F N   1 
ATOM   17693 C CA  . ALA F  1 369 ? 136.121 50.751  7.894   1.00   51.67  ? 369 ALA F CA  1 
ATOM   17694 C C   . ALA F  1 369 ? 135.247 51.494  6.918   1.00   53.49  ? 369 ALA F C   1 
ATOM   17695 O O   . ALA F  1 369 ? 135.066 51.055  5.774   1.00   55.08  ? 369 ALA F O   1 
ATOM   17696 C CB  . ALA F  1 369 ? 137.563 51.215  7.791   1.00   46.25  ? 369 ALA F CB  1 
ATOM   17697 N N   . ARG F  1 370 ? 134.742 52.636  7.373   1.00   51.90  ? 370 ARG F N   1 
ATOM   17698 C CA  . ARG F  1 370 ? 133.795 53.446  6.623   1.00   52.84  ? 370 ARG F CA  1 
ATOM   17699 C C   . ARG F  1 370 ? 134.422 53.973  5.323   1.00   47.54  ? 370 ARG F C   1 
ATOM   17700 O O   . ARG F  1 370 ? 133.809 53.952  4.252   1.00   48.28  ? 370 ARG F O   1 
ATOM   17701 C CB  . ARG F  1 370 ? 133.317 54.613  7.509   1.00   56.06  ? 370 ARG F CB  1 
ATOM   17702 C CG  . ARG F  1 370 ? 132.659 55.735  6.739   1.00   59.37  ? 370 ARG F CG  1 
ATOM   17703 C CD  . ARG F  1 370 ? 131.401 55.202  6.103   1.00   67.37  ? 370 ARG F CD  1 
ATOM   17704 N NE  . ARG F  1 370 ? 130.759 56.137  5.185   1.00   70.92  ? 370 ARG F NE  1 
ATOM   17705 C CZ  . ARG F  1 370 ? 130.970 56.145  3.870   1.00   73.91  ? 370 ARG F CZ  1 
ATOM   17706 N NH1 . ARG F  1 370 ? 131.828 55.288  3.327   1.00   77.04  ? 370 ARG F NH1 1 
ATOM   17707 N NH2 . ARG F  1 370 ? 130.341 57.016  3.094   1.00   73.31  ? 370 ARG F NH2 1 
ATOM   17708 N N   . ALA F  1 371 ? 135.666 54.414  5.420   1.00   41.44  ? 371 ALA F N   1 
ATOM   17709 C CA  . ALA F  1 371 ? 136.394 54.897  4.261   1.00   38.22  ? 371 ALA F CA  1 
ATOM   17710 C C   . ALA F  1 371 ? 137.847 54.393  4.278   1.00   38.65  ? 371 ALA F C   1 
ATOM   17711 O O   . ALA F  1 371 ? 138.349 53.942  5.317   1.00   39.13  ? 371 ALA F O   1 
ATOM   17712 C CB  . ALA F  1 371 ? 136.344 56.412  4.225   1.00   34.96  ? 371 ALA F CB  1 
ATOM   17713 N N   . GLY F  1 372 ? 138.528 54.479  3.141   1.00   37.18  ? 372 GLY F N   1 
ATOM   17714 C CA  . GLY F  1 372 ? 139.915 54.050  3.073   1.00   38.21  ? 372 GLY F CA  1 
ATOM   17715 C C   . GLY F  1 372 ? 140.841 54.881  3.938   1.00   34.10  ? 372 GLY F C   1 
ATOM   17716 O O   . GLY F  1 372 ? 141.746 54.365  4.568   1.00   35.13  ? 372 GLY F O   1 
ATOM   17717 N N   . ILE F  1 373 ? 140.587 56.179  3.950   1.00   34.23  ? 373 ILE F N   1 
ATOM   17718 C CA  . ILE F  1 373 ? 141.302 57.160  4.759   1.00   31.35  ? 373 ILE F CA  1 
ATOM   17719 C C   . ILE F  1 373 ? 140.283 58.017  5.516   1.00   30.93  ? 373 ILE F C   1 
ATOM   17720 O O   . ILE F  1 373 ? 139.328 58.501  4.924   1.00   30.93  ? 373 ILE F O   1 
ATOM   17721 C CB  . ILE F  1 373 ? 142.177 58.063  3.876   1.00   29.44  ? 373 ILE F CB  1 
ATOM   17722 C CG1 . ILE F  1 373 ? 143.127 57.221  3.018   1.00   32.59  ? 373 ILE F CG1 1 
ATOM   17723 C CG2 . ILE F  1 373 ? 142.931 59.063  4.711   1.00   29.07  ? 373 ILE F CG2 1 
ATOM   17724 C CD1 . ILE F  1 373 ? 143.871 58.019  1.977   1.00   32.59  ? 373 ILE F CD1 1 
ATOM   17725 N N   . ALA F  1 374 ? 140.451 58.172  6.823   1.00   31.40  ? 374 ALA F N   1 
ATOM   17726 C CA  . ALA F  1 374 ? 139.603 59.088  7.564   1.00   28.40  ? 374 ALA F CA  1 
ATOM   17727 C C   . ALA F  1 374 ? 140.472 60.085  8.324   1.00   30.67  ? 374 ALA F C   1 
ATOM   17728 O O   . ALA F  1 374 ? 141.047 59.752  9.351   1.00   33.66  ? 374 ALA F O   1 
ATOM   17729 C CB  . ALA F  1 374 ? 138.680 58.322  8.516   1.00   28.23  ? 374 ALA F CB  1 
ATOM   17730 N N   . LEU F  1 375 ? 140.563 61.307  7.809   1.00   28.88  ? 375 LEU F N   1 
ATOM   17731 C CA  . LEU F  1 375 ? 141.375 62.338  8.426   1.00   26.85  ? 375 LEU F CA  1 
ATOM   17732 C C   . LEU F  1 375 ? 140.650 62.936  9.599   1.00   28.07  ? 375 LEU F C   1 
ATOM   17733 O O   . LEU F  1 375 ? 139.570 63.448  9.431   1.00   31.44  ? 375 LEU F O   1 
ATOM   17734 C CB  . LEU F  1 375 ? 141.701 63.423  7.418   1.00   25.94  ? 375 LEU F CB  1 
ATOM   17735 C CG  . LEU F  1 375 ? 142.268 62.920  6.094   1.00   26.38  ? 375 LEU F CG  1 
ATOM   17736 C CD1 . LEU F  1 375 ? 142.308 64.043  5.084   1.00   26.62  ? 375 LEU F CD1 1 
ATOM   17737 C CD2 . LEU F  1 375 ? 143.648 62.314  6.283   1.00   26.15  ? 375 LEU F CD2 1 
ATOM   17738 N N   . GLY F  1 376 ? 141.251 62.917  10.778  1.00   26.78  ? 376 GLY F N   1 
ATOM   17739 C CA  . GLY F  1 376 ? 140.538 63.324  11.979  1.00   26.42  ? 376 GLY F CA  1 
ATOM   17740 C C   . GLY F  1 376 ? 140.995 64.664  12.522  1.00   28.55  ? 376 GLY F C   1 
ATOM   17741 O O   . GLY F  1 376 ? 141.588 65.442  11.795  1.00   28.93  ? 376 GLY F O   1 
ATOM   17742 N N   . ALA F  1 377 ? 140.695 64.947  13.786  1.00   29.74  ? 377 ALA F N   1 
ATOM   17743 C CA  . ALA F  1 377 ? 140.971 66.256  14.382  1.00   29.67  ? 377 ALA F CA  1 
ATOM   17744 C C   . ALA F  1 377 ? 142.461 66.582  14.432  1.00   32.14  ? 377 ALA F C   1 
ATOM   17745 O O   . ALA F  1 377 ? 142.859 67.725  14.282  1.00   35.74  ? 377 ALA F O   1 
ATOM   17746 C CB  . ALA F  1 377 ? 140.378 66.341  15.776  1.00   31.08  ? 377 ALA F CB  1 
ATOM   17747 N N   . HIS F  1 378 ? 143.293 65.592  14.697  1.00   34.29  ? 378 HIS F N   1 
ATOM   17748 C CA  . HIS F  1 378 ? 144.716 65.854  14.810  1.00   33.53  ? 378 HIS F CA  1 
ATOM   17749 C C   . HIS F  1 378 ? 145.278 66.309  13.472  1.00   32.94  ? 378 HIS F C   1 
ATOM   17750 O O   . HIS F  1 378 ? 146.212 67.103  13.418  1.00   35.58  ? 378 HIS F O   1 
ATOM   17751 C CB  A HIS F  1 378 ? 145.476 64.642  15.344  0.50   33.60  ? 378 HIS F CB  1 
ATOM   17752 C CB  B HIS F  1 378 ? 145.431 64.590  15.302  0.50   33.55  ? 378 HIS F CB  1 
ATOM   17753 C CG  A HIS F  1 378 ? 145.561 64.616  16.836  0.50   35.28  ? 378 HIS F CG  1 
ATOM   17754 C CG  B HIS F  1 378 ? 146.748 64.845  15.959  0.50   34.84  ? 378 HIS F CG  1 
ATOM   17755 N ND1 A HIS F  1 378 ? 146.562 63.964  17.517  0.50   38.68  ? 378 HIS F ND1 1 
ATOM   17756 N ND1 B HIS F  1 378 ? 146.864 65.261  17.267  0.50   37.86  ? 378 HIS F ND1 1 
ATOM   17757 C CD2 A HIS F  1 378 ? 144.771 65.182  17.778  0.50   34.43  ? 378 HIS F CD2 1 
ATOM   17758 C CD2 B HIS F  1 378 ? 148.008 64.726  15.490  0.50   35.73  ? 378 HIS F CD2 1 
ATOM   17759 C CE1 A HIS F  1 378 ? 146.382 64.123  18.817  0.50   40.03  ? 378 HIS F CE1 1 
ATOM   17760 C CE1 B HIS F  1 378 ? 148.142 65.399  17.571  0.50   40.22  ? 378 HIS F CE1 1 
ATOM   17761 N NE2 A HIS F  1 378 ? 145.300 64.856  19.002  0.50   36.45  ? 378 HIS F NE2 1 
ATOM   17762 N NE2 B HIS F  1 378 ? 148.859 65.080  16.509  0.50   38.71  ? 378 HIS F NE2 1 
ATOM   17763 N N   . HIS F  1 379 ? 144.735 65.769  12.395  1.00   30.71  ? 379 HIS F N   1 
ATOM   17764 C CA  . HIS F  1 379 ? 145.130 66.193  11.068  1.00   29.10  ? 379 HIS F CA  1 
ATOM   17765 C C   . HIS F  1 379 ? 144.783 67.649  10.815  1.00   32.32  ? 379 HIS F C   1 
ATOM   17766 O O   . HIS F  1 379 ? 145.567 68.398  10.225  1.00   35.21  ? 379 HIS F O   1 
ATOM   17767 C CB  . HIS F  1 379 ? 144.464 65.319  10.015  1.00   30.13  ? 379 HIS F CB  1 
ATOM   17768 C CG  . HIS F  1 379 ? 144.798 65.713  8.612   1.00   29.27  ? 379 HIS F CG  1 
ATOM   17769 N ND1 . HIS F  1 379 ? 145.900 65.231  7.946   1.00   29.27  ? 379 HIS F ND1 1 
ATOM   17770 C CD2 . HIS F  1 379 ? 144.186 66.563  7.756   1.00   28.69  ? 379 HIS F CD2 1 
ATOM   17771 C CE1 . HIS F  1 379 ? 145.944 65.747  6.732   1.00   26.04  ? 379 HIS F CE1 1 
ATOM   17772 N NE2 . HIS F  1 379 ? 144.918 66.560  6.593   1.00   28.48  ? 379 HIS F NE2 1 
ATOM   17773 N N   . LEU F  1 380 ? 143.594 68.038  11.265  1.00   31.53  ? 380 LEU F N   1 
ATOM   17774 C CA  . LEU F  1 380 ? 143.058 69.381  11.020  1.00   29.80  ? 380 LEU F CA  1 
ATOM   17775 C C   . LEU F  1 380 ? 143.692 70.472  11.853  1.00   30.28  ? 380 LEU F C   1 
ATOM   17776 O O   . LEU F  1 380 ? 143.679 71.619  11.464  1.00   34.83  ? 380 LEU F O   1 
ATOM   17777 C CB  . LEU F  1 380 ? 141.563 69.403  11.271  1.00   26.68  ? 380 LEU F CB  1 
ATOM   17778 C CG  . LEU F  1 380 ? 140.740 68.452  10.392  1.00   27.27  ? 380 LEU F CG  1 
ATOM   17779 C CD1 . LEU F  1 380 ? 139.326 68.383  10.905  1.00   23.28  ? 380 LEU F CD1 1 
ATOM   17780 C CD2 . LEU F  1 380 ? 140.766 68.908  8.956   1.00   26.75  ? 380 LEU F CD2 1 
ATOM   17781 N N   . GLU F  1 381 ? 144.202 70.115  13.016  1.00   31.46  ? 381 GLU F N   1 
ATOM   17782 C CA  . GLU F  1 381 ? 144.741 71.087  13.939  1.00   35.71  ? 381 GLU F CA  1 
ATOM   17783 C C   . GLU F  1 381 ? 145.897 71.910  13.366  1.00   35.82  ? 381 GLU F C   1 
ATOM   17784 O O   . GLU F  1 381 ? 146.762 71.387  12.643  1.00   33.91  ? 381 GLU F O   1 
ATOM   17785 C CB  . GLU F  1 381 ? 145.178 70.382  15.212  1.00   37.63  ? 381 GLU F CB  1 
ATOM   17786 C CG  . GLU F  1 381 ? 144.013 69.976  16.045  1.00   38.24  ? 381 GLU F CG  1 
ATOM   17787 C CD  . GLU F  1 381 ? 144.370 68.962  17.109  1.00   39.21  ? 381 GLU F CD  1 
ATOM   17788 O OE1 . GLU F  1 381 ? 145.556 68.573  17.234  1.00   38.63  ? 381 GLU F OE1 1 
ATOM   17789 O OE2 . GLU F  1 381 ? 143.439 68.551  17.827  1.00   40.12  1 381 GLU F OE2 1 
ATOM   17790 N N   . GLU F  1 382 ? 145.852 73.214  13.666  1.00   35.94  ? 382 GLU F N   1 
ATOM   17791 C CA  . GLU F  1 382 ? 146.836 74.210  13.235  1.00   37.55  ? 382 GLU F CA  1 
ATOM   17792 C C   . GLU F  1 382 ? 146.917 74.299  11.708  1.00   35.87  ? 382 GLU F C   1 
ATOM   17793 O O   . GLU F  1 382 ? 147.938 74.727  11.154  1.00   35.69  ? 382 GLU F O   1 
ATOM   17794 C CB  . GLU F  1 382 ? 148.211 73.932  13.847  1.00   38.04  ? 382 GLU F CB  1 
ATOM   17795 C CG  . GLU F  1 382 ? 148.258 74.003  15.365  1.00   39.59  ? 382 GLU F CG  1 
ATOM   17796 C CD  . GLU F  1 382 ? 147.756 75.311  15.910  1.00   41.16  ? 382 GLU F CD  1 
ATOM   17797 O OE1 . GLU F  1 382 ? 148.057 76.355  15.306  1.00   42.28  ? 382 GLU F OE1 1 
ATOM   17798 O OE2 . GLU F  1 382 ? 147.080 75.303  16.956  1.00   42.84  1 382 GLU F OE2 1 
ATOM   17799 N N   . ASN F  1 383 ? 145.819 73.908  11.051  1.00   34.05  ? 383 ASN F N   1 
ATOM   17800 C CA  . ASN F  1 383 ? 145.601 74.169  9.636   1.00   31.93  ? 383 ASN F CA  1 
ATOM   17801 C C   . ASN F  1 383 ? 144.299 74.933  9.485   1.00   31.97  ? 383 ASN F C   1 
ATOM   17802 O O   . ASN F  1 383 ? 143.347 74.702  10.225  1.00   34.61  ? 383 ASN F O   1 
ATOM   17803 C CB  . ASN F  1 383 ? 145.529 72.889  8.819   1.00   30.86  ? 383 ASN F CB  1 
ATOM   17804 C CG  . ASN F  1 383 ? 146.843 72.166  8.737   1.00   35.74  ? 383 ASN F CG  1 
ATOM   17805 O OD1 . ASN F  1 383 ? 147.800 72.637  8.110   1.00   37.73  ? 383 ASN F OD1 1 
ATOM   17806 N ND2 . ASN F  1 383 ? 146.891 70.983  9.338   1.00   38.06  ? 383 ASN F ND2 1 
ATOM   17807 N N   . LEU F  1 384 ? 144.264 75.853  8.533   1.00   31.35  ? 384 LEU F N   1 
ATOM   17808 C CA  . LEU F  1 384 ? 143.027 76.519  8.165   1.00   31.76  ? 384 LEU F CA  1 
ATOM   17809 C C   . LEU F  1 384 ? 142.428 75.793  6.986   1.00   33.41  ? 384 LEU F C   1 
ATOM   17810 O O   . LEU F  1 384 ? 143.044 75.742  5.926   1.00   33.30  ? 384 LEU F O   1 
ATOM   17811 C CB  . LEU F  1 384 ? 143.257 77.981  7.811   1.00   33.17  ? 384 LEU F CB  1 
ATOM   17812 C CG  . LEU F  1 384 ? 141.999 78.672  7.283   1.00   33.20  ? 384 LEU F CG  1 
ATOM   17813 C CD1 . LEU F  1 384 ? 140.983 78.873  8.374   1.00   32.57  ? 384 LEU F CD1 1 
ATOM   17814 C CD2 . LEU F  1 384 ? 142.333 79.967  6.591   1.00   32.91  ? 384 LEU F CD2 1 
ATOM   17815 N N   . VAL F  1 385 ? 141.231 75.239  7.167   1.00   33.87  ? 385 VAL F N   1 
ATOM   17816 C CA  . VAL F  1 385 ? 140.604 74.415  6.147   1.00   31.36  ? 385 VAL F CA  1 
ATOM   17817 C C   . VAL F  1 385 ? 139.310 75.073  5.742   1.00   29.41  ? 385 VAL F C   1 
ATOM   17818 O O   . VAL F  1 385 ? 138.448 75.324  6.572   1.00   29.27  ? 385 VAL F O   1 
ATOM   17819 C CB  . VAL F  1 385 ? 140.358 72.980  6.643   1.00   28.46  ? 385 VAL F CB  1 
ATOM   17820 C CG1 . VAL F  1 385 ? 139.799 72.121  5.527   1.00   25.63  ? 385 VAL F CG1 1 
ATOM   17821 C CG2 . VAL F  1 385 ? 141.643 72.372  7.182   1.00   29.09  ? 385 VAL F CG2 1 
ATOM   17822 N N   . VAL F  1 386 ? 139.211 75.418  4.469   1.00   30.03  ? 386 VAL F N   1 
ATOM   17823 C CA  . VAL F  1 386 ? 138.060 76.174  3.965   1.00   28.93  ? 386 VAL F CA  1 
ATOM   17824 C C   . VAL F  1 386 ? 137.041 75.293  3.244   1.00   26.48  ? 386 VAL F C   1 
ATOM   17825 O O   . VAL F  1 386 ? 137.358 74.607  2.287   1.00   26.50  ? 386 VAL F O   1 
ATOM   17826 C CB  . VAL F  1 386 ? 138.507 77.293  3.010   1.00   26.24  ? 386 VAL F CB  1 
ATOM   17827 C CG1 . VAL F  1 386 ? 137.301 78.049  2.467   1.00   27.72  ? 386 VAL F CG1 1 
ATOM   17828 C CG2 . VAL F  1 386 ? 139.451 78.235  3.711   1.00   25.82  ? 386 VAL F CG2 1 
ATOM   17829 N N   . PHE F  1 387 ? 135.821 75.276  3.742   1.00   26.60  ? 387 PHE F N   1 
ATOM   17830 C CA  . PHE F  1 387 ? 134.777 74.538  3.063   1.00   27.25  ? 387 PHE F CA  1 
ATOM   17831 C C   . PHE F  1 387 ? 133.936 75.460  2.207   1.00   27.47  ? 387 PHE F C   1 
ATOM   17832 O O   . PHE F  1 387 ? 132.990 76.088  2.683   1.00   27.30  ? 387 PHE F O   1 
ATOM   17833 C CB  . PHE F  1 387 ? 133.919 73.803  4.072   1.00   27.22  ? 387 PHE F CB  1 
ATOM   17834 C CG  . PHE F  1 387 ? 134.636 72.713  4.747   1.00   26.78  ? 387 PHE F CG  1 
ATOM   17835 C CD1 . PHE F  1 387 ? 135.524 72.990  5.765   1.00   24.72  ? 387 PHE F CD1 1 
ATOM   17836 C CD2 . PHE F  1 387 ? 134.435 71.396  4.356   1.00   30.83  ? 387 PHE F CD2 1 
ATOM   17837 C CE1 . PHE F  1 387 ? 136.217 71.982  6.376   1.00   27.24  ? 387 PHE F CE1 1 
ATOM   17838 C CE2 . PHE F  1 387 ? 135.116 70.359  4.970   1.00   31.90  ? 387 PHE F CE2 1 
ATOM   17839 C CZ  . PHE F  1 387 ? 136.011 70.647  5.986   1.00   31.22  ? 387 PHE F CZ  1 
ATOM   17840 N N   . ASP F  1 388 ? 134.300 75.507  0.933   1.00   28.72  ? 388 ASP F N   1 
ATOM   17841 C CA  . ASP F  1 388 ? 133.640 76.329  -0.058  1.00   29.35  ? 388 ASP F CA  1 
ATOM   17842 C C   . ASP F  1 388 ? 132.524 75.525  -0.717  1.00   28.36  ? 388 ASP F C   1 
ATOM   17843 O O   . ASP F  1 388 ? 132.718 74.836  -1.705  1.00   30.49  ? 388 ASP F O   1 
ATOM   17844 C CB  . ASP F  1 388 ? 134.647 76.801  -1.088  1.00   32.62  ? 388 ASP F CB  1 
ATOM   17845 C CG  . ASP F  1 388 ? 134.085 77.808  -2.036  1.00   38.72  ? 388 ASP F CG  1 
ATOM   17846 O OD1 . ASP F  1 388 ? 132.864 78.042  -2.034  1.00   44.42  ? 388 ASP F OD1 1 
ATOM   17847 O OD2 . ASP F  1 388 ? 134.874 78.355  -2.818  1.00   38.86  1 388 ASP F OD2 1 
ATOM   17848 N N   . LEU F  1 389 ? 131.339 75.633  -0.157  1.00   24.53  ? 389 LEU F N   1 
ATOM   17849 C CA  . LEU F  1 389 ? 130.240 74.842  -0.616  1.00   26.34  ? 389 LEU F CA  1 
ATOM   17850 C C   . LEU F  1 389 ? 129.753 75.385  -1.938  1.00   32.60  ? 389 LEU F C   1 
ATOM   17851 O O   . LEU F  1 389 ? 129.225 74.677  -2.800  1.00   33.89  ? 389 LEU F O   1 
ATOM   17852 C CB  . LEU F  1 389 ? 129.148 74.891  0.435   1.00   26.16  ? 389 LEU F CB  1 
ATOM   17853 C CG  . LEU F  1 389 ? 129.865 74.615  1.747   1.00   25.62  ? 389 LEU F CG  1 
ATOM   17854 C CD1 . LEU F  1 389 ? 129.007 75.042  2.858   1.00   25.56  ? 389 LEU F CD1 1 
ATOM   17855 C CD2 . LEU F  1 389 ? 130.145 73.106  1.821   1.00   26.37  ? 389 LEU F CD2 1 
ATOM   17856 N N   . GLU F  1 390 ? 129.999 76.663  -2.122  1.00   35.58  ? 390 GLU F N   1 
ATOM   17857 C CA  . GLU F  1 390 ? 129.510 77.328  -3.297  1.00   39.19  ? 390 GLU F CA  1 
ATOM   17858 C C   . GLU F  1 390 ? 130.226 76.836  -4.546  1.00   35.96  ? 390 GLU F C   1 
ATOM   17859 O O   . GLU F  1 390 ? 129.656 76.812  -5.631  1.00   35.83  ? 390 GLU F O   1 
ATOM   17860 C CB  . GLU F  1 390 ? 129.684 78.825  -3.119  1.00   46.90  ? 390 GLU F CB  1 
ATOM   17861 C CG  . GLU F  1 390 ? 129.366 79.611  -4.322  1.00   57.25  ? 390 GLU F CG  1 
ATOM   17862 C CD  . GLU F  1 390 ? 129.916 80.989  -4.209  1.00   62.91  ? 390 GLU F CD  1 
ATOM   17863 O OE1 . GLU F  1 390 ? 130.735 81.378  -5.077  1.00   64.87  ? 390 GLU F OE1 1 
ATOM   17864 O OE2 . GLU F  1 390 ? 129.530 81.669  -3.235  1.00   63.26  ? 390 GLU F OE2 1 
ATOM   17865 N N   . ARG F  1 391 ? 131.478 76.438  -4.405  1.00   33.06  ? 391 ARG F N   1 
ATOM   17866 C CA  . ARG F  1 391 ? 132.199 75.932  -5.559  1.00   35.18  ? 391 ARG F CA  1 
ATOM   17867 C C   . ARG F  1 391 ? 132.495 74.454  -5.408  1.00   31.81  ? 391 ARG F C   1 
ATOM   17868 O O   . ARG F  1 391 ? 133.169 73.874  -6.244  1.00   34.11  ? 391 ARG F O   1 
ATOM   17869 C CB  . ARG F  1 391 ? 133.483 76.724  -5.777  1.00   38.74  ? 391 ARG F CB  1 
ATOM   17870 C CG  . ARG F  1 391 ? 133.254 78.190  -6.070  1.00   46.84  ? 391 ARG F CG  1 
ATOM   17871 C CD  . ARG F  1 391 ? 134.541 78.872  -6.534  1.00   55.00  ? 391 ARG F CD  1 
ATOM   17872 N NE  . ARG F  1 391 ? 135.205 78.101  -7.590  1.00   62.07  ? 391 ARG F NE  1 
ATOM   17873 C CZ  . ARG F  1 391 ? 136.240 78.529  -8.309  1.00   66.95  ? 391 ARG F CZ  1 
ATOM   17874 N NH1 . ARG F  1 391 ? 136.740 79.742  -8.106  1.00   67.09  ? 391 ARG F NH1 1 
ATOM   17875 N NH2 . ARG F  1 391 ? 136.769 77.742  -9.240  1.00   70.63  ? 391 ARG F NH2 1 
ATOM   17876 N N   . SER F  1 392 ? 131.992 73.863  -4.333  1.00   27.87  ? 392 SER F N   1 
ATOM   17877 C CA  . SER F  1 392 ? 132.219 72.455  -4.036  1.00   26.36  ? 392 SER F CA  1 
ATOM   17878 C C   . SER F  1 392 ? 133.684 72.090  -4.014  1.00   28.50  ? 392 SER F C   1 
ATOM   17879 O O   . SER F  1 392 ? 134.116 71.200  -4.749  1.00   30.01  ? 392 SER F O   1 
ATOM   17880 C CB  . SER F  1 392 ? 131.518 71.560  -5.049  1.00   27.57  ? 392 SER F CB  1 
ATOM   17881 O OG  . SER F  1 392 ? 131.415 70.243  -4.539  1.00   27.03  ? 392 SER F OG  1 
ATOM   17882 N N   . ARG F  1 393 ? 134.448 72.771  -3.168  1.00   28.34  ? 393 ARG F N   1 
ATOM   17883 C CA  . ARG F  1 393 ? 135.877 72.514  -3.065  1.00   28.29  ? 393 ARG F CA  1 
ATOM   17884 C C   . ARG F  1 393 ? 136.389 72.764  -1.651  1.00   30.02  ? 393 ARG F C   1 
ATOM   17885 O O   . ARG F  1 393 ? 135.734 73.441  -0.862  1.00   29.63  ? 393 ARG F O   1 
ATOM   17886 C CB  . ARG F  1 393 ? 136.656 73.374  -4.059  1.00   25.30  ? 393 ARG F CB  1 
ATOM   17887 C CG  . ARG F  1 393 ? 136.585 74.869  -3.793  1.00   27.98  ? 393 ARG F CG  1 
ATOM   17888 C CD  . ARG F  1 393 ? 137.212 75.679  -4.911  1.00   30.78  ? 393 ARG F CD  1 
ATOM   17889 N NE  . ARG F  1 393 ? 137.295 77.075  -4.510  1.00   33.51  ? 393 ARG F NE  1 
ATOM   17890 C CZ  . ARG F  1 393 ? 138.081 77.987  -5.070  1.00   33.95  ? 393 ARG F CZ  1 
ATOM   17891 N NH1 . ARG F  1 393 ? 138.864 77.677  -6.091  1.00   36.67  ? 393 ARG F NH1 1 
ATOM   17892 N NH2 . ARG F  1 393 ? 138.081 79.221  -4.596  1.00   33.23  ? 393 ARG F NH2 1 
ATOM   17893 N N   . VAL F  1 394 ? 137.536 72.166  -1.330  1.00   29.24  ? 394 VAL F N   1 
ATOM   17894 C CA  . VAL F  1 394 ? 138.233 72.434  -0.077  1.00   31.29  ? 394 VAL F CA  1 
ATOM   17895 C C   . VAL F  1 394 ? 139.618 73.100  -0.294  1.00   28.24  ? 394 VAL F C   1 
ATOM   17896 O O   . VAL F  1 394 ? 140.399 72.676  -1.147  1.00   31.12  ? 394 VAL F O   1 
ATOM   17897 C CB  . VAL F  1 394 ? 138.419 71.147  0.734   1.00   32.54  ? 394 VAL F CB  1 
ATOM   17898 C CG1 . VAL F  1 394 ? 139.152 71.462  2.020   1.00   35.22  ? 394 VAL F CG1 1 
ATOM   17899 C CG2 . VAL F  1 394 ? 137.086 70.559  1.075   1.00   31.37  ? 394 VAL F CG2 1 
ATOM   17900 N N   . GLY F  1 395 ? 139.901 74.145  0.481   1.00   26.90  ? 395 GLY F N   1 
ATOM   17901 C CA  . GLY F  1 395 ? 141.181 74.815  0.453   1.00   24.76  ? 395 GLY F CA  1 
ATOM   17902 C C   . GLY F  1 395 ? 141.915 74.670  1.773   1.00   26.46  ? 395 GLY F C   1 
ATOM   17903 O O   . GLY F  1 395 ? 141.293 74.532  2.820   1.00   29.21  ? 395 GLY F O   1 
ATOM   17904 N N   . PHE F  1 396 ? 143.242 74.683  1.732   1.00   27.01  ? 396 PHE F N   1 
ATOM   17905 C CA  . PHE F  1 396 ? 144.025 74.562  2.952   1.00   27.41  ? 396 PHE F CA  1 
ATOM   17906 C C   . PHE F  1 396 ? 145.321 75.304  2.779   1.00   32.02  ? 396 PHE F C   1 
ATOM   17907 O O   . PHE F  1 396 ? 145.723 75.573  1.656   1.00   36.16  ? 396 PHE F O   1 
ATOM   17908 C CB  . PHE F  1 396 ? 144.276 73.092  3.295   1.00   27.58  ? 396 PHE F CB  1 
ATOM   17909 C CG  . PHE F  1 396 ? 144.858 72.299  2.161   1.00   33.35  ? 396 PHE F CG  1 
ATOM   17910 C CD1 . PHE F  1 396 ? 146.230 72.242  1.958   1.00   38.45  ? 396 PHE F CD1 1 
ATOM   17911 C CD2 . PHE F  1 396 ? 144.036 71.629  1.278   1.00   33.01  ? 396 PHE F CD2 1 
ATOM   17912 C CE1 . PHE F  1 396 ? 146.753 71.528  0.911   1.00   38.42  ? 396 PHE F CE1 1 
ATOM   17913 C CE2 . PHE F  1 396 ? 144.560 70.913  0.238   1.00   32.51  ? 396 PHE F CE2 1 
ATOM   17914 C CZ  . PHE F  1 396 ? 145.917 70.867  0.051   1.00   36.03  ? 396 PHE F CZ  1 
ATOM   17915 N N   . ASN F  1 397 ? 145.977 75.651  3.880   1.00   32.84  ? 397 ASN F N   1 
ATOM   17916 C CA  . ASN F  1 397 ? 147.253 76.355  3.777   1.00   35.46  ? 397 ASN F CA  1 
ATOM   17917 C C   . ASN F  1 397 ? 148.318 75.462  3.166   1.00   36.75  ? 397 ASN F C   1 
ATOM   17918 O O   . ASN F  1 397 ? 148.496 74.330  3.592   1.00   36.48  ? 397 ASN F O   1 
ATOM   17919 C CB  . ASN F  1 397 ? 147.694 76.889  5.154   1.00   36.72  ? 397 ASN F CB  1 
ATOM   17920 C CG  . ASN F  1 397 ? 147.494 75.881  6.270   1.00   38.57  ? 397 ASN F CG  1 
ATOM   17921 O OD1 . ASN F  1 397 ? 146.363 75.541  6.614   1.00   39.11  ? 397 ASN F OD1 1 
ATOM   17922 N ND2 . ASN F  1 397 ? 148.580 75.381  6.818   1.00   40.42  ? 397 ASN F ND2 1 
ATOM   17923 N N   . SER F  1 398 ? 149.024 75.977  2.163   1.00   43.26  ? 398 SER F N   1 
ATOM   17924 C CA  . SER F  1 398 ? 150.033 75.189  1.460   1.00   48.35  ? 398 SER F CA  1 
ATOM   17925 C C   . SER F  1 398 ? 151.398 75.237  2.158   1.00   49.00  ? 398 SER F C   1 
ATOM   17926 O O   . SER F  1 398 ? 152.278 74.448  1.831   1.00   52.82  ? 398 SER F O   1 
ATOM   17927 C CB  . SER F  1 398 ? 150.167 75.654  0.008   1.00   52.18  ? 398 SER F CB  1 
ATOM   17928 O OG  . SER F  1 398 ? 150.505 77.027  -0.068  1.00   54.61  ? 398 SER F OG  1 
ATOM   17929 N N   . ASN F  1 399 ? 151.558 76.154  3.112   1.00   46.88  ? 399 ASN F N   1 
ATOM   17930 C CA  . ASN F  1 399 ? 152.694 76.169  4.045   1.00   50.13  ? 399 ASN F CA  1 
ATOM   17931 C C   . ASN F  1 399 ? 152.135 76.184  5.461   1.00   46.45  ? 399 ASN F C   1 
ATOM   17932 O O   . ASN F  1 399 ? 150.978 76.493  5.638   1.00   45.41  ? 399 ASN F O   1 
ATOM   17933 C CB  . ASN F  1 399 ? 153.636 77.370  3.838   1.00   53.45  ? 399 ASN F CB  1 
ATOM   17934 C CG  . ASN F  1 399 ? 154.294 77.386  2.469   1.00   58.23  ? 399 ASN F CG  1 
ATOM   17935 O OD1 . ASN F  1 399 ? 155.199 76.603  2.197   1.00   64.57  ? 399 ASN F OD1 1 
ATOM   17936 N ND2 . ASN F  1 399 ? 153.873 78.306  1.620   1.00   57.76  ? 399 ASN F ND2 1 
ATOM   17937 N N   . SER F  1 400 ? 152.934 75.816  6.461   1.00   49.58  ? 400 SER F N   1 
ATOM   17938 C CA  . SER F  1 400 ? 152.468 75.774  7.852   1.00   49.03  ? 400 SER F CA  1 
ATOM   17939 C C   . SER F  1 400 ? 152.119 77.150  8.404   1.00   48.00  ? 400 SER F C   1 
ATOM   17940 O O   . SER F  1 400 ? 152.671 78.157  7.998   1.00   51.74  ? 400 SER F O   1 
ATOM   17941 C CB  . SER F  1 400 ? 153.503 75.098  8.758   1.00   54.99  ? 400 SER F CB  1 
ATOM   17942 O OG  . SER F  1 400 ? 154.637 75.918  8.979   1.00   60.00  ? 400 SER F OG  1 
ATOM   17943 N N   . LEU F  1 401 ? 151.171 77.187  9.317   1.00   44.02  ? 401 LEU F N   1 
ATOM   17944 C CA  . LEU F  1 401 ? 150.814 78.426  9.954   1.00   43.36  ? 401 LEU F CA  1 
ATOM   17945 C C   . LEU F  1 401 ? 152.007 78.999  10.698  1.00   48.18  ? 401 LEU F C   1 
ATOM   17946 O O   . LEU F  1 401 ? 152.231 80.205  10.738  1.00   50.28  ? 401 LEU F O   1 
ATOM   17947 C CB  . LEU F  1 401 ? 149.645 78.198  10.887  1.00   40.84  ? 401 LEU F CB  1 
ATOM   17948 C CG  . LEU F  1 401 ? 148.347 77.789  10.183  1.00   37.37  ? 401 LEU F CG  1 
ATOM   17949 C CD1 . LEU F  1 401 ? 147.180 77.872  11.138  1.00   35.27  ? 401 LEU F CD1 1 
ATOM   17950 C CD2 . LEU F  1 401 ? 148.085 78.626  8.966   1.00   34.70  ? 401 LEU F CD2 1 
ATOM   17951 N N   . LYS F  1 402 ? 152.784 78.113  11.288  1.00   51.41  ? 402 LYS F N   1 
ATOM   17952 C CA  . LYS F  1 402 ? 153.927 78.536  12.083  1.00   53.91  ? 402 LYS F CA  1 
ATOM   17953 C C   . LYS F  1 402 ? 154.948 79.249  11.198  1.00   54.46  ? 402 LYS F C   1 
ATOM   17954 O O   . LYS F  1 402 ? 155.574 80.209  11.631  1.00   56.07  ? 402 LYS F O   1 
ATOM   17955 C CB  . LYS F  1 402 ? 154.539 77.313  12.772  1.00   57.32  ? 402 LYS F CB  1 
ATOM   17956 C CG  . LYS F  1 402 ? 155.871 77.473  13.456  1.00   61.77  ? 402 LYS F CG  1 
ATOM   17957 C CD  . LYS F  1 402 ? 156.341 76.081  13.961  1.00   84.06  ? 402 LYS F CD  1 
ATOM   17958 C CE  . LYS F  1 402 ? 157.344 76.120  15.137  1.00   88.82  ? 402 LYS F CE  1 
ATOM   17959 N NZ  . LYS F  1 402 ? 156.798 75.614  16.441  1.00   88.49  ? 402 LYS F NZ  1 
ATOM   17960 N N   . SER F  1 403 ? 155.045 78.843  9.934   1.00   52.65  ? 403 SER F N   1 
ATOM   17961 C CA  . SER F  1 403 ? 155.971 79.481  9.006   1.00   52.67  ? 403 SER F CA  1 
ATOM   17962 C C   . SER F  1 403 ? 155.530 80.876  8.663   1.00   50.79  ? 403 SER F C   1 
ATOM   17963 O O   . SER F  1 403 ? 156.294 81.648  8.098   1.00   55.08  ? 403 SER F O   1 
ATOM   17964 C CB  . SER F  1 403 ? 156.103 78.694  7.714   1.00   54.08  ? 403 SER F CB  1 
ATOM   17965 O OG  . SER F  1 403 ? 155.109 79.090  6.795   1.00   50.57  ? 403 SER F OG  1 
ATOM   17966 N N   . TYR F  1 404 ? 154.280 81.187  8.963   1.00   52.80  ? 404 TYR F N   1 
ATOM   17967 C CA  . TYR F  1 404 ? 153.804 82.546  8.800   1.00   49.03  ? 404 TYR F CA  1 
ATOM   17968 C C   . TYR F  1 404 ? 153.913 83.271  10.123  1.00   51.06  ? 404 TYR F C   1 
ATOM   17969 O O   . TYR F  1 404 ? 153.574 84.453  10.230  1.00   52.27  ? 404 TYR F O   1 
ATOM   17970 C CB  . TYR F  1 404 ? 152.375 82.574  8.307   1.00   43.06  ? 404 TYR F CB  1 
ATOM   17971 C CG  . TYR F  1 404 ? 152.170 81.964  6.944   1.00   40.89  ? 404 TYR F CG  1 
ATOM   17972 C CD1 . TYR F  1 404 ? 152.423 82.705  5.799   1.00   43.41  ? 404 TYR F CD1 1 
ATOM   17973 C CD2 . TYR F  1 404 ? 151.659 80.676  6.795   1.00   38.94  ? 404 TYR F CD2 1 
ATOM   17974 C CE1 . TYR F  1 404 ? 152.220 82.162  4.539   1.00   45.46  ? 404 TYR F CE1 1 
ATOM   17975 C CE2 . TYR F  1 404 ? 151.443 80.125  5.535   1.00   39.00  ? 404 TYR F CE2 1 
ATOM   17976 C CZ  . TYR F  1 404 ? 151.730 80.875  4.413   1.00   44.83  ? 404 TYR F CZ  1 
ATOM   17977 O OH  . TYR F  1 404 ? 151.531 80.370  3.152   1.00   45.57  ? 404 TYR F OH  1 
ATOM   17978 N N   . GLY F  1 405 ? 154.387 82.551  11.134  1.00   50.69  ? 405 GLY F N   1 
ATOM   17979 C CA  . GLY F  1 405 ? 154.437 83.084  12.477  1.00   51.12  ? 405 GLY F CA  1 
ATOM   17980 C C   . GLY F  1 405 ? 153.066 83.049  13.122  1.00   49.09  ? 405 GLY F C   1 
ATOM   17981 O O   . GLY F  1 405 ? 152.788 83.797  14.055  1.00   48.13  ? 405 GLY F O   1 
ATOM   17982 N N   . LYS F  1 406 ? 152.197 82.186  12.612  1.00   46.90  ? 406 LYS F N   1 
ATOM   17983 C CA  . LYS F  1 406 ? 150.826 82.151  13.087  1.00   45.05  ? 406 LYS F CA  1 
ATOM   17984 C C   . LYS F  1 406 ? 150.475 80.829  13.750  1.00   46.45  ? 406 LYS F C   1 
ATOM   17985 O O   . LYS F  1 406 ? 151.180 79.816  13.579  1.00   47.20  ? 406 LYS F O   1 
ATOM   17986 C CB  . LYS F  1 406 ? 149.847 82.400  11.934  1.00   43.44  ? 406 LYS F CB  1 
ATOM   17987 C CG  . LYS F  1 406 ? 150.123 83.635  11.082  1.00   46.11  ? 406 LYS F CG  1 
ATOM   17988 C CD  . LYS F  1 406 ? 149.780 84.925  11.799  1.00   48.61  ? 406 LYS F CD  1 
ATOM   17989 C CE  . LYS F  1 406 ? 150.318 86.120  11.034  1.00   52.28  ? 406 LYS F CE  1 
ATOM   17990 N NZ  . LYS F  1 406 ? 150.091 85.973  9.569   1.00   52.58  ? 406 LYS F NZ  1 
ATOM   17991 N N   . THR F  1 407 ? 149.379 80.870  14.512  1.00   44.74  ? 407 THR F N   1 
ATOM   17992 C CA  . THR F  1 407 ? 148.713 79.674  15.042  1.00   43.64  ? 407 THR F CA  1 
ATOM   17993 C C   . THR F  1 407 ? 147.212 79.797  14.778  1.00   39.52  ? 407 THR F C   1 
ATOM   17994 O O   . THR F  1 407 ? 146.728 80.857  14.359  1.00   39.80  ? 407 THR F O   1 
ATOM   17995 C CB  . THR F  1 407 ? 148.937 79.457  16.559  1.00   46.02  ? 407 THR F CB  1 
ATOM   17996 O OG1 . THR F  1 407 ? 148.182 80.405  17.313  1.00   45.07  ? 407 THR F OG1 1 
ATOM   17997 C CG2 . THR F  1 407 ? 150.393 79.573  16.921  1.00   49.97  ? 407 THR F CG2 1 
ATOM   17998 N N   . CYS F  1 408 ? 146.473 78.717  15.004  1.00   35.72  ? 408 CYS F N   1 
ATOM   17999 C CA  . CYS F  1 408 ? 145.028 78.751  14.837  1.00   32.44  ? 408 CYS F CA  1 
ATOM   18000 C C   . CYS F  1 408 ? 144.386 79.609  15.906  1.00   34.87  ? 408 CYS F C   1 
ATOM   18001 O O   . CYS F  1 408 ? 143.212 79.956  15.797  1.00   34.47  ? 408 CYS F O   1 
ATOM   18002 C CB  . CYS F  1 408 ? 144.430 77.342  14.836  1.00   32.31  ? 408 CYS F CB  1 
ATOM   18003 S SG  . CYS F  1 408 ? 144.322 76.655  13.165  1.00   35.66  ? 408 CYS F SG  1 
ATOM   18004 N N   . SER F  1 409 ? 145.136 79.904  16.965  1.00   37.16  ? 409 SER F N   1 
ATOM   18005 C CA  . SER F  1 409 ? 144.663 80.789  18.026  1.00   38.83  ? 409 SER F CA  1 
ATOM   18006 C C   . SER F  1 409 ? 144.808 82.294  17.703  1.00   37.21  ? 409 SER F C   1 
ATOM   18007 O O   . SER F  1 409 ? 144.061 83.128  18.220  1.00   37.71  ? 409 SER F O   1 
ATOM   18008 C CB  . SER F  1 409 ? 145.396 80.468  19.318  1.00   42.89  ? 409 SER F CB  1 
ATOM   18009 O OG  . SER F  1 409 ? 145.149 79.119  19.661  1.00   46.20  ? 409 SER F OG  1 
ATOM   18010 N N   . ASN F  1 410 ? 145.805 82.659  16.909  1.00   36.06  ? 410 ASN F N   1 
ATOM   18011 C CA  . ASN F  1 410 ? 145.997 84.075  16.625  1.00   36.95  ? 410 ASN F CA  1 
ATOM   18012 C C   . ASN F  1 410 ? 145.873 84.447  15.157  1.00   36.02  ? 410 ASN F C   1 
ATOM   18013 O O   . ASN F  1 410 ? 146.191 85.566  14.780  1.00   39.44  ? 410 ASN F O   1 
ATOM   18014 C CB  . ASN F  1 410 ? 147.335 84.586  17.202  1.00   40.94  ? 410 ASN F CB  1 
ATOM   18015 C CG  . ASN F  1 410 ? 148.565 83.953  16.575  1.00   44.26  ? 410 ASN F CG  1 
ATOM   18016 O OD1 . ASN F  1 410 ? 148.598 83.620  15.392  1.00   44.37  ? 410 ASN F OD1 1 
ATOM   18017 N ND2 . ASN F  1 410 ? 149.615 83.830  17.380  1.00   46.53  ? 410 ASN F ND2 1 
ATOM   18018 N N   . LEU F  1 411 ? 145.446 83.513  14.320  1.00   32.90  ? 411 LEU F N   1 
ATOM   18019 C CA  . LEU F  1 411 ? 145.190 83.848  12.932  1.00   31.40  ? 411 LEU F CA  1 
ATOM   18020 C C   . LEU F  1 411 ? 144.092 84.905  12.870  1.00   33.03  ? 411 LEU F C   1 
ATOM   18021 O O   . LEU F  1 411 ? 144.111 85.812  12.042  1.00   34.58  ? 411 LEU F O   1 
ATOM   18022 C CB  . LEU F  1 411 ? 144.786 82.606  12.151  1.00   31.34  ? 411 LEU F CB  1 
ATOM   18023 C CG  . LEU F  1 411 ? 144.711 82.779  10.635  1.00   32.86  ? 411 LEU F CG  1 
ATOM   18024 C CD1 . LEU F  1 411 ? 146.054 83.211  10.018  1.00   34.13  ? 411 LEU F CD1 1 
ATOM   18025 C CD2 . LEU F  1 411 ? 144.241 81.491  10.035  1.00   31.80  ? 411 LEU F CD2 1 
ATOM   18026 N N   . PHE F  1 412 ? 143.123 84.753  13.759  1.00   31.10  ? 412 PHE F N   1 
ATOM   18027 C CA  . PHE F  1 412 ? 142.040 85.700  13.913  1.00   30.45  ? 412 PHE F CA  1 
ATOM   18028 C C   . PHE F  1 412 ? 141.964 86.136  15.360  1.00   32.53  ? 412 PHE F C   1 
ATOM   18029 O O   . PHE F  1 412 ? 142.459 85.439  16.242  1.00   34.33  ? 412 PHE F O   1 
ATOM   18030 C CB  . PHE F  1 412 ? 140.726 85.092  13.444  1.00   31.42  ? 412 PHE F CB  1 
ATOM   18031 C CG  . PHE F  1 412 ? 140.785 84.544  12.048  1.00   32.83  ? 412 PHE F CG  1 
ATOM   18032 C CD1 . PHE F  1 412 ? 140.719 85.401  10.955  1.00   35.46  ? 412 PHE F CD1 1 
ATOM   18033 C CD2 . PHE F  1 412 ? 140.911 83.180  11.826  1.00   34.89  ? 412 PHE F CD2 1 
ATOM   18034 C CE1 . PHE F  1 412 ? 140.789 84.917  9.670   1.00   35.26  ? 412 PHE F CE1 1 
ATOM   18035 C CE2 . PHE F  1 412 ? 140.978 82.678  10.535  1.00   34.08  ? 412 PHE F CE2 1 
ATOM   18036 C CZ  . PHE F  1 412 ? 140.924 83.558  9.454   1.00   33.92  ? 412 PHE F CZ  1 
ATOM   18037 N N   . ASP F  1 413 ? 141.376 87.308  15.593  1.00   36.43  ? 413 ASP F N   1 
ATOM   18038 C CA  . ASP F  1 413 ? 141.219 87.850  16.938  1.00   40.25  ? 413 ASP F CA  1 
ATOM   18039 C C   . ASP F  1 413 ? 140.078 87.148  17.625  1.00   42.70  ? 413 ASP F C   1 
ATOM   18040 O O   . ASP F  1 413 ? 138.922 87.350  17.237  1.00   41.41  ? 413 ASP F O   1 
ATOM   18041 C CB  . ASP F  1 413 ? 140.937 89.349  16.903  1.00   40.41  ? 413 ASP F CB  1 
ATOM   18042 C CG  . ASP F  1 413 ? 141.156 90.007  18.243  1.00   44.25  ? 413 ASP F CG  1 
ATOM   18043 O OD1 . ASP F  1 413 ? 140.966 89.362  19.288  1.00   44.99  ? 413 ASP F OD1 1 
ATOM   18044 O OD2 . ASP F  1 413 ? 141.532 91.193  18.255  1.00   48.69  1 413 ASP F OD2 1 
ATOM   18045 N N   . LEU F  1 414 ? 140.391 86.347  18.646  1.00   42.22  ? 414 LEU F N   1 
ATOM   18046 C CA  . LEU F  1 414 ? 139.363 85.565  19.334  1.00   41.61  ? 414 LEU F CA  1 
ATOM   18047 C C   . LEU F  1 414 ? 139.086 86.017  20.760  1.00   45.98  ? 414 LEU F C   1 
ATOM   18048 O O   . LEU F  1 414 ? 138.495 85.280  21.535  1.00   48.85  ? 414 LEU F O   1 
ATOM   18049 C CB  . LEU F  1 414 ? 139.760 84.093  19.334  1.00   39.97  ? 414 LEU F CB  1 
ATOM   18050 C CG  . LEU F  1 414 ? 139.979 83.452  17.962  1.00   36.97  ? 414 LEU F CG  1 
ATOM   18051 C CD1 . LEU F  1 414 ? 140.411 82.001  18.116  1.00   36.51  ? 414 LEU F CD1 1 
ATOM   18052 C CD2 . LEU F  1 414 ? 138.715 83.526  17.149  1.00   36.39  ? 414 LEU F CD2 1 
ATOM   18053 N N   . ASN F  1 415 ? 139.503 87.233  21.090  1.00   48.54  ? 415 ASN F N   1 
ATOM   18054 C CA  . ASN F  1 415 ? 139.292 87.846  22.404  1.00   54.96  ? 415 ASN F CA  1 
ATOM   18055 C C   . ASN F  1 415 ? 137.887 88.419  22.540  1.00   60.27  ? 415 ASN F C   1 
ATOM   18056 O O   . ASN F  1 415 ? 137.356 88.984  21.597  1.00   60.11  ? 415 ASN F O   1 
ATOM   18057 C CB  . ASN F  1 415 ? 140.337 88.928  22.628  1.00   58.51  ? 415 ASN F CB  1 
ATOM   18058 C CG  . ASN F  1 415 ? 141.757 88.397  22.489  1.00   58.97  ? 415 ASN F CG  1 
ATOM   18059 O OD1 . ASN F  1 415 ? 142.105 87.375  23.075  1.00   62.03  ? 415 ASN F OD1 1 
ATOM   18060 N ND2 . ASN F  1 415 ? 142.574 89.080  21.692  1.00   55.02  ? 415 ASN F ND2 1 
ATOM   18061 N N   . ASN F  1 416 ? 137.280 88.247  23.706  1.00   67.35  ? 416 ASN F N   1 
ATOM   18062 C CA  . ASN F  1 416 ? 135.915 88.717  23.948  1.00   74.95  ? 416 ASN F CA  1 
ATOM   18063 C C   . ASN F  1 416 ? 135.588 90.140  23.492  1.00   78.78  ? 416 ASN F C   1 
ATOM   18064 O O   . ASN F  1 416 ? 134.487 90.397  22.984  1.00   78.81  ? 416 ASN F O   1 
ATOM   18065 C CB  . ASN F  1 416 ? 135.621 88.620  25.436  1.00   80.95  ? 416 ASN F CB  1 
ATOM   18066 C CG  . ASN F  1 416 ? 135.618 87.211  25.910  1.00   78.70  ? 416 ASN F CG  1 
ATOM   18067 O OD1 . ASN F  1 416 ? 135.472 86.299  25.104  1.00   75.89  ? 416 ASN F OD1 1 
ATOM   18068 N ND2 . ASN F  1 416 ? 135.767 87.009  27.220  1.00   80.54  ? 416 ASN F ND2 1 
HETATM 18069 C C1  . NAG G  2 .   ? 128.187 59.349  -22.022 1.00   57.42  ? 501 NAG A C1  1 
HETATM 18070 C C2  . NAG G  2 .   ? 128.773 59.726  -23.387 1.00   65.41  ? 501 NAG A C2  1 
HETATM 18071 C C3  . NAG G  2 .   ? 128.499 58.609  -24.409 1.00   70.65  ? 501 NAG A C3  1 
HETATM 18072 C C4  . NAG G  2 .   ? 128.977 57.258  -23.895 1.00   74.34  ? 501 NAG A C4  1 
HETATM 18073 C C5  . NAG G  2 .   ? 128.350 56.948  -22.532 1.00   69.98  ? 501 NAG A C5  1 
HETATM 18074 C C6  . NAG G  2 .   ? 128.887 55.681  -21.910 1.00   70.70  ? 501 NAG A C6  1 
HETATM 18075 C C7  . NAG G  2 .   ? 128.958 62.128  -23.888 1.00   65.24  ? 501 NAG A C7  1 
HETATM 18076 C C8  . NAG G  2 .   ? 130.382 62.030  -23.421 1.00   67.10  ? 501 NAG A C8  1 
HETATM 18077 N N2  . NAG G  2 .   ? 128.248 60.993  -23.856 1.00   64.78  ? 501 NAG A N2  1 
HETATM 18078 O O3  . NAG G  2 .   ? 129.127 58.918  -25.653 1.00   72.15  ? 501 NAG A O3  1 
HETATM 18079 O O4  . NAG G  2 .   ? 128.697 56.225  -24.842 1.00   80.76  ? 501 NAG A O4  1 
HETATM 18080 O O5  . NAG G  2 .   ? 128.670 58.010  -21.614 1.00   64.65  ? 501 NAG A O5  1 
HETATM 18081 O O6  . NAG G  2 .   ? 130.285 55.802  -21.674 1.00   72.31  ? 501 NAG A O6  1 
HETATM 18082 O O7  . NAG G  2 .   ? 128.478 63.180  -24.289 1.00   65.25  ? 501 NAG A O7  1 
HETATM 18083 C C1  . NAG H  2 .   ? 129.688 55.349  -25.499 1.00   86.12  ? 502 NAG A C1  1 
HETATM 18084 C C2  . NAG H  2 .   ? 129.102 53.962  -25.754 1.00   91.03  ? 502 NAG A C2  1 
HETATM 18085 C C3  . NAG H  2 .   ? 130.217 52.979  -26.139 1.00   93.17  ? 502 NAG A C3  1 
HETATM 18086 C C4  . NAG H  2 .   ? 131.016 53.511  -27.317 1.00   93.65  ? 502 NAG A C4  1 
HETATM 18087 C C5  . NAG H  2 .   ? 131.551 54.911  -26.988 1.00   90.49  ? 502 NAG A C5  1 
HETATM 18088 C C6  . NAG H  2 .   ? 132.274 55.574  -28.133 1.00   91.15  ? 502 NAG A C6  1 
HETATM 18089 C C7  . NAG H  2 .   ? 127.046 53.242  -24.617 1.00   93.24  ? 502 NAG A C7  1 
HETATM 18090 C C8  . NAG H  2 .   ? 126.450 52.790  -23.318 1.00   92.47  ? 502 NAG A C8  1 
HETATM 18091 N N2  . NAG H  2 .   ? 128.363 53.490  -24.600 1.00   93.01  ? 502 NAG A N2  1 
HETATM 18092 O O3  . NAG H  2 .   ? 129.677 51.691  -26.439 1.00   93.28  ? 502 NAG A O3  1 
HETATM 18093 O O4  . NAG H  2 .   ? 132.078 52.610  -27.647 1.00   94.74  ? 502 NAG A O4  1 
HETATM 18094 O O5  . NAG H  2 .   ? 130.456 55.780  -26.658 1.00   86.97  ? 502 NAG A O5  1 
HETATM 18095 O O6  . NAG H  2 .   ? 131.835 55.036  -29.374 1.00   91.65  ? 502 NAG A O6  1 
HETATM 18096 O O7  . NAG H  2 .   ? 126.383 53.341  -25.645 1.00   93.46  ? 502 NAG A O7  1 
HETATM 18097 C C1  . FUC I  3 .   ? 128.225 59.464  -26.690 1.00   72.05  ? 503 FUC A C1  1 
HETATM 18098 C C2  . FUC I  3 .   ? 129.339 59.897  -27.685 1.00   82.81  ? 503 FUC A C2  1 
HETATM 18099 C C3  . FUC I  3 .   ? 129.924 58.671  -28.419 1.00   81.53  ? 503 FUC A C3  1 
HETATM 18100 C C4  . FUC I  3 .   ? 128.785 57.820  -29.046 1.00   66.68  ? 503 FUC A C4  1 
HETATM 18101 C C5  . FUC I  3 .   ? 127.785 57.424  -27.888 1.00   71.03  ? 503 FUC A C5  1 
HETATM 18102 C C6  . FUC I  3 .   ? 126.625 56.539  -28.286 1.00   70.71  ? 503 FUC A C6  1 
HETATM 18103 O O2  . FUC I  3 .   ? 130.368 60.640  -27.077 1.00   83.23  ? 503 FUC A O2  1 
HETATM 18104 O O3  . FUC I  3 .   ? 130.828 59.077  -29.424 1.00   80.16  ? 503 FUC A O3  1 
HETATM 18105 O O4  . FUC I  3 .   ? 128.107 58.523  -30.098 1.00   64.39  ? 503 FUC A O4  1 
HETATM 18106 O O5  . FUC I  3 .   ? 127.242 58.598  -27.246 1.00   70.51  ? 503 FUC A O5  1 
HETATM 18107 C C1  . EDO J  4 .   ? 110.362 77.595  8.125   1.00   36.85  ? 504 EDO A C1  1 
HETATM 18108 O O1  . EDO J  4 .   ? 111.009 77.304  6.875   1.00   39.96  ? 504 EDO A O1  1 
HETATM 18109 C C2  . EDO J  4 .   ? 110.972 76.794  9.272   1.00   34.41  ? 504 EDO A C2  1 
HETATM 18110 O O2  . EDO J  4 .   ? 112.325 77.216  9.537   1.00   33.63  ? 504 EDO A O2  1 
HETATM 18111 C C1  . EDO K  4 .   ? 87.543  91.894  11.539  1.00   50.87  ? 505 EDO A C1  1 
HETATM 18112 O O1  . EDO K  4 .   ? 87.726  92.025  10.122  1.00   47.39  ? 505 EDO A O1  1 
HETATM 18113 C C2  . EDO K  4 .   ? 88.867  91.585  12.250  1.00   52.55  ? 505 EDO A C2  1 
HETATM 18114 O O2  . EDO K  4 .   ? 89.528  90.425  11.714  1.00   52.56  ? 505 EDO A O2  1 
HETATM 18115 C C1  . EDO L  4 .   ? 83.384  92.441  4.551   1.00   37.95  ? 506 EDO A C1  1 
HETATM 18116 O O1  . EDO L  4 .   ? 83.444  93.686  5.243   1.00   37.41  ? 506 EDO A O1  1 
HETATM 18117 C C2  . EDO L  4 .   ? 84.029  92.456  3.189   1.00   40.42  ? 506 EDO A C2  1 
HETATM 18118 O O2  . EDO L  4 .   ? 83.758  91.215  2.538   1.00   40.93  ? 506 EDO A O2  1 
HETATM 18119 C C1  . EDO M  4 .   ? 104.126 87.998  -15.238 1.00   41.16  ? 507 EDO A C1  1 
HETATM 18120 O O1  . EDO M  4 .   ? 105.441 88.292  -14.761 1.00   41.76  ? 507 EDO A O1  1 
HETATM 18121 C C2  . EDO M  4 .   ? 103.942 88.613  -16.611 1.00   44.16  ? 507 EDO A C2  1 
HETATM 18122 O O2  . EDO M  4 .   ? 104.762 89.785  -16.667 1.00   47.47  ? 507 EDO A O2  1 
HETATM 18123 C C1  . EDO N  4 .   ? 103.881 68.551  -5.155  1.00   55.53  ? 508 EDO A C1  1 
HETATM 18124 O O1  . EDO N  4 .   ? 104.943 68.804  -4.227  1.00   51.97  ? 508 EDO A O1  1 
HETATM 18125 C C2  . EDO N  4 .   ? 104.480 67.886  -6.376  1.00   56.28  ? 508 EDO A C2  1 
HETATM 18126 O O2  . EDO N  4 .   ? 105.445 66.944  -5.901  1.00   56.00  ? 508 EDO A O2  1 
HETATM 18127 C C1  . EDO O  4 .   ? 108.183 68.047  -8.253  1.00   41.09  ? 509 EDO A C1  1 
HETATM 18128 O O1  . EDO O  4 .   ? 107.089 68.975  -8.131  1.00   41.33  ? 509 EDO A O1  1 
HETATM 18129 C C2  . EDO O  4 .   ? 108.737 68.038  -9.673  1.00   40.78  ? 509 EDO A C2  1 
HETATM 18130 O O2  . EDO O  4 .   ? 108.655 69.337  -10.285 1.00   41.33  ? 509 EDO A O2  1 
HETATM 18131 C C1  . NAG P  2 .   ? 99.551  19.016  24.603  1.00   61.28  ? 501 NAG B C1  1 
HETATM 18132 C C2  . NAG P  2 .   ? 99.580  18.299  25.961  1.00   68.76  ? 501 NAG B C2  1 
HETATM 18133 C C3  . NAG P  2 .   ? 100.976 18.390  26.607  1.00   72.75  ? 501 NAG B C3  1 
HETATM 18134 C C4  . NAG P  2 .   ? 102.068 17.973  25.623  1.00   72.24  ? 501 NAG B C4  1 
HETATM 18135 C C5  . NAG P  2 .   ? 101.918 18.741  24.313  1.00   69.92  ? 501 NAG B C5  1 
HETATM 18136 C C6  . NAG P  2 .   ? 102.891 18.284  23.255  1.00   69.08  ? 501 NAG B C6  1 
HETATM 18137 C C7  . NAG P  2 .   ? 97.761  18.120  27.595  1.00   70.11  ? 501 NAG B C7  1 
HETATM 18138 C C8  . NAG P  2 .   ? 96.770  18.868  28.442  1.00   68.80  ? 501 NAG B C8  1 
HETATM 18139 N N2  . NAG P  2 .   ? 98.567  18.871  26.846  1.00   69.29  ? 501 NAG B N2  1 
HETATM 18140 O O3  . NAG P  2 .   ? 101.055 17.567  27.769  1.00   74.48  ? 501 NAG B O3  1 
HETATM 18141 O O4  . NAG P  2 .   ? 103.358 18.220  26.173  1.00   74.03  ? 501 NAG B O4  1 
HETATM 18142 O O5  . NAG P  2 .   ? 100.607 18.513  23.779  1.00   67.31  ? 501 NAG B O5  1 
HETATM 18143 O O6  . NAG P  2 .   ? 102.715 16.901  22.981  1.00   67.64  ? 501 NAG B O6  1 
HETATM 18144 O O7  . NAG P  2 .   ? 97.823  16.890  27.592  1.00   72.58  ? 501 NAG B O7  1 
HETATM 18145 C C1  . EDO Q  4 .   ? 68.222  36.985  8.448   1.00   53.73  ? 502 EDO B C1  1 
HETATM 18146 O O1  . EDO Q  4 .   ? 68.775  35.990  9.324   1.00   55.03  ? 502 EDO B O1  1 
HETATM 18147 C C2  . EDO Q  4 .   ? 67.296  36.357  7.420   1.00   52.37  ? 502 EDO B C2  1 
HETATM 18148 O O2  . EDO Q  4 .   ? 67.953  35.229  6.852   1.00   52.27  ? 502 EDO B O2  1 
HETATM 18149 C C1  . EDO R  4 .   ? 72.585  60.549  23.311  1.00   32.86  ? 503 EDO B C1  1 
HETATM 18150 O O1  . EDO R  4 .   ? 72.982  59.397  24.035  1.00   33.94  ? 503 EDO B O1  1 
HETATM 18151 C C2  . EDO R  4 .   ? 71.956  60.114  22.000  1.00   34.04  ? 503 EDO B C2  1 
HETATM 18152 O O2  . EDO R  4 .   ? 72.905  59.474  21.136  1.00   32.80  ? 503 EDO B O2  1 
HETATM 18153 C C1  . EDO S  4 .   ? 77.854  41.316  38.455  1.00   51.69  ? 504 EDO B C1  1 
HETATM 18154 O O1  . EDO S  4 .   ? 77.432  40.348  39.436  1.00   56.20  ? 504 EDO B O1  1 
HETATM 18155 C C2  . EDO S  4 .   ? 77.752  42.724  39.033  1.00   49.92  ? 504 EDO B C2  1 
HETATM 18156 O O2  . EDO S  4 .   ? 78.573  43.630  38.295  1.00   49.30  ? 504 EDO B O2  1 
HETATM 18157 C C1  . EDO T  4 .   ? 84.705  37.828  19.150  1.00   33.85  ? 505 EDO B C1  1 
HETATM 18158 O O1  . EDO T  4 .   ? 84.438  38.025  20.543  1.00   33.27  ? 505 EDO B O1  1 
HETATM 18159 C C2  . EDO T  4 .   ? 84.581  39.137  18.385  1.00   31.11  ? 505 EDO B C2  1 
HETATM 18160 O O2  . EDO T  4 .   ? 83.265  39.682  18.551  1.00   27.61  ? 505 EDO B O2  1 
HETATM 18161 C C1  . EDO U  4 .   ? 70.445  40.366  36.432  1.00   37.40  ? 506 EDO B C1  1 
HETATM 18162 O O1  . EDO U  4 .   ? 69.440  39.392  36.739  1.00   39.15  ? 506 EDO B O1  1 
HETATM 18163 C C2  . EDO U  4 .   ? 70.483  40.594  34.927  1.00   36.53  ? 506 EDO B C2  1 
HETATM 18164 O O2  . EDO U  4 .   ? 70.158  39.360  34.269  1.00   37.76  ? 506 EDO B O2  1 
HETATM 18165 C C1  . NAG V  2 .   ? 73.044  48.546  -13.591 1.00   69.13  ? 501 NAG C C1  1 
HETATM 18166 C C2  . NAG V  2 .   ? 72.092  48.654  -14.791 1.00   78.04  ? 501 NAG C C2  1 
HETATM 18167 C C3  . NAG V  2 .   ? 72.834  49.183  -16.034 1.00   82.17  ? 501 NAG C C3  1 
HETATM 18168 C C4  . NAG V  2 .   ? 73.629  50.444  -15.711 1.00   81.13  ? 501 NAG C C4  1 
HETATM 18169 C C5  . NAG V  2 .   ? 74.521  50.188  -14.501 1.00   78.66  ? 501 NAG C C5  1 
HETATM 18170 C C6  . NAG V  2 .   ? 75.293  51.410  -14.064 1.00   81.34  ? 501 NAG C C6  1 
HETATM 18171 C C7  . NAG V  2 .   ? 70.189  47.106  -14.856 1.00   76.76  ? 501 NAG C C7  1 
HETATM 18172 C C8  . NAG V  2 .   ? 69.722  45.726  -15.206 1.00   76.47  ? 501 NAG C C8  1 
HETATM 18173 N N2  . NAG V  2 .   ? 71.480  47.360  -15.073 1.00   76.76  ? 501 NAG C N2  1 
HETATM 18174 O O3  . NAG V  2 .   ? 71.921  49.428  -17.105 1.00   83.74  ? 501 NAG C O3  1 
HETATM 18175 O O4  . NAG V  2 .   ? 74.434  50.829  -16.822 1.00   82.22  ? 501 NAG C O4  1 
HETATM 18176 O O5  . NAG V  2 .   ? 73.705  49.791  -13.390 1.00   74.76  ? 501 NAG C O5  1 
HETATM 18177 O O6  . NAG V  2 .   ? 76.332  51.067  -13.155 1.00   83.53  ? 501 NAG C O6  1 
HETATM 18178 O O7  . NAG V  2 .   ? 69.426  47.951  -14.398 1.00   76.85  ? 501 NAG C O7  1 
HETATM 18179 C C1  . EDO W  4 .   ? 76.968  20.921  14.747  1.00   57.06  ? 502 EDO C C1  1 
HETATM 18180 O O1  . EDO W  4 .   ? 75.788  20.670  13.973  1.00   57.59  ? 502 EDO C O1  1 
HETATM 18181 C C2  . EDO W  4 .   ? 76.634  21.015  16.229  1.00   58.07  ? 502 EDO C C2  1 
HETATM 18182 O O2  . EDO W  4 .   ? 75.860  22.192  16.496  1.00   57.66  ? 502 EDO C O2  1 
HETATM 18183 C C1  . EDO X  4 .   ? 79.775  25.432  -3.887  1.00   27.52  ? 503 EDO C C1  1 
HETATM 18184 O O1  . EDO X  4 .   ? 79.131  24.253  -3.376  1.00   28.22  ? 503 EDO C O1  1 
HETATM 18185 C C2  . EDO X  4 .   ? 78.742  26.467  -4.294  1.00   30.31  ? 503 EDO C C2  1 
HETATM 18186 O O2  . EDO X  4 .   ? 77.798  25.930  -5.235  1.00   32.32  ? 503 EDO C O2  1 
HETATM 18187 C C1  . EDO Y  4 .   ? 89.560  8.449   15.064  1.00   54.50  ? 504 EDO C C1  1 
HETATM 18188 O O1  . EDO Y  4 .   ? 89.293  8.037   16.415  1.00   58.36  ? 504 EDO C O1  1 
HETATM 18189 C C2  . EDO Y  4 .   ? 88.794  7.544   14.107  1.00   51.04  ? 504 EDO C C2  1 
HETATM 18190 O O2  . EDO Y  4 .   ? 88.816  8.097   12.784  1.00   48.34  ? 504 EDO C O2  1 
HETATM 18191 C C1  . EDO Z  4 .   ? 61.562  12.005  -7.841  1.00   38.42  ? 505 EDO C C1  1 
HETATM 18192 O O1  . EDO Z  4 .   ? 60.288  12.596  -7.603  1.00   40.72  ? 505 EDO C O1  1 
HETATM 18193 C C2  . EDO Z  4 .   ? 62.598  12.923  -7.231  1.00   36.17  ? 505 EDO C C2  1 
HETATM 18194 O O2  . EDO Z  4 .   ? 61.946  13.705  -6.220  1.00   38.97  ? 505 EDO C O2  1 
HETATM 18195 C C1  . EDO AA 4 .   ? 59.349  17.235  -1.318  1.00   50.57  ? 506 EDO C C1  1 
HETATM 18196 O O1  . EDO AA 4 .   ? 59.402  16.700  0.023   1.00   44.68  ? 506 EDO C O1  1 
HETATM 18197 C C2  . EDO AA 4 .   ? 60.034  18.607  -1.390  1.00   55.00  ? 506 EDO C C2  1 
HETATM 18198 O O2  . EDO AA 4 .   ? 59.746  19.299  -2.609  1.00   56.01  ? 506 EDO C O2  1 
HETATM 18199 C C1  . NAG BA 2 .   ? 135.918 37.473  20.112  1.00   61.68  ? 501 NAG D C1  1 
HETATM 18200 C C2  . NAG BA 2 .   ? 136.678 37.708  21.421  1.00   66.84  ? 501 NAG D C2  1 
HETATM 18201 C C3  . NAG BA 2 .   ? 135.842 38.553  22.383  1.00   69.68  ? 501 NAG D C3  1 
HETATM 18202 C C4  . NAG BA 2 .   ? 135.438 39.854  21.712  1.00   71.68  ? 501 NAG D C4  1 
HETATM 18203 C C5  . NAG BA 2 .   ? 134.630 39.530  20.461  1.00   69.26  ? 501 NAG D C5  1 
HETATM 18204 C C6  . NAG BA 2 .   ? 134.176 40.756  19.705  1.00   68.55  ? 501 NAG D C6  1 
HETATM 18205 C C7  . NAG BA 2 .   ? 138.324 36.042  22.099  1.00   71.16  ? 501 NAG D C7  1 
HETATM 18206 C C8  . NAG BA 2 .   ? 138.548 34.715  22.743  1.00   71.91  ? 501 NAG D C8  1 
HETATM 18207 N N2  . NAG BA 2 .   ? 137.054 36.451  22.035  1.00   68.90  ? 501 NAG D N2  1 
HETATM 18208 O O3  . NAG BA 2 .   ? 136.580 38.818  23.573  1.00   69.50  ? 501 NAG D O3  1 
HETATM 18209 O O4  . NAG BA 2 .   ? 134.681 40.689  22.590  1.00   74.32  ? 501 NAG D O4  1 
HETATM 18210 O O5  . NAG BA 2 .   ? 135.455 38.765  19.566  1.00   67.15  ? 501 NAG D O5  1 
HETATM 18211 O O6  . NAG BA 2 .   ? 134.367 40.603  18.305  1.00   68.78  ? 501 NAG D O6  1 
HETATM 18212 O O7  . NAG BA 2 .   ? 139.252 36.728  21.667  1.00   71.61  ? 501 NAG D O7  1 
HETATM 18213 C C1  . EDO CA 4 .   ? 133.325 -0.016  24.184  1.00   47.09  ? 502 EDO D C1  1 
HETATM 18214 O O1  . EDO CA 4 .   ? 134.070 -1.223  24.283  1.00   48.86  ? 502 EDO D O1  1 
HETATM 18215 C C2  . EDO CA 4 .   ? 132.723 -0.021  22.794  1.00   46.44  ? 502 EDO D C2  1 
HETATM 18216 O O2  . EDO CA 4 .   ? 133.756 0.289   21.853  1.00   48.86  ? 502 EDO D O2  1 
HETATM 18217 C C1  . EDO DA 4 .   ? 130.140 5.913   -3.989  1.00   49.02  ? 503 EDO D C1  1 
HETATM 18218 O O1  . EDO DA 4 .   ? 130.115 5.999   -2.562  1.00   49.33  ? 503 EDO D O1  1 
HETATM 18219 C C2  . EDO DA 4 .   ? 131.341 6.684   -4.530  1.00   52.09  ? 503 EDO D C2  1 
HETATM 18220 O O2  . EDO DA 4 .   ? 131.704 6.205   -5.837  1.00   55.32  ? 503 EDO D O2  1 
HETATM 18221 C C1  . EDO EA 4 .   ? 125.131 16.564  12.590  1.00   34.91  ? 504 EDO D C1  1 
HETATM 18222 O O1  . EDO EA 4 .   ? 124.950 16.243  13.964  1.00   35.62  ? 504 EDO D O1  1 
HETATM 18223 C C2  . EDO EA 4 .   ? 123.828 16.389  11.830  1.00   36.65  ? 504 EDO D C2  1 
HETATM 18224 O O2  . EDO EA 4 .   ? 123.427 15.012  11.826  1.00   36.49  ? 504 EDO D O2  1 
HETATM 18225 C C1  . EDO FA 4 .   ? 112.504 -4.958  16.108  1.00   47.49  ? 505 EDO D C1  1 
HETATM 18226 O O1  . EDO FA 4 .   ? 111.869 -4.048  17.019  1.00   47.76  ? 505 EDO D O1  1 
HETATM 18227 C C2  . EDO FA 4 .   ? 111.477 -5.587  15.173  1.00   50.50  ? 505 EDO D C2  1 
HETATM 18228 O O2  . EDO FA 4 .   ? 111.957 -5.559  13.817  1.00   54.08  ? 505 EDO D O2  1 
HETATM 18229 C C1  . EDO GA 4 .   ? 123.100 12.284  29.046  1.00   54.04  ? 506 EDO D C1  1 
HETATM 18230 O O1  . EDO GA 4 .   ? 122.825 12.508  27.661  1.00   53.44  ? 506 EDO D O1  1 
HETATM 18231 C C2  . EDO GA 4 .   ? 124.235 11.282  29.230  1.00   54.11  ? 506 EDO D C2  1 
HETATM 18232 O O2  . EDO GA 4 .   ? 125.456 11.740  28.635  1.00   55.06  ? 506 EDO D O2  1 
HETATM 18233 C C1  . EDO HA 4 .   ? 147.958 23.295  9.588   1.00   58.56  ? 507 EDO D C1  1 
HETATM 18234 O O1  . EDO HA 4 .   ? 148.192 21.901  9.842   1.00   59.36  ? 507 EDO D O1  1 
HETATM 18235 C C2  . EDO HA 4 .   ? 146.476 23.512  9.269   1.00   58.24  ? 507 EDO D C2  1 
HETATM 18236 O O2  . EDO HA 4 .   ? 146.214 24.806  8.691   1.00   57.31  ? 507 EDO D O2  1 
HETATM 18237 C C1  . EDO IA 4 .   ? 92.141  -6.042  9.579   1.00   52.80  ? 508 EDO D C1  1 
HETATM 18238 O O1  . EDO IA 4 .   ? 92.486  -5.070  10.594  1.00   51.49  ? 508 EDO D O1  1 
HETATM 18239 C C2  . EDO IA 4 .   ? 92.893  -7.366  9.774   1.00   52.31  ? 508 EDO D C2  1 
HETATM 18240 O O2  . EDO IA 4 .   ? 92.515  -8.366  8.806   1.00   51.49  ? 508 EDO D O2  1 
HETATM 18241 C C1  . EDO JA 4 .   ? 115.229 -14.774 0.811   1.00   60.27  ? 509 EDO D C1  1 
HETATM 18242 O O1  . EDO JA 4 .   ? 115.986 -15.034 2.007   1.00   61.83  ? 509 EDO D O1  1 
HETATM 18243 C C2  . EDO JA 4 .   ? 115.434 -13.343 0.305   1.00   57.01  ? 509 EDO D C2  1 
HETATM 18244 O O2  . EDO JA 4 .   ? 114.597 -13.081 -0.830  1.00   54.14  ? 509 EDO D O2  1 
HETATM 18245 C C1  . EDO KA 4 .   ? 149.250 4.698   11.091  1.00   53.23  ? 510 EDO D C1  1 
HETATM 18246 O O1  . EDO KA 4 .   ? 149.836 4.560   12.391  1.00   54.22  ? 510 EDO D O1  1 
HETATM 18247 C C2  . EDO KA 4 .   ? 149.343 6.165   10.694  1.00   55.60  ? 510 EDO D C2  1 
HETATM 18248 O O2  . EDO KA 4 .   ? 148.423 6.422   9.625   1.00   58.16  ? 510 EDO D O2  1 
HETATM 18249 C C1  . EDO LA 4 .   ? 132.315 23.830  -12.175 1.00   39.06  ? 501 EDO E C1  1 
HETATM 18250 O O1  . EDO LA 4 .   ? 132.204 25.050  -11.430 1.00   41.38  ? 501 EDO E O1  1 
HETATM 18251 C C2  . EDO LA 4 .   ? 130.961 23.332  -12.687 1.00   35.62  ? 501 EDO E C2  1 
HETATM 18252 O O2  . EDO LA 4 .   ? 131.221 22.417  -13.764 1.00   32.94  ? 501 EDO E O2  1 
HETATM 18253 C C1  . NAG MA 2 .   ? 101.157 61.175  25.500  1.00   55.09  ? 501 NAG F C1  1 
HETATM 18254 C C2  . NAG MA 2 .   ? 100.910 61.505  26.987  1.00   63.58  ? 501 NAG F C2  1 
HETATM 18255 C C3  . NAG MA 2 .   ? 100.767 60.233  27.831  1.00   71.01  ? 501 NAG F C3  1 
HETATM 18256 C C4  . NAG MA 2 .   ? 99.844  59.211  27.179  1.00   75.90  ? 501 NAG F C4  1 
HETATM 18257 C C5  . NAG MA 2 .   ? 100.176 59.042  25.699  1.00   70.25  ? 501 NAG F C5  1 
HETATM 18258 C C6  . NAG MA 2 .   ? 99.186  58.176  24.959  1.00   72.24  ? 501 NAG F C6  1 
HETATM 18259 C C7  . NAG MA 2 .   ? 101.888 63.620  27.754  1.00   65.27  ? 501 NAG F C7  1 
HETATM 18260 C C8  . NAG MA 2 .   ? 103.117 64.292  28.276  1.00   65.73  ? 501 NAG F C8  1 
HETATM 18261 N N2  . NAG MA 2 .   ? 102.010 62.317  27.495  1.00   63.64  ? 501 NAG F N2  1 
HETATM 18262 O O3  . NAG MA 2 .   ? 100.275 60.584  29.125  1.00   71.84  ? 501 NAG F O3  1 
HETATM 18263 O O4  . NAG MA 2 .   ? 100.042 57.946  27.806  1.00   85.08  ? 501 NAG F O4  1 
HETATM 18264 O O5  . NAG MA 2 .   ? 100.163 60.319  25.057  1.00   63.06  ? 501 NAG F O5  1 
HETATM 18265 O O6  . NAG MA 2 .   ? 98.022  58.912  24.602  1.00   74.36  ? 501 NAG F O6  1 
HETATM 18266 O O7  . NAG MA 2 .   ? 100.829 64.222  27.582  1.00   65.53  ? 501 NAG F O7  1 
HETATM 18267 C C1  . NAG NA 2 .   ? 98.789  57.446  28.378  1.00   91.48  ? 502 NAG F C1  1 
HETATM 18268 C C2  . NAG NA 2 .   ? 99.019  56.051  28.952  1.00   94.04  ? 502 NAG F C2  1 
HETATM 18269 C C3  . NAG NA 2 .   ? 97.675  55.464  29.421  1.00   94.07  ? 502 NAG F C3  1 
HETATM 18270 C C4  . NAG NA 2 .   ? 96.911  56.436  30.295  1.00   94.84  ? 502 NAG F C4  1 
HETATM 18271 C C5  . NAG NA 2 .   ? 96.810  57.792  29.602  1.00   95.87  ? 502 NAG F C5  1 
HETATM 18272 C C6  . NAG NA 2 .   ? 96.142  58.852  30.439  1.00   98.04  ? 502 NAG F C6  1 
HETATM 18273 C C7  . NAG NA 2 .   ? 100.948 54.827  28.078  1.00   94.63  ? 502 NAG F C7  1 
HETATM 18274 C C8  . NAG NA 2 .   ? 101.451 53.927  26.995  1.00   93.67  ? 502 NAG F C8  1 
HETATM 18275 N N2  . NAG NA 2 .   ? 99.654  55.194  28.000  1.00   95.19  ? 502 NAG F N2  1 
HETATM 18276 O O3  . NAG NA 2 .   ? 97.920  54.265  30.156  1.00   93.12  ? 502 NAG F O3  1 
HETATM 18277 O O4  . NAG NA 2 .   ? 95.608  55.925  30.573  1.00   94.09  ? 502 NAG F O4  1 
HETATM 18278 O O5  . NAG NA 2 .   ? 98.132  58.277  29.310  1.00   94.15  ? 502 NAG F O5  1 
HETATM 18279 O O6  . NAG NA 2 .   ? 95.060  59.449  29.737  1.00   99.18  ? 502 NAG F O6  1 
HETATM 18280 O O7  . NAG NA 2 .   ? 101.661 55.220  28.998  1.00   94.03  ? 502 NAG F O7  1 
HETATM 18281 C C1  . EDO OA 4 .   ? 135.314 77.125  24.573  1.00   49.30  ? 503 EDO F C1  1 
HETATM 18282 O O1  . EDO OA 4 .   ? 134.766 78.447  24.726  1.00   53.16  ? 503 EDO F O1  1 
HETATM 18283 C C2  . EDO OA 4 .   ? 135.117 76.699  23.133  1.00   44.77  ? 503 EDO F C2  1 
HETATM 18284 O O2  . EDO OA 4 .   ? 133.985 77.449  22.686  1.00   45.72  ? 503 EDO F O2  1 
HETATM 18285 C C1  . EDO PA 4 .   ? 141.099 57.149  15.942  1.00   44.73  ? 504 EDO F C1  1 
HETATM 18286 O O1  . EDO PA 4 .   ? 139.835 56.503  16.158  1.00   45.55  ? 504 EDO F O1  1 
HETATM 18287 C C2  . EDO PA 4 .   ? 141.343 58.151  17.057  1.00   45.10  ? 504 EDO F C2  1 
HETATM 18288 O O2  . EDO PA 4 .   ? 141.404 57.529  18.356  1.00   48.60  ? 504 EDO F O2  1 
HETATM 18289 C C1  . EDO QA 4 .   ? 142.825 60.857  23.112  1.00   60.04  ? 505 EDO F C1  1 
HETATM 18290 O O1  . EDO QA 4 .   ? 142.970 59.521  22.613  1.00   60.92  ? 505 EDO F O1  1 
HETATM 18291 C C2  . EDO QA 4 .   ? 144.187 61.508  23.229  1.00   58.58  ? 505 EDO F C2  1 
HETATM 18292 O O2  . EDO QA 4 .   ? 144.994 60.583  23.956  1.00   60.11  ? 505 EDO F O2  1 
HETATM 18293 C C1  . EDO RA 4 .   ? 122.250 63.004  13.453  1.00   29.00  ? 506 EDO F C1  1 
HETATM 18294 O O1  . EDO RA 4 .   ? 122.923 63.248  14.690  1.00   30.74  ? 506 EDO F O1  1 
HETATM 18295 C C2  . EDO RA 4 .   ? 123.135 62.228  12.497  1.00   28.69  ? 506 EDO F C2  1 
HETATM 18296 O O2  . EDO RA 4 .   ? 124.361 62.931  12.294  1.00   31.67  ? 506 EDO F O2  1 
HETATM 18297 C C1  . EDO SA 4 .   ? 126.083 75.260  -2.213  1.00   53.80  ? 507 EDO F C1  1 
HETATM 18298 O O1  . EDO SA 4 .   ? 125.566 74.912  -0.918  1.00   55.78  ? 507 EDO F O1  1 
HETATM 18299 C C2  . EDO SA 4 .   ? 124.978 75.268  -3.267  1.00   53.36  ? 507 EDO F C2  1 
HETATM 18300 O O2  . EDO SA 4 .   ? 124.092 76.387  -3.113  1.00   55.16  ? 507 EDO F O2  1 
HETATM 18301 C C1  . EDO TA 4 .   ? 148.089 63.109  9.628   1.00   50.88  ? 508 EDO F C1  1 
HETATM 18302 O O1  . EDO TA 4 .   ? 146.695 63.131  9.289   1.00   52.38  ? 508 EDO F O1  1 
HETATM 18303 C C2  . EDO TA 4 .   ? 148.287 62.388  10.950  1.00   47.77  ? 508 EDO F C2  1 
HETATM 18304 O O2  . EDO TA 4 .   ? 147.599 63.077  11.995  1.00   46.72  ? 508 EDO F O2  1 
HETATM 18305 O O   . HOH UA 5 .   ? 114.688 75.267  -8.213  1.00   23.85  ? 601 HOH A O   1 
HETATM 18306 O O   . HOH UA 5 .   ? 123.994 68.336  -12.605 1.00   27.47  ? 602 HOH A O   1 
HETATM 18307 O O   . HOH UA 5 .   ? 89.768  77.323  -7.170  1.00   31.07  ? 603 HOH A O   1 
HETATM 18308 O O   . HOH UA 5 .   ? 96.108  84.928  -4.148  1.00   24.67  ? 604 HOH A O   1 
HETATM 18309 O O   . HOH UA 5 .   ? 91.808  91.564  6.064   1.00   31.65  ? 605 HOH A O   1 
HETATM 18310 O O   . HOH UA 5 .   ? 121.807 70.987  -16.815 1.00   50.79  ? 606 HOH A O   1 
HETATM 18311 O O   . HOH UA 5 .   ? 110.441 90.283  -10.319 0.50   15.54  ? 607 HOH A O   1 
HETATM 18312 O O   . HOH UA 5 .   ? 97.806  86.748  -11.386 1.00   28.47  ? 608 HOH A O   1 
HETATM 18313 O O   . HOH UA 5 .   ? 105.452 87.975  2.716   1.00   31.85  ? 609 HOH A O   1 
HETATM 18314 O O   . HOH UA 5 .   ? 98.972  78.197  -12.074 1.00   39.44  ? 610 HOH A O   1 
HETATM 18315 O O   . HOH UA 5 .   ? 89.677  66.999  -4.642  1.00   38.89  ? 611 HOH A O   1 
HETATM 18316 O O   . HOH UA 5 .   ? 96.484  72.034  8.664   1.00   33.87  ? 612 HOH A O   1 
HETATM 18317 O O   . HOH UA 5 .   ? 119.104 69.718  1.422   1.00   30.19  ? 613 HOH A O   1 
HETATM 18318 O O   . HOH UA 5 .   ? 100.431 73.810  -7.207  1.00   35.03  ? 614 HOH A O   1 
HETATM 18319 O O   . HOH UA 5 .   ? 112.125 89.888  4.999   1.00   26.96  ? 615 HOH A O   1 
HETATM 18320 O O   . HOH UA 5 .   ? 99.529  94.561  -6.338  1.00   45.42  ? 616 HOH A O   1 
HETATM 18321 O O   . HOH UA 5 .   ? 94.070  74.650  9.217   1.00   28.24  ? 617 HOH A O   1 
HETATM 18322 O O   . HOH UA 5 .   ? 116.447 78.698  2.741   1.00   35.74  ? 618 HOH A O   1 
HETATM 18323 O O   . HOH UA 5 .   ? 129.580 71.157  -8.945  1.00   34.31  ? 619 HOH A O   1 
HETATM 18324 O O   . HOH UA 5 .   ? 109.688 75.149  5.982   1.00   30.55  ? 620 HOH A O   1 
HETATM 18325 O O   . HOH UA 5 .   ? 117.402 79.266  -17.247 1.00   32.82  ? 621 HOH A O   1 
HETATM 18326 O O   . HOH UA 5 .   ? 118.006 76.368  3.084   1.00   35.03  ? 622 HOH A O   1 
HETATM 18327 O O   . HOH UA 5 .   ? 88.731  67.745  3.407   1.00   40.17  ? 623 HOH A O   1 
HETATM 18328 O O   . HOH UA 5 .   ? 103.385 99.470  -3.646  1.00   37.91  ? 624 HOH A O   1 
HETATM 18329 O O   . HOH UA 5 .   ? 113.138 68.132  -6.501  1.00   33.37  ? 625 HOH A O   1 
HETATM 18330 O O   . HOH UA 5 .   ? 113.706 70.883  -4.070  1.00   29.14  ? 626 HOH A O   1 
HETATM 18331 O O   . HOH UA 5 .   ? 101.930 62.983  3.615   1.00   45.91  ? 627 HOH A O   1 
HETATM 18332 O O   . HOH UA 5 .   ? 86.377  77.273  -8.085  1.00   32.89  ? 628 HOH A O   1 
HETATM 18333 O O   . HOH UA 5 .   ? 123.905 64.777  0.956   1.00   33.18  ? 629 HOH A O   1 
HETATM 18334 O O   . HOH UA 5 .   ? 89.822  85.890  1.890   1.00   41.95  ? 630 HOH A O   1 
HETATM 18335 O O   . HOH UA 5 .   ? 108.557 71.957  -9.660  1.00   42.29  ? 631 HOH A O   1 
HETATM 18336 O O   . HOH UA 5 .   ? 89.776  72.875  -12.353 1.00   39.40  ? 632 HOH A O   1 
HETATM 18337 O O   . HOH UA 5 .   ? 91.615  77.553  12.179  1.00   38.24  ? 633 HOH A O   1 
HETATM 18338 O O   . HOH UA 5 .   ? 97.724  79.787  13.235  1.00   39.97  ? 634 HOH A O   1 
HETATM 18339 O O   . HOH UA 5 .   ? 115.937 83.073  5.493   0.50   13.64  ? 635 HOH A O   1 
HETATM 18340 O O   . HOH UA 5 .   ? 98.072  81.906  14.398  1.00   36.69  ? 636 HOH A O   1 
HETATM 18341 O O   . HOH UA 5 .   ? 120.724 79.438  -4.279  0.30   7.17   ? 637 HOH A O   1 
HETATM 18342 O O   . HOH UA 5 .   ? 123.745 81.973  -5.218  1.00   47.82  ? 638 HOH A O   1 
HETATM 18343 O O   . HOH UA 5 .   ? 88.446  89.542  -1.853  1.00   37.46  ? 639 HOH A O   1 
HETATM 18344 O O   . HOH UA 5 .   ? 118.292 74.025  1.328   0.50   19.80  ? 640 HOH A O   1 
HETATM 18345 O O   . HOH UA 5 .   ? 114.717 68.688  -4.412  1.00   35.82  ? 641 HOH A O   1 
HETATM 18346 O O   . HOH UA 5 .   ? 120.402 80.407  -2.277  0.70   18.49  ? 642 HOH A O   1 
HETATM 18347 O O   . HOH UA 5 .   ? 91.898  64.990  2.330   1.00   36.05  ? 643 HOH A O   1 
HETATM 18348 O O   . HOH UA 5 .   ? 126.539 77.083  -5.943  1.00   39.37  ? 644 HOH A O   1 
HETATM 18349 O O   . HOH UA 5 .   ? 91.627  81.105  -12.438 1.00   45.11  ? 645 HOH A O   1 
HETATM 18350 O O   . HOH UA 5 .   ? 89.267  80.667  -12.939 1.00   40.02  ? 646 HOH A O   1 
HETATM 18351 O O   . HOH UA 5 .   ? 113.840 66.642  -2.334  1.00   31.88  ? 647 HOH A O   1 
HETATM 18352 O O   . HOH UA 5 .   ? 95.641  64.859  3.957   1.00   43.91  ? 648 HOH A O   1 
HETATM 18353 O O   . HOH UA 5 .   ? 125.056 63.909  -6.014  1.00   36.69  ? 649 HOH A O   1 
HETATM 18354 O O   . HOH UA 5 .   ? 85.780  85.069  -2.287  1.00   39.52  ? 650 HOH A O   1 
HETATM 18355 O O   . HOH UA 5 .   ? 113.088 81.592  10.545  1.00   47.50  ? 651 HOH A O   1 
HETATM 18356 O O   . HOH UA 5 .   ? 99.937  98.183  -9.788  1.00   40.67  ? 652 HOH A O   1 
HETATM 18357 O O   . HOH UA 5 .   ? 105.975 71.296  -11.459 1.00   33.86  ? 653 HOH A O   1 
HETATM 18358 O O   . HOH UA 5 .   ? 93.293  92.212  -10.030 1.00   37.10  ? 654 HOH A O   1 
HETATM 18359 O O   . HOH UA 5 .   ? 83.514  82.891  -11.075 1.00   44.71  ? 655 HOH A O   1 
HETATM 18360 O O   . HOH UA 5 .   ? 126.940 72.047  -21.831 1.00   39.90  ? 656 HOH A O   1 
HETATM 18361 O O   . HOH UA 5 .   ? 87.963  82.829  -2.166  1.00   44.57  ? 657 HOH A O   1 
HETATM 18362 O O   . HOH UA 5 .   ? 97.369  70.373  -7.716  1.00   43.13  ? 658 HOH A O   1 
HETATM 18363 O O   . HOH UA 5 .   ? 118.872 72.249  2.137   0.50   20.66  ? 659 HOH A O   1 
HETATM 18364 O O   . HOH UA 5 .   ? 88.939  92.186  -5.612  1.00   45.01  ? 660 HOH A O   1 
HETATM 18365 O O   . HOH UA 5 .   ? 126.206 79.927  -12.169 1.00   37.27  ? 661 HOH A O   1 
HETATM 18366 O O   . HOH UA 5 .   ? 113.176 95.110  -1.350  1.00   43.70  ? 662 HOH A O   1 
HETATM 18367 O O   . HOH UA 5 .   ? 117.713 67.249  -19.608 1.00   42.64  ? 663 HOH A O   1 
HETATM 18368 O O   . HOH UA 5 .   ? 88.338  84.473  -8.806  1.00   46.21  ? 664 HOH A O   1 
HETATM 18369 O O   . HOH UA 5 .   ? 95.975  71.426  11.110  0.50   22.62  ? 665 HOH A O   1 
HETATM 18370 O O   . HOH UA 5 .   ? 87.733  91.738  -3.554  1.00   37.79  ? 666 HOH A O   1 
HETATM 18371 O O   . HOH UA 5 .   ? 110.049 68.204  1.204   1.00   43.98  ? 667 HOH A O   1 
HETATM 18372 O O   . HOH UA 5 .   ? 105.472 85.779  12.383  1.00   48.59  ? 668 HOH A O   1 
HETATM 18373 O O   . HOH UA 5 .   ? 112.048 65.636  -7.569  1.00   35.58  ? 669 HOH A O   1 
HETATM 18374 O O   . HOH UA 5 .   ? 118.418 60.819  -5.083  1.00   49.34  ? 670 HOH A O   1 
HETATM 18375 O O   . HOH UA 5 .   ? 120.605 59.104  -16.333 1.00   45.30  ? 671 HOH A O   1 
HETATM 18376 O O   . HOH UA 5 .   ? 114.408 64.099  -7.413  1.00   63.01  ? 672 HOH A O   1 
HETATM 18377 O O   . HOH UA 5 .   ? 89.180  69.057  5.637   1.00   34.55  ? 673 HOH A O   1 
HETATM 18378 O O   . HOH UA 5 .   ? 83.354  89.658  -3.470  1.00   40.48  ? 674 HOH A O   1 
HETATM 18379 O O   . HOH UA 5 .   ? 115.111 77.115  -22.186 1.00   44.49  ? 675 HOH A O   1 
HETATM 18380 O O   . HOH UA 5 .   ? 86.852  85.367  5.382   1.00   36.60  ? 676 HOH A O   1 
HETATM 18381 O O   . HOH UA 5 .   ? 93.449  76.316  15.483  1.00   52.60  ? 677 HOH A O   1 
HETATM 18382 O O   . HOH UA 5 .   ? 70.098  76.655  5.853   1.00   39.99  ? 678 HOH A O   1 
HETATM 18383 O O   . HOH UA 5 .   ? 117.330 68.849  -21.693 1.00   35.43  ? 679 HOH A O   1 
HETATM 18384 O O   . HOH UA 5 .   ? 122.766 88.001  -15.792 1.00   37.34  ? 680 HOH A O   1 
HETATM 18385 O O   . HOH UA 5 .   ? 100.871 98.408  -0.538  1.00   35.65  ? 681 HOH A O   1 
HETATM 18386 O O   . HOH UA 5 .   ? 104.670 69.615  -9.001  1.00   37.07  ? 682 HOH A O   1 
HETATM 18387 O O   . HOH UA 5 .   ? 89.543  84.115  -12.972 1.00   39.92  ? 683 HOH A O   1 
HETATM 18388 O O   . HOH UA 5 .   ? 96.228  88.376  -13.622 1.00   42.05  ? 684 HOH A O   1 
HETATM 18389 O O   . HOH UA 5 .   ? 93.621  84.210  13.398  1.00   41.35  ? 685 HOH A O   1 
HETATM 18390 O O   . HOH UA 5 .   ? 92.038  66.209  -6.166  1.00   46.40  ? 686 HOH A O   1 
HETATM 18391 O O   . HOH UA 5 .   ? 122.244 91.833  -6.976  1.00   43.48  ? 687 HOH A O   1 
HETATM 18392 O O   . HOH UA 5 .   ? 89.956  99.100  -6.951  1.00   44.62  ? 688 HOH A O   1 
HETATM 18393 O O   . HOH UA 5 .   ? 92.419  95.572  -10.506 1.00   57.54  ? 689 HOH A O   1 
HETATM 18394 O O   . HOH UA 5 .   ? 91.885  71.270  -14.919 1.00   50.22  ? 690 HOH A O   1 
HETATM 18395 O O   . HOH UA 5 .   ? 125.990 65.037  -3.652  1.00   47.36  ? 691 HOH A O   1 
HETATM 18396 O O   . HOH UA 5 .   ? 86.867  85.440  7.668   0.50   18.29  ? 692 HOH A O   1 
HETATM 18397 O O   . HOH UA 5 .   ? 85.112  86.471  7.744   0.50   27.96  ? 693 HOH A O   1 
HETATM 18398 O O   . HOH UA 5 .   ? 125.375 69.763  -29.069 1.00   40.30  ? 694 HOH A O   1 
HETATM 18399 O O   . HOH UA 5 .   ? 70.019  70.126  2.343   1.00   39.35  ? 695 HOH A O   1 
HETATM 18400 O O   . HOH UA 5 .   ? 95.059  84.906  -21.795 1.00   49.81  ? 696 HOH A O   1 
HETATM 18401 O O   . HOH UA 5 .   ? 104.687 76.834  15.081  1.00   37.83  ? 697 HOH A O   1 
HETATM 18402 O O   . HOH UA 5 .   ? 117.099 76.024  -24.259 1.00   53.33  ? 698 HOH A O   1 
HETATM 18403 O O   . HOH UA 5 .   ? 94.823  71.789  -14.645 1.00   35.89  ? 699 HOH A O   1 
HETATM 18404 O O   . HOH UA 5 .   ? 124.128 56.754  -9.456  1.00   50.46  ? 700 HOH A O   1 
HETATM 18405 O O   . HOH UA 5 .   ? 126.749 60.917  -2.919  1.00   42.49  ? 701 HOH A O   1 
HETATM 18406 O O   . HOH UA 5 .   ? 122.418 90.519  -18.306 1.00   58.49  ? 702 HOH A O   1 
HETATM 18407 O O   . HOH UA 5 .   ? 116.486 68.289  2.196   1.00   40.02  ? 703 HOH A O   1 
HETATM 18408 O O   . HOH UA 5 .   ? 76.742  77.288  12.338  1.00   39.58  ? 704 HOH A O   1 
HETATM 18409 O O   . HOH UA 5 .   ? 77.077  80.662  6.225   1.00   50.04  ? 705 HOH A O   1 
HETATM 18410 O O   . HOH UA 5 .   ? 79.169  83.542  1.053   0.50   13.16  ? 706 HOH A O   1 
HETATM 18411 O O   . HOH UA 5 .   ? 112.542 78.726  11.630  1.00   38.70  ? 707 HOH A O   1 
HETATM 18412 O O   . HOH UA 5 .   ? 107.643 80.286  15.105  1.00   33.73  ? 708 HOH A O   1 
HETATM 18413 O O   . HOH UA 5 .   ? 115.510 72.644  3.222   1.00   38.13  ? 709 HOH A O   1 
HETATM 18414 O O   . HOH UA 5 .   ? 79.776  76.098  13.592  1.00   51.86  ? 710 HOH A O   1 
HETATM 18415 O O   . HOH UA 5 .   ? 88.395  65.012  3.450   1.00   45.42  ? 711 HOH A O   1 
HETATM 18416 O O   . HOH UA 5 .   ? 109.701 64.751  -7.280  1.00   49.05  ? 712 HOH A O   1 
HETATM 18417 O O   . HOH UA 5 .   ? 100.698 67.790  -9.872  1.00   64.54  ? 713 HOH A O   1 
HETATM 18418 O O   . HOH UA 5 .   ? 97.239  69.886  -10.585 1.00   47.55  ? 714 HOH A O   1 
HETATM 18419 O O   . HOH UA 5 .   ? 94.734  68.494  -7.243  1.00   47.26  ? 715 HOH A O   1 
HETATM 18420 O O   . HOH UA 5 .   ? 100.335 70.402  -6.877  1.00   51.97  ? 716 HOH A O   1 
HETATM 18421 O O   . HOH UA 5 .   ? 79.168  83.640  3.011   0.50   21.23  ? 717 HOH A O   1 
HETATM 18422 O O   . HOH UA 5 .   ? 102.341 83.484  -22.132 1.00   41.91  ? 718 HOH A O   1 
HETATM 18423 O O   . HOH UA 5 .   ? 119.940 69.054  -23.887 1.00   49.80  ? 719 HOH A O   1 
HETATM 18424 O O   . HOH UA 5 .   ? 116.797 87.910  8.654   1.00   59.17  ? 720 HOH A O   1 
HETATM 18425 O O   . HOH UA 5 .   ? 120.030 59.577  -13.597 1.00   59.48  ? 721 HOH A O   1 
HETATM 18426 O O   . HOH UA 5 .   ? 67.738  69.907  3.582   1.00   53.24  ? 722 HOH A O   1 
HETATM 18427 O O   . HOH UA 5 .   ? 124.744 83.933  -0.637  1.00   55.67  ? 723 HOH A O   1 
HETATM 18428 O O   . HOH UA 5 .   ? 127.010 82.507  -11.783 1.00   54.95  ? 724 HOH A O   1 
HETATM 18429 O O   . HOH UA 5 .   ? 94.635  82.878  -22.945 1.00   57.56  ? 725 HOH A O   1 
HETATM 18430 O O   . HOH UA 5 .   ? 102.761 62.791  0.256   1.00   43.59  ? 726 HOH A O   1 
HETATM 18431 O O   . HOH UA 5 .   ? 85.859  78.865  -5.569  1.00   34.91  ? 727 HOH A O   1 
HETATM 18432 O O   . HOH UA 5 .   ? 86.582  77.721  -3.576  1.00   30.06  ? 728 HOH A O   1 
HETATM 18433 O O   . HOH UA 5 .   ? 111.641 83.453  9.419   1.00   34.41  ? 729 HOH A O   1 
HETATM 18434 O O   . HOH UA 5 .   ? 89.971  70.672  13.816  1.00   36.71  ? 730 HOH A O   1 
HETATM 18435 O O   . HOH UA 5 .   ? 119.272 62.177  -21.985 1.00   38.03  ? 731 HOH A O   1 
HETATM 18436 O O   . HOH UA 5 .   ? 109.013 86.363  -22.699 1.00   50.81  ? 732 HOH A O   1 
HETATM 18437 O O   . HOH UA 5 .   ? 99.665  96.104  -12.808 0.50   25.52  ? 733 HOH A O   1 
HETATM 18438 O O   . HOH UA 5 .   ? 89.114  98.086  -9.336  1.00   47.94  ? 734 HOH A O   1 
HETATM 18439 O O   . HOH UA 5 .   ? 110.315 77.390  2.677   0.50   7.01   ? 735 HOH A O   1 
HETATM 18440 O O   . HOH UA 5 .   ? 111.748 73.518  3.199   1.00   49.81  ? 736 HOH A O   1 
HETATM 18441 O O   . HOH UA 5 .   ? 125.197 71.167  -31.752 1.00   47.47  ? 737 HOH A O   1 
HETATM 18442 O O   . HOH UA 5 .   ? 102.484 69.868  -8.078  1.00   52.20  ? 738 HOH A O   1 
HETATM 18443 O O   . HOH UA 5 .   ? 110.488 89.219  -12.369 0.50   34.17  ? 739 HOH A O   1 
HETATM 18444 O O   . HOH UA 5 .   ? 79.669  85.646  -10.529 1.00   48.02  ? 740 HOH A O   1 
HETATM 18445 O O   . HOH UA 5 .   ? 111.832 75.487  4.557   0.50   25.32  ? 741 HOH A O   1 
HETATM 18446 O O   . HOH UA 5 .   ? 79.034  72.674  -10.506 1.00   40.10  ? 742 HOH A O   1 
HETATM 18447 O O   . HOH UA 5 .   ? 99.819  94.936  -14.639 0.50   25.63  ? 743 HOH A O   1 
HETATM 18448 O O   . HOH VA 5 .   ? 78.468  31.410  21.279  1.00   28.81  ? 601 HOH B O   1 
HETATM 18449 O O   . HOH VA 5 .   ? 67.011  49.522  24.336  1.00   23.49  ? 602 HOH B O   1 
HETATM 18450 O O   . HOH VA 5 .   ? 87.150  22.699  20.669  1.00   21.71  ? 603 HOH B O   1 
HETATM 18451 O O   . HOH VA 5 .   ? 61.452  40.262  19.043  1.00   32.46  ? 604 HOH B O   1 
HETATM 18452 O O   . HOH VA 5 .   ? 69.163  47.092  31.293  1.00   26.13  ? 605 HOH B O   1 
HETATM 18453 O O   . HOH VA 5 .   ? 79.846  33.058  15.535  1.00   22.35  ? 606 HOH B O   1 
HETATM 18454 O O   . HOH VA 5 .   ? 56.201  53.848  19.537  1.00   30.89  ? 607 HOH B O   1 
HETATM 18455 O O   . HOH VA 5 .   ? 78.411  45.837  21.040  1.00   25.66  ? 608 HOH B O   1 
HETATM 18456 O O   . HOH VA 5 .   ? 60.315  45.231  30.401  1.00   33.79  ? 609 HOH B O   1 
HETATM 18457 O O   . HOH VA 5 .   ? 82.165  57.193  16.115  1.00   27.52  ? 610 HOH B O   1 
HETATM 18458 O O   . HOH VA 5 .   ? 76.742  46.566  27.688  1.00   27.16  ? 611 HOH B O   1 
HETATM 18459 O O   . HOH VA 5 .   ? 82.795  39.927  23.051  1.00   31.69  ? 612 HOH B O   1 
HETATM 18460 O O   . HOH VA 5 .   ? 74.853  56.202  23.465  1.00   30.97  ? 613 HOH B O   1 
HETATM 18461 O O   . HOH VA 5 .   ? 81.836  38.074  21.660  1.00   24.60  ? 614 HOH B O   1 
HETATM 18462 O O   . HOH VA 5 .   ? 86.484  23.929  25.688  1.00   33.62  ? 615 HOH B O   1 
HETATM 18463 O O   . HOH VA 5 .   ? 83.026  17.034  18.211  1.00   34.45  ? 616 HOH B O   1 
HETATM 18464 O O   . HOH VA 5 .   ? 82.346  32.405  14.626  1.00   31.53  ? 617 HOH B O   1 
HETATM 18465 O O   . HOH VA 5 .   ? 82.759  33.879  12.195  1.00   27.36  ? 618 HOH B O   1 
HETATM 18466 O O   . HOH VA 5 .   ? 83.656  34.093  16.494  1.00   26.92  ? 619 HOH B O   1 
HETATM 18467 O O   . HOH VA 5 .   ? 66.281  34.167  30.854  1.00   34.20  ? 620 HOH B O   1 
HETATM 18468 O O   . HOH VA 5 .   ? 79.648  27.332  30.890  1.00   27.80  ? 621 HOH B O   1 
HETATM 18469 O O   . HOH VA 5 .   ? 82.204  46.018  6.085   1.00   34.12  ? 622 HOH B O   1 
HETATM 18470 O O   . HOH VA 5 .   ? 63.263  51.019  32.996  1.00   33.86  ? 623 HOH B O   1 
HETATM 18471 O O   . HOH VA 5 .   ? 64.852  30.295  12.887  1.00   33.74  ? 624 HOH B O   1 
HETATM 18472 O O   . HOH VA 5 .   ? 71.263  25.918  18.008  1.00   30.23  ? 625 HOH B O   1 
HETATM 18473 O O   . HOH VA 5 .   ? 54.553  40.955  30.078  1.00   29.08  ? 626 HOH B O   1 
HETATM 18474 O O   . HOH VA 5 .   ? 68.649  76.637  14.528  1.00   38.45  ? 627 HOH B O   1 
HETATM 18475 O O   . HOH VA 5 .   ? 80.066  67.005  24.902  0.50   27.13  ? 628 HOH B O   1 
HETATM 18476 O O   . HOH VA 5 .   ? 75.629  36.347  39.288  1.00   39.14  ? 629 HOH B O   1 
HETATM 18477 O O   . HOH VA 5 .   ? 68.787  53.255  7.977   1.00   29.10  ? 630 HOH B O   1 
HETATM 18478 O O   . HOH VA 5 .   ? 73.503  24.954  19.311  1.00   40.64  ? 631 HOH B O   1 
HETATM 18479 O O   . HOH VA 5 .   ? 81.397  56.392  25.432  1.00   28.17  ? 632 HOH B O   1 
HETATM 18480 O O   . HOH VA 5 .   ? 77.500  23.827  37.627  1.00   33.91  ? 633 HOH B O   1 
HETATM 18481 O O   . HOH VA 5 .   ? 86.280  35.039  16.487  1.00   34.36  ? 634 HOH B O   1 
HETATM 18482 O O   . HOH VA 5 .   ? 57.363  31.775  25.469  1.00   42.16  ? 635 HOH B O   1 
HETATM 18483 O O   . HOH VA 5 .   ? 71.237  21.782  33.219  1.00   28.19  ? 636 HOH B O   1 
HETATM 18484 O O   . HOH VA 5 .   ? 71.799  50.969  6.867   1.00   27.99  ? 637 HOH B O   1 
HETATM 18485 O O   . HOH VA 5 .   ? 75.051  59.222  25.030  1.00   38.56  ? 638 HOH B O   1 
HETATM 18486 O O   . HOH VA 5 .   ? 58.854  33.412  16.889  1.00   34.90  ? 639 HOH B O   1 
HETATM 18487 O O   . HOH VA 5 .   ? 78.748  28.541  9.952   1.00   34.13  ? 640 HOH B O   1 
HETATM 18488 O O   . HOH VA 5 .   ? 60.355  48.689  6.493   1.00   37.99  ? 641 HOH B O   1 
HETATM 18489 O O   . HOH VA 5 .   ? 86.942  43.484  34.127  1.00   31.00  ? 642 HOH B O   1 
HETATM 18490 O O   . HOH VA 5 .   ? 80.683  47.015  18.620  1.00   36.51  ? 643 HOH B O   1 
HETATM 18491 O O   . HOH VA 5 .   ? 81.389  42.070  15.289  1.00   33.27  ? 644 HOH B O   1 
HETATM 18492 O O   . HOH VA 5 .   ? 64.857  55.465  6.747   1.00   31.93  ? 645 HOH B O   1 
HETATM 18493 O O   . HOH VA 5 .   ? 63.285  56.069  20.122  1.00   35.14  ? 646 HOH B O   1 
HETATM 18494 O O   . HOH VA 5 .   ? 67.541  58.017  22.314  0.50   18.55  ? 647 HOH B O   1 
HETATM 18495 O O   . HOH VA 5 .   ? 69.984  57.991  2.240   1.00   48.63  ? 648 HOH B O   1 
HETATM 18496 O O   . HOH VA 5 .   ? 59.858  51.064  36.296  1.00   48.58  ? 649 HOH B O   1 
HETATM 18497 O O   . HOH VA 5 .   ? 69.811  56.867  28.979  1.00   30.52  ? 650 HOH B O   1 
HETATM 18498 O O   . HOH VA 5 .   ? 65.072  66.585  20.149  1.00   44.21  ? 651 HOH B O   1 
HETATM 18499 O O   . HOH VA 5 .   ? 91.343  28.601  26.794  1.00   41.28  ? 652 HOH B O   1 
HETATM 18500 O O   . HOH VA 5 .   ? 74.840  62.394  4.632   1.00   34.47  ? 653 HOH B O   1 
HETATM 18501 O O   . HOH VA 5 .   ? 96.003  34.424  23.282  1.00   43.76  ? 654 HOH B O   1 
HETATM 18502 O O   . HOH VA 5 .   ? 85.504  16.677  25.647  1.00   41.29  ? 655 HOH B O   1 
HETATM 18503 O O   . HOH VA 5 .   ? 83.061  42.090  19.945  0.50   14.49  ? 656 HOH B O   1 
HETATM 18504 O O   . HOH VA 5 .   ? 82.311  47.022  16.801  1.00   40.17  ? 657 HOH B O   1 
HETATM 18505 O O   . HOH VA 5 .   ? 73.615  18.360  27.407  1.00   35.93  ? 658 HOH B O   1 
HETATM 18506 O O   . HOH VA 5 .   ? 61.147  55.664  30.386  1.00   34.69  ? 659 HOH B O   1 
HETATM 18507 O O   . HOH VA 5 .   ? 70.052  21.145  36.645  1.00   46.70  ? 660 HOH B O   1 
HETATM 18508 O O   . HOH VA 5 .   ? 90.371  31.152  14.921  1.00   44.38  ? 661 HOH B O   1 
HETATM 18509 O O   . HOH VA 5 .   ? 59.722  59.041  11.240  1.00   43.66  ? 662 HOH B O   1 
HETATM 18510 O O   . HOH VA 5 .   ? 68.579  33.816  31.884  1.00   36.99  ? 663 HOH B O   1 
HETATM 18511 O O   . HOH VA 5 .   ? 83.561  55.508  24.703  1.00   43.73  ? 664 HOH B O   1 
HETATM 18512 O O   . HOH VA 5 .   ? 81.589  49.462  20.188  1.00   41.17  ? 665 HOH B O   1 
HETATM 18513 O O   . HOH VA 5 .   ? 51.698  35.317  25.193  1.00   37.54  ? 666 HOH B O   1 
HETATM 18514 O O   . HOH VA 5 .   ? 71.165  52.380  4.438   1.00   46.53  ? 667 HOH B O   1 
HETATM 18515 O O   . HOH VA 5 .   ? 80.141  25.309  37.320  1.00   40.28  ? 668 HOH B O   1 
HETATM 18516 O O   . HOH VA 5 .   ? 78.281  50.031  39.377  1.00   38.99  ? 669 HOH B O   1 
HETATM 18517 O O   . HOH VA 5 .   ? 70.999  18.328  29.312  0.50   26.46  ? 670 HOH B O   1 
HETATM 18518 O O   . HOH VA 5 .   ? 60.614  57.091  28.328  1.00   40.44  ? 671 HOH B O   1 
HETATM 18519 O O   . HOH VA 5 .   ? 88.258  22.474  12.808  1.00   36.51  ? 672 HOH B O   1 
HETATM 18520 O O   . HOH VA 5 .   ? 61.807  56.786  25.448  1.00   45.45  ? 673 HOH B O   1 
HETATM 18521 O O   . HOH VA 5 .   ? 82.630  24.155  41.568  1.00   37.61  ? 674 HOH B O   1 
HETATM 18522 O O   . HOH VA 5 .   ? 95.344  34.196  30.496  1.00   37.50  ? 675 HOH B O   1 
HETATM 18523 O O   . HOH VA 5 .   ? 64.646  47.699  5.118   1.00   43.38  ? 676 HOH B O   1 
HETATM 18524 O O   . HOH VA 5 .   ? 61.418  59.486  17.353  1.00   37.38  ? 677 HOH B O   1 
HETATM 18525 O O   . HOH VA 5 .   ? 80.726  56.023  9.096   1.00   35.49  ? 678 HOH B O   1 
HETATM 18526 O O   . HOH VA 5 .   ? 61.987  39.743  3.573   1.00   55.73  ? 679 HOH B O   1 
HETATM 18527 O O   . HOH VA 5 .   ? 96.035  24.556  12.987  1.00   43.24  ? 680 HOH B O   1 
HETATM 18528 O O   . HOH VA 5 .   ? 78.130  58.819  9.519   1.00   37.12  ? 681 HOH B O   1 
HETATM 18529 O O   . HOH VA 5 .   ? 71.003  18.694  31.486  0.50   25.24  ? 682 HOH B O   1 
HETATM 18530 O O   . HOH VA 5 .   ? 52.865  33.883  26.498  1.00   47.03  ? 683 HOH B O   1 
HETATM 18531 O O   . HOH VA 5 .   ? 82.235  43.899  19.449  0.50   19.90  ? 684 HOH B O   1 
HETATM 18532 O O   . HOH VA 5 .   ? 84.381  50.026  31.306  1.00   43.23  ? 685 HOH B O   1 
HETATM 18533 O O   . HOH VA 5 .   ? 85.366  42.326  36.107  1.00   43.09  ? 686 HOH B O   1 
HETATM 18534 O O   . HOH VA 5 .   ? 87.325  17.852  30.118  1.00   38.72  ? 687 HOH B O   1 
HETATM 18535 O O   . HOH VA 5 .   ? 63.935  22.582  27.446  1.00   36.72  ? 688 HOH B O   1 
HETATM 18536 O O   . HOH VA 5 .   ? 69.206  47.876  33.851  1.00   46.55  ? 689 HOH B O   1 
HETATM 18537 O O   . HOH VA 5 .   ? 87.065  67.095  8.330   1.00   36.74  ? 690 HOH B O   1 
HETATM 18538 O O   . HOH VA 5 .   ? 58.460  53.205  8.963   1.00   43.98  ? 691 HOH B O   1 
HETATM 18539 O O   . HOH VA 5 .   ? 76.866  19.392  25.488  1.00   46.83  ? 692 HOH B O   1 
HETATM 18540 O O   . HOH VA 5 .   ? 58.468  43.854  35.061  1.00   43.96  ? 693 HOH B O   1 
HETATM 18541 O O   . HOH VA 5 .   ? 82.603  51.820  30.114  1.00   43.11  ? 694 HOH B O   1 
HETATM 18542 O O   . HOH VA 5 .   ? 76.607  19.730  19.119  1.00   34.85  ? 695 HOH B O   1 
HETATM 18543 O O   . HOH VA 5 .   ? 54.466  44.812  33.140  1.00   41.46  ? 696 HOH B O   1 
HETATM 18544 O O   . HOH VA 5 .   ? 83.432  51.408  26.813  1.00   40.94  ? 697 HOH B O   1 
HETATM 18545 O O   . HOH VA 5 .   ? 72.277  55.316  31.864  1.00   47.22  ? 698 HOH B O   1 
HETATM 18546 O O   . HOH VA 5 .   ? 90.763  58.023  16.403  1.00   42.60  ? 699 HOH B O   1 
HETATM 18547 O O   . HOH VA 5 .   ? 96.618  27.187  20.215  1.00   40.46  ? 700 HOH B O   1 
HETATM 18548 O O   . HOH VA 5 .   ? 64.098  70.697  14.506  1.00   49.55  ? 701 HOH B O   1 
HETATM 18549 O O   . HOH VA 5 .   ? 84.847  63.437  10.789  1.00   48.29  ? 702 HOH B O   1 
HETATM 18550 O O   . HOH VA 5 .   ? 80.022  37.632  9.780   1.00   45.29  ? 703 HOH B O   1 
HETATM 18551 O O   . HOH VA 5 .   ? 89.081  29.124  29.827  1.00   41.23  ? 704 HOH B O   1 
HETATM 18552 O O   . HOH VA 5 .   ? 74.682  30.300  40.233  1.00   34.09  ? 705 HOH B O   1 
HETATM 18553 O O   . HOH VA 5 .   ? 58.870  43.784  12.956  0.50   25.53  ? 706 HOH B O   1 
HETATM 18554 O O   . HOH VA 5 .   ? 70.305  32.518  30.598  1.00   44.79  ? 707 HOH B O   1 
HETATM 18555 O O   . HOH VA 5 .   ? 53.779  43.627  27.354  1.00   43.15  ? 708 HOH B O   1 
HETATM 18556 O O   . HOH VA 5 .   ? 68.988  63.683  32.013  1.00   51.93  ? 709 HOH B O   1 
HETATM 18557 O O   . HOH VA 5 .   ? 65.576  58.869  22.446  0.50   21.88  ? 710 HOH B O   1 
HETATM 18558 O O   . HOH VA 5 .   ? 80.019  56.454  32.745  1.00   43.99  ? 711 HOH B O   1 
HETATM 18559 O O   . HOH VA 5 .   ? 65.097  22.085  24.295  1.00   51.20  ? 712 HOH B O   1 
HETATM 18560 O O   . HOH VA 5 .   ? 71.503  21.719  21.325  1.00   39.17  ? 713 HOH B O   1 
HETATM 18561 O O   . HOH VA 5 .   ? 56.995  32.496  15.566  1.00   44.67  ? 714 HOH B O   1 
HETATM 18562 O O   . HOH VA 5 .   ? 90.504  63.816  19.202  1.00   53.45  ? 715 HOH B O   1 
HETATM 18563 O O   . HOH VA 5 .   ? 84.677  64.120  24.223  1.00   38.99  ? 716 HOH B O   1 
HETATM 18564 O O   . HOH VA 5 .   ? 83.307  49.392  22.397  1.00   41.64  ? 717 HOH B O   1 
HETATM 18565 O O   . HOH VA 5 .   ? 61.913  26.369  35.274  1.00   42.18  ? 718 HOH B O   1 
HETATM 18566 O O   . HOH VA 5 .   ? 60.718  23.778  30.028  1.00   45.78  ? 719 HOH B O   1 
HETATM 18567 O O   . HOH VA 5 .   ? 54.756  30.813  23.267  1.00   43.72  ? 720 HOH B O   1 
HETATM 18568 O O   . HOH VA 5 .   ? 78.900  60.697  0.693   1.00   49.01  ? 721 HOH B O   1 
HETATM 18569 O O   . HOH VA 5 .   ? 93.788  31.298  31.249  1.00   53.37  ? 722 HOH B O   1 
HETATM 18570 O O   . HOH VA 5 .   ? 85.669  21.707  10.813  1.00   49.49  ? 723 HOH B O   1 
HETATM 18571 O O   . HOH VA 5 .   ? 86.682  37.417  15.389  1.00   38.34  ? 724 HOH B O   1 
HETATM 18572 O O   . HOH VA 5 .   ? 91.083  41.362  37.762  1.00   60.84  ? 725 HOH B O   1 
HETATM 18573 O O   . HOH VA 5 .   ? 74.654  55.774  30.151  1.00   36.68  ? 726 HOH B O   1 
HETATM 18574 O O   . HOH VA 5 .   ? 74.458  53.517  30.261  1.00   39.19  ? 727 HOH B O   1 
HETATM 18575 O O   . HOH VA 5 .   ? 82.845  51.464  18.424  1.00   47.40  ? 728 HOH B O   1 
HETATM 18576 O O   . HOH VA 5 .   ? 83.019  54.569  16.871  1.00   47.85  ? 729 HOH B O   1 
HETATM 18577 O O   . HOH VA 5 .   ? 61.955  51.928  35.711  1.00   66.50  ? 730 HOH B O   1 
HETATM 18578 O O   . HOH VA 5 .   ? 71.083  37.676  9.290   0.50   27.59  ? 731 HOH B O   1 
HETATM 18579 O O   . HOH VA 5 .   ? 81.751  74.917  22.149  1.00   50.45  ? 732 HOH B O   1 
HETATM 18580 O O   . HOH VA 5 .   ? 87.996  33.005  14.922  1.00   40.69  ? 733 HOH B O   1 
HETATM 18581 O O   . HOH VA 5 .   ? 55.783  53.811  34.349  1.00   51.70  ? 734 HOH B O   1 
HETATM 18582 O O   . HOH VA 5 .   ? 79.283  42.403  41.871  1.00   59.98  ? 735 HOH B O   1 
HETATM 18583 O O   . HOH VA 5 .   ? 60.537  45.134  4.538   1.00   50.42  ? 736 HOH B O   1 
HETATM 18584 O O   . HOH VA 5 .   ? 65.134  48.568  2.278   1.00   45.75  ? 737 HOH B O   1 
HETATM 18585 O O   . HOH VA 5 .   ? 67.679  49.617  1.380   1.00   41.60  ? 738 HOH B O   1 
HETATM 18586 O O   . HOH VA 5 .   ? 75.835  59.752  4.913   1.00   48.57  ? 739 HOH B O   1 
HETATM 18587 O O   . HOH VA 5 .   ? 70.686  36.238  13.226  0.50   6.99   ? 740 HOH B O   1 
HETATM 18588 O O   . HOH VA 5 .   ? 61.737  58.808  20.144  1.00   43.54  ? 741 HOH B O   1 
HETATM 18589 O O   . HOH VA 5 .   ? 89.263  43.017  19.765  1.00   52.08  ? 742 HOH B O   1 
HETATM 18590 O O   . HOH VA 5 .   ? 74.549  31.688  10.004  1.00   47.32  ? 743 HOH B O   1 
HETATM 18591 O O   . HOH VA 5 .   ? 75.886  27.839  10.040  1.00   45.02  ? 744 HOH B O   1 
HETATM 18592 O O   . HOH VA 5 .   ? 81.375  16.889  31.893  1.00   41.73  ? 745 HOH B O   1 
HETATM 18593 O O   . HOH VA 5 .   ? 81.297  45.499  3.649   1.00   45.63  ? 746 HOH B O   1 
HETATM 18594 O O   . HOH WA 5 .   ? 65.010  37.107  5.000   1.00   43.63  ? 601 HOH C O   1 
HETATM 18595 O O   . HOH WA 5 .   ? 72.612  6.193   0.663   1.00   26.78  ? 602 HOH C O   1 
HETATM 18596 O O   . HOH WA 5 .   ? 67.972  11.864  10.121  1.00   29.32  ? 603 HOH C O   1 
HETATM 18597 O O   . HOH WA 5 .   ? 70.750  27.501  -0.426  1.00   24.26  ? 604 HOH C O   1 
HETATM 18598 O O   . HOH WA 5 .   ? 72.188  -1.886  10.343  1.00   32.56  ? 605 HOH C O   1 
HETATM 18599 O O   . HOH WA 5 .   ? 67.701  7.629   -5.116  1.00   37.08  ? 606 HOH C O   1 
HETATM 18600 O O   . HOH WA 5 .   ? 90.169  10.050  -5.241  1.00   41.35  ? 607 HOH C O   1 
HETATM 18601 O O   . HOH WA 5 .   ? 74.060  13.078  -7.511  1.00   32.25  ? 608 HOH C O   1 
HETATM 18602 O O   . HOH WA 5 .   ? 86.052  8.097   10.669  1.00   28.36  ? 609 HOH C O   1 
HETATM 18603 O O   . HOH WA 5 .   ? 86.906  11.603  10.087  1.00   23.28  ? 610 HOH C O   1 
HETATM 18604 O O   . HOH WA 5 .   ? 80.773  5.059   -5.406  1.00   25.79  ? 611 HOH C O   1 
HETATM 18605 O O   . HOH WA 5 .   ? 76.413  22.608  -6.385  1.00   33.94  ? 612 HOH C O   1 
HETATM 18606 O O   . HOH WA 5 .   ? 73.251  19.683  -18.280 1.00   36.05  ? 613 HOH C O   1 
HETATM 18607 O O   . HOH WA 5 .   ? 71.077  39.727  -3.602  1.00   29.72  ? 614 HOH C O   1 
HETATM 18608 O O   . HOH WA 5 .   ? 78.752  15.798  -3.382  1.00   26.15  ? 615 HOH C O   1 
HETATM 18609 O O   . HOH WA 5 .   ? 76.271  28.472  2.428   1.00   27.61  ? 616 HOH C O   1 
HETATM 18610 O O   . HOH WA 5 .   ? 77.502  30.303  1.716   1.00   30.87  ? 617 HOH C O   1 
HETATM 18611 O O   . HOH WA 5 .   ? 78.557  -0.008  -0.245  1.00   36.08  ? 618 HOH C O   1 
HETATM 18612 O O   . HOH WA 5 .   ? 63.463  42.221  -5.094  1.00   42.60  ? 619 HOH C O   1 
HETATM 18613 O O   . HOH WA 5 .   ? 88.590  10.888  12.151  1.00   42.46  ? 620 HOH C O   1 
HETATM 18614 O O   . HOH WA 5 .   ? 77.821  29.348  -0.855  1.00   30.27  ? 621 HOH C O   1 
HETATM 18615 O O   . HOH WA 5 .   ? 80.083  30.326  2.916   1.00   30.47  ? 622 HOH C O   1 
HETATM 18616 O O   . HOH WA 5 .   ? 81.769  7.847   16.470  1.00   33.93  ? 623 HOH C O   1 
HETATM 18617 O O   . HOH WA 5 .   ? 76.458  -0.269  5.031   1.00   31.56  ? 624 HOH C O   1 
HETATM 18618 O O   . HOH WA 5 .   ? 78.246  39.575  8.206   1.00   36.74  ? 625 HOH C O   1 
HETATM 18619 O O   . HOH WA 5 .   ? 63.420  29.250  -7.376  1.00   34.05  ? 626 HOH C O   1 
HETATM 18620 O O   . HOH WA 5 .   ? 72.728  -2.820  1.685   1.00   27.53  ? 627 HOH C O   1 
HETATM 18621 O O   . HOH WA 5 .   ? 65.914  29.241  7.825   1.00   36.88  ? 628 HOH C O   1 
HETATM 18622 O O   . HOH WA 5 .   ? 80.168  7.197   17.830  1.00   44.21  ? 629 HOH C O   1 
HETATM 18623 O O   . HOH WA 5 .   ? 76.167  32.822  8.535   1.00   34.38  ? 630 HOH C O   1 
HETATM 18624 O O   . HOH WA 5 .   ? 53.757  28.897  -2.070  1.00   35.81  ? 631 HOH C O   1 
HETATM 18625 O O   . HOH WA 5 .   ? 79.891  2.186   16.294  1.00   34.15  ? 632 HOH C O   1 
HETATM 18626 O O   . HOH WA 5 .   ? 82.813  -8.097  0.700   1.00   33.69  ? 633 HOH C O   1 
HETATM 18627 O O   . HOH WA 5 .   ? 82.583  11.183  16.526  1.00   39.62  ? 634 HOH C O   1 
HETATM 18628 O O   . HOH WA 5 .   ? 94.119  -12.616 0.299   1.00   28.78  ? 635 HOH C O   1 
HETATM 18629 O O   . HOH WA 5 .   ? 68.258  23.208  14.561  1.00   31.99  ? 636 HOH C O   1 
HETATM 18630 O O   . HOH WA 5 .   ? 67.189  42.388  1.999   1.00   35.48  ? 637 HOH C O   1 
HETATM 18631 O O   . HOH WA 5 .   ? 60.168  3.068   8.368   1.00   37.93  ? 638 HOH C O   1 
HETATM 18632 O O   . HOH WA 5 .   ? 65.844  30.255  5.404   1.00   40.49  ? 639 HOH C O   1 
HETATM 18633 O O   . HOH WA 5 .   ? 68.108  36.948  -7.069  1.00   36.71  ? 640 HOH C O   1 
HETATM 18634 O O   . HOH WA 5 .   ? 94.949  7.273   11.000  1.00   42.52  ? 641 HOH C O   1 
HETATM 18635 O O   . HOH WA 5 .   ? 64.042  16.466  14.728  1.00   34.21  ? 642 HOH C O   1 
HETATM 18636 O O   . HOH WA 5 .   ? 90.754  21.783  4.243   1.00   39.33  ? 643 HOH C O   1 
HETATM 18637 O O   . HOH WA 5 .   ? 75.649  24.218  -4.299  1.00   31.46  ? 644 HOH C O   1 
HETATM 18638 O O   . HOH WA 5 .   ? 73.261  2.238   -9.944  1.00   39.27  ? 645 HOH C O   1 
HETATM 18639 O O   . HOH WA 5 .   ? 81.970  22.155  -0.409  1.00   36.01  ? 646 HOH C O   1 
HETATM 18640 O O   . HOH WA 5 .   ? 74.638  -8.402  5.816   1.00   40.46  ? 647 HOH C O   1 
HETATM 18641 O O   . HOH WA 5 .   ? 98.552  -9.038  -3.512  1.00   36.29  ? 648 HOH C O   1 
HETATM 18642 O O   . HOH WA 5 .   ? 57.727  3.296   0.009   1.00   40.13  ? 649 HOH C O   1 
HETATM 18643 O O   . HOH WA 5 .   ? 81.785  2.126   -7.151  1.00   38.29  ? 650 HOH C O   1 
HETATM 18644 O O   . HOH WA 5 .   ? 63.442  31.170  9.018   1.00   36.81  ? 651 HOH C O   1 
HETATM 18645 O O   . HOH WA 5 .   ? 77.515  16.311  20.993  1.00   40.36  ? 652 HOH C O   1 
HETATM 18646 O O   . HOH WA 5 .   ? 82.563  15.123  -5.363  1.00   41.99  ? 653 HOH C O   1 
HETATM 18647 O O   . HOH WA 5 .   ? 72.582  11.898  18.647  1.00   41.85  ? 654 HOH C O   1 
HETATM 18648 O O   . HOH WA 5 .   ? 66.355  15.714  -23.761 1.00   51.88  ? 655 HOH C O   1 
HETATM 18649 O O   . HOH WA 5 .   ? 76.545  42.012  1.841   1.00   29.70  ? 656 HOH C O   1 
HETATM 18650 O O   . HOH WA 5 .   ? 62.051  4.620   1.729   1.00   35.88  ? 657 HOH C O   1 
HETATM 18651 O O   . HOH WA 5 .   ? 65.520  0.611   -3.573  1.00   44.77  ? 658 HOH C O   1 
HETATM 18652 O O   . HOH WA 5 .   ? 91.860  7.601   4.424   1.00   38.40  ? 659 HOH C O   1 
HETATM 18653 O O   . HOH WA 5 .   ? 88.522  -1.258  -12.554 1.00   37.51  ? 660 HOH C O   1 
HETATM 18654 O O   . HOH WA 5 .   ? 92.416  7.929   2.099   1.00   32.74  ? 661 HOH C O   1 
HETATM 18655 O O   . HOH WA 5 .   ? 81.370  1.094   -5.029  1.00   36.11  ? 662 HOH C O   1 
HETATM 18656 O O   . HOH WA 5 .   ? 71.047  -4.286  0.677   1.00   39.43  ? 663 HOH C O   1 
HETATM 18657 O O   . HOH WA 5 .   ? 71.934  35.757  -11.968 1.00   49.10  ? 664 HOH C O   1 
HETATM 18658 O O   . HOH WA 5 .   ? 80.439  18.955  -4.642  1.00   49.09  ? 665 HOH C O   1 
HETATM 18659 O O   . HOH WA 5 .   ? 88.835  12.557  14.783  1.00   42.95  ? 666 HOH C O   1 
HETATM 18660 O O   . HOH WA 5 .   ? 80.209  21.773  -5.060  1.00   36.65  ? 667 HOH C O   1 
HETATM 18661 O O   . HOH WA 5 .   ? 75.892  41.976  4.893   1.00   33.59  ? 668 HOH C O   1 
HETATM 18662 O O   . HOH WA 5 .   ? 70.724  -8.832  9.184   1.00   31.82  ? 669 HOH C O   1 
HETATM 18663 O O   . HOH WA 5 .   ? 56.594  15.204  13.630  1.00   50.92  ? 670 HOH C O   1 
HETATM 18664 O O   . HOH WA 5 .   ? 56.673  15.365  10.491  1.00   34.87  ? 671 HOH C O   1 
HETATM 18665 O O   . HOH WA 5 .   ? 57.457  4.865   6.603   1.00   41.75  ? 672 HOH C O   1 
HETATM 18666 O O   . HOH WA 5 .   ? 79.439  -2.563  7.130   1.00   26.99  ? 673 HOH C O   1 
HETATM 18667 O O   . HOH WA 5 .   ? 85.819  13.503  -6.073  1.00   54.46  ? 674 HOH C O   1 
HETATM 18668 O O   . HOH WA 5 .   ? 68.087  -5.967  14.314  1.00   45.02  ? 675 HOH C O   1 
HETATM 18669 O O   . HOH WA 5 .   ? 74.968  0.490   -6.194  1.00   35.38  ? 676 HOH C O   1 
HETATM 18670 O O   . HOH WA 5 .   ? 90.155  3.452   -14.231 1.00   46.85  ? 677 HOH C O   1 
HETATM 18671 O O   . HOH WA 5 .   ? 91.850  14.788  3.573   1.00   52.30  ? 678 HOH C O   1 
HETATM 18672 O O   . HOH WA 5 .   ? 81.951  37.917  0.027   1.00   50.34  ? 679 HOH C O   1 
HETATM 18673 O O   . HOH WA 5 .   ? 70.515  12.218  -18.188 1.00   38.60  ? 680 HOH C O   1 
HETATM 18674 O O   . HOH WA 5 .   ? 79.881  4.224   18.180  1.00   55.14  ? 681 HOH C O   1 
HETATM 18675 O O   . HOH WA 5 .   ? 83.179  1.918   -2.982  1.00   31.29  ? 682 HOH C O   1 
HETATM 18676 O O   . HOH WA 5 .   ? 78.881  44.524  4.231   1.00   48.51  ? 683 HOH C O   1 
HETATM 18677 O O   . HOH WA 5 .   ? 79.454  37.254  6.685   1.00   46.28  ? 684 HOH C O   1 
HETATM 18678 O O   . HOH WA 5 .   ? 50.843  22.187  6.201   1.00   40.77  ? 685 HOH C O   1 
HETATM 18679 O O   . HOH WA 5 .   ? 85.837  4.516   13.516  1.00   38.00  ? 686 HOH C O   1 
HETATM 18680 O O   . HOH WA 5 .   ? 82.878  -11.898 0.924   1.00   42.53  ? 687 HOH C O   1 
HETATM 18681 O O   . HOH WA 5 .   ? 68.545  -3.365  -0.334  1.00   38.97  ? 688 HOH C O   1 
HETATM 18682 O O   . HOH WA 5 .   ? 59.270  38.678  5.837   1.00   55.63  ? 689 HOH C O   1 
HETATM 18683 O O   . HOH WA 5 .   ? 79.912  33.940  -14.275 1.00   39.99  ? 690 HOH C O   1 
HETATM 18684 O O   . HOH WA 5 .   ? 88.933  21.903  8.769   1.00   40.94  ? 691 HOH C O   1 
HETATM 18685 O O   . HOH WA 5 .   ? 80.079  30.030  -2.801  1.00   34.15  ? 692 HOH C O   1 
HETATM 18686 O O   . HOH WA 5 .   ? 73.919  5.612   -10.097 1.00   60.68  ? 693 HOH C O   1 
HETATM 18687 O O   . HOH WA 5 .   ? 60.237  35.437  0.392   1.00   32.89  ? 694 HOH C O   1 
HETATM 18688 O O   . HOH WA 5 .   ? 53.025  31.387  -0.412  1.00   40.42  ? 695 HOH C O   1 
HETATM 18689 O O   . HOH WA 5 .   ? 79.801  -3.111  9.503   1.00   44.30  ? 696 HOH C O   1 
HETATM 18690 O O   . HOH WA 5 .   ? 89.249  12.731  -6.140  1.00   42.38  ? 697 HOH C O   1 
HETATM 18691 O O   . HOH WA 5 .   ? 82.087  15.431  -8.251  1.00   50.73  ? 698 HOH C O   1 
HETATM 18692 O O   . HOH WA 5 .   ? 71.908  -11.628 8.709   1.00   47.71  ? 699 HOH C O   1 
HETATM 18693 O O   . HOH WA 5 .   ? 79.921  -0.035  1.986   1.00   63.33  ? 700 HOH C O   1 
HETATM 18694 O O   . HOH WA 5 .   ? 92.208  -11.781 -11.910 1.00   57.95  ? 701 HOH C O   1 
HETATM 18695 O O   . HOH WA 5 .   ? 59.692  14.297  -12.726 1.00   48.99  ? 702 HOH C O   1 
HETATM 18696 O O   . HOH WA 5 .   ? 60.310  18.356  -13.105 1.00   48.84  ? 703 HOH C O   1 
HETATM 18697 O O   . HOH WA 5 .   ? 60.591  29.594  11.863  0.40   16.42  ? 704 HOH C O   1 
HETATM 18698 O O   . HOH WA 5 .   ? 61.639  31.890  6.080   0.50   25.58  ? 705 HOH C O   1 
HETATM 18699 O O   . HOH WA 5 .   ? 82.168  16.860  -3.354  1.00   47.60  ? 706 HOH C O   1 
HETATM 18700 O O   . HOH WA 5 .   ? 74.194  -9.955  7.922   1.00   33.39  ? 707 HOH C O   1 
HETATM 18701 O O   . HOH WA 5 .   ? 72.451  9.126   15.559  1.00   46.34  ? 708 HOH C O   1 
HETATM 18702 O O   . HOH WA 5 .   ? 52.591  3.752   5.820   1.00   57.40  ? 709 HOH C O   1 
HETATM 18703 O O   . HOH WA 5 .   ? 61.610  26.915  -13.535 1.00   40.69  ? 710 HOH C O   1 
HETATM 18704 O O   . HOH WA 5 .   ? 61.782  5.526   17.184  1.00   62.33  ? 711 HOH C O   1 
HETATM 18705 O O   . HOH WA 5 .   ? 73.959  -12.338 10.156  1.00   56.33  ? 712 HOH C O   1 
HETATM 18706 O O   . HOH WA 5 .   ? 65.446  30.252  10.557  0.50   26.43  ? 713 HOH C O   1 
HETATM 18707 O O   . HOH WA 5 .   ? 87.917  5.533   11.317  1.00   41.64  ? 714 HOH C O   1 
HETATM 18708 O O   . HOH WA 5 .   ? 86.956  5.309   15.711  1.00   63.57  ? 715 HOH C O   1 
HETATM 18709 O O   . HOH WA 5 .   ? 62.428  -0.813  -8.158  1.00   50.95  ? 716 HOH C O   1 
HETATM 18710 O O   . HOH WA 5 .   ? 72.834  14.895  20.028  1.00   44.01  ? 717 HOH C O   1 
HETATM 18711 O O   . HOH WA 5 .   ? 99.484  -13.451 0.572   1.00   49.84  ? 718 HOH C O   1 
HETATM 18712 O O   . HOH WA 5 .   ? 92.444  0.262   12.314  1.00   40.99  ? 719 HOH C O   1 
HETATM 18713 O O   . HOH WA 5 .   ? 63.918  -3.020  9.961   1.00   51.49  ? 720 HOH C O   1 
HETATM 18714 O O   . HOH WA 5 .   ? 60.962  15.478  -3.781  1.00   52.12  ? 721 HOH C O   1 
HETATM 18715 O O   . HOH WA 5 .   ? 58.896  37.727  -9.663  1.00   38.03  ? 722 HOH C O   1 
HETATM 18716 O O   . HOH WA 5 .   ? 70.689  26.196  11.304  0.70   32.75  ? 723 HOH C O   1 
HETATM 18717 O O   . HOH WA 5 .   ? 77.291  21.634  11.760  1.00   33.09  ? 724 HOH C O   1 
HETATM 18718 O O   . HOH WA 5 .   ? 82.988  8.227   -11.493 0.50   15.24  ? 725 HOH C O   1 
HETATM 18719 O O   . HOH WA 5 .   ? 84.461  9.622   -11.790 0.50   28.27  ? 726 HOH C O   1 
HETATM 18720 O O   . HOH WA 5 .   ? 74.398  21.414  9.227   0.30   0.04   ? 727 HOH C O   1 
HETATM 18721 O O   . HOH WA 5 .   ? 75.205  -6.333  13.473  1.00   37.66  ? 728 HOH C O   1 
HETATM 18722 O O   . HOH XA 5 .   ? 123.853 -5.001  12.970  1.00   35.69  ? 601 HOH D O   1 
HETATM 18723 O O   . HOH XA 5 .   ? 130.560 7.342   2.194   0.50   14.30  ? 602 HOH D O   1 
HETATM 18724 O O   . HOH XA 5 .   ? 133.623 13.921  11.566  1.00   30.08  ? 603 HOH D O   1 
HETATM 18725 O O   . HOH XA 5 .   ? 126.782 -3.774  19.732  1.00   27.52  ? 604 HOH D O   1 
HETATM 18726 O O   . HOH XA 5 .   ? 123.248 -15.303 5.481   1.00   35.73  ? 605 HOH D O   1 
HETATM 18727 O O   . HOH XA 5 .   ? 137.042 25.880  12.761  1.00   34.62  ? 606 HOH D O   1 
HETATM 18728 O O   . HOH XA 5 .   ? 132.546 -3.750  5.642   1.00   35.57  ? 607 HOH D O   1 
HETATM 18729 O O   . HOH XA 5 .   ? 122.515 3.874   18.746  1.00   39.19  ? 608 HOH D O   1 
HETATM 18730 O O   . HOH XA 5 .   ? 132.180 -10.093 15.848  1.00   39.62  ? 609 HOH D O   1 
HETATM 18731 O O   . HOH XA 5 .   ? 139.111 0.189   17.015  0.50   20.60  ? 610 HOH D O   1 
HETATM 18732 O O   . HOH XA 5 .   ? 139.116 -2.229  1.703   1.00   26.81  ? 611 HOH D O   1 
HETATM 18733 O O   . HOH XA 5 .   ? 129.809 16.107  7.034   1.00   36.09  ? 612 HOH D O   1 
HETATM 18734 O O   . HOH XA 5 .   ? 114.195 -1.920  15.679  1.00   42.93  ? 613 HOH D O   1 
HETATM 18735 O O   . HOH XA 5 .   ? 115.359 -1.198  -1.365  1.00   29.62  ? 614 HOH D O   1 
HETATM 18736 O O   . HOH XA 5 .   ? 140.347 11.698  5.414   1.00   30.10  ? 615 HOH D O   1 
HETATM 18737 O O   . HOH XA 5 .   ? 148.243 10.336  19.221  1.00   36.12  ? 616 HOH D O   1 
HETATM 18738 O O   . HOH XA 5 .   ? 138.138 -12.603 12.661  1.00   33.47  ? 617 HOH D O   1 
HETATM 18739 O O   . HOH XA 5 .   ? 120.976 6.890   13.291  1.00   37.53  ? 618 HOH D O   1 
HETATM 18740 O O   . HOH XA 5 .   ? 126.343 -10.818 20.418  1.00   36.69  ? 619 HOH D O   1 
HETATM 18741 O O   . HOH XA 5 .   ? 139.389 -5.911  3.575   1.00   34.35  ? 620 HOH D O   1 
HETATM 18742 O O   . HOH XA 5 .   ? 130.720 -4.086  -4.205  1.00   44.98  ? 621 HOH D O   1 
HETATM 18743 O O   . HOH XA 5 .   ? 120.733 -4.412  -5.192  1.00   31.10  ? 622 HOH D O   1 
HETATM 18744 O O   . HOH XA 5 .   ? 137.496 23.469  17.586  1.00   44.16  ? 623 HOH D O   1 
HETATM 18745 O O   . HOH XA 5 .   ? 129.278 -6.323  -0.718  1.00   35.31  ? 624 HOH D O   1 
HETATM 18746 O O   . HOH XA 5 .   ? 107.999 5.907   11.283  1.00   37.78  ? 625 HOH D O   1 
HETATM 18747 O O   . HOH XA 5 .   ? 124.815 13.351  15.678  1.00   45.01  ? 626 HOH D O   1 
HETATM 18748 O O   . HOH XA 5 .   ? 138.598 14.989  20.616  1.00   37.23  ? 627 HOH D O   1 
HETATM 18749 O O   . HOH XA 5 .   ? 129.283 18.513  6.959   1.00   29.90  ? 628 HOH D O   1 
HETATM 18750 O O   . HOH XA 5 .   ? 135.869 9.814   1.172   0.50   22.60  ? 629 HOH D O   1 
HETATM 18751 O O   . HOH XA 5 .   ? 143.745 -4.751  7.759   1.00   44.26  ? 630 HOH D O   1 
HETATM 18752 O O   . HOH XA 5 .   ? 115.994 2.140   -1.652  1.00   36.24  ? 631 HOH D O   1 
HETATM 18753 O O   . HOH XA 5 .   ? 138.234 5.021   -0.988  1.00   31.65  ? 632 HOH D O   1 
HETATM 18754 O O   . HOH XA 5 .   ? 114.940 -5.778  -3.205  1.00   36.91  ? 633 HOH D O   1 
HETATM 18755 O O   . HOH XA 5 .   ? 122.719 -6.591  -5.790  1.00   46.83  ? 634 HOH D O   1 
HETATM 18756 O O   . HOH XA 5 .   ? 97.420  -15.187 7.983   1.00   42.29  ? 635 HOH D O   1 
HETATM 18757 O O   . HOH XA 5 .   ? 128.400 7.757   -0.942  1.00   38.09  ? 636 HOH D O   1 
HETATM 18758 O O   . HOH XA 5 .   ? 126.394 13.699  13.866  1.00   32.13  ? 637 HOH D O   1 
HETATM 18759 O O   . HOH XA 5 .   ? 141.792 -10.056 18.298  1.00   34.80  ? 638 HOH D O   1 
HETATM 18760 O O   . HOH XA 5 .   ? 143.413 26.034  8.943   1.00   39.22  ? 639 HOH D O   1 
HETATM 18761 O O   . HOH XA 5 .   ? 120.152 -13.030 13.733  1.00   48.10  ? 640 HOH D O   1 
HETATM 18762 O O   . HOH XA 5 .   ? 130.728 -6.347  -5.307  1.00   47.27  ? 641 HOH D O   1 
HETATM 18763 O O   . HOH XA 5 .   ? 143.481 10.808  1.253   1.00   25.94  ? 642 HOH D O   1 
HETATM 18764 O O   . HOH XA 5 .   ? 127.698 18.495  9.097   1.00   38.51  ? 643 HOH D O   1 
HETATM 18765 O O   . HOH XA 5 .   ? 134.593 30.671  2.140   1.00   37.51  ? 644 HOH D O   1 
HETATM 18766 O O   . HOH XA 5 .   ? 116.464 8.567   14.274  1.00   44.62  ? 645 HOH D O   1 
HETATM 18767 O O   . HOH XA 5 .   ? 133.056 18.556  0.784   0.50   26.18  ? 646 HOH D O   1 
HETATM 18768 O O   . HOH XA 5 .   ? 118.955 -5.561  22.585  1.00   42.88  ? 647 HOH D O   1 
HETATM 18769 O O   . HOH XA 5 .   ? 134.903 29.018  5.905   1.00   43.67  ? 648 HOH D O   1 
HETATM 18770 O O   . HOH XA 5 .   ? 134.278 -5.720  -3.770  1.00   43.30  ? 649 HOH D O   1 
HETATM 18771 O O   . HOH XA 5 .   ? 102.979 2.621   20.040  1.00   42.94  ? 650 HOH D O   1 
HETATM 18772 O O   . HOH XA 5 .   ? 137.747 -14.822 10.903  1.00   61.51  ? 651 HOH D O   1 
HETATM 18773 O O   . HOH XA 5 .   ? 117.435 -7.484  19.130  1.00   36.89  ? 652 HOH D O   1 
HETATM 18774 O O   . HOH XA 5 .   ? 145.866 -17.608 4.330   1.00   38.39  ? 653 HOH D O   1 
HETATM 18775 O O   . HOH XA 5 .   ? 109.824 7.941   12.013  1.00   56.82  ? 654 HOH D O   1 
HETATM 18776 O O   . HOH XA 5 .   ? 126.930 -12.809 -0.763  1.00   37.54  ? 655 HOH D O   1 
HETATM 18777 O O   . HOH XA 5 .   ? 134.608 16.475  0.133   0.50   28.38  ? 656 HOH D O   1 
HETATM 18778 O O   . HOH XA 5 .   ? 146.048 17.606  13.742  1.00   51.48  ? 657 HOH D O   1 
HETATM 18779 O O   . HOH XA 5 .   ? 129.519 -9.948  -0.037  1.00   53.36  ? 658 HOH D O   1 
HETATM 18780 O O   . HOH XA 5 .   ? 143.540 -17.944 1.026   1.00   42.28  ? 659 HOH D O   1 
HETATM 18781 O O   . HOH XA 5 .   ? 120.189 10.738  13.223  1.00   51.10  ? 660 HOH D O   1 
HETATM 18782 O O   . HOH XA 5 .   ? 147.974 -18.293 3.295   1.00   40.16  ? 661 HOH D O   1 
HETATM 18783 O O   . HOH XA 5 .   ? 103.927 -0.967  -1.475  1.00   41.82  ? 662 HOH D O   1 
HETATM 18784 O O   . HOH XA 5 .   ? 121.435 -1.397  -5.993  1.00   46.10  ? 663 HOH D O   1 
HETATM 18785 O O   . HOH XA 5 .   ? 142.256 11.723  3.033   1.00   48.72  ? 664 HOH D O   1 
HETATM 18786 O O   . HOH XA 5 .   ? 135.303 -13.971 10.651  1.00   40.69  ? 665 HOH D O   1 
HETATM 18787 O O   . HOH XA 5 .   ? 127.626 27.297  5.999   1.00   46.75  ? 666 HOH D O   1 
HETATM 18788 O O   . HOH XA 5 .   ? 100.458 11.527  15.913  1.00   56.26  ? 667 HOH D O   1 
HETATM 18789 O O   . HOH XA 5 .   ? 97.399  -6.319  23.968  1.00   56.38  ? 668 HOH D O   1 
HETATM 18790 O O   . HOH XA 5 .   ? 127.408 -18.474 19.465  1.00   44.03  ? 669 HOH D O   1 
HETATM 18791 O O   . HOH XA 5 .   ? 115.084 13.462  0.987   1.00   47.94  ? 670 HOH D O   1 
HETATM 18792 O O   . HOH XA 5 .   ? 135.871 27.652  3.572   1.00   51.34  ? 671 HOH D O   1 
HETATM 18793 O O   . HOH XA 5 .   ? 141.069 -15.444 15.785  1.00   46.09  ? 672 HOH D O   1 
HETATM 18794 O O   . HOH XA 5 .   ? 122.980 -14.523 17.510  1.00   37.63  ? 673 HOH D O   1 
HETATM 18795 O O   . HOH XA 5 .   ? 134.070 25.117  -0.923  1.00   48.46  ? 674 HOH D O   1 
HETATM 18796 O O   . HOH XA 5 .   ? 114.558 1.989   -4.097  1.00   40.64  ? 675 HOH D O   1 
HETATM 18797 O O   . HOH XA 5 .   ? 120.505 -10.833 -3.517  1.00   43.09  ? 676 HOH D O   1 
HETATM 18798 O O   . HOH XA 5 .   ? 118.044 9.147   11.769  1.00   51.77  ? 677 HOH D O   1 
HETATM 18799 O O   . HOH XA 5 .   ? 127.288 19.097  5.031   1.00   50.83  ? 678 HOH D O   1 
HETATM 18800 O O   . HOH XA 5 .   ? 131.902 -18.388 16.067  1.00   51.81  ? 679 HOH D O   1 
HETATM 18801 O O   . HOH XA 5 .   ? 128.143 -13.607 21.601  1.00   59.01  ? 680 HOH D O   1 
HETATM 18802 O O   . HOH XA 5 .   ? 129.297 0.316   -8.862  0.50   21.94  ? 681 HOH D O   1 
HETATM 18803 O O   . HOH XA 5 .   ? 103.138 -3.125  20.027  1.00   45.85  ? 682 HOH D O   1 
HETATM 18804 O O   . HOH XA 5 .   ? 122.137 13.362  13.511  1.00   39.89  ? 683 HOH D O   1 
HETATM 18805 O O   . HOH XA 5 .   ? 145.765 21.090  24.304  1.00   39.38  ? 684 HOH D O   1 
HETATM 18806 O O   . HOH XA 5 .   ? 115.849 -13.052 5.115   0.50   21.99  ? 685 HOH D O   1 
HETATM 18807 O O   . HOH XA 5 .   ? 107.304 2.280   3.815   1.00   45.10  ? 686 HOH D O   1 
HETATM 18808 O O   . HOH XA 5 .   ? 126.564 -4.564  22.722  1.00   46.66  ? 687 HOH D O   1 
HETATM 18809 O O   . HOH XA 5 .   ? 120.719 -14.891 15.590  1.00   44.18  ? 688 HOH D O   1 
HETATM 18810 O O   . HOH XA 5 .   ? 143.372 -16.498 3.239   1.00   69.53  ? 689 HOH D O   1 
HETATM 18811 O O   . HOH XA 5 .   ? 121.302 12.723  8.238   1.00   42.85  ? 690 HOH D O   1 
HETATM 18812 O O   . HOH XA 5 .   ? 111.447 -12.878 -3.793  1.00   40.90  ? 691 HOH D O   1 
HETATM 18813 O O   . HOH XA 5 .   ? 125.281 20.135  9.467   1.00   62.03  ? 692 HOH D O   1 
HETATM 18814 O O   . HOH XA 5 .   ? 126.836 22.110  7.215   1.00   47.96  ? 693 HOH D O   1 
HETATM 18815 O O   . HOH XA 5 .   ? 126.078 22.744  9.536   1.00   43.71  ? 694 HOH D O   1 
HETATM 18816 O O   . HOH XA 5 .   ? 139.808 1.569   -3.010  0.50   22.81  ? 695 HOH D O   1 
HETATM 18817 O O   . HOH XA 5 .   ? 129.234 31.973  16.111  1.00   41.32  ? 696 HOH D O   1 
HETATM 18818 O O   . HOH XA 5 .   ? 152.377 -8.889  10.560  1.00   42.35  ? 697 HOH D O   1 
HETATM 18819 O O   . HOH XA 5 .   ? 92.866  -2.780  12.287  1.00   49.63  ? 698 HOH D O   1 
HETATM 18820 O O   . HOH XA 5 .   ? 116.906 -18.927 9.406   1.00   48.27  ? 699 HOH D O   1 
HETATM 18821 O O   . HOH XA 5 .   ? 95.957  -11.529 19.271  1.00   50.61  ? 700 HOH D O   1 
HETATM 18822 O O   . HOH XA 5 .   ? 146.645 -8.952  16.849  1.00   53.77  ? 701 HOH D O   1 
HETATM 18823 O O   . HOH XA 5 .   ? 148.228 -0.472  18.912  1.00   48.66  ? 702 HOH D O   1 
HETATM 18824 O O   . HOH XA 5 .   ? 148.987 -6.506  16.689  1.00   35.83  ? 703 HOH D O   1 
HETATM 18825 O O   . HOH XA 5 .   ? 136.998 -15.215 13.848  1.00   43.24  ? 704 HOH D O   1 
HETATM 18826 O O   . HOH XA 5 .   ? 126.983 -0.781  27.760  1.00   52.63  ? 705 HOH D O   1 
HETATM 18827 O O   . HOH XA 5 .   ? 124.503 -1.342  29.887  1.00   55.54  ? 706 HOH D O   1 
HETATM 18828 O O   . HOH XA 5 .   ? 103.167 7.573   -2.824  1.00   52.86  ? 707 HOH D O   1 
HETATM 18829 O O   . HOH XA 5 .   ? 147.660 -3.788  1.871   1.00   51.40  ? 708 HOH D O   1 
HETATM 18830 O O   . HOH XA 5 .   ? 144.378 13.125  7.722   1.00   46.52  ? 709 HOH D O   1 
HETATM 18831 O O   . HOH XA 5 .   ? 142.458 -1.319  0.251   1.00   40.85  ? 710 HOH D O   1 
HETATM 18832 O O   . HOH XA 5 .   ? 132.358 -2.131  -6.210  1.00   44.57  ? 711 HOH D O   1 
HETATM 18833 O O   . HOH XA 5 .   ? 123.933 -3.756  -8.279  1.00   47.45  ? 712 HOH D O   1 
HETATM 18834 O O   . HOH XA 5 .   ? 134.169 -3.572  -6.666  1.00   56.69  ? 713 HOH D O   1 
HETATM 18835 O O   . HOH XA 5 .   ? 116.837 -12.198 -3.445  1.00   47.97  ? 714 HOH D O   1 
HETATM 18836 O O   . HOH XA 5 .   ? 100.448 3.124   21.196  1.00   47.49  ? 715 HOH D O   1 
HETATM 18837 O O   . HOH XA 5 .   ? 141.099 17.613  5.051   1.00   42.51  ? 716 HOH D O   1 
HETATM 18838 O O   . HOH XA 5 .   ? 102.003 3.722   -4.946  1.00   53.46  ? 717 HOH D O   1 
HETATM 18839 O O   . HOH XA 5 .   ? 135.161 -11.748 19.963  1.00   36.83  ? 718 HOH D O   1 
HETATM 18840 O O   . HOH XA 5 .   ? 135.465 -15.033 16.680  1.00   46.95  ? 719 HOH D O   1 
HETATM 18841 O O   . HOH XA 5 .   ? 131.042 -1.836  -8.411  0.50   37.08  ? 720 HOH D O   1 
HETATM 18842 O O   . HOH XA 5 .   ? 137.853 1.514   -3.733  0.50   30.02  ? 721 HOH D O   1 
HETATM 18843 O O   . HOH XA 5 .   ? 138.588 2.945   18.452  0.50   26.82  ? 722 HOH D O   1 
HETATM 18844 O O   . HOH XA 5 .   ? 115.806 -9.094  12.262  1.00   43.11  ? 723 HOH D O   1 
HETATM 18845 O O   . HOH XA 5 .   ? 135.090 14.549  1.904   1.00   78.85  ? 724 HOH D O   1 
HETATM 18846 O O   . HOH YA 5 .   ? 130.466 4.192   -7.260  1.00   50.97  ? 601 HOH E O   1 
HETATM 18847 O O   . HOH YA 5 .   ? 122.893 9.498   -12.893 1.00   41.37  ? 602 HOH E O   1 
HETATM 18848 O O   . HOH YA 5 .   ? 143.580 25.771  -19.063 1.00   28.53  ? 603 HOH E O   1 
HETATM 18849 O O   . HOH YA 5 .   ? 134.279 14.397  -11.548 1.00   25.08  ? 604 HOH E O   1 
HETATM 18850 O O   . HOH YA 5 .   ? 152.484 26.324  -12.961 1.00   26.94  ? 605 HOH E O   1 
HETATM 18851 O O   . HOH YA 5 .   ? 147.846 35.167  -16.253 1.00   39.01  ? 606 HOH E O   1 
HETATM 18852 O O   . HOH YA 5 .   ? 151.372 22.847  -19.637 1.00   33.72  ? 607 HOH E O   1 
HETATM 18853 O O   . HOH YA 5 .   ? 158.310 18.181  -15.755 1.00   40.62  ? 608 HOH E O   1 
HETATM 18854 O O   . HOH YA 5 .   ? 132.077 18.061  -6.836  0.50   14.67  ? 609 HOH E O   1 
HETATM 18855 O O   . HOH YA 5 .   ? 162.288 27.824  -5.250  1.00   37.07  ? 610 HOH E O   1 
HETATM 18856 O O   . HOH YA 5 .   ? 158.348 24.113  -19.774 1.00   36.26  ? 611 HOH E O   1 
HETATM 18857 O O   . HOH YA 5 .   ? 148.793 10.147  -16.414 0.50   14.76  ? 612 HOH E O   1 
HETATM 18858 O O   . HOH YA 5 .   ? 139.418 40.404  -12.226 1.00   37.29  ? 613 HOH E O   1 
HETATM 18859 O O   . HOH YA 5 .   ? 161.545 28.337  -17.272 1.00   43.31  ? 614 HOH E O   1 
HETATM 18860 O O   . HOH YA 5 .   ? 152.042 17.542  -4.703  1.00   35.27  ? 615 HOH E O   1 
HETATM 18861 O O   . HOH YA 5 .   ? 134.478 23.328  -15.660 1.00   35.27  ? 616 HOH E O   1 
HETATM 18862 O O   . HOH YA 5 .   ? 144.096 41.164  -2.270  1.00   46.31  ? 617 HOH E O   1 
HETATM 18863 O O   . HOH YA 5 .   ? 123.794 3.623   -8.333  1.00   47.20  ? 618 HOH E O   1 
HETATM 18864 O O   . HOH YA 5 .   ? 129.821 19.533  -9.115  1.00   34.78  ? 619 HOH E O   1 
HETATM 18865 O O   . HOH YA 5 .   ? 129.757 18.445  -7.007  0.50   23.50  ? 620 HOH E O   1 
HETATM 18866 O O   . HOH YA 5 .   ? 147.719 34.486  1.108   1.00   32.08  ? 621 HOH E O   1 
HETATM 18867 O O   . HOH YA 5 .   ? 134.185 26.078  -13.692 1.00   38.51  ? 622 HOH E O   1 
HETATM 18868 O O   . HOH YA 5 .   ? 149.432 30.085  -22.211 1.00   49.85  ? 623 HOH E O   1 
HETATM 18869 O O   . HOH YA 5 .   ? 136.474 12.254  -0.103  1.00   31.47  ? 624 HOH E O   1 
HETATM 18870 O O   . HOH YA 5 .   ? 140.295 27.607  -13.388 1.00   29.68  ? 625 HOH E O   1 
HETATM 18871 O O   . HOH YA 5 .   ? 125.302 9.426   -17.543 1.00   48.65  ? 626 HOH E O   1 
HETATM 18872 O O   . HOH YA 5 .   ? 137.259 7.949   -5.187  1.00   37.47  ? 627 HOH E O   1 
HETATM 18873 O O   . HOH YA 5 .   ? 154.199 6.251   -7.693  1.00   44.14  ? 628 HOH E O   1 
HETATM 18874 O O   . HOH YA 5 .   ? 142.993 41.633  -4.753  1.00   44.67  ? 629 HOH E O   1 
HETATM 18875 O O   . HOH YA 5 .   ? 161.763 12.302  -12.660 1.00   31.26  ? 630 HOH E O   1 
HETATM 18876 O O   . HOH YA 5 .   ? 152.825 30.409  -22.824 1.00   39.97  ? 631 HOH E O   1 
HETATM 18877 O O   . HOH YA 5 .   ? 160.036 30.732  -13.273 1.00   34.07  ? 632 HOH E O   1 
HETATM 18878 O O   . HOH YA 5 .   ? 134.504 8.756   -20.354 1.00   37.08  ? 633 HOH E O   1 
HETATM 18879 O O   . HOH YA 5 .   ? 161.534 30.288  -15.477 1.00   41.60  ? 634 HOH E O   1 
HETATM 18880 O O   . HOH YA 5 .   ? 142.837 36.788  -20.238 1.00   36.38  ? 635 HOH E O   1 
HETATM 18881 O O   . HOH YA 5 .   ? 157.500 30.265  3.795   1.00   51.53  ? 636 HOH E O   1 
HETATM 18882 O O   . HOH YA 5 .   ? 161.975 28.803  -19.595 1.00   36.82  ? 637 HOH E O   1 
HETATM 18883 O O   . HOH YA 5 .   ? 129.342 20.300  -4.769  1.00   37.52  ? 638 HOH E O   1 
HETATM 18884 O O   . HOH YA 5 .   ? 134.113 26.457  -8.589  1.00   45.52  ? 639 HOH E O   1 
HETATM 18885 O O   . HOH YA 5 .   ? 137.196 6.124   -2.949  1.00   36.55  ? 640 HOH E O   1 
HETATM 18886 O O   . HOH YA 5 .   ? 132.178 1.751   -13.347 1.00   37.17  ? 641 HOH E O   1 
HETATM 18887 O O   . HOH YA 5 .   ? 127.492 21.802  -9.972  1.00   47.52  ? 642 HOH E O   1 
HETATM 18888 O O   . HOH YA 5 .   ? 148.332 28.992  5.982   1.00   39.64  ? 643 HOH E O   1 
HETATM 18889 O O   . HOH YA 5 .   ? 136.563 2.586   -24.968 1.00   46.35  ? 644 HOH E O   1 
HETATM 18890 O O   . HOH YA 5 .   ? 150.919 10.890  -0.852  1.00   41.93  ? 645 HOH E O   1 
HETATM 18891 O O   . HOH YA 5 .   ? 151.966 35.443  2.955   1.00   46.89  ? 646 HOH E O   1 
HETATM 18892 O O   . HOH YA 5 .   ? 123.648 13.804  1.002   1.00   40.68  ? 647 HOH E O   1 
HETATM 18893 O O   . HOH YA 5 .   ? 155.002 34.545  -12.701 1.00   44.19  ? 648 HOH E O   1 
HETATM 18894 O O   . HOH YA 5 .   ? 137.619 29.950  -12.017 1.00   33.56  ? 649 HOH E O   1 
HETATM 18895 O O   . HOH YA 5 .   ? 162.780 15.302  -10.696 1.00   38.06  ? 650 HOH E O   1 
HETATM 18896 O O   . HOH YA 5 .   ? 144.466 34.953  3.848   1.00   34.33  ? 651 HOH E O   1 
HETATM 18897 O O   . HOH YA 5 .   ? 149.709 37.995  -17.889 0.50   22.10  ? 652 HOH E O   1 
HETATM 18898 O O   . HOH YA 5 .   ? 139.965 0.257   -18.589 1.00   43.98  ? 653 HOH E O   1 
HETATM 18899 O O   . HOH YA 5 .   ? 147.291 9.094   3.572   1.00   34.41  ? 654 HOH E O   1 
HETATM 18900 O O   . HOH YA 5 .   ? 120.492 19.025  -6.175  1.00   48.60  ? 655 HOH E O   1 
HETATM 18901 O O   . HOH YA 5 .   ? 119.886 11.926  -6.147  1.00   36.62  ? 656 HOH E O   1 
HETATM 18902 O O   . HOH YA 5 .   ? 154.664 32.179  -19.329 1.00   46.18  ? 657 HOH E O   1 
HETATM 18903 O O   . HOH YA 5 .   ? 164.780 27.972  -20.079 1.00   40.33  ? 658 HOH E O   1 
HETATM 18904 O O   . HOH YA 5 .   ? 132.619 23.578  -2.555  1.00   39.83  ? 659 HOH E O   1 
HETATM 18905 O O   . HOH YA 5 .   ? 124.169 20.776  -9.601  1.00   47.43  ? 660 HOH E O   1 
HETATM 18906 O O   . HOH YA 5 .   ? 132.165 42.775  -16.377 1.00   43.53  ? 661 HOH E O   1 
HETATM 18907 O O   . HOH YA 5 .   ? 135.858 48.522  -10.273 1.00   44.78  ? 662 HOH E O   1 
HETATM 18908 O O   . HOH YA 5 .   ? 164.748 34.950  -10.022 1.00   39.14  ? 663 HOH E O   1 
HETATM 18909 O O   . HOH YA 5 .   ? 132.641 32.192  -0.685  1.00   57.10  ? 664 HOH E O   1 
HETATM 18910 O O   . HOH YA 5 .   ? 121.551 19.038  -3.847  1.00   45.33  ? 665 HOH E O   1 
HETATM 18911 O O   . HOH YA 5 .   ? 151.170 37.450  -15.994 0.50   19.55  ? 666 HOH E O   1 
HETATM 18912 O O   . HOH YA 5 .   ? 133.795 21.654  -14.006 1.00   46.11  ? 667 HOH E O   1 
HETATM 18913 O O   . HOH YA 5 .   ? 165.718 26.835  -17.979 1.00   38.58  ? 668 HOH E O   1 
HETATM 18914 O O   . HOH YA 5 .   ? 150.886 37.862  -13.902 0.50   25.26  ? 669 HOH E O   1 
HETATM 18915 O O   . HOH YA 5 .   ? 113.931 15.526  -8.569  1.00   45.04  ? 670 HOH E O   1 
HETATM 18916 O O   . HOH YA 5 .   ? 136.780 4.622   -4.823  0.50   25.56  ? 671 HOH E O   1 
HETATM 18917 O O   . HOH YA 5 .   ? 136.956 -0.390  -6.340  1.00   46.88  ? 672 HOH E O   1 
HETATM 18918 O O   . HOH YA 5 .   ? 154.605 21.556  1.602   1.00   45.50  ? 673 HOH E O   1 
HETATM 18919 O O   . HOH YA 5 .   ? 168.610 30.631  -8.012  1.00   44.50  ? 674 HOH E O   1 
HETATM 18920 O O   . HOH YA 5 .   ? 166.569 21.606  -8.298  1.00   51.59  ? 675 HOH E O   1 
HETATM 18921 O O   . HOH YA 5 .   ? 166.310 19.234  -15.297 1.00   61.18  ? 676 HOH E O   1 
HETATM 18922 O O   . HOH YA 5 .   ? 134.841 -0.116  -13.497 1.00   53.53  ? 677 HOH E O   1 
HETATM 18923 O O   . HOH YA 5 .   ? 147.233 40.566  4.979   1.00   47.35  ? 678 HOH E O   1 
HETATM 18924 O O   . HOH YA 5 .   ? 147.194 46.637  -20.401 1.00   56.73  ? 679 HOH E O   1 
HETATM 18925 O O   . HOH YA 5 .   ? 121.607 19.627  -9.206  1.00   64.25  ? 680 HOH E O   1 
HETATM 18926 O O   . HOH YA 5 .   ? 140.529 36.915  -20.141 1.00   41.45  ? 681 HOH E O   1 
HETATM 18927 O O   . HOH YA 5 .   ? 136.332 3.241   -7.638  1.00   36.35  ? 682 HOH E O   1 
HETATM 18928 O O   . HOH YA 5 .   ? 147.361 10.485  -18.005 0.50   31.92  ? 683 HOH E O   1 
HETATM 18929 O O   . HOH YA 5 .   ? 145.250 10.128  -17.600 0.50   28.41  ? 684 HOH E O   1 
HETATM 18930 O O   . HOH YA 5 .   ? 157.600 42.267  2.470   1.00   57.01  ? 685 HOH E O   1 
HETATM 18931 O O   . HOH YA 5 .   ? 159.395 35.953  0.305   1.00   53.59  ? 686 HOH E O   1 
HETATM 18932 O O   . HOH YA 5 .   ? 131.559 9.685   -27.161 1.00   49.12  ? 687 HOH E O   1 
HETATM 18933 O O   . HOH YA 5 .   ? 159.442 7.541   -7.388  1.00   49.45  ? 688 HOH E O   1 
HETATM 18934 O O   . HOH YA 5 .   ? 156.242 5.804   -5.232  1.00   63.77  ? 689 HOH E O   1 
HETATM 18935 O O   . HOH YA 5 .   ? 153.241 28.472  -27.336 1.00   63.40  ? 690 HOH E O   1 
HETATM 18936 O O   . HOH YA 5 .   ? 147.335 33.847  -26.379 1.00   51.89  ? 691 HOH E O   1 
HETATM 18937 O O   . HOH YA 5 .   ? 138.923 35.137  -13.909 1.00   49.59  ? 692 HOH E O   1 
HETATM 18938 O O   . HOH YA 5 .   ? 138.311 31.827  -14.255 1.00   48.37  ? 693 HOH E O   1 
HETATM 18939 O O   . HOH YA 5 .   ? 140.875 18.250  -2.251  0.30   4.67   ? 694 HOH E O   1 
HETATM 18940 O O   . HOH YA 5 .   ? 155.525 27.788  -27.679 1.00   36.70  ? 695 HOH E O   1 
HETATM 18941 O O   . HOH YA 5 .   ? 148.442 15.385  -22.101 1.00   47.08  ? 696 HOH E O   1 
HETATM 18942 O O   . HOH YA 5 .   ? 144.379 33.933  1.622   1.00   56.12  ? 697 HOH E O   1 
HETATM 18943 O O   . HOH YA 5 .   ? 128.567 1.740   -23.691 1.00   49.15  ? 698 HOH E O   1 
HETATM 18944 O O   . HOH YA 5 .   ? 137.034 27.764  -13.471 1.00   59.85  ? 699 HOH E O   1 
HETATM 18945 O O   . HOH YA 5 .   ? 137.714 31.989  -16.823 1.00   55.18  ? 700 HOH E O   1 
HETATM 18946 O O   . HOH YA 5 .   ? 143.838 20.653  -28.717 1.00   43.99  ? 701 HOH E O   1 
HETATM 18947 O O   . HOH YA 5 .   ? 144.910 -0.096  -10.749 1.00   45.57  ? 702 HOH E O   1 
HETATM 18948 O O   . HOH ZA 5 .   ? 123.027 81.925  1.810   0.50   15.17  ? 601 HOH F O   1 
HETATM 18949 O O   . HOH ZA 5 .   ? 122.304 80.817  0.050   0.50   19.01  ? 602 HOH F O   1 
HETATM 18950 O O   . HOH ZA 5 .   ? 120.191 71.741  13.979  1.00   23.47  ? 603 HOH F O   1 
HETATM 18951 O O   . HOH ZA 5 .   ? 108.650 68.715  17.302  1.00   25.58  ? 604 HOH F O   1 
HETATM 18952 O O   . HOH ZA 5 .   ? 141.428 73.086  11.182  1.00   31.07  ? 605 HOH F O   1 
HETATM 18953 O O   . HOH ZA 5 .   ? 140.295 74.226  18.762  1.00   27.38  ? 606 HOH F O   1 
HETATM 18954 O O   . HOH ZA 5 .   ? 143.840 62.967  12.205  1.00   30.58  ? 607 HOH F O   1 
HETATM 18955 O O   . HOH ZA 5 .   ? 135.446 67.106  17.897  1.00   26.28  ? 608 HOH F O   1 
HETATM 18956 O O   . HOH ZA 5 .   ? 139.651 65.922  -4.097  1.00   26.12  ? 609 HOH F O   1 
HETATM 18957 O O   . HOH ZA 5 .   ? 119.412 68.396  8.971   1.00   23.01  ? 610 HOH F O   1 
HETATM 18958 O O   . HOH ZA 5 .   ? 139.294 54.492  7.609   1.00   36.29  ? 611 HOH F O   1 
HETATM 18959 O O   . HOH ZA 5 .   ? 134.621 80.905  5.450   1.00   29.18  ? 612 HOH F O   1 
HETATM 18960 O O   . HOH ZA 5 .   ? 132.765 64.559  12.122  1.00   27.87  ? 613 HOH F O   1 
HETATM 18961 O O   . HOH ZA 5 .   ? 126.024 64.041  16.204  1.00   32.82  ? 614 HOH F O   1 
HETATM 18962 O O   . HOH ZA 5 .   ? 117.635 66.858  8.986   1.00   41.15  ? 615 HOH F O   1 
HETATM 18963 O O   . HOH ZA 5 .   ? 104.824 74.073  14.437  1.00   34.28  ? 616 HOH F O   1 
HETATM 18964 O O   . HOH ZA 5 .   ? 124.454 65.571  14.837  1.00   32.05  ? 617 HOH F O   1 
HETATM 18965 O O   . HOH ZA 5 .   ? 142.202 82.623  15.406  1.00   37.33  ? 618 HOH F O   1 
HETATM 18966 O O   . HOH ZA 5 .   ? 129.498 86.303  3.872   1.00   30.79  ? 619 HOH F O   1 
HETATM 18967 O O   . HOH ZA 5 .   ? 114.448 70.247  3.795   1.00   32.25  ? 620 HOH F O   1 
HETATM 18968 O O   . HOH ZA 5 .   ? 118.295 85.521  24.183  1.00   33.99  ? 621 HOH F O   1 
HETATM 18969 O O   . HOH ZA 5 .   ? 118.786 65.047  10.960  1.00   28.21  ? 622 HOH F O   1 
HETATM 18970 O O   . HOH ZA 5 .   ? 111.560 80.221  19.018  1.00   30.05  ? 623 HOH F O   1 
HETATM 18971 O O   . HOH ZA 5 .   ? 130.173 82.857  18.895  1.00   28.56  ? 624 HOH F O   1 
HETATM 18972 O O   . HOH ZA 5 .   ? 117.690 64.830  6.522   1.00   32.07  ? 625 HOH F O   1 
HETATM 18973 O O   . HOH ZA 5 .   ? 125.609 74.080  3.636   1.00   18.68  ? 626 HOH F O   1 
HETATM 18974 O O   . HOH ZA 5 .   ? 111.499 69.701  21.756  1.00   35.12  ? 627 HOH F O   1 
HETATM 18975 O O   . HOH ZA 5 .   ? 120.731 77.592  3.926   1.00   43.07  ? 628 HOH F O   1 
HETATM 18976 O O   . HOH ZA 5 .   ? 110.354 78.610  12.746  1.00   33.49  ? 629 HOH F O   1 
HETATM 18977 O O   . HOH ZA 5 .   ? 131.630 61.608  10.627  1.00   35.06  ? 630 HOH F O   1 
HETATM 18978 O O   . HOH ZA 5 .   ? 142.778 87.763  10.205  1.00   37.02  ? 631 HOH F O   1 
HETATM 18979 O O   . HOH ZA 5 .   ? 118.011 76.818  30.668  1.00   36.47  ? 632 HOH F O   1 
HETATM 18980 O O   . HOH ZA 5 .   ? 133.851 60.127  12.068  1.00   35.11  ? 633 HOH F O   1 
HETATM 18981 O O   . HOH ZA 5 .   ? 116.421 78.505  11.377  1.00   36.08  ? 634 HOH F O   1 
HETATM 18982 O O   . HOH ZA 5 .   ? 126.638 62.628  8.177   1.00   34.51  ? 635 HOH F O   1 
HETATM 18983 O O   . HOH ZA 5 .   ? 117.758 80.844  30.070  1.00   39.86  ? 636 HOH F O   1 
HETATM 18984 O O   . HOH ZA 5 .   ? 114.847 82.344  12.878  1.00   45.05  ? 637 HOH F O   1 
HETATM 18985 O O   . HOH ZA 5 .   ? 146.818 77.551  18.300  1.00   37.18  ? 638 HOH F O   1 
HETATM 18986 O O   . HOH ZA 5 .   ? 140.935 89.226  13.342  1.00   36.04  ? 639 HOH F O   1 
HETATM 18987 O O   . HOH ZA 5 .   ? 127.367 57.796  -0.633  1.00   33.49  ? 640 HOH F O   1 
HETATM 18988 O O   . HOH ZA 5 .   ? 106.223 66.179  10.207  1.00   32.71  ? 641 HOH F O   1 
HETATM 18989 O O   . HOH ZA 5 .   ? 123.377 72.048  4.911   1.00   39.04  ? 642 HOH F O   1 
HETATM 18990 O O   . HOH ZA 5 .   ? 118.697 74.806  23.829  1.00   30.94  ? 643 HOH F O   1 
HETATM 18991 O O   . HOH ZA 5 .   ? 108.454 67.766  2.963   1.00   36.13  ? 644 HOH F O   1 
HETATM 18992 O O   . HOH ZA 5 .   ? 118.828 61.982  11.376  1.00   38.00  ? 645 HOH F O   1 
HETATM 18993 O O   . HOH ZA 5 .   ? 122.107 71.222  2.806   1.00   45.44  ? 646 HOH F O   1 
HETATM 18994 O O   . HOH ZA 5 .   ? 117.637 79.758  9.428   1.00   31.47  ? 647 HOH F O   1 
HETATM 18995 O O   . HOH ZA 5 .   ? 138.356 90.220  19.664  1.00   41.32  ? 648 HOH F O   1 
HETATM 18996 O O   . HOH ZA 5 .   ? 113.577 63.937  23.699  0.50   26.54  ? 649 HOH F O   1 
HETATM 18997 O O   . HOH ZA 5 .   ? 132.567 88.212  5.175   1.00   32.70  ? 650 HOH F O   1 
HETATM 18998 O O   . HOH ZA 5 .   ? 116.926 74.344  4.766   1.00   45.29  ? 651 HOH F O   1 
HETATM 18999 O O   . HOH ZA 5 .   ? 126.987 62.212  13.415  1.00   35.86  ? 652 HOH F O   1 
HETATM 19000 O O   . HOH ZA 5 .   ? 136.095 64.426  -3.837  1.00   33.09  ? 653 HOH F O   1 
HETATM 19001 O O   . HOH ZA 5 .   ? 128.947 81.240  20.741  0.50   27.82  ? 654 HOH F O   1 
HETATM 19002 O O   . HOH ZA 5 .   ? 143.186 68.025  -6.472  1.00   39.00  ? 655 HOH F O   1 
HETATM 19003 O O   . HOH ZA 5 .   ? 141.919 74.272  21.311  1.00   37.51  ? 656 HOH F O   1 
HETATM 19004 O O   . HOH ZA 5 .   ? 125.270 79.984  31.097  1.00   41.71  ? 657 HOH F O   1 
HETATM 19005 O O   . HOH ZA 5 .   ? 140.827 93.188  5.518   1.00   62.39  ? 658 HOH F O   1 
HETATM 19006 O O   . HOH ZA 5 .   ? 134.061 80.772  -3.884  1.00   38.34  ? 659 HOH F O   1 
HETATM 19007 O O   . HOH ZA 5 .   ? 143.002 91.210  10.514  1.00   45.30  ? 660 HOH F O   1 
HETATM 19008 O O   . HOH ZA 5 .   ? 144.276 56.181  -5.968  1.00   40.47  ? 661 HOH F O   1 
HETATM 19009 O O   . HOH ZA 5 .   ? 126.219 57.692  25.607  0.50   29.03  ? 662 HOH F O   1 
HETATM 19010 O O   . HOH ZA 5 .   ? 136.694 59.217  18.683  1.00   47.08  ? 663 HOH F O   1 
HETATM 19011 O O   . HOH ZA 5 .   ? 142.960 85.415  19.527  1.00   44.05  ? 664 HOH F O   1 
HETATM 19012 O O   . HOH ZA 5 .   ? 129.667 77.311  -8.187  1.00   55.44  ? 665 HOH F O   1 
HETATM 19013 O O   . HOH ZA 5 .   ? 115.462 60.943  11.528  0.50   24.58  ? 666 HOH F O   1 
HETATM 19014 O O   . HOH ZA 5 .   ? 129.025 64.328  28.978  0.50   32.81  ? 667 HOH F O   1 
HETATM 19015 O O   . HOH ZA 5 .   ? 130.189 90.070  10.863  1.00   41.96  ? 668 HOH F O   1 
HETATM 19016 O O   . HOH ZA 5 .   ? 115.103 86.601  22.719  1.00   46.45  ? 669 HOH F O   1 
HETATM 19017 O O   . HOH ZA 5 .   ? 125.528 72.433  0.035   1.00   38.82  ? 670 HOH F O   1 
HETATM 19018 O O   . HOH ZA 5 .   ? 116.073 81.520  7.069   0.50   22.12  ? 671 HOH F O   1 
HETATM 19019 O O   . HOH ZA 5 .   ? 104.419 58.720  12.535  1.00   38.31  ? 672 HOH F O   1 
HETATM 19020 O O   . HOH ZA 5 .   ? 115.701 82.046  9.321   1.00   54.00  ? 673 HOH F O   1 
HETATM 19021 O O   . HOH ZA 5 .   ? 136.586 64.111  -6.076  1.00   44.99  ? 674 HOH F O   1 
HETATM 19022 O O   . HOH ZA 5 .   ? 148.849 79.150  2.986   1.00   36.64  ? 675 HOH F O   1 
HETATM 19023 O O   . HOH ZA 5 .   ? 138.837 99.388  6.217   1.00   41.37  ? 676 HOH F O   1 
HETATM 19024 O O   . HOH ZA 5 .   ? 150.831 76.780  14.314  1.00   34.74  ? 677 HOH F O   1 
HETATM 19025 O O   . HOH ZA 5 .   ? 161.582 56.424  -0.709  1.00   55.47  ? 678 HOH F O   1 
HETATM 19026 O O   . HOH ZA 5 .   ? 147.950 67.958  15.832  1.00   41.49  ? 679 HOH F O   1 
HETATM 19027 O O   . HOH ZA 5 .   ? 146.110 50.567  15.018  1.00   40.72  ? 680 HOH F O   1 
HETATM 19028 O O   . HOH ZA 5 .   ? 137.181 65.114  28.942  1.00   54.64  ? 681 HOH F O   1 
HETATM 19029 O O   . HOH ZA 5 .   ? 119.431 87.213  27.005  1.00   37.78  ? 682 HOH F O   1 
HETATM 19030 O O   . HOH ZA 5 .   ? 120.275 89.641  16.478  1.00   34.81  ? 683 HOH F O   1 
HETATM 19031 O O   . HOH ZA 5 .   ? 131.949 79.412  21.359  1.00   40.90  ? 684 HOH F O   1 
HETATM 19032 O O   . HOH ZA 5 .   ? 130.870 59.668  9.395   1.00   48.21  ? 685 HOH F O   1 
HETATM 19033 O O   . HOH ZA 5 .   ? 125.289 61.279  10.017  1.00   36.17  ? 686 HOH F O   1 
HETATM 19034 O O   . HOH ZA 5 .   ? 135.526 71.470  -7.335  1.00   44.87  ? 687 HOH F O   1 
HETATM 19035 O O   . HOH ZA 5 .   ? 137.958 59.727  21.514  0.50   27.84  ? 688 HOH F O   1 
HETATM 19036 O O   . HOH ZA 5 .   ? 142.360 93.115  16.448  1.00   46.21  ? 689 HOH F O   1 
HETATM 19037 O O   . HOH ZA 5 .   ? 121.692 52.660  19.535  1.00   38.78  ? 690 HOH F O   1 
HETATM 19038 O O   . HOH ZA 5 .   ? 112.861 60.698  11.416  1.00   45.71  ? 691 HOH F O   1 
HETATM 19039 O O   . HOH ZA 5 .   ? 148.338 72.497  5.567   1.00   53.71  ? 692 HOH F O   1 
HETATM 19040 O O   . HOH ZA 5 .   ? 141.097 56.149  -0.139  1.00   38.00  ? 693 HOH F O   1 
HETATM 19041 O O   . HOH ZA 5 .   ? 141.429 58.042  -1.695  1.00   37.94  ? 694 HOH F O   1 
HETATM 19042 O O   . HOH ZA 5 .   ? 116.629 76.101  34.931  1.00   39.75  ? 695 HOH F O   1 
HETATM 19043 O O   . HOH ZA 5 .   ? 140.365 66.564  29.340  1.00   47.52  ? 696 HOH F O   1 
HETATM 19044 O O   . HOH ZA 5 .   ? 137.034 54.928  0.640   1.00   39.38  ? 697 HOH F O   1 
HETATM 19045 O O   . HOH ZA 5 .   ? 111.181 77.006  30.251  0.50   24.37  ? 698 HOH F O   1 
HETATM 19046 O O   . HOH ZA 5 .   ? 118.857 80.785  32.399  1.00   35.79  ? 699 HOH F O   1 
HETATM 19047 O O   . HOH ZA 5 .   ? 149.211 87.137  14.071  1.00   52.11  ? 700 HOH F O   1 
HETATM 19048 O O   . HOH ZA 5 .   ? 118.768 71.198  29.478  1.00   30.33  ? 701 HOH F O   1 
HETATM 19049 O O   . HOH ZA 5 .   ? 150.984 71.776  1.749   1.00   41.25  ? 702 HOH F O   1 
HETATM 19050 O O   . HOH ZA 5 .   ? 139.924 74.916  -7.551  1.00   55.11  ? 703 HOH F O   1 
HETATM 19051 O O   . HOH ZA 5 .   ? 137.105 55.181  9.023   1.00   34.81  ? 704 HOH F O   1 
HETATM 19052 O O   . HOH ZA 5 .   ? 143.589 66.975  19.687  1.00   58.83  ? 705 HOH F O   1 
HETATM 19053 O O   . HOH ZA 5 .   ? 140.528 46.920  3.969   1.00   36.88  ? 706 HOH F O   1 
HETATM 19054 O O   . HOH ZA 5 .   ? 121.649 82.842  31.498  1.00   53.40  ? 707 HOH F O   1 
HETATM 19055 O O   . HOH ZA 5 .   ? 112.413 82.546  30.950  1.00   46.87  ? 708 HOH F O   1 
HETATM 19056 O O   . HOH ZA 5 .   ? 110.292 76.283  28.563  0.50   30.56  ? 709 HOH F O   1 
HETATM 19057 O O   . HOH ZA 5 .   ? 146.439 67.923  20.033  1.00   41.82  ? 710 HOH F O   1 
HETATM 19058 O O   . HOH ZA 5 .   ? 135.000 57.492  10.437  1.00   49.68  ? 711 HOH F O   1 
HETATM 19059 O O   . HOH ZA 5 .   ? 143.110 81.896  -2.422  1.00   41.28  ? 712 HOH F O   1 
HETATM 19060 O O   . HOH ZA 5 .   ? 132.372 96.355  11.230  1.00   40.20  ? 713 HOH F O   1 
HETATM 19061 O O   . HOH ZA 5 .   ? 134.533 94.531  19.517  1.00   53.63  ? 714 HOH F O   1 
HETATM 19062 O O   . HOH ZA 5 .   ? 137.922 102.533 5.515   1.00   52.82  ? 715 HOH F O   1 
HETATM 19063 O O   . HOH ZA 5 .   ? 136.466 59.786  23.120  0.50   24.28  ? 716 HOH F O   1 
HETATM 19064 O O   . HOH ZA 5 .   ? 140.418 57.977  21.367  1.00   60.27  ? 717 HOH F O   1 
HETATM 19065 O O   . HOH ZA 5 .   ? 152.589 46.366  8.506   1.00   43.67  ? 718 HOH F O   1 
HETATM 19066 O O   . HOH ZA 5 .   ? 150.999 53.410  13.659  1.00   48.94  ? 719 HOH F O   1 
HETATM 19067 O O   . HOH ZA 5 .   ? 139.197 71.684  26.431  1.00   42.69  ? 720 HOH F O   1 
HETATM 19068 O O   . HOH ZA 5 .   ? 123.492 80.880  32.337  1.00   65.77  ? 721 HOH F O   1 
HETATM 19069 O O   . HOH ZA 5 .   ? 112.822 85.514  29.544  0.50   32.89  ? 722 HOH F O   1 
HETATM 19070 O O   . HOH ZA 5 .   ? 110.454 86.084  25.435  1.00   38.86  ? 723 HOH F O   1 
HETATM 19071 O O   . HOH ZA 5 .   ? 107.538 80.809  23.369  1.00   52.47  ? 724 HOH F O   1 
HETATM 19072 O O   . HOH ZA 5 .   ? 150.317 74.505  10.062  1.00   47.06  ? 725 HOH F O   1 
HETATM 19073 O O   . HOH ZA 5 .   ? 120.778 60.086  10.573  0.50   26.85  ? 726 HOH F O   1 
HETATM 19074 O O   . HOH ZA 5 .   ? 141.757 56.414  -4.852  1.00   60.66  ? 727 HOH F O   1 
HETATM 19075 O O   . HOH ZA 5 .   ? 114.740 62.360  10.156  0.50   26.68  ? 728 HOH F O   1 
HETATM 19076 O O   . HOH ZA 5 .   ? 139.054 72.800  -6.983  1.00   46.57  ? 729 HOH F O   1 
HETATM 19077 O O   . HOH ZA 5 .   ? 142.468 75.891  -7.353  0.50   28.28  ? 730 HOH F O   1 
HETATM 19078 O O   . HOH ZA 5 .   ? 143.280 70.763  -7.308  1.00   38.62  ? 731 HOH F O   1 
HETATM 19079 O O   . HOH ZA 5 .   ? 150.726 72.066  -2.786  1.00   55.07  ? 732 HOH F O   1 
HETATM 19080 O O   . HOH ZA 5 .   ? 145.257 87.944  15.617  1.00   38.30  ? 733 HOH F O   1 
HETATM 19081 O O   . HOH ZA 5 .   ? 105.556 68.104  7.577   1.00   45.36  ? 734 HOH F O   1 
HETATM 19082 O O   . HOH ZA 5 .   ? 103.967 65.358  7.022   1.00   42.32  ? 735 HOH F O   1 
HETATM 19083 O O   . HOH ZA 5 .   ? 127.308 80.359  20.130  0.50   24.98  ? 736 HOH F O   1 
HETATM 19084 O O   . HOH ZA 5 .   ? 147.085 45.530  1.962   1.00   40.63  ? 737 HOH F O   1 
HETATM 19085 O O   . HOH ZA 5 .   ? 129.828 62.507  12.391  1.00   38.34  ? 738 HOH F O   1 
HETATM 19086 O O   . HOH ZA 5 .   ? 166.207 54.958  7.889   1.00   46.14  ? 739 HOH F O   1 
HETATM 19087 O O   . HOH ZA 5 .   ? 115.968 64.783  31.080  1.00   47.84  ? 740 HOH F O   1 
HETATM 19088 O O   . HOH ZA 5 .   ? 127.406 81.470  -1.562  1.00   35.09  ? 741 HOH F O   1 
HETATM 19089 O O   . HOH ZA 5 .   ? 121.725 72.875  29.853  1.00   39.36  ? 742 HOH F O   1 
HETATM 19090 O O   . HOH ZA 5 .   ? 149.687 85.685  7.162   1.00   47.58  ? 743 HOH F O   1 
HETATM 19091 O O   . HOH ZA 5 .   ? 148.226 68.222  8.727   1.00   38.60  ? 744 HOH F O   1 
HETATM 19092 O O   . HOH ZA 5 .   ? 118.938 88.334  14.003  1.00   46.33  ? 745 HOH F O   1 
HETATM 19093 O O   . HOH ZA 5 .   ? 113.650 86.413  19.851  1.00   46.78  ? 746 HOH F O   1 
HETATM 19094 O O   . HOH ZA 5 .   ? 123.478 92.404  17.881  1.00   41.93  ? 747 HOH F O   1 
HETATM 19095 O O   . HOH ZA 5 .   ? 146.988 61.572  13.710  1.00   34.22  ? 748 HOH F O   1 
HETATM 19096 O O   . HOH ZA 5 .   ? 130.367 62.490  28.222  1.00   61.97  ? 749 HOH F O   1 
HETATM 19097 O O   . HOH ZA 5 .   ? 133.513 71.410  29.118  0.50   23.58  ? 750 HOH F O   1 
HETATM 19098 O O   . HOH ZA 5 .   ? 134.440 69.592  28.686  0.50   31.40  ? 751 HOH F O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . LYS A 11  ? 0.7632 0.6533 1.3149 -0.0369 0.0653  -0.0447 11  LYS A N   
2     C CA  . LYS A 11  ? 0.7604 0.6557 1.2672 -0.0365 0.0539  -0.0596 11  LYS A CA  
3     C C   . LYS A 11  ? 0.7293 0.6154 1.2120 -0.0276 0.0533  -0.0589 11  LYS A C   
4     O O   . LYS A 11  ? 0.7171 0.6036 1.2014 -0.0251 0.0474  -0.0854 11  LYS A O   
5     C CB  . LYS A 11  ? 0.7895 0.6977 1.2990 -0.0414 0.0408  -0.0980 11  LYS A CB  
6     C CG  . LYS A 11  ? 0.8099 0.7325 1.3231 -0.0491 0.0367  -0.1006 11  LYS A CG  
7     C CD  . LYS A 11  ? 0.8329 0.7720 1.3527 -0.0521 0.0232  -0.1386 11  LYS A CD  
8     C CE  . LYS A 11  ? 0.8252 0.7802 1.3568 -0.0591 0.0193  -0.1414 11  LYS A CE  
9     N NZ  . LYS A 11  ? 0.8138 0.7917 1.3262 -0.0595 0.0030  -0.1722 11  LYS A NZ  
10    N N   . PRO A 12  ? 0.6873 0.5718 1.1424 -0.0211 0.0587  -0.0286 12  PRO A N   
11    C CA  . PRO A 12  ? 0.6337 0.5136 1.0700 -0.0112 0.0595  -0.0226 12  PRO A CA  
12    C C   . PRO A 12  ? 0.5703 0.4623 0.9636 -0.0064 0.0483  -0.0435 12  PRO A C   
13    O O   . PRO A 12  ? 0.5205 0.4285 0.8793 -0.0082 0.0402  -0.0504 12  PRO A O   
14    C CB  . PRO A 12  ? 0.6157 0.5005 1.0302 -0.0057 0.0661  0.0154  12  PRO A CB  
15    C CG  . PRO A 12  ? 0.6312 0.5292 1.0282 -0.0110 0.0642  0.0214  12  PRO A CG  
16    C CD  . PRO A 12  ? 0.6734 0.5673 1.1100 -0.0212 0.0637  0.0012  12  PRO A CD  
17    N N   . ASN A 13  ? 0.5551 0.4398 0.9526 0.0005  0.0495  -0.0508 13  ASN A N   
18    C CA  . ASN A 13  ? 0.5426 0.4392 0.9031 0.0066  0.0417  -0.0669 13  ASN A CA  
19    C C   . ASN A 13  ? 0.4488 0.3494 0.7816 0.0146  0.0437  -0.0441 13  ASN A C   
20    O O   . ASN A 13  ? 0.4549 0.3666 0.7574 0.0194  0.0385  -0.0530 13  ASN A O   
21    C CB  . ASN A 13  ? 0.6679 0.5581 1.0497 0.0098  0.0409  -0.0968 13  ASN A CB  
22    C CG  . ASN A 13  ? 0.8040 0.7023 1.1929 0.0041  0.0327  -0.1305 13  ASN A CG  
23    O OD1 . ASN A 13  ? 0.8699 0.7609 1.2990 -0.0024 0.0341  -0.1426 13  ASN A OD1 
24    N ND2 . ASN A 13  ? 0.8486 0.7678 1.1956 0.0063  0.0235  -0.1427 13  ASN A ND2 
25    N N   . LEU A 14  ? 0.3680 0.2620 0.7119 0.0166  0.0512  -0.0144 14  LEU A N   
26    C CA  . LEU A 14  ? 0.3301 0.2308 0.6503 0.0246  0.0517  0.0065  14  LEU A CA  
27    C C   . LEU A 14  ? 0.3464 0.2493 0.6659 0.0254  0.0568  0.0388  14  LEU A C   
28    O O   . LEU A 14  ? 0.3913 0.2831 0.7450 0.0243  0.0655  0.0522  14  LEU A O   
29    C CB  . LEU A 14  ? 0.3187 0.2098 0.6613 0.0326  0.0565  0.0038  14  LEU A CB  
30    C CG  . LEU A 14  ? 0.3106 0.2112 0.6325 0.0417  0.0556  0.0176  14  LEU A CG  
31    C CD1 . LEU A 14  ? 0.2944 0.2099 0.5803 0.0424  0.0476  0.0005  14  LEU A CD1 
32    C CD2 . LEU A 14  ? 0.3270 0.2145 0.6842 0.0496  0.0632  0.0184  14  LEU A CD2 
33    N N   . LEU A 15  ? 0.3268 0.2451 0.6083 0.0279  0.0518  0.0513  15  LEU A N   
34    C CA  . LEU A 15  ? 0.3242 0.2499 0.5976 0.0303  0.0553  0.0799  15  LEU A CA  
35    C C   . LEU A 15  ? 0.3152 0.2513 0.5729 0.0392  0.0533  0.0962  15  LEU A C   
36    O O   . LEU A 15  ? 0.3208 0.2615 0.5641 0.0413  0.0475  0.0843  15  LEU A O   
37    C CB  . LEU A 15  ? 0.3009 0.2385 0.5448 0.0248  0.0503  0.0781  15  LEU A CB  
38    C CG  . LEU A 15  ? 0.3132 0.2454 0.5691 0.0159  0.0501  0.0601  15  LEU A CG  
39    C CD1 . LEU A 15  ? 0.3007 0.2463 0.5231 0.0127  0.0444  0.0583  15  LEU A CD1 
40    C CD2 . LEU A 15  ? 0.2883 0.2097 0.5853 0.0129  0.0604  0.0712  15  LEU A CD2 
41    N N   . VAL A 16  ? 0.3117 0.2534 0.5742 0.0451  0.0585  0.1244  16  VAL A N   
42    C CA  . VAL A 16  ? 0.3567 0.3111 0.6083 0.0545  0.0559  0.1410  16  VAL A CA  
43    C C   . VAL A 16  ? 0.3868 0.3621 0.6111 0.0582  0.0534  0.1621  16  VAL A C   
44    O O   . VAL A 16  ? 0.3634 0.3402 0.5936 0.0586  0.0604  0.1785  16  VAL A O   
45    C CB  . VAL A 16  ? 0.3861 0.3295 0.6771 0.0629  0.0651  0.1567  16  VAL A CB  
46    C CG1 . VAL A 16  ? 0.3197 0.2799 0.6008 0.0737  0.0618  0.1756  16  VAL A CG1 
47    C CG2 . VAL A 16  ? 0.3641 0.2881 0.6815 0.0604  0.0673  0.1323  16  VAL A CG2 
48    N N   . LEU A 17  ? 0.4019 0.3947 0.5967 0.0607  0.0433  0.1595  17  LEU A N   
49    C CA  . LEU A 17  ? 0.3914 0.4076 0.5590 0.0655  0.0386  0.1752  17  LEU A CA  
50    C C   . LEU A 17  ? 0.3931 0.4257 0.5595 0.0752  0.0338  0.1888  17  LEU A C   
51    O O   . LEU A 17  ? 0.3760 0.4137 0.5341 0.0740  0.0255  0.1754  17  LEU A O   
52    C CB  . LEU A 17  ? 0.3640 0.3889 0.4980 0.0584  0.0292  0.1568  17  LEU A CB  
53    C CG  . LEU A 17  ? 0.3724 0.4228 0.4778 0.0634  0.0232  0.1678  17  LEU A CG  
54    C CD1 . LEU A 17  ? 0.4064 0.4627 0.5102 0.0671  0.0317  0.1866  17  LEU A CD1 
55    C CD2 . LEU A 17  ? 0.3395 0.3958 0.4183 0.0566  0.0130  0.1463  17  LEU A CD2 
56    N N   . PRO A 18  ? 0.4201 0.4627 0.5968 0.0855  0.0395  0.2171  18  PRO A N   
57    C CA  . PRO A 18  ? 0.4383 0.5015 0.6142 0.0968  0.0345  0.2338  18  PRO A CA  
58    C C   . PRO A 18  ? 0.4515 0.5431 0.5897 0.0972  0.0210  0.2286  18  PRO A C   
59    O O   . PRO A 18  ? 0.4168 0.5161 0.5321 0.0944  0.0203  0.2269  18  PRO A O   
60    C CB  . PRO A 18  ? 0.4644 0.5325 0.6567 0.1040  0.0459  0.2598  18  PRO A CB  
61    C CG  . PRO A 18  ? 0.4452 0.4867 0.6622 0.0970  0.0583  0.2570  18  PRO A CG  
62    C CD  . PRO A 18  ? 0.4175 0.4524 0.6127 0.0879  0.0524  0.2372  18  PRO A CD  
63    N N   . VAL A 19  ? 0.4303 0.5370 0.5647 0.1000  0.0108  0.2240  19  VAL A N   
64    C CA  . VAL A 19  ? 0.4173 0.5509 0.5213 0.0991  -0.0036 0.2148  19  VAL A CA  
65    C C   . VAL A 19  ? 0.3874 0.5495 0.4950 0.1116  -0.0103 0.2333  19  VAL A C   
66    O O   . VAL A 19  ? 0.3728 0.5278 0.5060 0.1163  -0.0044 0.2429  19  VAL A O   
67    C CB  . VAL A 19  ? 0.2967 0.4221 0.3937 0.0870  -0.0116 0.1848  19  VAL A CB  
68    C CG1 . VAL A 19  ? 0.2861 0.3859 0.3808 0.0767  -0.0051 0.1688  19  VAL A CG1 
69    C CG2 . VAL A 19  ? 0.3682 0.4880 0.4881 0.0880  -0.0118 0.1813  19  VAL A CG2 
70    N N   . GLN A 20  ? 0.3874 0.5807 0.4685 0.1146  -0.0219 0.2322  20  GLN A N   
71    C CA  . GLN A 20  ? 0.3547 0.5755 0.4341 0.1222  -0.0281 0.2406  20  GLN A CA  
72    C C   . GLN A 20  ? 0.4584 0.7054 0.5230 0.1196  -0.0467 0.2232  20  GLN A C   
73    O O   . GLN A 20  ? 0.4592 0.7136 0.5025 0.1140  -0.0552 0.2069  20  GLN A O   
74    C CB  . GLN A 20  ? 0.4254 0.6641 0.4888 0.1298  -0.0227 0.2566  20  GLN A CB  
75    C CG  . GLN A 20  ? 0.5266 0.7926 0.5924 0.1392  -0.0274 0.2683  20  GLN A CG  
76    C CD  . GLN A 20  ? 0.5981 0.8840 0.6520 0.1487  -0.0202 0.2874  20  GLN A CD  
77    O OE1 . GLN A 20  ? 0.5958 0.8670 0.6615 0.1505  -0.0044 0.3033  20  GLN A OE1 
78    N NE2 . GLN A 20  ? 0.6362 0.9578 0.6683 0.1548  -0.0317 0.2852  20  GLN A NE2 
79    N N   . GLU A 21  ? 0.4676 0.7297 0.5458 0.1235  -0.0528 0.2258  21  GLU A N   
80    C CA  . GLU A 21  ? 0.4737 0.7637 0.5433 0.1208  -0.0708 0.2096  21  GLU A CA  
81    C C   . GLU A 21  ? 0.4500 0.7717 0.4936 0.1271  -0.0786 0.2111  21  GLU A C   
82    O O   . GLU A 21  ? 0.4364 0.7668 0.4789 0.1369  -0.0713 0.2312  21  GLU A O   
83    C CB  . GLU A 21  ? 0.5081 0.8029 0.6054 0.1226  -0.0738 0.2118  21  GLU A CB  
84    C CG  . GLU A 21  ? 0.3392 0.6557 0.4397 0.1159  -0.0909 0.1918  21  GLU A CG  
85    C CD  . GLU A 21  ? 0.3968 0.7471 0.4919 0.1220  -0.1028 0.1935  21  GLU A CD  
86    O OE1 . GLU A 21  ? 0.4352 0.7938 0.5216 0.1322  -0.0975 0.2115  21  GLU A OE1 
87    O OE2 . GLU A 21  ? 0.4219 0.7917 0.5240 0.1167  -0.1172 0.1773  21  GLU A OE2 
88    N N   . ASP A 22  ? 0.4370 0.7764 0.4614 0.1214  -0.0930 0.1890  22  ASP A N   
89    C CA  . ASP A 22  ? 0.4494 0.8206 0.4499 0.1272  -0.1022 0.1853  22  ASP A CA  
90    C C   . ASP A 22  ? 0.4597 0.8554 0.4726 0.1277  -0.1170 0.1778  22  ASP A C   
91    O O   . ASP A 22  ? 0.4654 0.8626 0.4897 0.1180  -0.1285 0.1572  22  ASP A O   
92    C CB  . ASP A 22  ? 0.4593 0.8355 0.4330 0.1211  -0.1090 0.1623  22  ASP A CB  
93    C CG  . ASP A 22  ? 0.5048 0.9155 0.4542 0.1275  -0.1190 0.1544  22  ASP A CG  
94    O OD1 . ASP A 22  ? 0.5303 0.9537 0.4679 0.1389  -0.1107 0.1742  22  ASP A OD1 
95    O OD2 . ASP A 22  ? 0.5143 0.9398 0.4582 0.1210  -0.1348 0.1280  22  ASP A OD2 
96    N N   . ALA A 23  ? 0.4677 0.8834 0.4813 0.1389  -0.1163 0.1956  23  ALA A N   
97    C CA  . ALA A 23  ? 0.5041 0.9430 0.5333 0.1410  -0.1288 0.1931  23  ALA A CA  
98    C C   . ALA A 23  ? 0.5646 1.0275 0.5823 0.1341  -0.1488 0.1639  23  ALA A C   
99    O O   . ALA A 23  ? 0.5747 1.0444 0.6130 0.1271  -0.1606 0.1496  23  ALA A O   
100   C CB  . ALA A 23  ? 0.4997 0.9591 0.5272 0.1556  -0.1244 0.2180  23  ALA A CB  
101   N N   . SER A 24  ? 0.5974 1.0723 0.5846 0.1356  -0.1516 0.1541  24  SER A N   
102   C CA  . SER A 24  ? 0.6049 1.1022 0.5813 0.1296  -0.1699 0.1243  24  SER A CA  
103   C C   . SER A 24  ? 0.5475 1.0283 0.5407 0.1131  -0.1777 0.0975  24  SER A C   
104   O O   . SER A 24  ? 0.5388 1.0342 0.5490 0.1061  -0.1929 0.0790  24  SER A O   
105   C CB  . SER A 24  ? 0.6433 1.1526 0.5839 0.1349  -0.1678 0.1185  24  SER A CB  
106   O OG  . SER A 24  ? 0.6619 1.1887 0.5936 0.1281  -0.1844 0.0861  24  SER A OG  
107   N N   . THR A 25  ? 0.5061 0.9576 0.4968 0.1070  -0.1671 0.0961  25  THR A N   
108   C CA  . THR A 25  ? 0.4090 0.8459 0.4132 0.0920  -0.1729 0.0712  25  THR A CA  
109   C C   . THR A 25  ? 0.4280 0.8456 0.4649 0.0865  -0.1667 0.0803  25  THR A C   
110   O O   . THR A 25  ? 0.4224 0.8336 0.4796 0.0743  -0.1718 0.0627  25  THR A O   
111   C CB  . THR A 25  ? 0.4223 0.8410 0.4040 0.0882  -0.1659 0.0609  25  THR A CB  
112   O OG1 . THR A 25  ? 0.4220 0.8167 0.4022 0.0926  -0.1486 0.0845  25  THR A OG1 
113   C CG2 . THR A 25  ? 0.4361 0.8737 0.3850 0.0950  -0.1691 0.0526  25  THR A CG2 
114   N N   . GLY A 26  ? 0.4102 0.8173 0.4540 0.0955  -0.1537 0.1078  26  GLY A N   
115   C CA  . GLY A 26  ? 0.3883 0.7764 0.4624 0.0915  -0.1458 0.1160  26  GLY A CA  
116   C C   . GLY A 26  ? 0.3873 0.7466 0.4591 0.0855  -0.1349 0.1149  26  GLY A C   
117   O O   . GLY A 26  ? 0.3778 0.7106 0.4708 0.0792  -0.1249 0.1153  26  GLY A O   
118   N N   . LEU A 27  ? 0.4498 0.8030 0.4930 0.0856  -0.1325 0.1095  27  LEU A N   
119   C CA  . LEU A 27  ? 0.4122 0.7251 0.4487 0.0776  -0.1178 0.1042  27  LEU A CA  
120   C C   . LEU A 27  ? 0.3902 0.6874 0.4205 0.0871  -0.1021 0.1295  27  LEU A C   
121   O O   . LEU A 27  ? 0.4074 0.7253 0.4335 0.1004  -0.1022 0.1508  27  LEU A O   
122   C CB  . LEU A 27  ? 0.4452 0.7587 0.4582 0.0712  -0.1233 0.0818  27  LEU A CB  
123   C CG  . LEU A 27  ? 0.4584 0.7834 0.4810 0.0603  -0.1380 0.0536  27  LEU A CG  
124   C CD1 . LEU A 27  ? 0.4757 0.8023 0.4746 0.0569  -0.1425 0.0324  27  LEU A CD1 
125   C CD2 . LEU A 27  ? 0.4346 0.7312 0.4850 0.0477  -0.1316 0.0464  27  LEU A CD2 
126   N N   . HIS A 28  ? 0.3703 0.6312 0.4019 0.0802  -0.0884 0.1267  28  HIS A N   
127   C CA  . HIS A 28  ? 0.3543 0.5962 0.3877 0.0867  -0.0730 0.1475  28  HIS A CA  
128   C C   . HIS A 28  ? 0.3515 0.5820 0.3626 0.0844  -0.0666 0.1435  28  HIS A C   
129   O O   . HIS A 28  ? 0.3674 0.5907 0.3675 0.0750  -0.0702 0.1219  28  HIS A O   
130   C CB  . HIS A 28  ? 0.3291 0.5398 0.3876 0.0816  -0.0619 0.1477  28  HIS A CB  
131   C CG  . HIS A 28  ? 0.3343 0.5552 0.4173 0.0859  -0.0649 0.1549  28  HIS A CG  
132   N ND1 . HIS A 28  ? 0.3299 0.5447 0.4327 0.0954  -0.0556 0.1755  28  HIS A ND1 
133   C CD2 . HIS A 28  ? 0.2860 0.5234 0.3799 0.0821  -0.0757 0.1443  28  HIS A CD2 
134   C CE1 . HIS A 28  ? 0.3072 0.5350 0.4300 0.0982  -0.0605 0.1774  28  HIS A CE1 
135   N NE2 . HIS A 28  ? 0.3151 0.5575 0.4333 0.0899  -0.0727 0.1590  28  HIS A NE2 
136   N N   . TRP A 29  ? 0.3657 0.5952 0.3731 0.0935  -0.0562 0.1656  29  TRP A N   
137   C CA  . TRP A 29  ? 0.3681 0.5907 0.3565 0.0929  -0.0487 0.1654  29  TRP A CA  
138   C C   . TRP A 29  ? 0.3777 0.5786 0.3824 0.0964  -0.0317 0.1869  29  TRP A C   
139   O O   . TRP A 29  ? 0.3859 0.5819 0.4138 0.1018  -0.0269 0.2035  29  TRP A O   
140   C CB  . TRP A 29  ? 0.3945 0.6538 0.3544 0.1028  -0.0565 0.1698  29  TRP A CB  
141   C CG  . TRP A 29  ? 0.4405 0.7183 0.4051 0.1152  -0.0529 0.1944  29  TRP A CG  
142   C CD1 . TRP A 29  ? 0.4455 0.7418 0.4189 0.1192  -0.0616 0.1966  29  TRP A CD1 
143   C CD2 . TRP A 29  ? 0.4543 0.7297 0.4203 0.1228  -0.0372 0.2178  29  TRP A CD2 
144   N NE1 . TRP A 29  ? 0.4532 0.7590 0.4312 0.1295  -0.0525 0.2200  29  TRP A NE1 
145   C CE2 . TRP A 29  ? 0.4806 0.7743 0.4554 0.1317  -0.0372 0.2336  29  TRP A CE2 
146   C CE3 . TRP A 29  ? 0.4270 0.6883 0.3904 0.1227  -0.0228 0.2272  29  TRP A CE3 
147   C CZ2 . TRP A 29  ? 0.5074 0.8059 0.4889 0.1408  -0.0231 0.2588  29  TRP A CZ2 
148   C CZ3 . TRP A 29  ? 0.4413 0.7072 0.4136 0.1309  -0.0089 0.2513  29  TRP A CZ3 
149   C CH2 . TRP A 29  ? 0.5085 0.7932 0.4898 0.1401  -0.0089 0.2673  29  TRP A CH2 
150   N N   . ALA A 30  ? 0.3654 0.5526 0.3616 0.0929  -0.0226 0.1852  30  ALA A N   
151   C CA  . ALA A 30  ? 0.3642 0.5318 0.3789 0.0948  -0.0065 0.2039  30  ALA A CA  
152   C C   . ALA A 30  ? 0.4047 0.5820 0.4019 0.0992  0.0011  0.2144  30  ALA A C   
153   O O   . ALA A 30  ? 0.3501 0.5372 0.3218 0.0963  -0.0042 0.1982  30  ALA A O   
154   C CB  . ALA A 30  ? 0.3575 0.4906 0.3913 0.0827  -0.0010 0.1877  30  ALA A CB  
155   N N   . ASN A 31  ? 0.4557 0.6306 0.4692 0.1066  0.0147  0.2423  31  ASN A N   
156   C CA  . ASN A 31  ? 0.4993 0.6766 0.5068 0.1082  0.0268  0.2521  31  ASN A CA  
157   C C   . ASN A 31  ? 0.5124 0.6575 0.5374 0.0964  0.0350  0.2414  31  ASN A C   
158   O O   . ASN A 31  ? 0.5021 0.6226 0.5603 0.0922  0.0424  0.2454  31  ASN A O   
159   C CB  . ASN A 31  ? 0.3959 0.5811 0.4231 0.1162  0.0396  0.2767  31  ASN A CB  
160   C CG  . ASN A 31  ? 0.4729 0.6951 0.4772 0.1273  0.0343  0.2834  31  ASN A CG  
161   O OD1 . ASN A 31  ? 0.4867 0.7300 0.4587 0.1295  0.0275  0.2720  31  ASN A OD1 
162   N ND2 . ASN A 31  ? 0.5169 0.7480 0.5388 0.1347  0.0378  0.3009  31  ASN A ND2 
163   N N   . ILE A 32  ? 0.5129 0.6588 0.5179 0.0906  0.0336  0.2239  32  ILE A N   
164   C CA  . ILE A 32  ? 0.5020 0.6214 0.5235 0.0794  0.0406  0.2114  32  ILE A CA  
165   C C   . ILE A 32  ? 0.5029 0.6281 0.5287 0.0833  0.0550  0.2308  32  ILE A C   
166   O O   . ILE A 32  ? 0.5077 0.6587 0.5070 0.0919  0.0560  0.2393  32  ILE A O   
167   C CB  . ILE A 32  ? 0.5043 0.6187 0.5063 0.0703  0.0309  0.1807  32  ILE A CB  
168   C CG1 . ILE A 32  ? 0.5238 0.6387 0.5201 0.0678  0.0170  0.1646  32  ILE A CG1 
169   C CG2 . ILE A 32  ? 0.4908 0.5796 0.5124 0.0596  0.0366  0.1685  32  ILE A CG2 
170   C CD1 . ILE A 32  ? 0.5293 0.6214 0.5535 0.0624  0.0182  0.1616  32  ILE A CD1 
171   N N   . HIS A 33  ? 0.4868 0.5898 0.5469 0.0774  0.0665  0.2372  33  HIS A N   
172   C CA  . HIS A 33  ? 0.4834 0.5911 0.5544 0.0799  0.0816  0.2566  33  HIS A CA  
173   C C   . HIS A 33  ? 0.4812 0.5838 0.5430 0.0712  0.0813  0.2355  33  HIS A C   
174   O O   . HIS A 33  ? 0.4847 0.5660 0.5596 0.0600  0.0766  0.2132  33  HIS A O   
175   C CB  . HIS A 33  ? 0.5016 0.5890 0.6204 0.0773  0.0941  0.2732  33  HIS A CB  
176   C CG  . HIS A 33  ? 0.5542 0.6492 0.6865 0.0859  0.0947  0.2880  33  HIS A CG  
177   N ND1 . HIS A 33  ? 0.5815 0.6713 0.7118 0.0871  0.0846  0.2818  33  HIS A ND1 
178   C CD2 . HIS A 33  ? 0.5650 0.6743 0.7147 0.0944  0.1049  0.3098  33  HIS A CD2 
179   C CE1 . HIS A 33  ? 0.5854 0.6858 0.7305 0.0955  0.0886  0.2986  33  HIS A CE1 
180   N NE2 . HIS A 33  ? 0.5809 0.6931 0.7380 0.1001  0.1011  0.3163  33  HIS A NE2 
181   N N   . LYS A 34  ? 0.4717 0.5966 0.5091 0.0776  0.0859  0.2421  34  LYS A N   
182   C CA  . LYS A 34  ? 0.4506 0.5740 0.4774 0.0715  0.0860  0.2230  34  LYS A CA  
183   C C   . LYS A 34  ? 0.4862 0.6274 0.5119 0.0780  0.1014  0.2427  34  LYS A C   
184   O O   . LYS A 34  ? 0.5194 0.6792 0.5442 0.0889  0.1092  0.2675  34  LYS A O   
185   C CB  . LYS A 34  ? 0.4263 0.5592 0.4152 0.0720  0.0711  0.1974  34  LYS A CB  
186   C CG  . LYS A 34  ? 0.4155 0.5337 0.4063 0.0661  0.0573  0.1801  34  LYS A CG  
187   C CD  . LYS A 34  ? 0.4202 0.5387 0.3872 0.0620  0.0448  0.1519  34  LYS A CD  
188   C CE  . LYS A 34  ? 0.3985 0.5040 0.3714 0.0542  0.0477  0.1366  34  LYS A CE  
189   N NZ  . LYS A 34  ? 0.3687 0.4838 0.3131 0.0556  0.0392  0.1166  34  LYS A NZ  
190   N N   . ARG A 35  ? 0.4486 0.5849 0.4773 0.0715  0.1045  0.2287  35  ARG A N   
191   C CA  . ARG A 35  ? 0.4276 0.5831 0.4510 0.0776  0.1184  0.2421  35  ARG A CA  
192   C C   . ARG A 35  ? 0.4304 0.5814 0.4965 0.0764  0.1348  0.2673  35  ARG A C   
193   O O   . ARG A 35  ? 0.4417 0.5757 0.5409 0.0722  0.1358  0.2755  35  ARG A O   
194   C CB  . ARG A 35  ? 0.4231 0.6113 0.4057 0.0930  0.1176  0.2497  35  ARG A CB  
195   C CG  . ARG A 35  ? 0.4280 0.6213 0.3727 0.0936  0.1007  0.2217  35  ARG A CG  
196   C CD  . ARG A 35  ? 0.4556 0.6808 0.3629 0.1078  0.0950  0.2234  35  ARG A CD  
197   N NE  . ARG A 35  ? 0.4773 0.7015 0.3604 0.1055  0.0766  0.1979  35  ARG A NE  
198   C CZ  . ARG A 35  ? 0.5034 0.7530 0.3537 0.1147  0.0662  0.1875  35  ARG A CZ  
199   N NH1 . ARG A 35  ? 0.5231 0.7991 0.3620 0.1262  0.0709  0.1957  35  ARG A NH1 
200   N NH2 . ARG A 35  ? 0.4690 0.7141 0.3065 0.1101  0.0492  0.1625  35  ARG A NH2 
201   N N   . THR A 36  ? 0.4441 0.6088 0.5125 0.0798  0.1450  0.2726  36  THR A N   
202   C CA  . THR A 36  ? 0.4540 0.6197 0.5608 0.0812  0.1582  0.2931  36  THR A CA  
203   C C   . THR A 36  ? 0.4389 0.6358 0.5216 0.0967  0.1647  0.3070  36  THR A C   
204   O O   . THR A 36  ? 0.4748 0.6861 0.5327 0.1000  0.1661  0.2975  36  THR A O   
205   C CB  . THR A 36  ? 0.4432 0.5944 0.5856 0.0688  0.1651  0.2864  36  THR A CB  
206   O OG1 . THR A 36  ? 0.4480 0.5730 0.6114 0.0548  0.1579  0.2704  36  THR A OG1 
207   C CG2 . THR A 36  ? 0.4615 0.6118 0.6472 0.0701  0.1772  0.3071  36  THR A CG2 
208   N N   . PRO A 37  ? 0.5694 0.7785 0.6604 0.1071  0.1689  0.3291  37  PRO A N   
209   C CA  . PRO A 37  ? 0.5611 0.7555 0.6846 0.1053  0.1689  0.3417  37  PRO A CA  
210   C C   . PRO A 37  ? 0.5440 0.7308 0.6461 0.1035  0.1543  0.3288  37  PRO A C   
211   O O   . PRO A 37  ? 0.5539 0.7568 0.6115 0.1090  0.1445  0.3167  37  PRO A O   
212   C CB  . PRO A 37  ? 0.5626 0.7829 0.6904 0.1210  0.1783  0.3693  37  PRO A CB  
213   C CG  . PRO A 37  ? 0.5735 0.8245 0.6529 0.1325  0.1758  0.3647  37  PRO A CG  
214   C CD  . PRO A 37  ? 0.5882 0.8308 0.6555 0.1234  0.1745  0.3433  37  PRO A CD  
215   N N   . LEU A 38  ? 0.5022 0.6654 0.6374 0.0963  0.1528  0.3303  38  LEU A N   
216   C CA  . LEU A 38  ? 0.4860 0.6385 0.6073 0.0936  0.1397  0.3184  38  LEU A CA  
217   C C   . LEU A 38  ? 0.4684 0.6461 0.5627 0.1073  0.1341  0.3283  38  LEU A C   
218   O O   . LEU A 38  ? 0.4742 0.6665 0.5839 0.1170  0.1424  0.3505  38  LEU A O   
219   C CB  . LEU A 38  ? 0.5208 0.6436 0.6884 0.0842  0.1412  0.3182  38  LEU A CB  
220   C CG  . LEU A 38  ? 0.5366 0.6375 0.7002 0.0757  0.1289  0.2990  38  LEU A CG  
221   C CD1 . LEU A 38  ? 0.5263 0.6176 0.6715 0.0656  0.1228  0.2771  38  LEU A CD1 
222   C CD2 . LEU A 38  ? 0.5480 0.6231 0.7628 0.0685  0.1332  0.2993  38  LEU A CD2 
223   N N   . MET A 39  ? 0.4673 0.6506 0.5244 0.1079  0.1198  0.3117  39  MET A N   
224   C CA  . MET A 39  ? 0.5002 0.7087 0.5327 0.1197  0.1121  0.3171  39  MET A CA  
225   C C   . MET A 39  ? 0.4806 0.6809 0.4952 0.1154  0.0957  0.2991  39  MET A C   
226   O O   . MET A 39  ? 0.4560 0.6334 0.4719 0.1045  0.0905  0.2824  39  MET A O   
227   C CB  . MET A 39  ? 0.5506 0.7928 0.5463 0.1307  0.1121  0.3162  39  MET A CB  
228   C CG  . MET A 39  ? 0.5662 0.8068 0.5346 0.1252  0.1078  0.2928  39  MET A CG  
229   S SD  . MET A 39  ? 0.9205 1.1614 0.8503 0.1215  0.0866  0.2620  39  MET A SD  
230   C CE  . MET A 39  ? 0.6424 0.9256 0.5379 0.1374  0.0786  0.2616  39  MET A CE  
231   N N   . GLN A 40  ? 0.5069 0.7278 0.5064 0.1245  0.0876  0.3031  40  GLN A N   
232   C CA  . GLN A 40  ? 0.5582 0.7731 0.5470 0.1211  0.0721  0.2884  40  GLN A CA  
233   C C   . GLN A 40  ? 0.5602 0.7971 0.5060 0.1240  0.0570  0.2672  40  GLN A C   
234   O O   . GLN A 40  ? 0.5719 0.8392 0.4945 0.1339  0.0558  0.2685  40  GLN A O   
235   C CB  . GLN A 40  ? 0.6095 0.8296 0.6178 0.1274  0.0722  0.3049  40  GLN A CB  
236   C CG  . GLN A 40  ? 0.6484 0.8406 0.7033 0.1222  0.0845  0.3184  40  GLN A CG  
237   C CD  . GLN A 40  ? 0.7067 0.9035 0.7831 0.1288  0.0860  0.3343  40  GLN A CD  
238   O OE1 . GLN A 40  ? 0.6970 0.8912 0.7693 0.1281  0.0750  0.3261  40  GLN A OE1 
239   N NE2 . GLN A 40  ? 0.7700 0.9748 0.8715 0.1358  0.1002  0.3581  40  GLN A NE2 
240   N N   . VAL A 41  ? 0.5334 0.7542 0.4714 0.1151  0.0456  0.2465  41  VAL A N   
241   C CA  . VAL A 41  ? 0.5617 0.7982 0.4662 0.1151  0.0295  0.2218  41  VAL A CA  
242   C C   . VAL A 41  ? 0.4884 0.7216 0.3980 0.1126  0.0151  0.2142  41  VAL A C   
243   O O   . VAL A 41  ? 0.4339 0.6385 0.3662 0.1023  0.0143  0.2060  41  VAL A O   
244   C CB  . VAL A 41  ? 0.6202 0.8404 0.5158 0.1052  0.0283  0.1977  41  VAL A CB  
245   C CG1 . VAL A 41  ? 0.6446 0.8829 0.5085 0.1059  0.0135  0.1696  41  VAL A CG1 
246   C CG2 . VAL A 41  ? 0.6515 0.8704 0.5506 0.1068  0.0449  0.2102  41  VAL A CG2 
247   N N   . PRO A 42  ? 0.4696 0.7298 0.3646 0.1195  0.0045  0.2101  42  PRO A N   
248   C CA  . PRO A 42  ? 0.4887 0.7490 0.3896 0.1166  -0.0101 0.2006  42  PRO A CA  
249   C C   . PRO A 42  ? 0.4625 0.7168 0.3517 0.1067  -0.0239 0.1684  42  PRO A C   
250   O O   . PRO A 42  ? 0.4818 0.7551 0.3451 0.1085  -0.0312 0.1508  42  PRO A O   
251   C CB  . PRO A 42  ? 0.5311 0.8246 0.4212 0.1269  -0.0160 0.2057  42  PRO A CB  
252   C CG  . PRO A 42  ? 0.5200 0.8342 0.3873 0.1341  -0.0098 0.2060  42  PRO A CG  
253   C CD  . PRO A 42  ? 0.4866 0.7790 0.3650 0.1310  0.0069  0.2178  42  PRO A CD  
254   N N   . LEU A 43  ? 0.3971 0.6226 0.3100 0.0950  -0.0257 0.1569  43  LEU A N   
255   C CA  . LEU A 43  ? 0.4069 0.6183 0.3186 0.0827  -0.0347 0.1257  43  LEU A CA  
256   C C   . LEU A 43  ? 0.4072 0.6145 0.3368 0.0776  -0.0446 0.1183  43  LEU A C   
257   O O   . LEU A 43  ? 0.4221 0.6209 0.3722 0.0795  -0.0399 0.1345  43  LEU A O   
258   C CB  . LEU A 43  ? 0.3997 0.5785 0.3223 0.0728  -0.0242 0.1182  43  LEU A CB  
259   C CG  . LEU A 43  ? 0.4219 0.6011 0.3325 0.0757  -0.0131 0.1233  43  LEU A CG  
260   C CD1 . LEU A 43  ? 0.3195 0.4680 0.2472 0.0659  -0.0041 0.1175  43  LEU A CD1 
261   C CD2 . LEU A 43  ? 0.4270 0.6263 0.3093 0.0786  -0.0200 0.1054  43  LEU A CD2 
262   N N   . LEU A 44  ? 0.3755 0.5883 0.3003 0.0711  -0.0572 0.0939  44  LEU A N   
263   C CA  . LEU A 44  ? 0.3573 0.5675 0.3016 0.0654  -0.0658 0.0865  44  LEU A CA  
264   C C   . LEU A 44  ? 0.3586 0.5349 0.3248 0.0561  -0.0573 0.0844  44  LEU A C   
265   O O   . LEU A 44  ? 0.3625 0.5186 0.3266 0.0496  -0.0514 0.0747  44  LEU A O   
266   C CB  . LEU A 44  ? 0.3350 0.5583 0.2738 0.0596  -0.0803 0.0603  44  LEU A CB  
267   C CG  . LEU A 44  ? 0.3099 0.5333 0.2724 0.0532  -0.0887 0.0536  44  LEU A CG  
268   C CD1 . LEU A 44  ? 0.3219 0.5762 0.2859 0.0625  -0.0974 0.0659  44  LEU A CD1 
269   C CD2 . LEU A 44  ? 0.3378 0.5608 0.3052 0.0431  -0.0987 0.0263  44  LEU A CD2 
270   N N   . LEU A 45  ? 0.3614 0.5340 0.3483 0.0566  -0.0569 0.0932  45  LEU A N   
271   C CA  . LEU A 45  ? 0.3303 0.4758 0.3359 0.0488  -0.0502 0.0883  45  LEU A CA  
272   C C   . LEU A 45  ? 0.3147 0.4577 0.3256 0.0393  -0.0579 0.0680  45  LEU A C   
273   O O   . LEU A 45  ? 0.3297 0.4892 0.3496 0.0390  -0.0673 0.0647  45  LEU A O   
274   C CB  . LEU A 45  ? 0.3337 0.4769 0.3603 0.0542  -0.0457 0.1042  45  LEU A CB  
275   C CG  . LEU A 45  ? 0.3546 0.4760 0.4003 0.0484  -0.0398 0.0980  45  LEU A CG  
276   C CD1 . LEU A 45  ? 0.3692 0.4665 0.4132 0.0443  -0.0298 0.0941  45  LEU A CD1 
277   C CD2 . LEU A 45  ? 0.3786 0.5020 0.4454 0.0555  -0.0363 0.1124  45  LEU A CD2 
278   N N   . ASP A 46  ? 0.3195 0.4433 0.3273 0.0319  -0.0536 0.0558  46  ASP A N   
279   C CA  . ASP A 46  ? 0.2906 0.4090 0.3059 0.0231  -0.0583 0.0391  46  ASP A CA  
280   C C   . ASP A 46  ? 0.2678 0.3638 0.2947 0.0187  -0.0491 0.0390  46  ASP A C   
281   O O   . ASP A 46  ? 0.3082 0.3888 0.3282 0.0167  -0.0427 0.0359  46  ASP A O   
282   C CB  . ASP A 46  ? 0.3277 0.4470 0.3284 0.0199  -0.0623 0.0240  46  ASP A CB  
283   C CG  . ASP A 46  ? 0.3663 0.4794 0.3801 0.0109  -0.0667 0.0080  46  ASP A CG  
284   O OD1 . ASP A 46  ? 0.3812 0.4930 0.4146 0.0074  -0.0670 0.0099  46  ASP A OD1 
285   O OD2 . ASP A 46  ? 0.3814 0.4917 0.3879 0.0080  -0.0691 -0.0059 46  ASP A OD2 
286   N N   . LEU A 47  ? 0.2537 0.3509 0.2980 0.0184  -0.0485 0.0428  47  LEU A N   
287   C CA  . LEU A 47  ? 0.2701 0.3511 0.3236 0.0168  -0.0396 0.0436  47  LEU A CA  
288   C C   . LEU A 47  ? 0.2784 0.3472 0.3285 0.0105  -0.0373 0.0334  47  LEU A C   
289   O O   . LEU A 47  ? 0.3288 0.3844 0.3750 0.0107  -0.0301 0.0330  47  LEU A O   
290   C CB  . LEU A 47  ? 0.2676 0.3565 0.3404 0.0177  -0.0398 0.0478  47  LEU A CB  
291   C CG  . LEU A 47  ? 0.2475 0.3242 0.3282 0.0176  -0.0304 0.0475  47  LEU A CG  
292   C CD1 . LEU A 47  ? 0.2455 0.3104 0.3222 0.0228  -0.0228 0.0514  47  LEU A CD1 
293   C CD2 . LEU A 47  ? 0.2309 0.3191 0.3307 0.0193  -0.0304 0.0519  47  LEU A CD2 
294   N N   . ASN A 48  ? 0.2848 0.3591 0.3383 0.0053  -0.0437 0.0249  48  ASN A N   
295   C CA  . ASN A 48  ? 0.2685 0.3311 0.3241 0.0000  -0.0408 0.0175  48  ASN A CA  
296   C C   . ASN A 48  ? 0.3054 0.3619 0.3459 -0.0009 -0.0420 0.0095  48  ASN A C   
297   O O   . ASN A 48  ? 0.3440 0.3906 0.3869 -0.0043 -0.0396 0.0039  48  ASN A O   
298   C CB  . ASN A 48  ? 0.2650 0.3346 0.3408 -0.0057 -0.0454 0.0131  48  ASN A CB  
299   C CG  . ASN A 48  ? 0.2720 0.3472 0.3648 -0.0046 -0.0415 0.0219  48  ASN A CG  
300   O OD1 . ASN A 48  ? 0.2997 0.3671 0.3916 -0.0018 -0.0325 0.0278  48  ASN A OD1 
301   N ND2 . ASN A 48  ? 0.2528 0.3439 0.3613 -0.0061 -0.0484 0.0219  48  ASN A ND2 
302   N N   . GLY A 49  ? 0.3006 0.3640 0.3263 0.0032  -0.0446 0.0104  49  GLY A N   
303   C CA  . GLY A 49  ? 0.2950 0.3559 0.3061 0.0035  -0.0451 0.0027  49  GLY A CA  
304   C C   . GLY A 49  ? 0.3544 0.3993 0.3613 0.0035  -0.0364 0.0042  49  GLY A C   
305   O O   . GLY A 49  ? 0.3911 0.4306 0.3997 0.0055  -0.0306 0.0125  49  GLY A O   
306   N N   . LYS A 50  ? 0.3621 0.4005 0.3655 0.0015  -0.0361 -0.0052 50  LYS A N   
307   C CA  . LYS A 50  ? 0.3457 0.3714 0.3475 0.0016  -0.0290 -0.0045 50  LYS A CA  
308   C C   . LYS A 50  ? 0.3468 0.3727 0.3362 0.0055  -0.0245 -0.0006 50  LYS A C   
309   O O   . LYS A 50  ? 0.3365 0.3549 0.3271 0.0058  -0.0191 0.0019  50  LYS A O   
310   C CB  . LYS A 50  ? 0.3582 0.3769 0.3645 -0.0009 -0.0295 -0.0145 50  LYS A CB  
311   C CG  . LYS A 50  ? 0.3809 0.3950 0.4060 -0.0053 -0.0304 -0.0154 50  LYS A CG  
312   C CD  . LYS A 50  ? 0.4019 0.4062 0.4354 -0.0070 -0.0292 -0.0237 50  LYS A CD  
313   C CE  . LYS A 50  ? 0.4577 0.4583 0.5153 -0.0120 -0.0297 -0.0234 50  LYS A CE  
314   N NZ  . LYS A 50  ? 0.5081 0.4977 0.5813 -0.0142 -0.0283 -0.0312 50  LYS A NZ  
315   N N   . HIS A 51  ? 0.3299 0.3668 0.3087 0.0087  -0.0268 0.0002  51  HIS A N   
316   C CA  . HIS A 51  ? 0.3238 0.3632 0.2934 0.0128  -0.0211 0.0070  51  HIS A CA  
317   C C   . HIS A 51  ? 0.3302 0.3857 0.2900 0.0179  -0.0231 0.0141  51  HIS A C   
318   O O   . HIS A 51  ? 0.3292 0.3960 0.2865 0.0185  -0.0308 0.0102  51  HIS A O   
319   C CB  . HIS A 51  ? 0.3284 0.3647 0.2913 0.0134  -0.0180 -0.0010 51  HIS A CB  
320   C CG  . HIS A 51  ? 0.2972 0.3412 0.2514 0.0145  -0.0234 -0.0137 51  HIS A CG  
321   N ND1 . HIS A 51  ? 0.3278 0.3636 0.2899 0.0110  -0.0266 -0.0265 51  HIS A ND1 
322   C CD2 . HIS A 51  ? 0.2845 0.3447 0.2239 0.0194  -0.0262 -0.0166 51  HIS A CD2 
323   C CE1 . HIS A 51  ? 0.3061 0.3513 0.2606 0.0127  -0.0318 -0.0394 51  HIS A CE1 
324   N NE2 . HIS A 51  ? 0.2959 0.3577 0.2344 0.0182  -0.0321 -0.0343 51  HIS A NE2 
325   N N   . LEU A 52  ? 0.3061 0.3647 0.2617 0.0220  -0.0161 0.0250  52  LEU A N   
326   C CA  . LEU A 52  ? 0.3291 0.4055 0.2738 0.0290  -0.0159 0.0353  52  LEU A CA  
327   C C   . LEU A 52  ? 0.3538 0.4432 0.2796 0.0330  -0.0172 0.0261  52  LEU A C   
328   O O   . LEU A 52  ? 0.3780 0.4606 0.3016 0.0320  -0.0125 0.0194  52  LEU A O   
329   C CB  . LEU A 52  ? 0.3315 0.4054 0.2843 0.0319  -0.0058 0.0535  52  LEU A CB  
330   C CG  . LEU A 52  ? 0.3304 0.4226 0.2759 0.0406  -0.0026 0.0712  52  LEU A CG  
331   C CD1 . LEU A 52  ? 0.3281 0.4113 0.2943 0.0410  0.0056  0.0887  52  LEU A CD1 
332   C CD2 . LEU A 52  ? 0.3168 0.4231 0.2451 0.0464  0.0028  0.0734  52  LEU A CD2 
333   N N   . TRP A 53  ? 0.3521 0.4619 0.2643 0.0382  -0.0242 0.0240  53  TRP A N   
334   C CA  . TRP A 53  ? 0.3367 0.4621 0.2287 0.0439  -0.0246 0.0146  53  TRP A CA  
335   C C   . TRP A 53  ? 0.3645 0.5177 0.2393 0.0544  -0.0254 0.0271  53  TRP A C   
336   O O   . TRP A 53  ? 0.4018 0.5646 0.2799 0.0563  -0.0308 0.0365  53  TRP A O   
337   C CB  . TRP A 53  ? 0.3320 0.4563 0.2228 0.0397  -0.0345 -0.0106 53  TRP A CB  
338   C CG  . TRP A 53  ? 0.3653 0.4993 0.2608 0.0376  -0.0467 -0.0171 53  TRP A CG  
339   C CD1 . TRP A 53  ? 0.3748 0.4955 0.2909 0.0297  -0.0510 -0.0184 53  TRP A CD1 
340   C CD2 . TRP A 53  ? 0.4138 0.5762 0.2944 0.0438  -0.0570 -0.0245 53  TRP A CD2 
341   N NE1 . TRP A 53  ? 0.4207 0.5586 0.3386 0.0297  -0.0628 -0.0252 53  TRP A NE1 
342   C CE2 . TRP A 53  ? 0.4417 0.6058 0.3380 0.0381  -0.0677 -0.0300 53  TRP A CE2 
343   C CE3 . TRP A 53  ? 0.4293 0.6187 0.2842 0.0543  -0.0580 -0.0267 53  TRP A CE3 
344   C CZ2 . TRP A 53  ? 0.4654 0.6575 0.3546 0.0419  -0.0810 -0.0389 53  TRP A CZ2 
345   C CZ3 . TRP A 53  ? 0.4536 0.6719 0.2979 0.0591  -0.0713 -0.0359 53  TRP A CZ3 
346   C CH2 . TRP A 53  ? 0.4780 0.6974 0.3405 0.0525  -0.0834 -0.0425 53  TRP A CH2 
347   N N   . VAL A 54  ? 0.3870 0.5551 0.2434 0.0622  -0.0193 0.0282  54  VAL A N   
348   C CA  . VAL A 54  ? 0.3659 0.5648 0.2023 0.0746  -0.0178 0.0428  54  VAL A CA  
349   C C   . VAL A 54  ? 0.4773 0.6952 0.2889 0.0812  -0.0197 0.0239  54  VAL A C   
350   O O   . VAL A 54  ? 0.4550 0.6577 0.2695 0.0766  -0.0170 0.0072  54  VAL A O   
351   C CB  . VAL A 54  ? 0.4064 0.6040 0.2502 0.0792  -0.0022 0.0731  54  VAL A CB  
352   C CG1 . VAL A 54  ? 0.3793 0.5680 0.2241 0.0784  0.0101  0.0718  54  VAL A CG1 
353   C CG2 . VAL A 54  ? 0.4552 0.6857 0.2817 0.0932  -0.0001 0.0945  54  VAL A CG2 
354   N N   . THR A 55  ? 0.5393 0.7914 0.3268 0.0926  -0.0250 0.0248  55  THR A N   
355   C CA  . THR A 55  ? 0.6209 0.8953 0.3818 0.1015  -0.0251 0.0072  55  THR A CA  
356   C C   . THR A 55  ? 0.5924 0.8733 0.3439 0.1099  -0.0067 0.0261  55  THR A C   
357   O O   . THR A 55  ? 0.5608 0.8488 0.3156 0.1153  0.0034  0.0575  55  THR A O   
358   C CB  . THR A 55  ? 0.7405 1.0489 0.4840 0.1105  -0.0359 0.0013  55  THR A CB  
359   O OG1 . THR A 55  ? 0.7944 1.1173 0.5386 0.1186  -0.0286 0.0342  55  THR A OG1 
360   C CG2 . THR A 55  ? 0.5211 0.8284 0.2741 0.1025  -0.0552 -0.0209 55  THR A CG2 
361   N N   . CYS A 56  ? 0.5957 0.8713 0.3417 0.1101  -0.0013 0.0083  56  CYS A N   
362   C CA  . CYS A 56  ? 0.5822 0.8661 0.3213 0.1181  0.0164  0.0241  56  CYS A CA  
363   C C   . CYS A 56  ? 0.6196 0.9263 0.3406 0.1279  0.0166  0.0085  56  CYS A C   
364   O O   . CYS A 56  ? 0.6543 0.9615 0.3686 0.1264  0.0054  -0.0233 56  CYS A O   
365   C CB  . CYS A 56  ? 0.5481 0.7988 0.3115 0.1077  0.0248  0.0199  56  CYS A CB  
366   S SG  . CYS A 56  ? 0.6244 0.8424 0.4239 0.0939  0.0261  0.0400  56  CYS A SG  
367   N N   . SER A 57  ? 0.6107 0.9358 0.3270 0.1378  0.0296  0.0308  57  SER A N   
368   C CA  . SER A 57  ? 0.6178 0.9678 0.3159 0.1491  0.0317  0.0195  57  SER A CA  
369   C C   . SER A 57  ? 0.6397 0.9959 0.3413 0.1558  0.0515  0.0426  57  SER A C   
370   O O   . SER A 57  ? 0.6418 0.9818 0.3627 0.1505  0.0628  0.0651  57  SER A O   
371   C CB  . SER A 57  ? 0.6393 1.0194 0.3240 0.1580  0.0225  0.0226  57  SER A CB  
372   O OG  . SER A 57  ? 0.6414 1.0319 0.3334 0.1635  0.0323  0.0599  57  SER A OG  
373   N N   . GLN A 58  ? 0.6390 1.0199 0.3245 0.1674  0.0558  0.0374  58  GLN A N   
374   C CA  . GLN A 58  ? 0.6363 1.0287 0.3257 0.1755  0.0744  0.0624  58  GLN A CA  
375   C C   . GLN A 58  ? 0.6284 1.0320 0.3291 0.1798  0.0815  0.1011  58  GLN A C   
376   O O   . GLN A 58  ? 0.6048 1.0155 0.3163 0.1851  0.0975  0.1269  58  GLN A O   
377   C CB  . GLN A 58  ? 0.7176 1.1378 0.3852 0.1887  0.0768  0.0488  58  GLN A CB  
378   C CG  . GLN A 58  ? 0.7864 1.2403 0.4325 0.2001  0.0665  0.0443  58  GLN A CG  
379   C CD  . GLN A 58  ? 0.8058 1.2579 0.4414 0.1956  0.0464  0.0081  58  GLN A CD  
380   O OE1 . GLN A 58  ? 0.7906 1.2138 0.4376 0.1826  0.0385  -0.0092 58  GLN A OE1 
381   N NE2 . GLN A 58  ? 0.8496 1.3341 0.4653 0.2066  0.0381  -0.0036 58  GLN A NE2 
382   N N   . HIS A 59  ? 0.5939 1.0008 0.2939 0.1785  0.0699  0.1048  59  HIS A N   
383   C CA  . HIS A 59  ? 0.7029 1.1201 0.4162 0.1834  0.0762  0.1403  59  HIS A CA  
384   C C   . HIS A 59  ? 0.6646 1.0507 0.4079 0.1712  0.0809  0.1594  59  HIS A C   
385   O O   . HIS A 59  ? 0.6590 1.0476 0.4202 0.1736  0.0870  0.1886  59  HIS A O   
386   C CB  . HIS A 59  ? 0.7080 1.1491 0.4065 0.1903  0.0622  0.1364  59  HIS A CB  
387   C CG  . HIS A 59  ? 0.7323 1.2068 0.4025 0.2026  0.0563  0.1168  59  HIS A CG  
388   N ND1 . HIS A 59  ? 0.7535 1.2556 0.4143 0.2169  0.0685  0.1312  59  HIS A ND1 
389   C CD2 . HIS A 59  ? 0.7252 1.2103 0.3765 0.2029  0.0395  0.0832  59  HIS A CD2 
390   C CE1 . HIS A 59  ? 0.7746 1.3037 0.4095 0.2260  0.0594  0.1069  59  HIS A CE1 
391   N NE2 . HIS A 59  ? 0.7597 1.2784 0.3896 0.2173  0.0416  0.0769  59  HIS A NE2 
392   N N   . TYR A 60  ? 0.6279 0.9856 0.3780 0.1588  0.0782  0.1421  60  TYR A N   
393   C CA  . TYR A 60  ? 0.6108 0.9388 0.3898 0.1469  0.0842  0.1570  60  TYR A CA  
394   C C   . TYR A 60  ? 0.6518 0.9753 0.4551 0.1471  0.1037  0.1815  60  TYR A C   
395   O O   . TYR A 60  ? 0.6959 1.0209 0.4957 0.1481  0.1112  0.1725  60  TYR A O   
396   C CB  . TYR A 60  ? 0.5739 0.8784 0.3503 0.1357  0.0760  0.1295  60  TYR A CB  
397   C CG  . TYR A 60  ? 0.5416 0.8165 0.3439 0.1232  0.0790  0.1389  60  TYR A CG  
398   C CD1 . TYR A 60  ? 0.5014 0.7637 0.3316 0.1186  0.0950  0.1585  60  TYR A CD1 
399   C CD2 . TYR A 60  ? 0.5369 0.7935 0.3421 0.1141  0.0640  0.1232  60  TYR A CD2 
400   C CE1 . TYR A 60  ? 0.4581 0.6889 0.3207 0.1047  0.0938  0.1593  60  TYR A CE1 
401   C CE2 . TYR A 60  ? 0.4846 0.7079 0.3232 0.1002  0.0632  0.1246  60  TYR A CE2 
402   C CZ  . TYR A 60  ? 0.4554 0.6664 0.3214 0.0958  0.0774  0.1413  60  TYR A CZ  
403   O OH  . TYR A 60  ? 0.4320 0.6128 0.3297 0.0826  0.0752  0.1392  60  TYR A OH  
404   N N   . SER A 61  ? 0.6526 0.9714 0.4834 0.1465  0.1122  0.2116  61  SER A N   
405   C CA  . SER A 61  ? 0.6689 0.9826 0.5296 0.1455  0.1300  0.2345  61  SER A CA  
406   C C   . SER A 61  ? 0.6124 0.8945 0.5125 0.1316  0.1348  0.2456  61  SER A C   
407   O O   . SER A 61  ? 0.6024 0.8750 0.5187 0.1290  0.1315  0.2577  61  SER A O   
408   C CB  . SER A 61  ? 0.7516 1.0905 0.6176 0.1589  0.1392  0.2622  61  SER A CB  
409   O OG  . SER A 61  ? 0.7859 1.1190 0.6847 0.1572  0.1560  0.2836  61  SER A OG  
410   N N   . SER A 62  ? 0.6026 0.8698 0.5204 0.1229  0.1425  0.2402  62  SER A N   
411   C CA  . SER A 62  ? 0.5581 0.7967 0.5157 0.1087  0.1467  0.2462  62  SER A CA  
412   C C   . SER A 62  ? 0.5729 0.8067 0.5529 0.1030  0.1582  0.2451  62  SER A C   
413   O O   . SER A 62  ? 0.5899 0.8321 0.5492 0.1053  0.1582  0.2276  62  SER A O   
414   C CB  . SER A 62  ? 0.4926 0.7119 0.4422 0.0992  0.1342  0.2268  62  SER A CB  
415   O OG  . SER A 62  ? 0.4475 0.6397 0.4380 0.0852  0.1366  0.2280  62  SER A OG  
416   N N   . SER A 63  ? 0.5239 0.7446 0.5491 0.0958  0.1676  0.2624  63  SER A N   
417   C CA  . SER A 63  ? 0.4719 0.6886 0.5246 0.0892  0.1774  0.2612  63  SER A CA  
418   C C   . SER A 63  ? 0.4597 0.6552 0.5301 0.0744  0.1722  0.2420  63  SER A C   
419   O O   . SER A 63  ? 0.4580 0.6506 0.5541 0.0674  0.1780  0.2372  63  SER A O   
420   C CB  . SER A 63  ? 0.4699 0.6840 0.5670 0.0882  0.1892  0.2862  63  SER A CB  
421   O OG  . SER A 63  ? 0.4590 0.6496 0.5918 0.0781  0.1864  0.2909  63  SER A OG  
422   N N   . THR A 64  ? 0.4378 0.6184 0.4962 0.0696  0.1586  0.2281  64  THR A N   
423   C CA  . THR A 64  ? 0.4083 0.5642 0.4827 0.0563  0.1453  0.2011  64  THR A CA  
424   C C   . THR A 64  ? 0.4086 0.5600 0.4464 0.0572  0.1286  0.1717  64  THR A C   
425   O O   . THR A 64  ? 0.3827 0.5150 0.4290 0.0479  0.1166  0.1511  64  THR A O   
426   C CB  . THR A 64  ? 0.3780 0.5115 0.4838 0.0467  0.1402  0.2039  64  THR A CB  
427   O OG1 . THR A 64  ? 0.4204 0.5572 0.5092 0.0538  0.1382  0.2173  64  THR A OG1 
428   C CG2 . THR A 64  ? 0.3489 0.4802 0.5045 0.0408  0.1549  0.2232  64  THR A CG2 
429   N N   . TYR A 65  ? 0.4244 0.5947 0.4231 0.0688  0.1282  0.1698  65  TYR A N   
430   C CA  . TYR A 65  ? 0.4336 0.6000 0.4015 0.0698  0.1134  0.1422  65  TYR A CA  
431   C C   . TYR A 65  ? 0.4475 0.6112 0.4170 0.0678  0.1135  0.1235  65  TYR A C   
432   O O   . TYR A 65  ? 0.4869 0.6656 0.4614 0.0728  0.1265  0.1315  65  TYR A O   
433   C CB  . TYR A 65  ? 0.4308 0.6207 0.3589 0.0830  0.1123  0.1434  65  TYR A CB  
434   C CG  . TYR A 65  ? 0.4146 0.6037 0.3152 0.0848  0.1000  0.1132  65  TYR A CG  
435   C CD1 . TYR A 65  ? 0.4135 0.5882 0.3065 0.0794  0.0836  0.0961  65  TYR A CD1 
436   C CD2 . TYR A 65  ? 0.4273 0.6294 0.3137 0.0918  0.1059  0.1018  65  TYR A CD2 
437   C CE1 . TYR A 65  ? 0.4255 0.5979 0.2997 0.0802  0.0733  0.0689  65  TYR A CE1 
438   C CE2 . TYR A 65  ? 0.4247 0.6236 0.2917 0.0932  0.0956  0.0735  65  TYR A CE2 
439   C CZ  . TYR A 65  ? 0.4376 0.6209 0.2998 0.0870  0.0792  0.0574  65  TYR A CZ  
440   O OH  . TYR A 65  ? 0.4744 0.6536 0.3226 0.0879  0.0699  0.0298  65  TYR A OH  
441   N N   . GLN A 66  ? 0.4312 0.5774 0.3973 0.0616  0.0997  0.1000  66  GLN A N   
442   C CA  . GLN A 66  ? 0.4338 0.5775 0.3988 0.0616  0.0984  0.0816  66  GLN A CA  
443   C C   . GLN A 66  ? 0.3944 0.5274 0.3391 0.0612  0.0843  0.0582  66  GLN A C   
444   O O   . GLN A 66  ? 0.3921 0.5124 0.3360 0.0558  0.0735  0.0544  66  GLN A O   
445   C CB  . GLN A 66  ? 0.5147 0.6457 0.5139 0.0519  0.0986  0.0808  66  GLN A CB  
446   C CG  . GLN A 66  ? 0.6510 0.7931 0.6774 0.0513  0.1132  0.0996  66  GLN A CG  
447   C CD  . GLN A 66  ? 0.7407 0.8712 0.8037 0.0404  0.1100  0.0956  66  GLN A CD  
448   O OE1 . GLN A 66  ? 0.7751 0.8981 0.8394 0.0377  0.1014  0.0785  66  GLN A OE1 
449   N NE2 . GLN A 66  ? 0.7583 0.8887 0.8531 0.0345  0.1170  0.1116  66  GLN A NE2 
450   N N   . ALA A 67  ? 0.3623 0.5000 0.2947 0.0670  0.0851  0.0426  67  ALA A N   
451   C CA  . ALA A 67  ? 0.3779 0.5022 0.3004 0.0654  0.0730  0.0198  67  ALA A CA  
452   C C   . ALA A 67  ? 0.4120 0.5229 0.3559 0.0609  0.0723  0.0123  67  ALA A C   
453   O O   . ALA A 67  ? 0.4305 0.5493 0.3780 0.0663  0.0804  0.0095  67  ALA A O   
454   C CB  . ALA A 67  ? 0.3805 0.5184 0.2763 0.0757  0.0735  0.0049  67  ALA A CB  
455   N N   . PRO A 68  ? 0.3770 0.4700 0.3350 0.0520  0.0629  0.0099  68  PRO A N   
456   C CA  . PRO A 68  ? 0.3251 0.4090 0.3028 0.0488  0.0612  0.0048  68  PRO A CA  
457   C C   . PRO A 68  ? 0.3422 0.4241 0.3146 0.0552  0.0617  -0.0102 68  PRO A C   
458   O O   . PRO A 68  ? 0.3689 0.4484 0.3241 0.0587  0.0581  -0.0223 68  PRO A O   
459   C CB  . PRO A 68  ? 0.3071 0.3752 0.2907 0.0409  0.0501  0.0028  68  PRO A CB  
460   C CG  . PRO A 68  ? 0.3418 0.4121 0.3203 0.0381  0.0493  0.0128  68  PRO A CG  
461   C CD  . PRO A 68  ? 0.3596 0.4438 0.3169 0.0457  0.0546  0.0142  68  PRO A CD  
462   N N   . PHE A 69  ? 0.3616 0.4448 0.3509 0.0569  0.0658  -0.0105 69  PHE A N   
463   C CA  . PHE A 69  ? 0.3503 0.4304 0.3384 0.0640  0.0674  -0.0240 69  PHE A CA  
464   C C   . PHE A 69  ? 0.3484 0.4097 0.3423 0.0609  0.0575  -0.0322 69  PHE A C   
465   O O   . PHE A 69  ? 0.3878 0.4421 0.3899 0.0541  0.0506  -0.0260 69  PHE A O   
466   C CB  . PHE A 69  ? 0.4523 0.5439 0.4574 0.0692  0.0769  -0.0199 69  PHE A CB  
467   C CG  . PHE A 69  ? 0.4353 0.5273 0.4654 0.0633  0.0739  -0.0106 69  PHE A CG  
468   C CD1 . PHE A 69  ? 0.4024 0.4845 0.4439 0.0629  0.0666  -0.0148 69  PHE A CD1 
469   C CD2 . PHE A 69  ? 0.4366 0.5412 0.4808 0.0589  0.0787  0.0022  69  PHE A CD2 
470   C CE1 . PHE A 69  ? 0.3523 0.4397 0.4144 0.0589  0.0626  -0.0079 69  PHE A CE1 
471   C CE2 . PHE A 69  ? 0.3946 0.5022 0.4637 0.0533  0.0745  0.0070  69  PHE A CE2 
472   C CZ  . PHE A 69  ? 0.3448 0.4453 0.4206 0.0538  0.0657  0.0010  69  PHE A CZ  
473   N N   . CYS A 70  ? 0.3718 0.4256 0.3627 0.0665  0.0575  -0.0464 70  CYS A N   
474   C CA  . CYS A 70  ? 0.3925 0.4283 0.3925 0.0641  0.0500  -0.0522 70  CYS A CA  
475   C C   . CYS A 70  ? 0.4127 0.4468 0.4329 0.0636  0.0492  -0.0420 70  CYS A C   
476   O O   . CYS A 70  ? 0.4438 0.4885 0.4744 0.0683  0.0554  -0.0379 70  CYS A O   
477   C CB  . CYS A 70  ? 0.4429 0.4705 0.4427 0.0706  0.0519  -0.0699 70  CYS A CB  
478   S SG  . CYS A 70  ? 0.4954 0.5002 0.5055 0.0659  0.0429  -0.0778 70  CYS A SG  
479   N N   . HIS A 71  ? 0.3881 0.4119 0.4137 0.0585  0.0416  -0.0375 71  HIS A N   
480   C CA  . HIS A 71  ? 0.3388 0.3646 0.3801 0.0588  0.0390  -0.0276 71  HIS A CA  
481   C C   . HIS A 71  ? 0.3145 0.3549 0.3588 0.0545  0.0379  -0.0186 71  HIS A C   
482   O O   . HIS A 71  ? 0.3256 0.3741 0.3833 0.0558  0.0358  -0.0127 71  HIS A O   
483   C CB  . HIS A 71  ? 0.3426 0.3695 0.3995 0.0679  0.0442  -0.0284 71  HIS A CB  
484   C CG  . HIS A 71  ? 0.3651 0.3767 0.4244 0.0729  0.0470  -0.0397 71  HIS A CG  
485   N ND1 . HIS A 71  ? 0.3712 0.3662 0.4353 0.0706  0.0425  -0.0408 71  HIS A ND1 
486   C CD2 . HIS A 71  ? 0.3793 0.3900 0.4401 0.0801  0.0542  -0.0513 71  HIS A CD2 
487   C CE1 . HIS A 71  ? 0.3742 0.3571 0.4452 0.0752  0.0463  -0.0535 71  HIS A CE1 
488   N NE2 . HIS A 71  ? 0.3869 0.3791 0.4547 0.0815  0.0531  -0.0612 71  HIS A NE2 
489   N N   . SER A 72  ? 0.2963 0.3413 0.3305 0.0498  0.0394  -0.0178 72  SER A N   
490   C CA  . SER A 72  ? 0.2851 0.3407 0.3271 0.0444  0.0384  -0.0101 72  SER A CA  
491   C C   . SER A 72  ? 0.2804 0.3305 0.3225 0.0386  0.0294  -0.0079 72  SER A C   
492   O O   . SER A 72  ? 0.3089 0.3477 0.3428 0.0382  0.0251  -0.0102 72  SER A O   
493   C CB  . SER A 72  ? 0.2864 0.3481 0.3208 0.0423  0.0444  -0.0070 72  SER A CB  
494   O OG  . SER A 72  ? 0.2924 0.3450 0.3092 0.0402  0.0410  -0.0097 72  SER A OG  
495   N N   . THR A 73  ? 0.2614 0.3207 0.3150 0.0342  0.0272  -0.0044 73  THR A N   
496   C CA  . THR A 73  ? 0.2644 0.3211 0.3176 0.0293  0.0195  -0.0043 73  THR A CA  
497   C C   . THR A 73  ? 0.2961 0.3424 0.3361 0.0252  0.0193  -0.0039 73  THR A C   
498   O O   . THR A 73  ? 0.3259 0.3659 0.3603 0.0232  0.0138  -0.0047 73  THR A O   
499   C CB  . THR A 73  ? 0.2691 0.3383 0.3402 0.0250  0.0171  -0.0043 73  THR A CB  
500   O OG1 . THR A 73  ? 0.2975 0.3703 0.3773 0.0215  0.0243  -0.0008 73  THR A OG1 
501   C CG2 . THR A 73  ? 0.2496 0.3329 0.3344 0.0294  0.0145  -0.0053 73  THR A CG2 
502   N N   . GLN A 74  ? 0.2897 0.3368 0.3249 0.0249  0.0256  -0.0014 74  GLN A N   
503   C CA  . GLN A 74  ? 0.2964 0.3369 0.3186 0.0227  0.0250  0.0001  74  GLN A CA  
504   C C   . GLN A 74  ? 0.2798 0.3110 0.2876 0.0248  0.0213  -0.0057 74  GLN A C   
505   O O   . GLN A 74  ? 0.3152 0.3403 0.3175 0.0219  0.0166  -0.0057 74  GLN A O   
506   C CB  . GLN A 74  ? 0.3420 0.3898 0.3609 0.0240  0.0331  0.0062  74  GLN A CB  
507   C CG  . GLN A 74  ? 0.3178 0.3732 0.3566 0.0203  0.0380  0.0142  74  GLN A CG  
508   C CD  . GLN A 74  ? 0.3484 0.4153 0.3997 0.0231  0.0451  0.0158  74  GLN A CD  
509   O OE1 . GLN A 74  ? 0.3632 0.4314 0.4127 0.0273  0.0441  0.0097  74  GLN A OE1 
510   N NE2 . GLN A 74  ? 0.4136 0.4892 0.4799 0.0214  0.0532  0.0255  74  GLN A NE2 
511   N N   . CYS A 75  ? 0.2799 0.3100 0.2853 0.0298  0.0236  -0.0111 75  CYS A N   
512   C CA  . CYS A 75  ? 0.2979 0.3180 0.2965 0.0311  0.0203  -0.0184 75  CYS A CA  
513   C C   . CYS A 75  ? 0.2881 0.3006 0.2944 0.0294  0.0151  -0.0164 75  CYS A C   
514   O O   . CYS A 75  ? 0.2871 0.2912 0.2911 0.0275  0.0115  -0.0187 75  CYS A O   
515   C CB  . CYS A 75  ? 0.3290 0.3488 0.3277 0.0373  0.0249  -0.0261 75  CYS A CB  
516   S SG  . CYS A 75  ? 0.4500 0.4826 0.4354 0.0412  0.0320  -0.0283 75  CYS A SG  
517   N N   . SER A 76  ? 0.2943 0.3122 0.3106 0.0308  0.0149  -0.0118 76  SER A N   
518   C CA  . SER A 76  ? 0.2875 0.3038 0.3087 0.0309  0.0105  -0.0077 76  SER A CA  
519   C C   . SER A 76  ? 0.3101 0.3254 0.3261 0.0258  0.0063  -0.0057 76  SER A C   
520   O O   . SER A 76  ? 0.3416 0.3512 0.3565 0.0254  0.0041  -0.0038 76  SER A O   
521   C CB  . SER A 76  ? 0.3105 0.3388 0.3418 0.0343  0.0100  -0.0042 76  SER A CB  
522   O OG  . SER A 76  ? 0.3483 0.3795 0.3812 0.0363  0.0058  0.0006  76  SER A OG  
523   N N   . ARG A 77  ? 0.3099 0.3306 0.3255 0.0222  0.0062  -0.0055 77  ARG A N   
524   C CA  . ARG A 77  ? 0.2905 0.3097 0.3035 0.0183  0.0031  -0.0044 77  ARG A CA  
525   C C   . ARG A 77  ? 0.3514 0.3625 0.3562 0.0165  0.0023  -0.0046 77  ARG A C   
526   O O   . ARG A 77  ? 0.3428 0.3514 0.3466 0.0151  -0.0005 -0.0032 77  ARG A O   
527   C CB  . ARG A 77  ? 0.3035 0.3276 0.3227 0.0149  0.0045  -0.0040 77  ARG A CB  
528   C CG  . ARG A 77  ? 0.3102 0.3324 0.3306 0.0119  0.0017  -0.0041 77  ARG A CG  
529   C CD  . ARG A 77  ? 0.3280 0.3525 0.3604 0.0085  0.0038  -0.0036 77  ARG A CD  
530   N NE  . ARG A 77  ? 0.3801 0.4010 0.4147 0.0067  0.0015  -0.0049 77  ARG A NE  
531   C CZ  . ARG A 77  ? 0.3689 0.3874 0.4154 0.0038  0.0038  -0.0035 77  ARG A CZ  
532   N NH1 . ARG A 77  ? 0.3998 0.4200 0.4581 0.0019  0.0090  0.0011  77  ARG A NH1 
533   N NH2 . ARG A 77  ? 0.3679 0.3827 0.4170 0.0034  0.0019  -0.0060 77  ARG A NH2 
534   N N   . ALA A 78  ? 0.3701 0.3796 0.3692 0.0172  0.0046  -0.0072 78  ALA A N   
535   C CA  . ALA A 78  ? 0.3804 0.3860 0.3720 0.0159  0.0023  -0.0100 78  ALA A CA  
536   C C   . ALA A 78  ? 0.3731 0.3709 0.3689 0.0162  0.0002  -0.0141 78  ALA A C   
537   O O   . ALA A 78  ? 0.3698 0.3650 0.3641 0.0142  -0.0029 -0.0181 78  ALA A O   
538   C CB  . ALA A 78  ? 0.3947 0.4056 0.3771 0.0180  0.0050  -0.0130 78  ALA A CB  
539   N N   . ASN A 79  ? 0.4065 0.4019 0.4102 0.0190  0.0019  -0.0124 79  ASN A N   
540   C CA  . ASN A 79  ? 0.4623 0.4495 0.4755 0.0199  0.0018  -0.0127 79  ASN A CA  
541   C C   . ASN A 79  ? 0.4725 0.4528 0.4879 0.0202  0.0022  -0.0233 79  ASN A C   
542   O O   . ASN A 79  ? 0.4573 0.4302 0.4814 0.0176  0.0002  -0.0270 79  ASN A O   
543   C CB  . ASN A 79  ? 0.5383 0.5239 0.5546 0.0166  -0.0008 -0.0075 79  ASN A CB  
544   C CG  . ASN A 79  ? 0.5853 0.5643 0.6156 0.0181  0.0010  -0.0023 79  ASN A CG  
545   O OD1 . ASN A 79  ? 0.5656 0.5426 0.6030 0.0228  0.0042  0.0009  79  ASN A OD1 
546   N ND2 . ASN A 79  ? 0.6446 0.6211 0.6814 0.0145  -0.0002 0.0005  79  ASN A ND2 
547   N N   . THR A 80  ? 0.4808 0.4649 0.4902 0.0235  0.0050  -0.0293 80  THR A N   
548   C CA  . THR A 80  ? 0.5174 0.4965 0.5287 0.0257  0.0060  -0.0422 80  THR A CA  
549   C C   . THR A 80  ? 0.5833 0.5617 0.6008 0.0322  0.0119  -0.0433 80  THR A C   
550   O O   . THR A 80  ? 0.5596 0.5479 0.5711 0.0350  0.0153  -0.0389 80  THR A O   
551   C CB  . THR A 80  ? 0.5103 0.4983 0.5055 0.0256  0.0042  -0.0513 80  THR A CB  
552   O OG1 . THR A 80  ? 0.5860 0.5718 0.5819 0.0296  0.0059  -0.0665 80  THR A OG1 
553   C CG2 . THR A 80  ? 0.4443 0.4449 0.4275 0.0275  0.0079  -0.0430 80  THR A CG2 
554   N N   . HIS A 81  ? 0.6479 0.6147 0.6810 0.0347  0.0137  -0.0484 81  HIS A N   
555   C CA  . HIS A 81  ? 0.7026 0.6677 0.7447 0.0421  0.0198  -0.0499 81  HIS A CA  
556   C C   . HIS A 81  ? 0.7137 0.6706 0.7614 0.0451  0.0217  -0.0687 81  HIS A C   
557   O O   . HIS A 81  ? 0.7396 0.6902 0.8014 0.0516  0.0272  -0.0719 81  HIS A O   
558   C CB  . HIS A 81  ? 0.7203 0.6806 0.7797 0.0452  0.0216  -0.0355 81  HIS A CB  
559   C CG  . HIS A 81  ? 0.7455 0.7188 0.7978 0.0445  0.0196  -0.0214 81  HIS A CG  
560   N ND1 . HIS A 81  ? 0.7398 0.7254 0.7915 0.0491  0.0218  -0.0166 81  HIS A ND1 
561   C CD2 . HIS A 81  ? 0.7334 0.7106 0.7801 0.0398  0.0153  -0.0134 81  HIS A CD2 
562   C CE1 . HIS A 81  ? 0.7107 0.7068 0.7576 0.0468  0.0180  -0.0078 81  HIS A CE1 
563   N NE2 . HIS A 81  ? 0.7054 0.6962 0.7480 0.0416  0.0145  -0.0059 81  HIS A NE2 
564   N N   . GLN A 82  ? 0.6691 0.6279 0.7061 0.0410  0.0169  -0.0821 82  GLN A N   
565   C CA  . GLN A 82  ? 0.6320 0.5882 0.6693 0.0440  0.0171  -0.1046 82  GLN A CA  
566   C C   . GLN A 82  ? 0.6054 0.5801 0.6181 0.0496  0.0202  -0.1106 82  GLN A C   
567   O O   . GLN A 82  ? 0.5653 0.5537 0.5586 0.0472  0.0173  -0.1052 82  GLN A O   
568   C CB  . GLN A 82  ? 0.6773 0.6300 0.7173 0.0370  0.0087  -0.1173 82  GLN A CB  
569   C CG  . GLN A 82  ? 0.7817 0.7407 0.8128 0.0401  0.0062  -0.1438 82  GLN A CG  
570   C CD  . GLN A 82  ? 0.8735 0.8334 0.9086 0.0329  -0.0042 -0.1586 82  GLN A CD  
571   O OE1 . GLN A 82  ? 0.9340 0.8882 0.9810 0.0252  -0.0085 -0.1480 82  GLN A OE1 
572   N NE2 . GLN A 82  ? 0.8723 0.8408 0.8992 0.0360  -0.0081 -0.1846 82  GLN A NE2 
573   N N   . CYS A 83  ? 0.6377 0.6136 0.6524 0.0580  0.0272  -0.1207 83  CYS A N   
574   C CA  . CYS A 83  ? 0.6197 0.6154 0.6123 0.0646  0.0325  -0.1232 83  CYS A CA  
575   C C   . CYS A 83  ? 0.6148 0.6229 0.5866 0.0660  0.0282  -0.1415 83  CYS A C   
576   O O   . CYS A 83  ? 0.6618 0.6618 0.6405 0.0639  0.0219  -0.1608 83  CYS A O   
577   C CB  . CYS A 83  ? 0.6132 0.6088 0.6148 0.0743  0.0424  -0.1281 83  CYS A CB  
578   S SG  . CYS A 83  ? 0.7028 0.6953 0.7229 0.0748  0.0471  -0.1039 83  CYS A SG  
579   N N   . PHE A 84  ? 0.5422 0.5720 0.4901 0.0701  0.0318  -0.1352 84  PHE A N   
580   C CA  . PHE A 84  ? 0.5254 0.5729 0.4495 0.0727  0.0271  -0.1482 84  PHE A CA  
581   C C   . PHE A 84  ? 0.5724 0.6349 0.4829 0.0848  0.0349  -0.1645 84  PHE A C   
582   O O   . PHE A 84  ? 0.5748 0.6436 0.4853 0.0912  0.0461  -0.1549 84  PHE A O   
583   C CB  . PHE A 84  ? 0.4801 0.5437 0.3868 0.0703  0.0262  -0.1273 84  PHE A CB  
584   C CG  . PHE A 84  ? 0.4441 0.5283 0.3263 0.0733  0.0199  -0.1363 84  PHE A CG  
585   C CD1 . PHE A 84  ? 0.4111 0.4920 0.2954 0.0661  0.0075  -0.1414 84  PHE A CD1 
586   C CD2 . PHE A 84  ? 0.4818 0.5918 0.3393 0.0842  0.0265  -0.1381 84  PHE A CD2 
587   C CE1 . PHE A 84  ? 0.4538 0.5570 0.3163 0.0696  0.0003  -0.1494 84  PHE A CE1 
588   C CE2 . PHE A 84  ? 0.5050 0.6383 0.3381 0.0887  0.0200  -0.1452 84  PHE A CE2 
589   C CZ  . PHE A 84  ? 0.4969 0.6270 0.3325 0.0812  0.0061  -0.1511 84  PHE A CZ  
590   N N   . THR A 85  ? 0.6416 0.7108 0.5421 0.0881  0.0286  -0.1909 85  THR A N   
591   C CA  . THR A 85  ? 0.6980 0.7859 0.5805 0.1010  0.0349  -0.2106 85  THR A CA  
592   C C   . THR A 85  ? 0.7135 0.8297 0.5644 0.1049  0.0275  -0.2200 85  THR A C   
593   O O   . THR A 85  ? 0.7046 0.8181 0.5578 0.0986  0.0140  -0.2346 85  THR A O   
594   C CB  . THR A 85  ? 0.7369 0.8071 0.6402 0.1037  0.0344  -0.2406 85  THR A CB  
595   O OG1 . THR A 85  ? 0.7375 0.7831 0.6711 0.1013  0.0412  -0.2284 85  THR A OG1 
596   C CG2 . THR A 85  ? 0.7466 0.8357 0.6316 0.1159  0.0407  -0.2582 85  THR A CG2 
597   N N   . CYS A 86  ? 0.7093 0.8547 0.5321 0.1156  0.0362  -0.2104 86  CYS A N   
598   C CA  . CYS A 86  ? 0.7341 0.9060 0.5303 0.1181  0.0287  -0.2097 86  CYS A CA  
599   C C   . CYS A 86  ? 0.7447 0.9235 0.5368 0.1224  0.0233  -0.2370 86  CYS A C   
600   O O   . CYS A 86  ? 0.7471 0.9297 0.5368 0.1305  0.0330  -0.2439 86  CYS A O   
601   C CB  . CYS A 86  ? 0.7536 0.9521 0.5275 0.1259  0.0398  -0.1807 86  CYS A CB  
602   S SG  . CYS A 86  ? 0.7926 1.0219 0.5398 0.1280  0.0293  -0.1700 86  CYS A SG  
603   N N   . THR A 87  ? 0.7506 0.9309 0.5444 0.1165  0.0077  -0.2533 87  THR A N   
604   C CA  . THR A 87  ? 0.7970 0.9853 0.5898 0.1194  0.0003  -0.2815 87  THR A CA  
605   C C   . THR A 87  ? 0.8546 1.0782 0.6204 0.1251  -0.0077 -0.2806 87  THR A C   
606   O O   . THR A 87  ? 0.9034 1.1383 0.6673 0.1278  -0.0158 -0.3053 87  THR A O   
607   C CB  . THR A 87  ? 0.7980 0.9611 0.6219 0.1079  -0.0119 -0.3043 87  THR A CB  
608   O OG1 . THR A 87  ? 0.8041 0.9665 0.6314 0.0987  -0.0224 -0.2935 87  THR A OG1 
609   C CG2 . THR A 87  ? 0.7778 0.9061 0.6318 0.1040  -0.0037 -0.3065 87  THR A CG2 
610   N N   . ASP A 88  ? 0.8703 1.1127 0.6166 0.1282  -0.0046 -0.2518 88  ASP A N   
611   C CA  . ASP A 88  ? 0.9372 1.2157 0.6581 0.1361  -0.0100 -0.2454 88  ASP A CA  
612   C C   . ASP A 88  ? 0.9546 1.2580 0.6524 0.1500  0.0038  -0.2311 88  ASP A C   
613   O O   . ASP A 88  ? 1.0585 1.3748 0.7476 0.1580  0.0045  -0.2510 88  ASP A O   
614   C CB  . ASP A 88  ? 0.9729 1.2586 0.6897 0.1315  -0.0162 -0.2216 88  ASP A CB  
615   C CG  . ASP A 88  ? 1.0273 1.2991 0.7636 0.1195  -0.0329 -0.2383 88  ASP A CG  
616   O OD1 . ASP A 88  ? 1.0370 1.3073 0.7836 0.1173  -0.0425 -0.2686 88  ASP A OD1 
617   O OD2 . ASP A 88  ? 1.0541 1.3170 0.7971 0.1122  -0.0360 -0.2211 88  ASP A OD2 
618   N N   . SER A 89  ? 0.8807 1.1923 0.5698 0.1532  0.0148  -0.1968 89  SER A N   
619   C CA  . SER A 89  ? 0.8954 1.2315 0.5663 0.1662  0.0290  -0.1806 89  SER A CA  
620   C C   . SER A 89  ? 0.9272 1.2470 0.6078 0.1683  0.0401  -0.1956 89  SER A C   
621   O O   . SER A 89  ? 0.8852 1.1738 0.5881 0.1593  0.0393  -0.2073 89  SER A O   
622   C CB  . SER A 89  ? 0.8458 1.1890 0.5142 0.1673  0.0399  -0.1392 89  SER A CB  
623   O OG  . SER A 89  ? 0.8466 1.2052 0.5078 0.1772  0.0573  -0.1191 89  SER A OG  
624   N N   . THR A 90  ? 0.9714 1.3130 0.6368 0.1807  0.0505  -0.1950 90  THR A N   
625   C CA  . THR A 90  ? 0.9465 1.2757 0.6211 0.1842  0.0636  -0.2045 90  THR A CA  
626   C C   . THR A 90  ? 0.8999 1.2362 0.5752 0.1884  0.0824  -0.1697 90  THR A C   
627   O O   . THR A 90  ? 0.8902 1.2220 0.5733 0.1927  0.0961  -0.1699 90  THR A O   
628   C CB  . THR A 90  ? 0.9229 1.2707 0.5827 0.1953  0.0632  -0.2313 90  THR A CB  
629   O OG1 . THR A 90  ? 0.9470 1.3343 0.5795 0.2073  0.0653  -0.2164 90  THR A OG1 
630   C CG2 . THR A 90  ? 0.9283 1.2658 0.5951 0.1897  0.0454  -0.2678 90  THR A CG2 
631   N N   . THR A 91  ? 0.8787 1.2258 0.5495 0.1867  0.0828  -0.1396 91  THR A N   
632   C CA  . THR A 91  ? 0.8662 1.2153 0.5461 0.1869  0.0986  -0.1041 91  THR A CA  
633   C C   . THR A 91  ? 0.8103 1.1379 0.5071 0.1744  0.0939  -0.0894 91  THR A C   
634   O O   . THR A 91  ? 0.7948 1.1147 0.4897 0.1681  0.0786  -0.1009 91  THR A O   
635   C CB  . THR A 91  ? 0.7953 1.1796 0.4572 0.1982  0.1062  -0.0767 91  THR A CB  
636   O OG1 . THR A 91  ? 0.7601 1.1588 0.4082 0.1988  0.0926  -0.0734 91  THR A OG1 
637   C CG2 . THR A 91  ? 0.7200 1.1270 0.3660 0.2117  0.1141  -0.0881 91  THR A CG2 
638   N N   . THR A 92  ? 0.7757 1.0942 0.4911 0.1707  0.1069  -0.0650 92  THR A N   
639   C CA  . THR A 92  ? 0.7345 1.0338 0.4663 0.1595  0.1035  -0.0514 92  THR A CA  
640   C C   . THR A 92  ? 0.7286 1.0431 0.4550 0.1600  0.1038  -0.0207 92  THR A C   
641   O O   . THR A 92  ? 0.7159 1.0537 0.4344 0.1687  0.1126  -0.0010 92  THR A O   
642   C CB  . THR A 92  ? 0.6880 0.9704 0.4470 0.1545  0.1159  -0.0407 92  THR A CB  
643   O OG1 . THR A 92  ? 0.6831 0.9819 0.4488 0.1591  0.1321  -0.0122 92  THR A OG1 
644   C CG2 . THR A 92  ? 0.6876 0.9559 0.4549 0.1560  0.1166  -0.0690 92  THR A CG2 
645   N N   . ARG A 93  ? 0.7093 1.0100 0.4419 0.1510  0.0943  -0.0165 93  ARG A N   
646   C CA  . ARG A 93  ? 0.7195 1.0296 0.4511 0.1504  0.0929  0.0108  93  ARG A CA  
647   C C   . ARG A 93  ? 0.6517 0.9372 0.3978 0.1383  0.0856  0.0107  93  ARG A C   
648   O O   . ARG A 93  ? 0.6287 0.8950 0.3810 0.1327  0.0806  -0.0124 93  ARG A O   
649   C CB  . ARG A 93  ? 0.8165 1.1503 0.5243 0.1583  0.0814  0.0034  93  ARG A CB  
650   C CG  . ARG A 93  ? 0.8972 1.2227 0.5967 0.1539  0.0631  -0.0312 93  ARG A CG  
651   C CD  . ARG A 93  ? 1.0173 1.3699 0.6951 0.1630  0.0530  -0.0448 93  ARG A CD  
652   N NE  . ARG A 93  ? 1.0965 1.4390 0.7739 0.1564  0.0347  -0.0772 93  ARG A NE  
653   C CZ  . ARG A 93  ? 1.1610 1.5228 0.8246 0.1614  0.0225  -0.0985 93  ARG A CZ  
654   N NH1 . ARG A 93  ? 1.1843 1.5786 0.8291 0.1748  0.0266  -0.0926 93  ARG A NH1 
655   N NH2 . ARG A 93  ? 1.1689 1.5184 0.8397 0.1533  0.0066  -0.1270 93  ARG A NH2 
656   N N   . PRO A 94  ? 0.5795 0.8645 0.3340 0.1346  0.0861  0.0372  94  PRO A N   
657   C CA  . PRO A 94  ? 0.5133 0.7717 0.2847 0.1217  0.0762  0.0348  94  PRO A CA  
658   C C   . PRO A 94  ? 0.5021 0.7546 0.2620 0.1186  0.0576  0.0044  94  PRO A C   
659   O O   . PRO A 94  ? 0.5094 0.7850 0.2450 0.1266  0.0498  -0.0041 94  PRO A O   
660   C CB  . PRO A 94  ? 0.4597 0.7241 0.2381 0.1215  0.0791  0.0665  94  PRO A CB  
661   C CG  . PRO A 94  ? 0.4825 0.7652 0.2639 0.1299  0.0961  0.0907  94  PRO A CG  
662   C CD  . PRO A 94  ? 0.5624 0.8635 0.3218 0.1398  0.0956  0.0708  94  PRO A CD  
663   N N   . GLY A 95  ? 0.4959 0.7174 0.2770 0.1068  0.0505  -0.0124 95  GLY A N   
664   C CA  . GLY A 95  ? 0.5173 0.7288 0.2962 0.1019  0.0343  -0.0405 95  GLY A CA  
665   C C   . GLY A 95  ? 0.5566 0.7695 0.3277 0.1069  0.0343  -0.0699 95  GLY A C   
666   O O   . GLY A 95  ? 0.5826 0.7816 0.3605 0.1015  0.0227  -0.0952 95  GLY A O   
667   N N   . CYS A 96  ? 0.5616 0.7907 0.3220 0.1174  0.0482  -0.0661 96  CYS A N   
668   C CA  . CYS A 96  ? 0.5877 0.8205 0.3402 0.1246  0.0504  -0.0941 96  CYS A CA  
669   C C   . CYS A 96  ? 0.5607 0.7875 0.3270 0.1274  0.0668  -0.0860 96  CYS A C   
670   O O   . CYS A 96  ? 0.5348 0.7834 0.2908 0.1369  0.0801  -0.0711 96  CYS A O   
671   C CB  . CYS A 96  ? 0.6409 0.9017 0.3698 0.1343  0.0466  -0.1019 96  CYS A CB  
672   S SG  . CYS A 96  ? 0.9745 1.2374 0.6999 0.1414  0.0484  -0.1338 96  CYS A SG  
673   N N   . HIS A 97  ? 0.5512 0.7475 0.3453 0.1181  0.0650  -0.0936 97  HIS A N   
674   C CA  . HIS A 97  ? 0.5660 0.7558 0.3766 0.1208  0.0778  -0.0912 97  HIS A CA  
675   C C   . HIS A 97  ? 0.5793 0.7440 0.4077 0.1174  0.0718  -0.1172 97  HIS A C   
676   O O   . HIS A 97  ? 0.6005 0.7506 0.4323 0.1109  0.0583  -0.1332 97  HIS A O   
677   C CB  . HIS A 97  ? 0.5529 0.7321 0.3877 0.1123  0.0841  -0.0621 97  HIS A CB  
678   C CG  . HIS A 97  ? 0.5718 0.7684 0.3991 0.1128  0.0893  -0.0345 97  HIS A CG  
679   N ND1 . HIS A 97  ? 0.5662 0.7576 0.3918 0.1057  0.0793  -0.0254 97  HIS A ND1 
680   C CD2 . HIS A 97  ? 0.5856 0.8033 0.4114 0.1195  0.1047  -0.0119 97  HIS A CD2 
681   C CE1 . HIS A 97  ? 0.5698 0.7776 0.3927 0.1086  0.0880  0.0012  97  HIS A CE1 
682   N NE2 . HIS A 97  ? 0.5855 0.8095 0.4092 0.1166  0.1037  0.0105  97  HIS A NE2 
683   N N   . ASN A 98  ? 0.5711 0.7312 0.4140 0.1220  0.0823  -0.1197 98  ASN A N   
684   C CA  . ASN A 98  ? 0.6230 0.7568 0.4899 0.1189  0.0789  -0.1367 98  ASN A CA  
685   C C   . ASN A 98  ? 0.5649 0.6818 0.4603 0.1106  0.0812  -0.1157 98  ASN A C   
686   O O   . ASN A 98  ? 0.5427 0.6702 0.4408 0.1088  0.0879  -0.0920 98  ASN A O   
687   C CB  . ASN A 98  ? 0.7759 0.9171 0.6403 0.1319  0.0881  -0.1582 98  ASN A CB  
688   C CG  . ASN A 98  ? 0.9387 1.0877 0.7829 0.1382  0.0810  -0.1903 98  ASN A CG  
689   O OD1 . ASN A 98  ? 0.9523 1.0933 0.7940 0.1306  0.0670  -0.2002 98  ASN A OD1 
690   N ND2 . ASN A 98  ? 1.0888 1.2491 0.9244 0.1473  0.0882  -0.2012 98  ASN A ND2 
691   N N   . ASN A 99  ? 0.5194 0.6110 0.4372 0.1052  0.0749  -0.1240 99  ASN A N   
692   C CA  . ASN A 99  ? 0.4982 0.5761 0.4412 0.0985  0.0749  -0.1064 99  ASN A CA  
693   C C   . ASN A 99  ? 0.4435 0.5216 0.3857 0.0883  0.0693  -0.0862 99  ASN A C   
694   O O   . ASN A 99  ? 0.4164 0.4953 0.3732 0.0847  0.0724  -0.0690 99  ASN A O   
695   C CB  . ASN A 99  ? 0.6161 0.7055 0.5705 0.1057  0.0878  -0.0972 99  ASN A CB  
696   C CG  . ASN A 99  ? 0.7584 0.8496 0.7139 0.1177  0.0954  -0.1173 99  ASN A CG  
697   O OD1 . ASN A 99  ? 0.8192 0.8911 0.7877 0.1184  0.0911  -0.1331 99  ASN A OD1 
698   N ND2 . ASN A 99  ? 0.7868 0.9016 0.7299 0.1279  0.1078  -0.1167 99  ASN A ND2 
699   N N   . THR A 100 ? 0.4432 0.5214 0.3700 0.0839  0.0608  -0.0896 100 THR A N   
700   C CA  . THR A 100 ? 0.4019 0.4765 0.3306 0.0743  0.0545  -0.0729 100 THR A CA  
701   C C   . THR A 100 ? 0.3944 0.4477 0.3344 0.0666  0.0434  -0.0801 100 THR A C   
702   O O   . THR A 100 ? 0.3818 0.4224 0.3333 0.0685  0.0425  -0.0935 100 THR A O   
703   C CB  . THR A 100 ? 0.4243 0.5169 0.3299 0.0757  0.0538  -0.0670 100 THR A CB  
704   O OG1 . THR A 100 ? 0.3745 0.4755 0.2610 0.0820  0.0504  -0.0874 100 THR A OG1 
705   C CG2 . THR A 100 ? 0.4282 0.5406 0.3295 0.0814  0.0664  -0.0508 100 THR A CG2 
706   N N   . CYS A 101 ? 0.4134 0.4626 0.3530 0.0586  0.0361  -0.0704 101 CYS A N   
707   C CA  . CYS A 101 ? 0.4200 0.4516 0.3705 0.0520  0.0268  -0.0763 101 CYS A CA  
708   C C   . CYS A 101 ? 0.3983 0.4337 0.3368 0.0485  0.0182  -0.0823 101 CYS A C   
709   O O   . CYS A 101 ? 0.3736 0.4235 0.2968 0.0491  0.0179  -0.0741 101 CYS A O   
710   C CB  A CYS A 101 ? 0.3840 0.4054 0.3507 0.0459  0.0253  -0.0612 101 CYS A CB  
711   C CB  B CYS A 101 ? 0.3832 0.4056 0.3487 0.0457  0.0251  -0.0607 101 CYS A CB  
712   S SG  A CYS A 101 ? 0.4762 0.5076 0.4408 0.0421  0.0273  -0.0415 101 CYS A SG  
713   S SG  B CYS A 101 ? 0.4727 0.5018 0.4483 0.0485  0.0335  -0.0479 101 CYS A SG  
714   N N   . GLY A 102 ? 0.4248 0.4473 0.3741 0.0450  0.0115  -0.0958 102 GLY A N   
715   C CA  . GLY A 102 ? 0.4985 0.5246 0.4419 0.0415  0.0019  -0.1064 102 GLY A CA  
716   C C   . GLY A 102 ? 0.5145 0.5326 0.4683 0.0330  -0.0041 -0.0946 102 GLY A C   
717   O O   . GLY A 102 ? 0.5028 0.5067 0.4734 0.0294  -0.0023 -0.0853 102 GLY A O   
718   N N   . LEU A 103 ? 0.5369 0.5668 0.4796 0.0310  -0.0109 -0.0943 103 LEU A N   
719   C CA  . LEU A 103 ? 0.5330 0.5589 0.4838 0.0242  -0.0161 -0.0829 103 LEU A CA  
720   C C   . LEU A 103 ? 0.5114 0.5459 0.4609 0.0216  -0.0265 -0.0961 103 LEU A C   
721   O O   . LEU A 103 ? 0.5349 0.5883 0.4657 0.0266  -0.0298 -0.1033 103 LEU A O   
722   C CB  . LEU A 103 ? 0.5654 0.6001 0.5055 0.0253  -0.0124 -0.0633 103 LEU A CB  
723   C CG  . LEU A 103 ? 0.5926 0.6212 0.5424 0.0199  -0.0139 -0.0486 103 LEU A CG  
724   C CD1 . LEU A 103 ? 0.6173 0.6293 0.5848 0.0164  -0.0116 -0.0459 103 LEU A CD1 
725   C CD2 . LEU A 103 ? 0.5876 0.6239 0.5300 0.0222  -0.0086 -0.0326 103 LEU A CD2 
726   N N   . LEU A 104 ? 0.4516 0.4751 0.4218 0.0145  -0.0317 -0.0992 104 LEU A N   
727   C CA  . LEU A 104 ? 0.4657 0.4988 0.4400 0.0108  -0.0426 -0.1117 104 LEU A CA  
728   C C   . LEU A 104 ? 0.3954 0.4416 0.3622 0.0096  -0.0469 -0.0973 104 LEU A C   
729   O O   . LEU A 104 ? 0.3686 0.4060 0.3461 0.0058  -0.0443 -0.0819 104 LEU A O   
730   C CB  . LEU A 104 ? 0.5163 0.5326 0.5216 0.0031  -0.0452 -0.1194 104 LEU A CB  
731   C CG  . LEU A 104 ? 0.5477 0.5723 0.5656 -0.0017 -0.0567 -0.1394 104 LEU A CG  
732   C CD1 . LEU A 104 ? 0.5841 0.6170 0.5931 0.0028  -0.0607 -0.1659 104 LEU A CD1 
733   C CD2 . LEU A 104 ? 0.5769 0.5823 0.6309 -0.0101 -0.0556 -0.1382 104 LEU A CD2 
734   N N   . SER A 105 ? 0.3836 0.4523 0.3324 0.0141  -0.0535 -0.1028 105 SER A N   
735   C CA  . SER A 105 ? 0.3670 0.4505 0.3091 0.0148  -0.0577 -0.0885 105 SER A CA  
736   C C   . SER A 105 ? 0.4279 0.5247 0.3799 0.0110  -0.0710 -0.1021 105 SER A C   
737   O O   . SER A 105 ? 0.4406 0.5444 0.3939 0.0107  -0.0781 -0.1252 105 SER A O   
738   C CB  . SER A 105 ? 0.3718 0.4752 0.2866 0.0246  -0.0543 -0.0784 105 SER A CB  
739   O OG  . SER A 105 ? 0.3607 0.4537 0.2706 0.0274  -0.0420 -0.0654 105 SER A OG  
740   N N   . SER A 106 ? 0.5187 0.6198 0.4802 0.0080  -0.0744 -0.0892 106 SER A N   
741   C CA  . SER A 106 ? 0.5733 0.6896 0.5479 0.0040  -0.0875 -0.1003 106 SER A CA  
742   C C   . SER A 106 ? 0.4934 0.6358 0.4558 0.0097  -0.0940 -0.0887 106 SER A C   
743   O O   . SER A 106 ? 0.4439 0.5839 0.4027 0.0126  -0.0875 -0.0662 106 SER A O   
744   C CB  . SER A 106 ? 0.6600 0.7588 0.6675 -0.0061 -0.0868 -0.0981 106 SER A CB  
745   O OG  . SER A 106 ? 0.7291 0.8111 0.7547 -0.0116 -0.0857 -0.1147 106 SER A OG  
746   N N   . ASN A 107 ? 0.4753 0.6664 0.4538 0.0023  -0.0718 -0.1011 107 ASN A N   
747   C CA  . ASN A 107 ? 0.4599 0.6794 0.4392 0.0050  -0.0835 -0.0930 107 ASN A CA  
748   C C   . ASN A 107 ? 0.4123 0.6289 0.4296 -0.0037 -0.0861 -0.0918 107 ASN A C   
749   O O   . ASN A 107 ? 0.3931 0.6108 0.4329 -0.0126 -0.0931 -0.1118 107 ASN A O   
750   C CB  . ASN A 107 ? 0.4893 0.7380 0.4520 0.0077  -0.0995 -0.1132 107 ASN A CB  
751   C CG  . ASN A 107 ? 0.5089 0.7900 0.4718 0.0120  -0.1141 -0.1051 107 ASN A CG  
752   O OD1 . ASN A 107 ? 0.4817 0.7647 0.4723 0.0084  -0.1163 -0.0950 107 ASN A OD1 
753   N ND2 . ASN A 107 ? 0.5425 0.8510 0.4737 0.0207  -0.1241 -0.1092 107 ASN A ND2 
754   N N   . PRO A 108 ? 0.3920 0.6056 0.4184 -0.0013 -0.0798 -0.0689 108 PRO A N   
755   C CA  . PRO A 108 ? 0.3752 0.5829 0.4380 -0.0092 -0.0772 -0.0658 108 PRO A CA  
756   C C   . PRO A 108 ? 0.4237 0.6616 0.5088 -0.0124 -0.0933 -0.0748 108 PRO A C   
757   O O   . PRO A 108 ? 0.4548 0.6929 0.5755 -0.0212 -0.0932 -0.0785 108 PRO A O   
758   C CB  . PRO A 108 ? 0.3529 0.5507 0.4129 -0.0030 -0.0658 -0.0403 108 PRO A CB  
759   C CG  . PRO A 108 ? 0.3409 0.5531 0.3710 0.0080  -0.0698 -0.0294 108 PRO A CG  
760   C CD  . PRO A 108 ? 0.3620 0.5763 0.3673 0.0087  -0.0733 -0.0453 108 PRO A CD  
761   N N   . VAL A 109 ? 0.4172 0.6825 0.4810 -0.0048 -0.1073 -0.0778 109 VAL A N   
762   C CA  . VAL A 109 ? 0.4001 0.6993 0.4807 -0.0057 -0.1260 -0.0873 109 VAL A CA  
763   C C   . VAL A 109 ? 0.4339 0.7401 0.5260 -0.0152 -0.1376 -0.1187 109 VAL A C   
764   O O   . VAL A 109 ? 0.4642 0.7797 0.5946 -0.0251 -0.1448 -0.1306 109 VAL A O   
765   C CB  . VAL A 109 ? 0.4019 0.7292 0.4518 0.0081  -0.1373 -0.0759 109 VAL A CB  
766   C CG1 . VAL A 109 ? 0.4200 0.7858 0.4813 0.0082  -0.1604 -0.0909 109 VAL A CG1 
767   C CG2 . VAL A 109 ? 0.3327 0.6542 0.3814 0.0169  -0.1275 -0.0448 109 VAL A CG2 
768   N N   . THR A 110 ? 0.4438 0.7451 0.5059 -0.0127 -0.1386 -0.1333 110 THR A N   
769   C CA  . THR A 110 ? 0.4813 0.7889 0.5538 -0.0209 -0.1503 -0.1662 110 THR A CA  
770   C C   . THR A 110 ? 0.5045 0.7755 0.5997 -0.0319 -0.1367 -0.1756 110 THR A C   
771   O O   . THR A 110 ? 0.5671 0.8364 0.6861 -0.0421 -0.1440 -0.2015 110 THR A O   
772   C CB  . THR A 110 ? 0.4752 0.7978 0.5046 -0.0121 -0.1586 -0.1819 110 THR A CB  
773   O OG1 . THR A 110 ? 0.4965 0.7920 0.4999 -0.0075 -0.1412 -0.1749 110 THR A OG1 
774   C CG2 . THR A 110 ? 0.4860 0.8433 0.4870 0.0007  -0.1703 -0.1679 110 THR A CG2 
775   N N   . GLN A 111 ? 0.4819 0.7238 0.5707 -0.0296 -0.1176 -0.1543 111 GLN A N   
776   C CA  . GLN A 111 ? 0.5290 0.7343 0.6332 -0.0372 -0.1035 -0.1585 111 GLN A CA  
777   C C   . GLN A 111 ? 0.5467 0.7407 0.6329 -0.0359 -0.1041 -0.1813 111 GLN A C   
778   O O   . GLN A 111 ? 0.5500 0.7160 0.6541 -0.0427 -0.0964 -0.1907 111 GLN A O   
779   C CB  . GLN A 111 ? 0.5959 0.7949 0.7479 -0.0510 -0.1032 -0.1640 111 GLN A CB  
780   C CG  . GLN A 111 ? 0.6754 0.8732 0.8419 -0.0506 -0.0934 -0.1371 111 GLN A CG  
781   C CD  . GLN A 111 ? 0.7885 0.9908 1.0030 -0.0634 -0.0942 -0.1410 111 GLN A CD  
782   O OE1 . GLN A 111 ? 0.8542 1.0301 1.0917 -0.0722 -0.0815 -0.1391 111 GLN A OE1 
783   N NE2 . GLN A 111 ? 0.8097 1.0467 1.0414 -0.0642 -0.1088 -0.1449 111 GLN A NE2 
784   N N   . GLU A 112 ? 0.5515 0.7684 0.6032 -0.0266 -0.1132 -0.1899 112 GLU A N   
785   C CA  . GLU A 112 ? 0.5439 0.7517 0.5697 -0.0212 -0.1098 -0.2062 112 GLU A CA  
786   C C   . GLU A 112 ? 0.5195 0.7013 0.5308 -0.0153 -0.0908 -0.1839 112 GLU A C   
787   O O   . GLU A 112 ? 0.4865 0.6691 0.4915 -0.0113 -0.0842 -0.1569 112 GLU A O   
788   C CB  . GLU A 112 ? 0.5852 0.8262 0.5720 -0.0107 -0.1207 -0.2146 112 GLU A CB  
789   C CG  . GLU A 112 ? 0.6629 0.9333 0.6525 -0.0133 -0.1416 -0.2434 112 GLU A CG  
790   C CD  . GLU A 112 ? 0.7494 1.0555 0.6944 -0.0001 -0.1506 -0.2401 112 GLU A CD  
791   O OE1 . GLU A 112 ? 0.8019 1.1192 0.7308 0.0032  -0.1575 -0.2602 112 GLU A OE1 
792   O OE2 . GLU A 112 ? 0.7629 1.0756 0.6904 0.0077  -0.1446 -0.2091 112 GLU A OE2 
793   N N   . SER A 113 ? 0.5376 0.6977 0.5445 -0.0141 -0.0827 -0.1962 113 SER A N   
794   C CA  . SER A 113 ? 0.5817 0.7232 0.5717 -0.0068 -0.0670 -0.1781 113 SER A CA  
795   C C   . SER A 113 ? 0.5738 0.7175 0.5377 0.0017  -0.0636 -0.1938 113 SER A C   
796   O O   . SER A 113 ? 0.6120 0.7653 0.5729 0.0014  -0.0722 -0.2216 113 SER A O   
797   C CB  . SER A 113 ? 0.6383 0.7451 0.6557 -0.0129 -0.0559 -0.1683 113 SER A CB  
798   O OG  . SER A 113 ? 0.6914 0.7792 0.7301 -0.0188 -0.0569 -0.1908 113 SER A OG  
799   N N   . GLY A 114 ? 0.5422 0.6801 0.4871 0.0097  -0.0513 -0.1767 114 GLY A N   
800   C CA  . GLY A 114 ? 0.5387 0.6809 0.4607 0.0184  -0.0455 -0.1888 114 GLY A CA  
801   C C   . GLY A 114 ? 0.4926 0.6161 0.4125 0.0237  -0.0302 -0.1728 114 GLY A C   
802   O O   . GLY A 114 ? 0.4630 0.5785 0.3875 0.0229  -0.0246 -0.1481 114 GLY A O   
803   N N   . LEU A 115 ? 0.5309 0.6489 0.4446 0.0298  -0.0239 -0.1885 115 LEU A N   
804   C CA  . LEU A 115 ? 0.5240 0.6271 0.4390 0.0354  -0.0106 -0.1756 115 LEU A CA  
805   C C   . LEU A 115 ? 0.4663 0.5922 0.3550 0.0429  -0.0030 -0.1607 115 LEU A C   
806   O O   . LEU A 115 ? 0.4944 0.6415 0.3612 0.0492  -0.0014 -0.1731 115 LEU A O   
807   C CB  . LEU A 115 ? 0.5399 0.6260 0.4655 0.0395  -0.0063 -0.1978 115 LEU A CB  
808   C CG  . LEU A 115 ? 0.5736 0.6409 0.5090 0.0444  0.0050  -0.1825 115 LEU A CG  
809   C CD1 . LEU A 115 ? 0.5629 0.6007 0.5237 0.0382  0.0042  -0.1697 115 LEU A CD1 
810   C CD2 . LEU A 115 ? 0.6582 0.7214 0.5949 0.0535  0.0121  -0.2005 115 LEU A CD2 
811   N N   . GLY A 116 ? 0.4246 0.5458 0.3162 0.0422  0.0025  -0.1342 116 GLY A N   
812   C CA  . GLY A 116 ? 0.4481 0.5872 0.3212 0.0479  0.0112  -0.1179 116 GLY A CA  
813   C C   . GLY A 116 ? 0.4543 0.5825 0.3359 0.0522  0.0231  -0.1127 116 GLY A C   
814   O O   . GLY A 116 ? 0.4933 0.5994 0.3937 0.0521  0.0239  -0.1200 116 GLY A O   
815   N N   . GLU A 117 ? 0.4134 0.5580 0.2829 0.0563  0.0322  -0.0987 117 GLU A N   
816   C CA  . GLU A 117 ? 0.4200 0.5597 0.3001 0.0602  0.0431  -0.0935 117 GLU A CA  
817   C C   . GLU A 117 ? 0.3944 0.5281 0.2836 0.0563  0.0451  -0.0685 117 GLU A C   
818   O O   . GLU A 117 ? 0.3842 0.5291 0.2631 0.0540  0.0440  -0.0536 117 GLU A O   
819   C CB  . GLU A 117 ? 0.4483 0.6126 0.3117 0.0673  0.0538  -0.0986 117 GLU A CB  
820   C CG  . GLU A 117 ? 0.4775 0.6402 0.3559 0.0720  0.0652  -0.0976 117 GLU A CG  
821   C CD  . GLU A 117 ? 0.5183 0.7093 0.3804 0.0786  0.0783  -0.0996 117 GLU A CD  
822   O OE1 . GLU A 117 ? 0.5115 0.7214 0.3557 0.0775  0.0825  -0.0835 117 GLU A OE1 
823   O OE2 . GLU A 117 ? 0.5255 0.7199 0.3931 0.0854  0.0852  -0.1164 117 GLU A OE2 
824   N N   . LEU A 118 ? 0.3430 0.4588 0.2521 0.0560  0.0469  -0.0644 118 LEU A N   
825   C CA  . LEU A 118 ? 0.3403 0.4508 0.2587 0.0526  0.0484  -0.0439 118 LEU A CA  
826   C C   . LEU A 118 ? 0.3518 0.4831 0.2644 0.0541  0.0586  -0.0314 118 LEU A C   
827   O O   . LEU A 118 ? 0.3733 0.5180 0.2834 0.0589  0.0670  -0.0384 118 LEU A O   
828   C CB  . LEU A 118 ? 0.2881 0.3789 0.2262 0.0534  0.0476  -0.0438 118 LEU A CB  
829   C CG  . LEU A 118 ? 0.2751 0.3574 0.2233 0.0498  0.0465  -0.0271 118 LEU A CG  
830   C CD1 . LEU A 118 ? 0.2662 0.3389 0.2111 0.0445  0.0397  -0.0200 118 LEU A CD1 
831   C CD2 . LEU A 118 ? 0.2792 0.3473 0.2429 0.0527  0.0451  -0.0294 118 LEU A CD2 
832   N N   . ALA A 119 ? 0.3594 0.4930 0.2712 0.0502  0.0587  -0.0127 119 ALA A N   
833   C CA  . ALA A 119 ? 0.2913 0.4421 0.1997 0.0505  0.0689  0.0024  119 ALA A CA  
834   C C   . ALA A 119 ? 0.3418 0.4819 0.2692 0.0459  0.0700  0.0186  119 ALA A C   
835   O O   . ALA A 119 ? 0.3294 0.4516 0.2657 0.0430  0.0621  0.0192  119 ALA A O   
836   C CB  . ALA A 119 ? 0.3084 0.4757 0.1934 0.0516  0.0680  0.0096  119 ALA A CB  
837   N N   . GLN A 120 ? 0.3784 0.5299 0.3132 0.0450  0.0807  0.0310  120 GLN A N   
838   C CA  . GLN A 120 ? 0.3621 0.5040 0.3180 0.0400  0.0820  0.0445  120 GLN A CA  
839   C C   . GLN A 120 ? 0.3801 0.5357 0.3340 0.0383  0.0923  0.0644  120 GLN A C   
840   O O   . GLN A 120 ? 0.3849 0.5601 0.3294 0.0411  0.1029  0.0665  120 GLN A O   
841   C CB  . GLN A 120 ? 0.3825 0.5212 0.3616 0.0397  0.0842  0.0368  120 GLN A CB  
842   C CG  . GLN A 120 ? 0.3984 0.5287 0.4015 0.0342  0.0843  0.0464  120 GLN A CG  
843   C CD  . GLN A 120 ? 0.4446 0.5779 0.4712 0.0345  0.0857  0.0380  120 GLN A CD  
844   O OE1 . GLN A 120 ? 0.4449 0.5683 0.4751 0.0376  0.0771  0.0256  120 GLN A OE1 
845   N NE2 . GLN A 120 ? 0.4855 0.6341 0.5293 0.0317  0.0970  0.0456  120 GLN A NE2 
846   N N   . ASP A 121 ? 0.3820 0.5275 0.3429 0.0347  0.0899  0.0795  121 ASP A N   
847   C CA  . ASP A 121 ? 0.3577 0.5123 0.3201 0.0331  0.1000  0.1018  121 ASP A CA  
848   C C   . ASP A 121 ? 0.3382 0.4751 0.3197 0.0287  0.0967  0.1146  121 ASP A C   
849   O O   . ASP A 121 ? 0.3736 0.4932 0.3657 0.0270  0.0872  0.1048  121 ASP A O   
850   C CB  . ASP A 121 ? 0.3637 0.5346 0.2950 0.0386  0.1005  0.1091  121 ASP A CB  
851   C CG  . ASP A 121 ? 0.4039 0.5920 0.3305 0.0393  0.1155  0.1304  121 ASP A CG  
852   O OD1 . ASP A 121 ? 0.4125 0.5948 0.3640 0.0340  0.1243  0.1456  121 ASP A OD1 
853   O OD2 . ASP A 121 ? 0.4513 0.6557 0.3511 0.0445  0.1165  0.1298  121 ASP A OD2 
854   N N   . VAL A 122 ? 0.3432 0.4839 0.3297 0.0272  0.1055  0.1367  122 VAL A N   
855   C CA  . VAL A 122 ? 0.3843 0.5072 0.3896 0.0241  0.1030  0.1496  122 VAL A CA  
856   C C   . VAL A 122 ? 0.4106 0.5270 0.4001 0.0287  0.0921  0.1532  122 VAL A C   
857   O O   . VAL A 122 ? 0.4248 0.5556 0.3897 0.0341  0.0911  0.1604  122 VAL A O   
858   C CB  . VAL A 122 ? 0.4321 0.5594 0.4510 0.0212  0.1171  0.1745  122 VAL A CB  
859   C CG1 . VAL A 122 ? 0.4281 0.5353 0.4662 0.0193  0.1144  0.1885  122 VAL A CG1 
860   C CG2 . VAL A 122 ? 0.4438 0.5762 0.4882 0.0147  0.1277  0.1706  122 VAL A CG2 
861   N N   . LEU A 123 ? 0.3987 0.4958 0.4030 0.0272  0.0837  0.1474  123 LEU A N   
862   C CA  . LEU A 123 ? 0.3777 0.4682 0.3772 0.0312  0.0760  0.1549  123 LEU A CA  
863   C C   . LEU A 123 ? 0.4022 0.4747 0.4289 0.0289  0.0788  0.1675  123 LEU A C   
864   O O   . LEU A 123 ? 0.4173 0.4765 0.4666 0.0236  0.0803  0.1591  123 LEU A O   
865   C CB  . LEU A 123 ? 0.3411 0.4254 0.3334 0.0326  0.0642  0.1357  123 LEU A CB  
866   C CG  . LEU A 123 ? 0.3544 0.4329 0.3471 0.0364  0.0560  0.1402  123 LEU A CG  
867   C CD1 . LEU A 123 ? 0.3219 0.4077 0.2981 0.0385  0.0466  0.1260  123 LEU A CD1 
868   C CD2 . LEU A 123 ? 0.3366 0.3939 0.3527 0.0345  0.0549  0.1371  123 LEU A CD2 
869   N N   . ALA A 124 ? 0.3751 0.4472 0.4003 0.0335  0.0787  0.1867  124 ALA A N   
870   C CA  . ALA A 124 ? 0.3426 0.3954 0.3950 0.0327  0.0809  0.1983  124 ALA A CA  
871   C C   . ALA A 124 ? 0.3821 0.4286 0.4335 0.0393  0.0712  0.1991  124 ALA A C   
872   O O   . ALA A 124 ? 0.3933 0.4546 0.4227 0.0452  0.0645  0.2011  124 ALA A O   
873   C CB  . ALA A 124 ? 0.3427 0.3980 0.4034 0.0324  0.0909  0.2213  124 ALA A CB  
874   N N   . ILE A 125 ? 0.3890 0.4145 0.4665 0.0383  0.0708  0.1966  125 ILE A N   
875   C CA  . ILE A 125 ? 0.3945 0.4120 0.4778 0.0447  0.0634  0.1954  125 ILE A CA  
876   C C   . ILE A 125 ? 0.3905 0.3848 0.5065 0.0448  0.0679  0.2032  125 ILE A C   
877   O O   . ILE A 125 ? 0.4365 0.4182 0.5722 0.0377  0.0739  0.1989  125 ILE A O   
878   C CB  . ILE A 125 ? 0.3627 0.3790 0.4390 0.0438  0.0559  0.1701  125 ILE A CB  
879   C CG1 . ILE A 125 ? 0.3413 0.3555 0.4219 0.0509  0.0494  0.1694  125 ILE A CG1 
880   C CG2 . ILE A 125 ? 0.3600 0.3609 0.4516 0.0372  0.0584  0.1530  125 ILE A CG2 
881   C CD1 . ILE A 125 ? 0.3259 0.3405 0.3994 0.0501  0.0441  0.1480  125 ILE A CD1 
882   N N   . HIS A 126 ? 0.3648 0.3546 0.4890 0.0528  0.0643  0.2127  126 HIS A N   
883   C CA  . HIS A 126 ? 0.3900 0.3592 0.5452 0.0536  0.0673  0.2149  126 HIS A CA  
884   C C   . HIS A 126 ? 0.3889 0.3362 0.5648 0.0515  0.0675  0.1963  126 HIS A C   
885   O O   . HIS A 126 ? 0.3636 0.3149 0.5289 0.0536  0.0614  0.1780  126 HIS A O   
886   C CB  . HIS A 126 ? 0.4266 0.4001 0.5840 0.0633  0.0621  0.2241  126 HIS A CB  
887   C CG  . HIS A 126 ? 0.4798 0.4663 0.6291 0.0662  0.0634  0.2447  126 HIS A CG  
888   N ND1 . HIS A 126 ? 0.5009 0.5109 0.6243 0.0721  0.0568  0.2524  126 HIS A ND1 
889   C CD2 . HIS A 126 ? 0.5163 0.4956 0.6799 0.0644  0.0706  0.2591  126 HIS A CD2 
890   C CE1 . HIS A 126 ? 0.5349 0.5516 0.6546 0.0745  0.0597  0.2707  126 HIS A CE1 
891   N NE2 . HIS A 126 ? 0.5489 0.5469 0.6930 0.0699  0.0687  0.2762  126 HIS A NE2 
892   N N   . SER A 127 ? 0.4143 0.3435 0.6178 0.0460  0.0728  0.1938  127 SER A N   
893   C CA  . SER A 127 ? 0.4591 0.3671 0.6844 0.0459  0.0717  0.1739  127 SER A CA  
894   C C   . SER A 127 ? 0.5195 0.4188 0.7618 0.0535  0.0708  0.1777  127 SER A C   
895   O O   . SER A 127 ? 0.5266 0.4379 0.7601 0.0596  0.0693  0.1944  127 SER A O   
896   C CB  . SER A 127 ? 0.4606 0.3553 0.7090 0.0352  0.0760  0.1642  127 SER A CB  
897   O OG  . SER A 127 ? 0.4698 0.3634 0.7349 0.0315  0.0824  0.1817  127 SER A OG  
898   N N   . THR A 128 ? 0.5280 0.4073 0.7939 0.0535  0.0712  0.1605  128 THR A N   
899   C CA  . THR A 128 ? 0.5109 0.3809 0.7957 0.0601  0.0715  0.1637  128 THR A CA  
900   C C   . THR A 128 ? 0.5407 0.3911 0.8576 0.0535  0.0760  0.1593  128 THR A C   
901   O O   . THR A 128 ? 0.5444 0.3869 0.8712 0.0444  0.0773  0.1462  128 THR A O   
902   C CB  . THR A 128 ? 0.4709 0.3369 0.7555 0.0688  0.0679  0.1456  128 THR A CB  
903   O OG1 . THR A 128 ? 0.5006 0.3506 0.7965 0.0651  0.0683  0.1192  128 THR A OG1 
904   C CG2 . THR A 128 ? 0.3802 0.2664 0.6367 0.0743  0.0637  0.1474  128 THR A CG2 
905   N N   . HIS A 129 ? 0.5354 0.3787 0.8699 0.0581  0.0781  0.1711  129 HIS A N   
906   C CA  . HIS A 129 ? 0.5580 0.3820 0.9263 0.0529  0.0824  0.1680  129 HIS A CA  
907   C C   . HIS A 129 ? 0.5233 0.3350 0.9085 0.0622  0.0815  0.1643  129 HIS A C   
908   O O   . HIS A 129 ? 0.5416 0.3572 0.9281 0.0691  0.0824  0.1854  129 HIS A O   
909   C CB  . HIS A 129 ? 0.6545 0.4829 1.0298 0.0480  0.0887  0.1937  129 HIS A CB  
910   C CG  . HIS A 129 ? 0.7744 0.5835 1.1875 0.0415  0.0940  0.1917  129 HIS A CG  
911   N ND1 . HIS A 129 ? 0.8177 0.6150 1.2513 0.0318  0.0939  0.1685  129 HIS A ND1 
912   C CD2 . HIS A 129 ? 0.8415 0.6408 1.2772 0.0437  0.0990  0.2091  129 HIS A CD2 
913   C CE1 . HIS A 129 ? 0.8572 0.6391 1.3257 0.0276  0.0986  0.1711  129 HIS A CE1 
914   N NE2 . HIS A 129 ? 0.8760 0.6576 1.3466 0.0348  0.1024  0.1964  129 HIS A NE2 
915   N N   . GLY A 130 ? 0.5252 0.3227 0.9227 0.0630  0.0796  0.1373  130 GLY A N   
916   C CA  . GLY A 130 ? 0.5569 0.3448 0.9676 0.0732  0.0790  0.1313  130 GLY A CA  
917   C C   . GLY A 130 ? 0.5759 0.3806 0.9643 0.0847  0.0756  0.1388  130 GLY A C   
918   O O   . GLY A 130 ? 0.5834 0.4005 0.9485 0.0858  0.0727  0.1287  130 GLY A O   
919   N N   . SER A 131 ? 0.6023 0.4086 0.9990 0.0936  0.0757  0.1567  131 SER A N   
920   C CA  . SER A 131 ? 0.5904 0.4150 0.9700 0.1044  0.0715  0.1631  131 SER A CA  
921   C C   . SER A 131 ? 0.5816 0.4278 0.9383 0.1037  0.0688  0.1880  131 SER A C   
922   O O   . SER A 131 ? 0.6011 0.4662 0.9429 0.1113  0.0639  0.1946  131 SER A O   
923   C CB  . SER A 131 ? 0.5912 0.4088 0.9918 0.1160  0.0715  0.1677  131 SER A CB  
924   O OG  . SER A 131 ? 0.5625 0.3794 0.9725 0.1182  0.0722  0.1955  131 SER A OG  
925   N N   . LYS A 132 ? 0.5632 0.4085 0.9176 0.0946  0.0719  0.2004  132 LYS A N   
926   C CA  . LYS A 132 ? 0.5315 0.3978 0.8623 0.0944  0.0701  0.2236  132 LYS A CA  
927   C C   . LYS A 132 ? 0.5063 0.3844 0.8133 0.0860  0.0697  0.2182  132 LYS A C   
928   O O   . LYS A 132 ? 0.4933 0.3617 0.8039 0.0792  0.0713  0.1984  132 LYS A O   
929   C CB  . LYS A 132 ? 0.5390 0.4000 0.8818 0.0927  0.0751  0.2475  132 LYS A CB  
930   C CG  . LYS A 132 ? 0.5923 0.4490 0.9501 0.1034  0.0740  0.2632  132 LYS A CG  
931   C CD  . LYS A 132 ? 0.6625 0.5324 1.0070 0.1048  0.0752  0.2928  132 LYS A CD  
932   C CE  . LYS A 132 ? 0.7622 0.6279 1.1207 0.1160  0.0741  0.3127  132 LYS A CE  
933   N NZ  . LYS A 132 ? 0.8139 0.6514 1.2106 0.1172  0.0790  0.3073  132 LYS A NZ  
934   N N   . LEU A 133 ? 0.5159 0.4155 0.7979 0.0870  0.0672  0.2355  133 LEU A N   
935   C CA  . LEU A 133 ? 0.5383 0.4502 0.7974 0.0792  0.0678  0.2344  133 LEU A CA  
936   C C   . LEU A 133 ? 0.5613 0.4605 0.8359 0.0693  0.0759  0.2373  133 LEU A C   
937   O O   . LEU A 133 ? 0.6145 0.5056 0.9066 0.0697  0.0805  0.2518  133 LEU A O   
938   C CB  . LEU A 133 ? 0.5384 0.4764 0.7687 0.0834  0.0635  0.2520  133 LEU A CB  
939   C CG  . LEU A 133 ? 0.4968 0.4520 0.7118 0.0917  0.0542  0.2476  133 LEU A CG  
940   C CD1 . LEU A 133 ? 0.4785 0.4597 0.6664 0.0952  0.0488  0.2633  133 LEU A CD1 
941   C CD2 . LEU A 133 ? 0.4154 0.3709 0.6221 0.0879  0.0527  0.2263  133 LEU A CD2 
942   N N   . GLY A 134 ? 0.5454 0.4430 0.8159 0.0604  0.0777  0.2238  134 GLY A N   
943   C CA  . GLY A 134 ? 0.5278 0.4161 0.8159 0.0501  0.0850  0.2248  134 GLY A CA  
944   C C   . GLY A 134 ? 0.5214 0.4290 0.7867 0.0454  0.0883  0.2372  134 GLY A C   
945   O O   . GLY A 134 ? 0.4898 0.4176 0.7254 0.0508  0.0845  0.2462  134 GLY A O   
946   N N   . PRO A 135 ? 0.5535 0.4567 0.8334 0.0352  0.0951  0.2359  135 PRO A N   
947   C CA  . PRO A 135 ? 0.5661 0.4887 0.8259 0.0310  0.0998  0.2470  135 PRO A CA  
948   C C   . PRO A 135 ? 0.5003 0.4385 0.7293 0.0310  0.0948  0.2364  135 PRO A C   
949   O O   . PRO A 135 ? 0.4852 0.4161 0.7135 0.0314  0.0891  0.2183  135 PRO A O   
950   C CB  . PRO A 135 ? 0.6005 0.5130 0.8904 0.0196  0.1077  0.2432  135 PRO A CB  
951   C CG  . PRO A 135 ? 0.5934 0.4832 0.9126 0.0167  0.1040  0.2221  135 PRO A CG  
952   C CD  . PRO A 135 ? 0.5786 0.4605 0.8961 0.0273  0.0987  0.2237  135 PRO A CD  
953   N N   . MET A 136 ? 0.4802 0.4401 0.6825 0.0316  0.0971  0.2476  136 MET A N   
954   C CA  . MET A 136 ? 0.4916 0.4672 0.6659 0.0308  0.0937  0.2375  136 MET A CA  
955   C C   . MET A 136 ? 0.4627 0.4312 0.6521 0.0207  0.0973  0.2221  136 MET A C   
956   O O   . MET A 136 ? 0.5123 0.4760 0.7255 0.0130  0.1047  0.2243  136 MET A O   
957   C CB  . MET A 136 ? 0.5134 0.5138 0.6580 0.0333  0.0962  0.2503  136 MET A CB  
958   C CG  . MET A 136 ? 0.5329 0.5408 0.6661 0.0426  0.0931  0.2671  136 MET A CG  
959   S SD  . MET A 136 ? 0.5829 0.5999 0.6938 0.0517  0.0794  0.2591  136 MET A SD  
960   C CE  . MET A 136 ? 0.6249 0.6680 0.6975 0.0509  0.0771  0.2515  136 MET A CE  
961   N N   . VAL A 137 ? 0.4036 0.3734 0.5803 0.0206  0.0913  0.2053  137 VAL A N   
962   C CA  . VAL A 137 ? 0.3970 0.3682 0.5807 0.0125  0.0904  0.1834  137 VAL A CA  
963   C C   . VAL A 137 ? 0.4026 0.3969 0.5526 0.0140  0.0879  0.1768  137 VAL A C   
964   O O   . VAL A 137 ? 0.4174 0.4212 0.5413 0.0210  0.0829  0.1796  137 VAL A O   
965   C CB  . VAL A 137 ? 0.3612 0.3161 0.5569 0.0125  0.0817  0.1583  137 VAL A CB  
966   C CG1 . VAL A 137 ? 0.4004 0.3319 0.6330 0.0103  0.0851  0.1620  137 VAL A CG1 
967   C CG2 . VAL A 137 ? 0.3419 0.2987 0.5142 0.0214  0.0735  0.1520  137 VAL A CG2 
968   N N   . LYS A 138 ? 0.3817 0.3854 0.5352 0.0076  0.0912  0.1676  138 LYS A N   
969   C CA  . LYS A 138 ? 0.3792 0.4043 0.5047 0.0093  0.0909  0.1624  138 LYS A CA  
970   C C   . LYS A 138 ? 0.3856 0.4121 0.5048 0.0085  0.0824  0.1364  138 LYS A C   
971   O O   . LYS A 138 ? 0.3989 0.4157 0.5392 0.0041  0.0793  0.1227  138 LYS A O   
972   C CB  . LYS A 138 ? 0.3995 0.4396 0.5311 0.0047  0.1038  0.1756  138 LYS A CB  
973   C CG  . LYS A 138 ? 0.4411 0.4843 0.5724 0.0065  0.1144  0.2056  138 LYS A CG  
974   C CD  . LYS A 138 ? 0.4993 0.5586 0.6352 0.0021  0.1271  0.2143  138 LYS A CD  
975   C CE  . LYS A 138 ? 0.5852 0.6470 0.7146 0.0060  0.1318  0.2347  138 LYS A CE  
976   N NZ  . LYS A 138 ? 0.6320 0.7102 0.7616 0.0027  0.1440  0.2417  138 LYS A NZ  
977   N N   . VAL A 139 ? 0.3748 0.4135 0.4651 0.0131  0.0782  0.1299  139 VAL A N   
978   C CA  . VAL A 139 ? 0.3271 0.3717 0.4086 0.0131  0.0732  0.1105  139 VAL A CA  
979   C C   . VAL A 139 ? 0.3655 0.4297 0.4388 0.0128  0.0812  0.1144  139 VAL A C   
980   O O   . VAL A 139 ? 0.4053 0.4811 0.4540 0.0172  0.0817  0.1178  139 VAL A O   
981   C CB  . VAL A 139 ? 0.3537 0.3959 0.4116 0.0186  0.0639  0.1002  139 VAL A CB  
982   C CG1 . VAL A 139 ? 0.3375 0.3826 0.3878 0.0193  0.0591  0.0824  139 VAL A CG1 
983   C CG2 . VAL A 139 ? 0.3607 0.3865 0.4254 0.0201  0.0585  0.0984  139 VAL A CG2 
984   N N   . PRO A 140 ? 0.3708 0.4407 0.4656 0.0077  0.0873  0.1123  140 PRO A N   
985   C CA  . PRO A 140 ? 0.3832 0.4736 0.4743 0.0074  0.0983  0.1188  140 PRO A CA  
986   C C   . PRO A 140 ? 0.3764 0.4793 0.4446 0.0128  0.0952  0.1043  140 PRO A C   
987   O O   . PRO A 140 ? 0.3584 0.4790 0.4141 0.0150  0.1041  0.1096  140 PRO A O   
988   C CB  . PRO A 140 ? 0.3762 0.4686 0.5034 -0.0002 0.1042  0.1172  140 PRO A CB  
989   C CG  . PRO A 140 ? 0.3596 0.4311 0.5085 -0.0042 0.0972  0.1139  140 PRO A CG  
990   C CD  . PRO A 140 ? 0.3540 0.4137 0.4795 0.0020  0.0846  0.1034  140 PRO A CD  
991   N N   . GLN A 141 ? 0.4048 0.4987 0.4688 0.0151  0.0840  0.0867  141 GLN A N   
992   C CA  . GLN A 141 ? 0.4465 0.5475 0.4911 0.0206  0.0804  0.0733  141 GLN A CA  
993   C C   . GLN A 141 ? 0.4200 0.5092 0.4440 0.0242  0.0701  0.0672  141 GLN A C   
994   O O   . GLN A 141 ? 0.4055 0.4863 0.4271 0.0264  0.0623  0.0539  141 GLN A O   
995   C CB  . GLN A 141 ? 0.5239 0.6266 0.5842 0.0211  0.0773  0.0585  141 GLN A CB  
996   C CG  . GLN A 141 ? 0.5999 0.7193 0.6823 0.0180  0.0880  0.0618  141 GLN A CG  
997   C CD  . GLN A 141 ? 0.7040 0.8178 0.8170 0.0106  0.0886  0.0669  141 GLN A CD  
998   O OE1 . GLN A 141 ? 0.7279 0.8250 0.8455 0.0094  0.0787  0.0621  141 GLN A OE1 
999   N NE2 . GLN A 141 ? 0.7823 0.9098 0.9172 0.0055  0.1011  0.0766  141 GLN A NE2 
1000  N N   . PHE A 142 ? 0.3741 0.4638 0.3848 0.0250  0.0702  0.0780  142 PHE A N   
1001  C CA  . PHE A 142 ? 0.3179 0.3999 0.3130 0.0277  0.0612  0.0727  142 PHE A CA  
1002  C C   . PHE A 142 ? 0.2857 0.3760 0.2629 0.0312  0.0590  0.0603  142 PHE A C   
1003  O O   . PHE A 142 ? 0.3114 0.4175 0.2778 0.0331  0.0646  0.0616  142 PHE A O   
1004  C CB  . PHE A 142 ? 0.3046 0.3880 0.2935 0.0284  0.0610  0.0877  142 PHE A CB  
1005  C CG  . PHE A 142 ? 0.2754 0.3526 0.2546 0.0305  0.0519  0.0829  142 PHE A CG  
1006  C CD1 . PHE A 142 ? 0.2767 0.3379 0.2667 0.0296  0.0473  0.0800  142 PHE A CD1 
1007  C CD2 . PHE A 142 ? 0.3174 0.4066 0.2778 0.0332  0.0482  0.0805  142 PHE A CD2 
1008  C CE1 . PHE A 142 ? 0.2843 0.3418 0.2683 0.0312  0.0407  0.0764  142 PHE A CE1 
1009  C CE2 . PHE A 142 ? 0.3027 0.3881 0.2592 0.0340  0.0399  0.0757  142 PHE A CE2 
1010  C CZ  . PHE A 142 ? 0.3067 0.3764 0.2761 0.0328  0.0370  0.0746  142 PHE A CZ  
1011  N N   . LEU A 143 ? 0.2695 0.3486 0.2441 0.0322  0.0515  0.0480  143 LEU A N   
1012  C CA  . LEU A 143 ? 0.2913 0.3738 0.2532 0.0350  0.0488  0.0350  143 LEU A CA  
1013  C C   . LEU A 143 ? 0.3008 0.3852 0.2494 0.0351  0.0430  0.0341  143 LEU A C   
1014  O O   . LEU A 143 ? 0.3351 0.4108 0.2869 0.0335  0.0383  0.0386  143 LEU A O   
1015  C CB  . LEU A 143 ? 0.2862 0.3548 0.2551 0.0363  0.0445  0.0235  143 LEU A CB  
1016  C CG  . LEU A 143 ? 0.2711 0.3408 0.2549 0.0371  0.0478  0.0221  143 LEU A CG  
1017  C CD1 . LEU A 143 ? 0.3074 0.3630 0.2957 0.0397  0.0416  0.0136  143 LEU A CD1 
1018  C CD2 . LEU A 143 ? 0.2687 0.3549 0.2525 0.0395  0.0551  0.0184  143 LEU A CD2 
1019  N N   . PHE A 144 ? 0.3387 0.4362 0.2734 0.0373  0.0432  0.0267  144 PHE A N   
1020  C CA  . PHE A 144 ? 0.3525 0.4563 0.2754 0.0374  0.0363  0.0232  144 PHE A CA  
1021  C C   . PHE A 144 ? 0.3596 0.4729 0.2704 0.0399  0.0357  0.0062  144 PHE A C   
1022  O O   . PHE A 144 ? 0.3554 0.4688 0.2683 0.0423  0.0413  -0.0017 144 PHE A O   
1023  C CB  . PHE A 144 ? 0.3306 0.4478 0.2457 0.0383  0.0367  0.0395  144 PHE A CB  
1024  C CG  . PHE A 144 ? 0.3568 0.4928 0.2589 0.0415  0.0448  0.0458  144 PHE A CG  
1025  C CD1 . PHE A 144 ? 0.3463 0.4820 0.2581 0.0408  0.0551  0.0567  144 PHE A CD1 
1026  C CD2 . PHE A 144 ? 0.3818 0.5372 0.2623 0.0451  0.0424  0.0406  144 PHE A CD2 
1027  C CE1 . PHE A 144 ? 0.3715 0.5255 0.2728 0.0433  0.0649  0.0644  144 PHE A CE1 
1028  C CE2 . PHE A 144 ? 0.4091 0.5833 0.2745 0.0489  0.0514  0.0474  144 PHE A CE2 
1029  C CZ  . PHE A 144 ? 0.3985 0.5719 0.2747 0.0479  0.0638  0.0605  144 PHE A CZ  
1030  N N   . SER A 145 ? 0.3513 0.4735 0.2514 0.0399  0.0283  -0.0008 145 SER A N   
1031  C CA  . SER A 145 ? 0.3424 0.4735 0.2314 0.0421  0.0260  -0.0201 145 SER A CA  
1032  C C   . SER A 145 ? 0.3676 0.5252 0.2331 0.0462  0.0263  -0.0187 145 SER A C   
1033  O O   . SER A 145 ? 0.3866 0.5548 0.2449 0.0463  0.0212  -0.0072 145 SER A O   
1034  C CB  . SER A 145 ? 0.3577 0.4782 0.2552 0.0380  0.0160  -0.0337 145 SER A CB  
1035  O OG  . SER A 145 ? 0.3931 0.5219 0.2819 0.0394  0.0119  -0.0551 145 SER A OG  
1036  N N   . CYS A 146 ? 0.4008 0.5701 0.2541 0.0508  0.0327  -0.0298 146 CYS A N   
1037  C CA  . CYS A 146 ? 0.4234 0.6191 0.2499 0.0558  0.0320  -0.0347 146 CYS A CA  
1038  C C   . CYS A 146 ? 0.4993 0.6972 0.3207 0.0554  0.0204  -0.0605 146 CYS A C   
1039  O O   . CYS A 146 ? 0.5260 0.7167 0.3521 0.0566  0.0224  -0.0812 146 CYS A O   
1040  C CB  . CYS A 146 ? 0.4127 0.6226 0.2276 0.0616  0.0461  -0.0357 146 CYS A CB  
1041  S SG  . CYS A 146 ? 0.5053 0.7257 0.3179 0.0624  0.0597  -0.0032 146 CYS A SG  
1042  N N   . ALA A 147 ? 0.5548 0.7627 0.3697 0.0539  0.0081  -0.0597 147 ALA A N   
1043  C CA  . ALA A 147 ? 0.5619 0.7717 0.3786 0.0513  -0.0052 -0.0846 147 ALA A CA  
1044  C C   . ALA A 147 ? 0.6000 0.8371 0.3873 0.0578  -0.0086 -0.1023 147 ALA A C   
1045  O O   . ALA A 147 ? 0.6550 0.9132 0.4170 0.0645  -0.0018 -0.0895 147 ALA A O   
1046  C CB  . ALA A 147 ? 0.5359 0.7457 0.3644 0.0462  -0.0174 -0.0764 147 ALA A CB  
1047  N N   . PRO A 148 ? 0.5808 0.8172 0.3716 0.0559  -0.0181 -0.1324 148 PRO A N   
1048  C CA  . PRO A 148 ? 0.6231 0.8853 0.3875 0.0615  -0.0246 -0.1528 148 PRO A CA  
1049  C C   . PRO A 148 ? 0.6430 0.9277 0.3937 0.0626  -0.0364 -0.1388 148 PRO A C   
1050  O O   . PRO A 148 ? 0.6529 0.9378 0.4153 0.0582  -0.0463 -0.1307 148 PRO A O   
1051  C CB  . PRO A 148 ? 0.6091 0.8580 0.3921 0.0563  -0.0340 -0.1870 148 PRO A CB  
1052  C CG  . PRO A 148 ? 0.5470 0.7666 0.3656 0.0470  -0.0352 -0.1789 148 PRO A CG  
1053  C CD  . PRO A 148 ? 0.5334 0.7416 0.3554 0.0484  -0.0216 -0.1487 148 PRO A CD  
1054  N N   . SER A 149 ? 0.6481 0.9516 0.3752 0.0690  -0.0350 -0.1347 149 SER A N   
1055  C CA  . SER A 149 ? 0.6757 0.9998 0.3887 0.0722  -0.0444 -0.1173 149 SER A CA  
1056  C C   . SER A 149 ? 0.6525 0.9851 0.3769 0.0677  -0.0655 -0.1309 149 SER A C   
1057  O O   . SER A 149 ? 0.6529 0.9962 0.3776 0.0687  -0.0734 -0.1117 149 SER A O   
1058  C CB  . SER A 149 ? 0.7563 1.0989 0.4405 0.0802  -0.0394 -0.1155 149 SER A CB  
1059  O OG  . SER A 149 ? 0.8235 1.1713 0.5028 0.0807  -0.0464 -0.1478 149 SER A OG  
1060  N N   . PHE A 150 ? 0.6366 0.9641 0.3739 0.0627  -0.0744 -0.1636 150 PHE A N   
1061  C CA  . PHE A 150 ? 0.6390 0.9760 0.3915 0.0572  -0.0945 -0.1797 150 PHE A CA  
1062  C C   . PHE A 150 ? 0.6254 0.9558 0.4047 0.0501  -0.1014 -0.1689 150 PHE A C   
1063  O O   . PHE A 150 ? 0.6293 0.9726 0.4222 0.0467  -0.1172 -0.1717 150 PHE A O   
1064  C CB  . PHE A 150 ? 0.6672 0.9940 0.4356 0.0515  -0.1002 -0.2169 150 PHE A CB  
1065  C CG  . PHE A 150 ? 0.6435 0.9428 0.4451 0.0420  -0.0977 -0.2280 150 PHE A CG  
1066  C CD1 . PHE A 150 ? 0.6383 0.9157 0.4415 0.0432  -0.0816 -0.2277 150 PHE A CD1 
1067  C CD2 . PHE A 150 ? 0.6441 0.9397 0.4775 0.0317  -0.1112 -0.2378 150 PHE A CD2 
1068  C CE1 . PHE A 150 ? 0.6048 0.8554 0.4377 0.0353  -0.0793 -0.2367 150 PHE A CE1 
1069  C CE2 . PHE A 150 ? 0.6236 0.8928 0.4886 0.0224  -0.1081 -0.2464 150 PHE A CE2 
1070  C CZ  . PHE A 150 ? 0.6010 0.8435 0.4670 0.0244  -0.0908 -0.2421 150 PHE A CZ  
1071  N N   . LEU A 151 ? 0.6261 0.9372 0.4146 0.0479  -0.0894 -0.1575 151 LEU A N   
1072  C CA  . LEU A 151 ? 0.5889 0.8798 0.4146 0.0386  -0.0909 -0.1484 151 LEU A CA  
1073  C C   . LEU A 151 ? 0.5617 0.8678 0.3908 0.0405  -0.0982 -0.1230 151 LEU A C   
1074  O O   . LEU A 151 ? 0.5362 0.8378 0.3961 0.0333  -0.1060 -0.1228 151 LEU A O   
1075  C CB  . LEU A 151 ? 0.5496 0.8070 0.3887 0.0362  -0.0721 -0.1349 151 LEU A CB  
1076  C CG  . LEU A 151 ? 0.5124 0.7429 0.3909 0.0259  -0.0713 -0.1327 151 LEU A CG  
1077  C CD1 . LEU A 151 ? 0.5491 0.7752 0.4481 0.0180  -0.0813 -0.1637 151 LEU A CD1 
1078  C CD2 . LEU A 151 ? 0.4756 0.6760 0.3627 0.0254  -0.0543 -0.1195 151 LEU A CD2 
1079  N N   . ALA A 152 ? 0.5617 0.8859 0.3607 0.0507  -0.0950 -0.1011 152 ALA A N   
1080  C CA  . ALA A 152 ? 0.5524 0.8898 0.3544 0.0547  -0.1013 -0.0748 152 ALA A CA  
1081  C C   . ALA A 152 ? 0.6211 0.9867 0.4090 0.0601  -0.1168 -0.0791 152 ALA A C   
1082  O O   . ALA A 152 ? 0.6540 1.0314 0.4437 0.0650  -0.1229 -0.0579 152 ALA A O   
1083  C CB  . ALA A 152 ? 0.4972 0.8265 0.2853 0.0613  -0.0851 -0.0419 152 ALA A CB  
1084  N N   . GLN A 153 ? 0.6371 1.0095 0.4152 0.0591  -0.1224 -0.1063 153 GLN A N   
1085  C CA  . GLN A 153 ? 0.6938 1.0896 0.4537 0.0655  -0.1337 -0.1078 153 GLN A CA  
1086  C C   . GLN A 153 ? 0.6914 1.1020 0.4763 0.0612  -0.1542 -0.1166 153 GLN A C   
1087  O O   . GLN A 153 ? 0.7194 1.1513 0.4928 0.0668  -0.1663 -0.1149 153 GLN A O   
1088  C CB  . GLN A 153 ? 0.7808 1.1801 0.5184 0.0677  -0.1311 -0.1320 153 GLN A CB  
1089  C CG  . GLN A 153 ? 0.8569 1.2531 0.5643 0.0761  -0.1120 -0.1127 153 GLN A CG  
1090  C CD  . GLN A 153 ? 0.9640 1.3641 0.6495 0.0794  -0.1065 -0.1344 153 GLN A CD  
1091  O OE1 . GLN A 153 ? 0.9821 1.3772 0.6785 0.0742  -0.1121 -0.1661 153 GLN A OE1 
1092  N NE2 . GLN A 153 ? 1.0165 1.4248 0.6732 0.0880  -0.0945 -0.1167 153 GLN A NE2 
1093  N N   . LYS A 154 ? 0.6661 1.0666 0.4869 0.0512  -0.1581 -0.1252 154 LYS A N   
1094  C CA  . LYS A 154 ? 0.6932 1.1086 0.5443 0.0459  -0.1762 -0.1338 154 LYS A CA  
1095  C C   . LYS A 154 ? 0.6732 1.0831 0.5587 0.0413  -0.1753 -0.1172 154 LYS A C   
1096  O O   . LYS A 154 ? 0.6626 1.0502 0.5618 0.0353  -0.1633 -0.1162 154 LYS A O   
1097  C CB  . LYS A 154 ? 0.7219 1.1352 0.5906 0.0357  -0.1853 -0.1720 154 LYS A CB  
1098  C CG  . LYS A 154 ? 0.8129 1.2421 0.6500 0.0426  -0.1917 -0.1858 154 LYS A CG  
1099  C CD  . LYS A 154 ? 0.8810 1.3109 0.7332 0.0343  -0.2024 -0.2238 154 LYS A CD  
1100  C CE  . LYS A 154 ? 0.8824 1.2839 0.7479 0.0262  -0.1908 -0.2448 154 LYS A CE  
1101  N NZ  . LYS A 154 ? 0.9123 1.3138 0.7897 0.0200  -0.2003 -0.2807 154 LYS A NZ  
1102  N N   . GLY A 155 ? 0.6587 1.0863 0.5590 0.0447  -0.1864 -0.1027 155 GLY A N   
1103  C CA  . GLY A 155 ? 0.6048 1.0321 0.5452 0.0401  -0.1874 -0.0913 155 GLY A CA  
1104  C C   . GLY A 155 ? 0.5662 0.9842 0.5052 0.0483  -0.1754 -0.0554 155 GLY A C   
1105  O O   . GLY A 155 ? 0.5230 0.9374 0.4966 0.0459  -0.1745 -0.0440 155 GLY A O   
1106  N N   . LEU A 156 ? 0.5728 0.9829 0.4752 0.0572  -0.1639 -0.0375 156 LEU A N   
1107  C CA  . LEU A 156 ? 0.5140 0.9065 0.4172 0.0634  -0.1493 -0.0042 156 LEU A CA  
1108  C C   . LEU A 156 ? 0.5096 0.9180 0.3992 0.0758  -0.1554 0.0193  156 LEU A C   
1109  O O   . LEU A 156 ? 0.5276 0.9518 0.3969 0.0796  -0.1651 0.0115  156 LEU A O   
1110  C CB  . LEU A 156 ? 0.4588 0.8244 0.3390 0.0632  -0.1289 0.0029  156 LEU A CB  
1111  C CG  . LEU A 156 ? 0.4197 0.7593 0.3106 0.0514  -0.1190 -0.0197 156 LEU A CG  
1112  C CD1 . LEU A 156 ? 0.3920 0.7087 0.2630 0.0530  -0.0998 -0.0097 156 LEU A CD1 
1113  C CD2 . LEU A 156 ? 0.4068 0.7273 0.3393 0.0423  -0.1152 -0.0203 156 LEU A CD2 
1114  N N   . PRO A 157 ? 0.4971 0.8955 0.3991 0.0818  -0.1477 0.0479  157 PRO A N   
1115  C CA  . PRO A 157 ? 0.5135 0.9175 0.4043 0.0931  -0.1499 0.0713  157 PRO A CA  
1116  C C   . PRO A 157 ? 0.6210 1.0241 0.4703 0.0982  -0.1432 0.0770  157 PRO A C   
1117  O O   . PRO A 157 ? 0.6872 1.0794 0.5182 0.0940  -0.1318 0.0685  157 PRO A O   
1118  C CB  . PRO A 157 ? 0.4503 0.8336 0.3601 0.0967  -0.1369 0.0981  157 PRO A CB  
1119  C CG  . PRO A 157 ? 0.3940 0.7719 0.3352 0.0884  -0.1352 0.0869  157 PRO A CG  
1120  C CD  . PRO A 157 ? 0.3925 0.7656 0.3219 0.0774  -0.1339 0.0583  157 PRO A CD  
1121  N N   . ASN A 158 ? 0.6394 1.0547 0.4750 0.1077  -0.1496 0.0914  158 ASN A N   
1122  C CA  . ASN A 158 ? 0.6986 1.1184 0.4955 0.1130  -0.1442 0.0961  158 ASN A CA  
1123  C C   . ASN A 158 ? 0.6798 1.0761 0.4655 0.1133  -0.1214 0.1156  158 ASN A C   
1124  O O   . ASN A 158 ? 0.6296 1.0078 0.4344 0.1146  -0.1121 0.1370  158 ASN A O   
1125  C CB  . ASN A 158 ? 0.7809 1.2186 0.5680 0.1238  -0.1559 0.1113  158 ASN A CB  
1126  C CG  . ASN A 158 ? 0.8628 1.3123 0.6091 0.1298  -0.1540 0.1127  158 ASN A CG  
1127  O OD1 . ASN A 158 ? 0.8968 1.3352 0.6264 0.1341  -0.1383 0.1341  158 ASN A OD1 
1128  N ND2 . ASN A 158 ? 0.8819 1.3547 0.6137 0.1299  -0.1699 0.0891  158 ASN A ND2 
1129  N N   . ASN A 159 ? 0.7308 1.1275 0.4888 0.1120  -0.1126 0.1063  159 ASN A N   
1130  C CA  . ASN A 159 ? 0.7806 1.1580 0.5295 0.1111  -0.0910 0.1213  159 ASN A CA  
1131  C C   . ASN A 159 ? 0.7099 1.0644 0.4786 0.1026  -0.0795 0.1169  159 ASN A C   
1132  O O   . ASN A 159 ? 0.7093 1.0477 0.4747 0.1012  -0.0623 0.1285  159 ASN A O   
1133  C CB  . ASN A 159 ? 0.8645 1.2344 0.6145 0.1186  -0.0832 0.1552  159 ASN A CB  
1134  C CG  . ASN A 159 ? 0.9718 1.3615 0.6921 0.1276  -0.0875 0.1637  159 ASN A CG  
1135  O OD1 . ASN A 159 ? 0.9785 1.3908 0.6814 0.1298  -0.1019 0.1450  159 ASN A OD1 
1136  N ND2 . ASN A 159 ? 1.0294 1.4110 0.7455 0.1331  -0.0761 0.1922  159 ASN A ND2 
1137  N N   . VAL A 160 ? 0.6275 0.9812 0.4185 0.0970  -0.0889 0.1014  160 VAL A N   
1138  C CA  . VAL A 160 ? 0.5564 0.8900 0.3639 0.0894  -0.0791 0.0963  160 VAL A CA  
1139  C C   . VAL A 160 ? 0.5417 0.8750 0.3336 0.0838  -0.0751 0.0712  160 VAL A C   
1140  O O   . VAL A 160 ? 0.5598 0.9086 0.3430 0.0823  -0.0865 0.0470  160 VAL A O   
1141  C CB  . VAL A 160 ? 0.4795 0.8134 0.3185 0.0860  -0.0896 0.0912  160 VAL A CB  
1142  C CG1 . VAL A 160 ? 0.4150 0.7262 0.2708 0.0754  -0.0810 0.0751  160 VAL A CG1 
1143  C CG2 . VAL A 160 ? 0.4445 0.7681 0.3034 0.0914  -0.0860 0.1189  160 VAL A CG2 
1144  N N   . GLN A 161 ? 0.5301 0.8446 0.3204 0.0808  -0.0585 0.0760  161 GLN A N   
1145  C CA  . GLN A 161 ? 0.5377 0.8511 0.3115 0.0777  -0.0515 0.0557  161 GLN A CA  
1146  C C   . GLN A 161 ? 0.4965 0.7856 0.2893 0.0692  -0.0431 0.0432  161 GLN A C   
1147  O O   . GLN A 161 ? 0.4899 0.7706 0.2746 0.0675  -0.0314 0.0349  161 GLN A O   
1148  C CB  . GLN A 161 ? 0.6357 0.9510 0.3889 0.0828  -0.0382 0.0703  161 GLN A CB  
1149  C CG  . GLN A 161 ? 0.7934 1.1324 0.5231 0.0881  -0.0486 0.0592  161 GLN A CG  
1150  C CD  . GLN A 161 ? 0.9410 1.2848 0.6504 0.0880  -0.0413 0.0395  161 GLN A CD  
1151  O OE1 . GLN A 161 ? 1.0054 1.3412 0.7209 0.0827  -0.0398 0.0170  161 GLN A OE1 
1152  N NE2 . GLN A 161 ? 1.0055 1.3664 0.6897 0.0949  -0.0410 0.0438  161 GLN A NE2 
1153  N N   . GLY A 162 ? 0.4336 0.7064 0.2580 0.0632  -0.0473 0.0422  162 GLY A N   
1154  C CA  . GLY A 162 ? 0.4163 0.6607 0.2645 0.0544  -0.0398 0.0306  162 GLY A CA  
1155  C C   . GLY A 162 ? 0.4120 0.6430 0.2907 0.0507  -0.0424 0.0385  162 GLY A C   
1156  O O   . GLY A 162 ? 0.4582 0.7041 0.3428 0.0542  -0.0525 0.0467  162 GLY A O   
1157  N N   . ALA A 163 ? 0.3591 0.5637 0.2564 0.0446  -0.0333 0.0357  163 ALA A N   
1158  C CA  . ALA A 163 ? 0.3405 0.5317 0.2647 0.0414  -0.0331 0.0415  163 ALA A CA  
1159  C C   . ALA A 163 ? 0.3472 0.5133 0.2779 0.0400  -0.0195 0.0502  163 ALA A C   
1160  O O   . ALA A 163 ? 0.3399 0.4970 0.2616 0.0385  -0.0123 0.0440  163 ALA A O   
1161  C CB  . ALA A 163 ? 0.3018 0.4897 0.2439 0.0338  -0.0393 0.0217  163 ALA A CB  
1162  N N   . LEU A 164 ? 0.3480 0.5042 0.2956 0.0410  -0.0166 0.0633  164 LEU A N   
1163  C CA  . LEU A 164 ? 0.3444 0.4770 0.3010 0.0391  -0.0058 0.0676  164 LEU A CA  
1164  C C   . LEU A 164 ? 0.3379 0.4590 0.3126 0.0344  -0.0059 0.0586  164 LEU A C   
1165  O O   . LEU A 164 ? 0.3852 0.5140 0.3737 0.0350  -0.0110 0.0606  164 LEU A O   
1166  C CB  . LEU A 164 ? 0.3627 0.4916 0.3246 0.0441  -0.0011 0.0878  164 LEU A CB  
1167  C CG  . LEU A 164 ? 0.4146 0.5493 0.3922 0.0483  -0.0062 0.0979  164 LEU A CG  
1168  C CD1 . LEU A 164 ? 0.4027 0.5170 0.3993 0.0477  0.0008  0.1003  164 LEU A CD1 
1169  C CD2 . LEU A 164 ? 0.4629 0.6116 0.4333 0.0559  -0.0092 0.1166  164 LEU A CD2 
1170  N N   . GLY A 165 ? 0.3267 0.4306 0.3020 0.0304  -0.0001 0.0495  165 GLY A N   
1171  C CA  . GLY A 165 ? 0.2972 0.3902 0.2867 0.0260  0.0012  0.0422  165 GLY A CA  
1172  C C   . GLY A 165 ? 0.3105 0.3861 0.3071 0.0272  0.0092  0.0488  165 GLY A C   
1173  O O   . GLY A 165 ? 0.3106 0.3760 0.3003 0.0287  0.0141  0.0515  165 GLY A O   
1174  N N   . LEU A 166 ? 0.2939 0.3676 0.3053 0.0264  0.0105  0.0500  166 LEU A N   
1175  C CA  . LEU A 166 ? 0.3023 0.3617 0.3191 0.0286  0.0179  0.0543  166 LEU A CA  
1176  C C   . LEU A 166 ? 0.3207 0.3692 0.3412 0.0251  0.0229  0.0482  166 LEU A C   
1177  O O   . LEU A 166 ? 0.3447 0.3866 0.3714 0.0271  0.0289  0.0509  166 LEU A O   
1178  C CB  . LEU A 166 ? 0.3161 0.3827 0.3468 0.0330  0.0178  0.0630  166 LEU A CB  
1179  C CG  . LEU A 166 ? 0.3281 0.4035 0.3576 0.0381  0.0140  0.0736  166 LEU A CG  
1180  C CD1 . LEU A 166 ? 0.3584 0.4406 0.4059 0.0434  0.0134  0.0815  166 LEU A CD1 
1181  C CD2 . LEU A 166 ? 0.3290 0.3901 0.3512 0.0394  0.0193  0.0770  166 LEU A CD2 
1182  N N   . GLY A 167 ? 0.2921 0.3386 0.3091 0.0204  0.0211  0.0402  167 GLY A N   
1183  C CA  . GLY A 167 ? 0.3054 0.3411 0.3277 0.0168  0.0263  0.0370  167 GLY A CA  
1184  C C   . GLY A 167 ? 0.3198 0.3377 0.3303 0.0196  0.0324  0.0383  167 GLY A C   
1185  O O   . GLY A 167 ? 0.3313 0.3458 0.3319 0.0234  0.0316  0.0394  167 GLY A O   
1186  N N   . GLN A 168 ? 0.3194 0.3271 0.3320 0.0178  0.0383  0.0387  168 GLN A N   
1187  C CA  . GLN A 168 ? 0.3349 0.3268 0.3342 0.0214  0.0428  0.0403  168 GLN A CA  
1188  C C   . GLN A 168 ? 0.3420 0.3251 0.3343 0.0207  0.0394  0.0354  168 GLN A C   
1189  O O   . GLN A 168 ? 0.3743 0.3487 0.3706 0.0178  0.0415  0.0347  168 GLN A O   
1190  C CB  . GLN A 168 ? 0.3393 0.3249 0.3420 0.0206  0.0517  0.0455  168 GLN A CB  
1191  C CG  . GLN A 168 ? 0.3060 0.2983 0.3125 0.0237  0.0568  0.0492  168 GLN A CG  
1192  C CD  . GLN A 168 ? 0.3568 0.3445 0.3492 0.0305  0.0559  0.0481  168 GLN A CD  
1193  O OE1 . GLN A 168 ? 0.4097 0.3869 0.3870 0.0343  0.0579  0.0483  168 GLN A OE1 
1194  N NE2 . GLN A 168 ? 0.3442 0.3397 0.3424 0.0324  0.0521  0.0471  168 GLN A NE2 
1195  N N   . ALA A 169 ? 0.3543 0.3400 0.3389 0.0236  0.0348  0.0322  169 ALA A N   
1196  C CA  . ALA A 169 ? 0.3455 0.3266 0.3260 0.0240  0.0316  0.0260  169 ALA A CA  
1197  C C   . ALA A 169 ? 0.3244 0.3077 0.2969 0.0286  0.0298  0.0257  169 ALA A C   
1198  O O   . ALA A 169 ? 0.3391 0.3300 0.3124 0.0293  0.0297  0.0291  169 ALA A O   
1199  C CB  . ALA A 169 ? 0.3472 0.3383 0.3342 0.0195  0.0273  0.0185  169 ALA A CB  
1200  N N   . PRO A 170 ? 0.3130 0.2901 0.2812 0.0318  0.0286  0.0219  170 PRO A N   
1201  C CA  . PRO A 170 ? 0.3096 0.2888 0.2741 0.0360  0.0273  0.0220  170 PRO A CA  
1202  C C   . PRO A 170 ? 0.3478 0.3408 0.3152 0.0348  0.0267  0.0220  170 PRO A C   
1203  O O   . PRO A 170 ? 0.3588 0.3534 0.3281 0.0362  0.0268  0.0243  170 PRO A O   
1204  C CB  . PRO A 170 ? 0.3121 0.2846 0.2753 0.0399  0.0257  0.0173  170 PRO A CB  
1205  C CG  . PRO A 170 ? 0.3153 0.2836 0.2822 0.0370  0.0262  0.0131  170 PRO A CG  
1206  C CD  . PRO A 170 ? 0.3291 0.2956 0.2986 0.0323  0.0285  0.0178  170 PRO A CD  
1207  N N   . ILE A 171 ? 0.3451 0.3482 0.3129 0.0324  0.0263  0.0197  171 ILE A N   
1208  C CA  . ILE A 171 ? 0.3039 0.3201 0.2723 0.0319  0.0272  0.0235  171 ILE A CA  
1209  C C   . ILE A 171 ? 0.3338 0.3589 0.3029 0.0297  0.0262  0.0292  171 ILE A C   
1210  O O   . ILE A 171 ? 0.3211 0.3592 0.2871 0.0297  0.0262  0.0321  171 ILE A O   
1211  C CB  . ILE A 171 ? 0.3121 0.3378 0.2774 0.0332  0.0282  0.0178  171 ILE A CB  
1212  C CG1 . ILE A 171 ? 0.2865 0.3149 0.2472 0.0323  0.0260  0.0089  171 ILE A CG1 
1213  C CG2 . ILE A 171 ? 0.3254 0.3458 0.2944 0.0366  0.0290  0.0137  171 ILE A CG2 
1214  C CD1 . ILE A 171 ? 0.2687 0.3118 0.2231 0.0340  0.0279  0.0033  171 ILE A CD1 
1215  N N   . SER A 172 ? 0.3473 0.3667 0.3206 0.0287  0.0258  0.0318  172 SER A N   
1216  C CA  . SER A 172 ? 0.3565 0.3851 0.3344 0.0279  0.0245  0.0380  172 SER A CA  
1217  C C   . SER A 172 ? 0.3862 0.4176 0.3669 0.0300  0.0265  0.0466  172 SER A C   
1218  O O   . SER A 172 ? 0.3726 0.3972 0.3544 0.0308  0.0289  0.0463  172 SER A O   
1219  C CB  . SER A 172 ? 0.3318 0.3543 0.3169 0.0272  0.0257  0.0393  172 SER A CB  
1220  O OG  . SER A 172 ? 0.3597 0.3711 0.3449 0.0297  0.0293  0.0411  172 SER A OG  
1221  N N   . LEU A 173 ? 0.3797 0.4212 0.3635 0.0309  0.0249  0.0546  173 LEU A N   
1222  C CA  . LEU A 173 ? 0.3718 0.4142 0.3608 0.0329  0.0275  0.0651  173 LEU A CA  
1223  C C   . LEU A 173 ? 0.3575 0.3856 0.3570 0.0339  0.0306  0.0654  173 LEU A C   
1224  O O   . LEU A 173 ? 0.3262 0.3489 0.3308 0.0336  0.0333  0.0672  173 LEU A O   
1225  C CB  . LEU A 173 ? 0.3743 0.4296 0.3654 0.0353  0.0244  0.0753  173 LEU A CB  
1226  C CG  . LEU A 173 ? 0.3863 0.4393 0.3870 0.0383  0.0274  0.0893  173 LEU A CG  
1227  C CD1 . LEU A 173 ? 0.3814 0.4354 0.3791 0.0373  0.0323  0.0956  173 LEU A CD1 
1228  C CD2 . LEU A 173 ? 0.4173 0.4832 0.4205 0.0424  0.0228  0.0998  173 LEU A CD2 
1229  N N   . GLN A 174 ? 0.3598 0.3829 0.3637 0.0349  0.0304  0.0626  174 GLN A N   
1230  C CA  . GLN A 174 ? 0.3439 0.3549 0.3557 0.0371  0.0335  0.0610  174 GLN A CA  
1231  C C   . GLN A 174 ? 0.3527 0.3540 0.3582 0.0363  0.0341  0.0521  174 GLN A C   
1232  O O   . GLN A 174 ? 0.3682 0.3621 0.3799 0.0372  0.0350  0.0496  174 GLN A O   
1233  C CB  . GLN A 174 ? 0.2933 0.3040 0.3106 0.0393  0.0350  0.0600  174 GLN A CB  
1234  C CG  . GLN A 174 ? 0.3001 0.3069 0.3096 0.0381  0.0368  0.0528  174 GLN A CG  
1235  C CD  . GLN A 174 ? 0.3278 0.3430 0.3340 0.0343  0.0340  0.0520  174 GLN A CD  
1236  O OE1 . GLN A 174 ? 0.3337 0.3598 0.3411 0.0331  0.0298  0.0552  174 GLN A OE1 
1237  N NE2 . GLN A 174 ? 0.3462 0.3561 0.3480 0.0325  0.0364  0.0476  174 GLN A NE2 
1238  N N   . ASN A 175 ? 0.3579 0.3597 0.3529 0.0349  0.0327  0.0468  175 ASN A N   
1239  C CA  . ASN A 175 ? 0.3581 0.3523 0.3468 0.0357  0.0319  0.0397  175 ASN A CA  
1240  C C   . ASN A 175 ? 0.3550 0.3515 0.3495 0.0347  0.0311  0.0392  175 ASN A C   
1241  O O   . ASN A 175 ? 0.3454 0.3366 0.3429 0.0358  0.0297  0.0337  175 ASN A O   
1242  C CB  A ASN A 175 ? 0.3809 0.3745 0.3601 0.0351  0.0308  0.0362  175 ASN A CB  
1243  C CB  B ASN A 175 ? 0.3856 0.3788 0.3648 0.0352  0.0310  0.0363  175 ASN A CB  
1244  C CG  A ASN A 175 ? 0.4265 0.4135 0.3995 0.0376  0.0288  0.0305  175 ASN A CG  
1245  C CG  B ASN A 175 ? 0.4438 0.4319 0.4201 0.0357  0.0336  0.0368  175 ASN A CG  
1246  O OD1 A ASN A 175 ? 0.4340 0.4246 0.4103 0.0378  0.0270  0.0282  175 ASN A OD1 
1247  O OD1 B ASN A 175 ? 0.4330 0.4213 0.4080 0.0335  0.0340  0.0366  175 ASN A OD1 
1248  N ND2 A ASN A 175 ? 0.4353 0.4141 0.4000 0.0401  0.0295  0.0295  175 ASN A ND2 
1249  N ND2 B ASN A 175 ? 0.4719 0.4559 0.4491 0.0385  0.0362  0.0369  175 ASN A ND2 
1250  N N   . GLN A 176 ? 0.3502 0.3562 0.3473 0.0327  0.0321  0.0448  176 GLN A N   
1251  C CA  . GLN A 176 ? 0.3200 0.3304 0.3251 0.0310  0.0338  0.0465  176 GLN A CA  
1252  C C   . GLN A 176 ? 0.3680 0.3740 0.3888 0.0299  0.0360  0.0520  176 GLN A C   
1253  O O   . GLN A 176 ? 0.4052 0.4097 0.4379 0.0279  0.0365  0.0492  176 GLN A O   
1254  C CB  . GLN A 176 ? 0.3094 0.3329 0.3092 0.0300  0.0359  0.0515  176 GLN A CB  
1255  C CG  . GLN A 176 ? 0.2775 0.3041 0.2664 0.0310  0.0342  0.0427  176 GLN A CG  
1256  C CD  . GLN A 176 ? 0.2547 0.2956 0.2381 0.0308  0.0372  0.0441  176 GLN A CD  
1257  O OE1 . GLN A 176 ? 0.2661 0.3136 0.2557 0.0303  0.0413  0.0454  176 GLN A OE1 
1258  N NE2 . GLN A 176 ? 0.2505 0.2980 0.2231 0.0312  0.0353  0.0431  176 GLN A NE2 
1259  N N   . LEU A 177 ? 0.3562 0.3602 0.3804 0.0312  0.0370  0.0593  177 LEU A N   
1260  C CA  . LEU A 177 ? 0.3277 0.3238 0.3693 0.0312  0.0392  0.0638  177 LEU A CA  
1261  C C   . LEU A 177 ? 0.2984 0.2825 0.3448 0.0324  0.0371  0.0512  177 LEU A C   
1262  O O   . LEU A 177 ? 0.3368 0.3147 0.3991 0.0304  0.0374  0.0479  177 LEU A O   
1263  C CB  . LEU A 177 ? 0.3205 0.3177 0.3653 0.0343  0.0401  0.0746  177 LEU A CB  
1264  C CG  . LEU A 177 ? 0.3036 0.3141 0.3430 0.0346  0.0411  0.0886  177 LEU A CG  
1265  C CD1 . LEU A 177 ? 0.2684 0.2816 0.3113 0.0391  0.0395  0.0976  177 LEU A CD1 
1266  C CD2 . LEU A 177 ? 0.3310 0.3429 0.3803 0.0318  0.0462  0.0993  177 LEU A CD2 
1267  N N   . PHE A 178 ? 0.2780 0.2598 0.3114 0.0355  0.0351  0.0438  178 PHE A N   
1268  C CA  . PHE A 178 ? 0.2665 0.2396 0.2985 0.0380  0.0332  0.0314  178 PHE A CA  
1269  C C   . PHE A 178 ? 0.2942 0.2672 0.3297 0.0359  0.0291  0.0227  178 PHE A C   
1270  O O   . PHE A 178 ? 0.3131 0.2801 0.3596 0.0358  0.0269  0.0136  178 PHE A O   
1271  C CB  . PHE A 178 ? 0.2607 0.2336 0.2741 0.0415  0.0330  0.0272  178 PHE A CB  
1272  C CG  . PHE A 178 ? 0.2974 0.2719 0.3109 0.0436  0.0370  0.0330  178 PHE A CG  
1273  C CD1 . PHE A 178 ? 0.2974 0.2713 0.3265 0.0447  0.0393  0.0389  178 PHE A CD1 
1274  C CD2 . PHE A 178 ? 0.2781 0.2549 0.2790 0.0447  0.0387  0.0331  178 PHE A CD2 
1275  C CE1 . PHE A 178 ? 0.2975 0.2756 0.3297 0.0475  0.0422  0.0439  178 PHE A CE1 
1276  C CE2 . PHE A 178 ? 0.3157 0.2967 0.3211 0.0460  0.0425  0.0378  178 PHE A CE2 
1277  C CZ  . PHE A 178 ? 0.2901 0.2729 0.3112 0.0477  0.0438  0.0427  178 PHE A CZ  
1278  N N   . SER A 179 ? 0.2939 0.2744 0.3213 0.0347  0.0276  0.0239  179 SER A N   
1279  C CA  . SER A 179 ? 0.3476 0.3308 0.3773 0.0343  0.0227  0.0151  179 SER A CA  
1280  C C   . SER A 179 ? 0.3149 0.3018 0.3680 0.0290  0.0237  0.0160  179 SER A C   
1281  O O   . SER A 179 ? 0.2752 0.2620 0.3401 0.0278  0.0190  0.0059  179 SER A O   
1282  C CB  . SER A 179 ? 0.4169 0.4064 0.4328 0.0360  0.0213  0.0160  179 SER A CB  
1283  O OG  . SER A 179 ? 0.4934 0.4914 0.5138 0.0328  0.0253  0.0236  179 SER A OG  
1284  N N   . HIS A 180 ? 0.2958 0.2867 0.3563 0.0257  0.0300  0.0286  180 HIS A N   
1285  C CA  . HIS A 180 ? 0.3055 0.3003 0.3891 0.0201  0.0337  0.0332  180 HIS A CA  
1286  C C   . HIS A 180 ? 0.3204 0.3037 0.4259 0.0176  0.0336  0.0300  180 HIS A C   
1287  O O   . HIS A 180 ? 0.3083 0.2921 0.4371 0.0125  0.0331  0.0252  180 HIS A O   
1288  C CB  . HIS A 180 ? 0.3040 0.3067 0.3860 0.0185  0.0413  0.0497  180 HIS A CB  
1289  C CG  . HIS A 180 ? 0.2769 0.2858 0.3810 0.0128  0.0476  0.0570  180 HIS A CG  
1290  N ND1 . HIS A 180 ? 0.3132 0.3343 0.4240 0.0104  0.0486  0.0526  180 HIS A ND1 
1291  C CD2 . HIS A 180 ? 0.2611 0.2652 0.3859 0.0088  0.0538  0.0686  180 HIS A CD2 
1292  C CE1 . HIS A 180 ? 0.2946 0.3199 0.4291 0.0044  0.0561  0.0615  180 HIS A CE1 
1293  N NE2 . HIS A 180 ? 0.3049 0.3189 0.4480 0.0031  0.0595  0.0720  180 HIS A NE2 
1294  N N   . PHE A 181 ? 0.3210 0.2941 0.4221 0.0211  0.0344  0.0318  181 PHE A N   
1295  C CA  . PHE A 181 ? 0.3133 0.2735 0.4369 0.0196  0.0352  0.0285  181 PHE A CA  
1296  C C   . PHE A 181 ? 0.3670 0.3193 0.4850 0.0237  0.0286  0.0091  181 PHE A C   
1297  O O   . PHE A 181 ? 0.4094 0.3505 0.5462 0.0229  0.0281  0.0010  181 PHE A O   
1298  C CB  . PHE A 181 ? 0.2932 0.2472 0.4219 0.0218  0.0414  0.0445  181 PHE A CB  
1299  C CG  . PHE A 181 ? 0.2990 0.2604 0.4347 0.0183  0.0481  0.0648  181 PHE A CG  
1300  C CD1 . PHE A 181 ? 0.2794 0.2370 0.4428 0.0119  0.0530  0.0713  181 PHE A CD1 
1301  C CD2 . PHE A 181 ? 0.2978 0.2710 0.4124 0.0212  0.0498  0.0771  181 PHE A CD2 
1302  C CE1 . PHE A 181 ? 0.2797 0.2456 0.4467 0.0092  0.0610  0.0917  181 PHE A CE1 
1303  C CE2 . PHE A 181 ? 0.2690 0.2513 0.3856 0.0192  0.0561  0.0953  181 PHE A CE2 
1304  C CZ  . PHE A 181 ? 0.2628 0.2417 0.4040 0.0136  0.0623  0.1035  181 PHE A CZ  
1305  N N   . GLY A 182 ? 0.3095 0.2673 0.4023 0.0282  0.0240  0.0012  182 GLY A N   
1306  C CA  . GLY A 182 ? 0.2805 0.2328 0.3639 0.0332  0.0186  -0.0159 182 GLY A CA  
1307  C C   . GLY A 182 ? 0.3113 0.2543 0.3914 0.0384  0.0232  -0.0161 182 GLY A C   
1308  O O   . GLY A 182 ? 0.3125 0.2476 0.3976 0.0412  0.0213  -0.0306 182 GLY A O   
1309  N N   . LEU A 183 ? 0.3303 0.2757 0.4028 0.0400  0.0289  -0.0012 183 LEU A N   
1310  C CA  . LEU A 183 ? 0.3148 0.2549 0.3873 0.0453  0.0340  0.0011  183 LEU A CA  
1311  C C   . LEU A 183 ? 0.3072 0.2495 0.3561 0.0516  0.0345  -0.0073 183 LEU A C   
1312  O O   . LEU A 183 ? 0.3515 0.2999 0.3806 0.0517  0.0316  -0.0088 183 LEU A O   
1313  C CB  . LEU A 183 ? 0.2990 0.2447 0.3739 0.0448  0.0383  0.0201  183 LEU A CB  
1314  C CG  . LEU A 183 ? 0.3052 0.2512 0.3984 0.0397  0.0398  0.0336  183 LEU A CG  
1315  C CD1 . LEU A 183 ? 0.3014 0.2569 0.3883 0.0410  0.0422  0.0506  183 LEU A CD1 
1316  C CD2 . LEU A 183 ? 0.3204 0.2526 0.4408 0.0396  0.0419  0.0322  183 LEU A CD2 
1317  N N   . LYS A 184 ? 0.3316 0.2690 0.3833 0.0573  0.0392  -0.0117 184 LYS A N   
1318  C CA  . LYS A 184 ? 0.3514 0.2934 0.3819 0.0632  0.0433  -0.0149 184 LYS A CA  
1319  C C   . LYS A 184 ? 0.3615 0.3129 0.3847 0.0610  0.0461  0.0010  184 LYS A C   
1320  O O   . LYS A 184 ? 0.3644 0.3182 0.4018 0.0581  0.0464  0.0127  184 LYS A O   
1321  C CB  . LYS A 184 ? 0.3846 0.3215 0.4245 0.0701  0.0496  -0.0222 184 LYS A CB  
1322  C CG  . LYS A 184 ? 0.4450 0.3896 0.4680 0.0758  0.0572  -0.0213 184 LYS A CG  
1323  C CD  . LYS A 184 ? 0.5439 0.4845 0.5714 0.0841  0.0635  -0.0345 184 LYS A CD  
1324  C CE  . LYS A 184 ? 0.6092 0.5598 0.6230 0.0897  0.0739  -0.0319 184 LYS A CE  
1325  N NZ  . LYS A 184 ? 0.6449 0.6047 0.6411 0.0854  0.0749  -0.0190 184 LYS A NZ  
1326  N N   . ARG A 185 ? 0.3436 0.3001 0.3452 0.0623  0.0477  0.0014  185 ARG A N   
1327  C CA  . ARG A 185 ? 0.3301 0.2944 0.3271 0.0592  0.0498  0.0139  185 ARG A CA  
1328  C C   . ARG A 185 ? 0.3353 0.3053 0.3409 0.0616  0.0571  0.0196  185 ARG A C   
1329  O O   . ARG A 185 ? 0.3530 0.3263 0.3489 0.0642  0.0635  0.0190  185 ARG A O   
1330  C CB  . ARG A 185 ? 0.3350 0.3000 0.3097 0.0592  0.0489  0.0132  185 ARG A CB  
1331  C CG  . ARG A 185 ? 0.3532 0.3154 0.3218 0.0578  0.0405  0.0076  185 ARG A CG  
1332  C CD  . ARG A 185 ? 0.3782 0.3408 0.3270 0.0590  0.0388  0.0096  185 ARG A CD  
1333  N NE  . ARG A 185 ? 0.4004 0.3657 0.3522 0.0543  0.0395  0.0193  185 ARG A NE  
1334  C CZ  . ARG A 185 ? 0.3987 0.3661 0.3565 0.0506  0.0344  0.0207  185 ARG A CZ  
1335  N NH1 . ARG A 185 ? 0.4147 0.3848 0.3740 0.0471  0.0352  0.0269  185 ARG A NH1 
1336  N NH2 . ARG A 185 ? 0.3759 0.3437 0.3397 0.0504  0.0288  0.0146  185 ARG A NH2 
1337  N N   . GLN A 186 ? 0.3266 0.2991 0.3521 0.0609  0.0563  0.0263  186 GLN A N   
1338  C CA  . GLN A 186 ? 0.3278 0.3076 0.3680 0.0642  0.0612  0.0316  186 GLN A CA  
1339  C C   . GLN A 186 ? 0.3291 0.3141 0.3853 0.0622  0.0565  0.0431  186 GLN A C   
1340  O O   . GLN A 186 ? 0.3141 0.2926 0.3753 0.0608  0.0526  0.0450  186 GLN A O   
1341  C CB  . GLN A 186 ? 0.3460 0.3195 0.3941 0.0716  0.0666  0.0222  186 GLN A CB  
1342  C CG  . GLN A 186 ? 0.3659 0.3467 0.4322 0.0772  0.0728  0.0255  186 GLN A CG  
1343  C CD  . GLN A 186 ? 0.3974 0.3684 0.4743 0.0849  0.0768  0.0143  186 GLN A CD  
1344  O OE1 . GLN A 186 ? 0.4179 0.3832 0.5162 0.0875  0.0747  0.0175  186 GLN A OE1 
1345  N NE2 . GLN A 186 ? 0.4388 0.4070 0.5002 0.0889  0.0823  0.0008  186 GLN A NE2 
1346  N N   . PHE A 187 ? 0.3361 0.3343 0.4000 0.0618  0.0565  0.0512  187 PHE A N   
1347  C CA  . PHE A 187 ? 0.3149 0.3202 0.3935 0.0628  0.0515  0.0625  187 PHE A CA  
1348  C C   . PHE A 187 ? 0.2926 0.3108 0.3889 0.0676  0.0536  0.0668  187 PHE A C   
1349  O O   . PHE A 187 ? 0.3347 0.3601 0.4306 0.0670  0.0583  0.0627  187 PHE A O   
1350  C CB  . PHE A 187 ? 0.3122 0.3252 0.3803 0.0565  0.0448  0.0687  187 PHE A CB  
1351  C CG  . PHE A 187 ? 0.3257 0.3506 0.3875 0.0521  0.0435  0.0672  187 PHE A CG  
1352  C CD1 . PHE A 187 ? 0.3172 0.3364 0.3639 0.0478  0.0457  0.0600  187 PHE A CD1 
1353  C CD2 . PHE A 187 ? 0.3092 0.3510 0.3819 0.0522  0.0392  0.0731  187 PHE A CD2 
1354  C CE1 . PHE A 187 ? 0.3095 0.3368 0.3545 0.0431  0.0450  0.0589  187 PHE A CE1 
1355  C CE2 . PHE A 187 ? 0.2723 0.3243 0.3433 0.0468  0.0375  0.0697  187 PHE A CE2 
1356  C CZ  . PHE A 187 ? 0.2780 0.3214 0.3362 0.0419  0.0410  0.0629  187 PHE A CZ  
1357  N N   . SER A 188 ? 0.2995 0.3210 0.4128 0.0727  0.0504  0.0764  188 SER A N   
1358  C CA  . SER A 188 ? 0.3295 0.3636 0.4646 0.0795  0.0514  0.0808  188 SER A CA  
1359  C C   . SER A 188 ? 0.3622 0.4126 0.5044 0.0803  0.0419  0.0944  188 SER A C   
1360  O O   . SER A 188 ? 0.3779 0.4235 0.5171 0.0811  0.0373  0.1039  188 SER A O   
1361  C CB  . SER A 188 ? 0.3246 0.3461 0.4772 0.0884  0.0565  0.0792  188 SER A CB  
1362  O OG  . SER A 188 ? 0.3637 0.3720 0.5074 0.0885  0.0642  0.0645  188 SER A OG  
1363  N N   . VAL A 189 ? 0.3515 0.4226 0.5056 0.0810  0.0394  0.0955  189 VAL A N   
1364  C CA  . VAL A 189 ? 0.3250 0.4165 0.4843 0.0820  0.0281  0.1059  189 VAL A CA  
1365  C C   . VAL A 189 ? 0.2787 0.3838 0.4667 0.0925  0.0262  0.1135  189 VAL A C   
1366  O O   . VAL A 189 ? 0.2644 0.3779 0.4706 0.0949  0.0318  0.1073  189 VAL A O   
1367  C CB  . VAL A 189 ? 0.2894 0.3969 0.4412 0.0728  0.0237  0.0991  189 VAL A CB  
1368  C CG1 . VAL A 189 ? 0.3011 0.4313 0.4546 0.0735  0.0100  0.1066  189 VAL A CG1 
1369  C CG2 . VAL A 189 ? 0.2440 0.3366 0.3706 0.0641  0.0267  0.0914  189 VAL A CG2 
1370  N N   . CYS A 190 ? 0.2975 0.4050 0.4901 0.0996  0.0188  0.1281  190 CYS A N   
1371  C CA  . CYS A 190 ? 0.3368 0.4592 0.5570 0.1111  0.0145  0.1375  190 CYS A CA  
1372  C C   . CYS A 190 ? 0.3540 0.4985 0.5695 0.1136  -0.0005 0.1511  190 CYS A C   
1373  O O   . CYS A 190 ? 0.2964 0.4354 0.5071 0.1199  -0.0047 0.1671  190 CYS A O   
1374  C CB  . CYS A 190 ? 0.2621 0.3634 0.4983 0.1216  0.0211  0.1441  190 CYS A CB  
1375  S SG  . CYS A 190 ? 0.3740 0.4881 0.6516 0.1364  0.0233  0.1460  190 CYS A SG  
1376  N N   . LEU A 191 ? 0.3602 0.5305 0.5780 0.1090  -0.0086 0.1448  191 LEU A N   
1377  C CA  . LEU A 191 ? 0.3676 0.5625 0.5791 0.1118  -0.0247 0.1546  191 LEU A CA  
1378  C C   . LEU A 191 ? 0.3714 0.5846 0.6099 0.1263  -0.0329 0.1686  191 LEU A C   
1379  O O   . LEU A 191 ? 0.3759 0.5963 0.6450 0.1312  -0.0289 0.1642  191 LEU A O   
1380  C CB  . LEU A 191 ? 0.3387 0.5551 0.5458 0.1012  -0.0320 0.1403  191 LEU A CB  
1381  C CG  . LEU A 191 ? 0.3173 0.5167 0.5006 0.0877  -0.0246 0.1265  191 LEU A CG  
1382  C CD1 . LEU A 191 ? 0.3110 0.5325 0.4958 0.0785  -0.0336 0.1137  191 LEU A CD1 
1383  C CD2 . LEU A 191 ? 0.2859 0.4668 0.4376 0.0863  -0.0230 0.1329  191 LEU A CD2 
1384  N N   . SER A 192 ? 0.3604 0.5810 0.5862 0.1334  -0.0437 0.1853  192 SER A N   
1385  C CA  . SER A 192 ? 0.3602 0.5921 0.6001 0.1431  -0.0523 0.1936  192 SER A CA  
1386  C C   . SER A 192 ? 0.3141 0.5840 0.5564 0.1427  -0.0700 0.1888  192 SER A C   
1387  O O   . SER A 192 ? 0.3163 0.5995 0.5334 0.1375  -0.0793 0.1872  192 SER A O   
1388  C CB  . SER A 192 ? 0.3934 0.6076 0.6142 0.1485  -0.0526 0.2112  192 SER A CB  
1389  O OG  . SER A 192 ? 0.4097 0.6368 0.6425 0.1588  -0.0625 0.2205  192 SER A OG  
1390  N N   . ARG A 193 ? 0.3163 0.6042 0.5896 0.1480  -0.0748 0.1846  193 ARG A N   
1391  C CA  . ARG A 193 ? 0.4735 0.7985 0.7558 0.1475  -0.0925 0.1778  193 ARG A CA  
1392  C C   . ARG A 193 ? 0.5066 0.8422 0.7649 0.1547  -0.1088 0.1897  193 ARG A C   
1393  O O   . ARG A 193 ? 0.5046 0.8701 0.7604 0.1531  -0.1257 0.1824  193 ARG A O   
1394  C CB  . ARG A 193 ? 0.5087 0.8491 0.8338 0.1518  -0.0916 0.1705  193 ARG A CB  
1395  C CG  . ARG A 193 ? 0.6218 0.9615 0.9588 0.1660  -0.0968 0.1822  193 ARG A CG  
1396  C CD  . ARG A 193 ? 0.7183 1.0797 1.0984 0.1701  -0.0976 0.1727  193 ARG A CD  
1397  N NE  . ARG A 193 ? 0.7822 1.1772 1.1783 0.1602  -0.1068 0.1569  193 ARG A NE  
1398  C CZ  . ARG A 193 ? 0.8024 1.2109 1.2337 0.1549  -0.0981 0.1434  193 ARG A CZ  
1399  N NH1 . ARG A 193 ? 0.8088 1.2008 1.2593 0.1599  -0.0804 0.1433  193 ARG A NH1 
1400  N NH2 . ARG A 193 ? 0.7886 1.2267 1.2361 0.1440  -0.1064 0.1293  193 ARG A NH2 
1401  N N   . TYR A 194 ? 0.5079 0.8192 0.7506 0.1623  -0.1033 0.2072  194 TYR A N   
1402  C CA  . TYR A 194 ? 0.5129 0.8322 0.7342 0.1705  -0.1160 0.2216  194 TYR A CA  
1403  C C   . TYR A 194 ? 0.4631 0.7739 0.6410 0.1649  -0.1145 0.2275  194 TYR A C   
1404  O O   . TYR A 194 ? 0.4271 0.7106 0.5934 0.1601  -0.0994 0.2318  194 TYR A O   
1405  C CB  . TYR A 194 ? 0.5656 0.8656 0.7995 0.1825  -0.1108 0.2388  194 TYR A CB  
1406  C CG  . TYR A 194 ? 0.5993 0.9006 0.8755 0.1886  -0.1071 0.2328  194 TYR A CG  
1407  C CD1 . TYR A 194 ? 0.6225 0.9544 0.9224 0.1959  -0.1220 0.2284  194 TYR A CD1 
1408  C CD2 . TYR A 194 ? 0.6190 0.8920 0.9117 0.1873  -0.0887 0.2300  194 TYR A CD2 
1409  C CE1 . TYR A 194 ? 0.6377 0.9726 0.9773 0.2019  -0.1173 0.2222  194 TYR A CE1 
1410  C CE2 . TYR A 194 ? 0.6470 0.9219 0.9767 0.1934  -0.0838 0.2231  194 TYR A CE2 
1411  C CZ  . TYR A 194 ? 0.6583 0.9646 1.0116 0.2008  -0.0975 0.2196  194 TYR A CZ  
1412  O OH  . TYR A 194 ? 0.6627 0.9727 1.0534 0.2071  -0.0914 0.2120  194 TYR A OH  
1413  N N   . SER A 195 ? 0.4770 0.8118 0.6316 0.1661  -0.1303 0.2271  195 SER A N   
1414  C CA  . SER A 195 ? 0.4863 0.8169 0.5988 0.1617  -0.1286 0.2312  195 SER A CA  
1415  C C   . SER A 195 ? 0.5327 0.8398 0.6305 0.1683  -0.1188 0.2545  195 SER A C   
1416  O O   . SER A 195 ? 0.5554 0.8503 0.6247 0.1636  -0.1099 0.2601  195 SER A O   
1417  C CB  . SER A 195 ? 0.4725 0.8359 0.5638 0.1617  -0.1480 0.2219  195 SER A CB  
1418  O OG  . SER A 195 ? 0.5175 0.8976 0.6161 0.1734  -0.1625 0.2312  195 SER A OG  
1419  N N   . THR A 196 ? 0.5690 0.8695 0.6896 0.1788  -0.1194 0.2677  196 THR A N   
1420  C CA  . THR A 196 ? 0.6092 0.8885 0.7210 0.1856  -0.1111 0.2909  196 THR A CA  
1421  C C   . THR A 196 ? 0.6242 0.8669 0.7518 0.1814  -0.0908 0.2954  196 THR A C   
1422  O O   . THR A 196 ? 0.6911 0.9140 0.8153 0.1851  -0.0823 0.3136  196 THR A O   
1423  C CB  . THR A 196 ? 0.6324 0.9210 0.7606 0.2002  -0.1224 0.3045  196 THR A CB  
1424  O OG1 . THR A 196 ? 0.5365 0.8221 0.7055 0.2034  -0.1213 0.2961  196 THR A OG1 
1425  C CG2 . THR A 196 ? 0.5793 0.9043 0.6903 0.2054  -0.1442 0.3016  196 THR A CG2 
1426  N N   . SER A 197 ? 0.5408 0.7746 0.6860 0.1738  -0.0831 0.2789  197 SER A N   
1427  C CA  . SER A 197 ? 0.5150 0.7145 0.6725 0.1692  -0.0649 0.2801  197 SER A CA  
1428  C C   . SER A 197 ? 0.5166 0.7113 0.6702 0.1575  -0.0578 0.2624  197 SER A C   
1429  O O   . SER A 197 ? 0.5268 0.7418 0.6851 0.1545  -0.0651 0.2473  197 SER A O   
1430  C CB  . SER A 197 ? 0.5423 0.7282 0.7366 0.1767  -0.0608 0.2806  197 SER A CB  
1431  O OG  . SER A 197 ? 0.5328 0.7359 0.7486 0.1771  -0.0660 0.2638  197 SER A OG  
1432  N N   . ASN A 198 ? 0.5211 0.6890 0.6691 0.1509  -0.0435 0.2643  198 ASN A N   
1433  C CA  . ASN A 198 ? 0.5024 0.6639 0.6422 0.1404  -0.0367 0.2499  198 ASN A CA  
1434  C C   . ASN A 198 ? 0.5019 0.6527 0.6688 0.1390  -0.0302 0.2353  198 ASN A C   
1435  O O   . ASN A 198 ? 0.4797 0.6164 0.6716 0.1448  -0.0253 0.2369  198 ASN A O   
1436  C CB  . ASN A 198 ? 0.5151 0.6533 0.6401 0.1338  -0.0243 0.2566  198 ASN A CB  
1437  C CG  . ASN A 198 ? 0.5627 0.7145 0.6552 0.1325  -0.0277 0.2667  198 ASN A CG  
1438  O OD1 . ASN A 198 ? 0.5782 0.7569 0.6533 0.1347  -0.0400 0.2641  198 ASN A OD1 
1439  N ND2 . ASN A 198 ? 0.5849 0.7189 0.6704 0.1289  -0.0167 0.2769  198 ASN A ND2 
1440  N N   . GLY A 199 ? 0.4855 0.7529 0.6533 0.1053  0.0545  0.3067  199 GLY A N   
1441  C CA  . GLY A 199 ? 0.4598 0.6763 0.6266 0.0985  0.0487  0.2827  199 GLY A CA  
1442  C C   . GLY A 199 ? 0.4268 0.6215 0.5950 0.0944  0.0508  0.2749  199 GLY A C   
1443  O O   . GLY A 199 ? 0.3921 0.6085 0.5674 0.0969  0.0585  0.2901  199 GLY A O   
1444  N N   . ALA A 200 ? 0.4272 0.5826 0.5889 0.0891  0.0436  0.2518  200 ALA A N   
1445  C CA  . ALA A 200 ? 0.4091 0.5444 0.5800 0.0853  0.0457  0.2462  200 ALA A CA  
1446  C C   . ALA A 200 ? 0.3746 0.4862 0.5107 0.0756  0.0325  0.2044  200 ALA A C   
1447  O O   . ALA A 200 ? 0.3464 0.4462 0.4638 0.0732  0.0242  0.1837  200 ALA A O   
1448  C CB  . ALA A 200 ? 0.4077 0.5153 0.6485 0.0834  0.0614  0.2567  200 ALA A CB  
1449  N N   . ILE A 201 ? 0.3718 0.4800 0.5012 0.0700  0.0318  0.1932  201 ILE A N   
1450  C CA  . ILE A 201 ? 0.3557 0.4411 0.4672 0.0601  0.0223  0.1564  201 ILE A CA  
1451  C C   . ILE A 201 ? 0.3167 0.3822 0.4724 0.0524  0.0287  0.1484  201 ILE A C   
1452  O O   . ILE A 201 ? 0.2979 0.3715 0.4844 0.0537  0.0389  0.1689  201 ILE A O   
1453  C CB  . ILE A 201 ? 0.3549 0.4568 0.4195 0.0599  0.0137  0.1454  201 ILE A CB  
1454  C CG1 . ILE A 201 ? 0.4019 0.5268 0.4336 0.0663  0.0086  0.1507  201 ILE A CG1 
1455  C CG2 . ILE A 201 ? 0.3354 0.4172 0.3824 0.0522  0.0040  0.1131  201 ILE A CG2 
1456  C CD1 . ILE A 201 ? 0.4481 0.5871 0.4409 0.0654  0.0017  0.1344  201 ILE A CD1 
1457  N N   . LEU A 202 ? 0.3450 0.3877 0.5058 0.0444  0.0231  0.1180  202 LEU A N   
1458  C CA  . LEU A 202 ? 0.3269 0.3539 0.5295 0.0349  0.0262  0.1001  202 LEU A CA  
1459  C C   . LEU A 202 ? 0.3099 0.3379 0.4832 0.0277  0.0127  0.0713  202 LEU A C   
1460  O O   . LEU A 202 ? 0.3111 0.3403 0.4410 0.0289  0.0024  0.0576  202 LEU A O   
1461  C CB  . LEU A 202 ? 0.3191 0.3255 0.5581 0.0314  0.0321  0.0852  202 LEU A CB  
1462  C CG  . LEU A 202 ? 0.3744 0.3740 0.6772 0.0354  0.0506  0.1112  202 LEU A CG  
1463  C CD1 . LEU A 202 ? 0.4013 0.4177 0.6909 0.0487  0.0553  0.1501  202 LEU A CD1 
1464  C CD2 . LEU A 202 ? 0.4060 0.3827 0.7489 0.0295  0.0568  0.0853  202 LEU A CD2 
1465  N N   . PHE A 203 ? 0.3089 0.3395 0.5097 0.0213  0.0136  0.0662  203 PHE A N   
1466  C CA  . PHE A 203 ? 0.3158 0.3537 0.4968 0.0154  0.0008  0.0435  203 PHE A CA  
1467  C C   . PHE A 203 ? 0.3298 0.3639 0.5489 0.0039  -0.0023 0.0149  203 PHE A C   
1468  O O   . PHE A 203 ? 0.3250 0.3569 0.5969 -0.0014 0.0063  0.0183  203 PHE A O   
1469  C CB  . PHE A 203 ? 0.2985 0.3517 0.4747 0.0181  0.0023  0.0609  203 PHE A CB  
1470  C CG  . PHE A 203 ? 0.2913 0.3547 0.4285 0.0282  0.0048  0.0820  203 PHE A CG  
1471  C CD1 . PHE A 203 ? 0.2909 0.3594 0.3824 0.0310  -0.0047 0.0721  203 PHE A CD1 
1472  C CD2 . PHE A 203 ? 0.2938 0.3653 0.4436 0.0351  0.0173  0.1111  203 PHE A CD2 
1473  C CE1 . PHE A 203 ? 0.2839 0.3636 0.3448 0.0385  -0.0022 0.0843  203 PHE A CE1 
1474  C CE2 . PHE A 203 ? 0.2957 0.3846 0.4081 0.0437  0.0181  0.1255  203 PHE A CE2 
1475  C CZ  . PHE A 203 ? 0.3117 0.4039 0.3803 0.0444  0.0081  0.1087  203 PHE A CZ  
1476  N N   . GLY A 204 ? 0.3250 0.3629 0.5184 0.0001  -0.0146 -0.0135 204 GLY A N   
1477  C CA  . GLY A 204 ? 0.3353 0.3780 0.5589 -0.0111 -0.0198 -0.0471 204 GLY A CA  
1478  C C   . GLY A 204 ? 0.3524 0.3857 0.5742 -0.0129 -0.0182 -0.0708 204 GLY A C   
1479  O O   . GLY A 204 ? 0.3512 0.3729 0.5500 -0.0051 -0.0133 -0.0585 204 GLY A O   
1480  N N   . ASP A 205 ? 0.3974 0.4384 0.6467 -0.0238 -0.0221 -0.1075 205 ASP A N   
1481  C CA  . ASP A 205 ? 0.4336 0.4714 0.6799 -0.0263 -0.0206 -0.1376 205 ASP A CA  
1482  C C   . ASP A 205 ? 0.4353 0.4446 0.7328 -0.0262 -0.0010 -0.1337 205 ASP A C   
1483  O O   . ASP A 205 ? 0.4085 0.4074 0.7728 -0.0334 0.0101  -0.1375 205 ASP A O   
1484  C CB  . ASP A 205 ? 0.4469 0.5096 0.7074 -0.0387 -0.0312 -0.1830 205 ASP A CB  
1485  C CG  . ASP A 205 ? 0.4920 0.5603 0.7385 -0.0407 -0.0307 -0.2185 205 ASP A CG  
1486  O OD1 . ASP A 205 ? 0.4641 0.5175 0.6820 -0.0314 -0.0238 -0.2058 205 ASP A OD1 
1487  O OD2 . ASP A 205 ? 0.5569 0.6488 0.8215 -0.0519 -0.0376 -0.2615 205 ASP A OD2 
1488  N N   . ILE A 206 ? 0.4608 0.4583 0.7332 -0.0179 0.0045  -0.1255 206 ILE A N   
1489  C CA  . ILE A 206 ? 0.4773 0.4501 0.8003 -0.0157 0.0235  -0.1177 206 ILE A CA  
1490  C C   . ILE A 206 ? 0.5862 0.5547 0.9393 -0.0238 0.0298  -0.1632 206 ILE A C   
1491  O O   . ILE A 206 ? 0.6662 0.6130 1.0703 -0.0226 0.0477  -0.1624 206 ILE A O   
1492  C CB  . ILE A 206 ? 0.4299 0.3942 0.7201 -0.0024 0.0275  -0.0840 206 ILE A CB  
1493  C CG1 . ILE A 206 ? 0.4306 0.4074 0.6535 0.0012  0.0152  -0.0974 206 ILE A CG1 
1494  C CG2 . ILE A 206 ? 0.3973 0.3663 0.6741 0.0051  0.0262  -0.0409 206 ILE A CG2 
1495  C CD1 . ILE A 206 ? 0.4320 0.4024 0.6273 0.0126  0.0184  -0.0697 206 ILE A CD1 
1496  N N   . ASN A 207 ? 0.6265 0.6190 0.9509 -0.0314 0.0162  -0.2030 207 ASN A N   
1497  C CA  . ASN A 207 ? 0.6920 0.6885 1.0404 -0.0399 0.0215  -0.2537 207 ASN A CA  
1498  C C   . ASN A 207 ? 0.7499 0.7623 1.1431 -0.0553 0.0163  -0.2899 207 ASN A C   
1499  O O   . ASN A 207 ? 0.8324 0.8705 1.2209 -0.0638 0.0098  -0.3372 207 ASN A O   
1500  C CB  . ASN A 207 ? 0.7439 0.7648 1.0230 -0.0360 0.0108  -0.2745 207 ASN A CB  
1501  C CG  . ASN A 207 ? 0.8188 0.8296 1.0483 -0.0215 0.0119  -0.2358 207 ASN A CG  
1502  O OD1 . ASN A 207 ? 0.8565 0.8458 1.1024 -0.0158 0.0265  -0.2288 207 ASN A OD1 
1503  N ND2 . ASN A 207 ? 0.8455 0.8738 1.0169 -0.0155 -0.0033 -0.2128 207 ASN A ND2 
1504  N N   . ASP A 208 ? 0.7083 0.7104 1.1444 -0.0579 0.0197  -0.2648 208 ASP A N   
1505  C CA  . ASP A 208 ? 0.7114 0.7304 1.1928 -0.0726 0.0136  -0.2948 208 ASP A CA  
1506  C C   . ASP A 208 ? 0.7626 0.7595 1.3334 -0.0761 0.0376  -0.2977 208 ASP A C   
1507  O O   . ASP A 208 ? 0.7586 0.7264 1.3722 -0.0705 0.0538  -0.2573 208 ASP A O   
1508  C CB  . ASP A 208 ? 0.7011 0.7320 1.1642 -0.0701 0.0021  -0.2597 208 ASP A CB  
1509  C CG  . ASP A 208 ? 0.7305 0.7841 1.2393 -0.0856 -0.0065 -0.2905 208 ASP A CG  
1510  O OD1 . ASP A 208 ? 0.7970 0.8603 1.3395 -0.0917 -0.0007 -0.3281 208 ASP A OD1 
1511  O OD2 . ASP A 208 ? 0.7042 0.7721 1.2011 -0.0846 -0.0165 -0.2675 208 ASP A OD2 
1512  N N   . PRO A 209 ? 0.8324 0.8491 1.4270 -0.0820 0.0415  -0.3402 209 PRO A N   
1513  C CA  . PRO A 209 ? 0.8565 0.8633 1.5377 -0.0845 0.0647  -0.3508 209 PRO A CA  
1514  C C   . PRO A 209 ? 0.8147 0.8065 1.5638 -0.0846 0.0758  -0.3205 209 PRO A C   
1515  O O   . PRO A 209 ? 0.8192 0.7942 1.6419 -0.0808 0.0994  -0.3057 209 PRO A O   
1516  C CB  . PRO A 209 ? 0.9006 0.9458 1.5820 -0.0942 0.0568  -0.4073 209 PRO A CB  
1517  C CG  . PRO A 209 ? 0.8920 0.9697 1.4946 -0.0963 0.0282  -0.4155 209 PRO A CG  
1518  C CD  . PRO A 209 ? 0.8514 0.9114 1.3913 -0.0870 0.0214  -0.3804 209 PRO A CD  
1519  N N   . ASN A 210 ? 0.7623 0.7650 1.4888 -0.0883 0.0595  -0.3102 210 ASN A N   
1520  C CA  . ASN A 210 ? 0.7527 0.7429 1.5348 -0.0869 0.0698  -0.2754 210 ASN A CA  
1521  C C   . ASN A 210 ? 0.7405 0.7016 1.5293 -0.0745 0.0848  -0.2170 210 ASN A C   
1522  O O   . ASN A 210 ? 0.7492 0.6986 1.5992 -0.0677 0.1042  -0.1825 210 ASN A O   
1523  C CB  . ASN A 210 ? 0.7619 0.7724 1.5117 -0.0931 0.0487  -0.2720 210 ASN A CB  
1524  C CG  . ASN A 210 ? 0.8319 0.8775 1.5774 -0.1035 0.0332  -0.3221 210 ASN A CG  
1525  O OD1 . ASN A 210 ? 0.8958 0.9578 1.6287 -0.1065 0.0307  -0.3635 210 ASN A OD1 
1526  N ND2 . ASN A 210 ? 0.8331 0.8943 1.5895 -0.1087 0.0233  -0.3172 210 ASN A ND2 
1527  N N   . ASN A 211 ? 0.7253 0.6785 1.4499 -0.0698 0.0763  -0.2049 211 ASN A N   
1528  C CA  . ASN A 211 ? 0.7212 0.6523 1.4423 -0.0570 0.0880  -0.1480 211 ASN A CA  
1529  C C   . ASN A 211 ? 0.7934 0.7109 1.5378 -0.0484 0.1057  -0.1447 211 ASN A C   
1530  O O   . ASN A 211 ? 0.8342 0.7391 1.5729 -0.0355 0.1153  -0.0991 211 ASN A O   
1531  C CB  . ASN A 211 ? 0.6407 0.5835 1.2632 -0.0487 0.0683  -0.1264 211 ASN A CB  
1532  C CG  . ASN A 211 ? 0.5857 0.5541 1.1733 -0.0528 0.0500  -0.1255 211 ASN A CG  
1533  O OD1 . ASN A 211 ? 0.5380 0.5081 1.1765 -0.0579 0.0563  -0.1129 211 ASN A OD1 
1534  N ND2 . ASN A 211 ? 0.5883 0.5770 1.0924 -0.0496 0.0289  -0.1359 211 ASN A ND2 
1535  N N   . ASN A 212 ? 0.7968 0.7226 1.5723 -0.0551 0.1109  -0.1908 212 ASN A N   
1536  C CA  . ASN A 212 ? 0.7833 0.7007 1.5823 -0.0497 0.1274  -0.1933 212 ASN A CA  
1537  C C   . ASN A 212 ? 0.7254 0.6328 1.5877 -0.0380 0.1511  -0.1404 212 ASN A C   
1538  O O   . ASN A 212 ? 0.7362 0.6360 1.5979 -0.0291 0.1612  -0.1165 212 ASN A O   
1539  C CB  . ASN A 212 ? 0.8682 0.8014 1.7048 -0.0603 0.1323  -0.2507 212 ASN A CB  
1540  C CG  . ASN A 212 ? 0.9377 0.8662 1.7806 -0.0576 0.1447  -0.2632 212 ASN A CG  
1541  O OD1 . ASN A 212 ? 0.9295 0.8417 1.7813 -0.0471 0.1571  -0.2231 212 ASN A OD1 
1542  N ND2 . ASN A 212 ? 1.0038 0.9511 1.8413 -0.0670 0.1412  -0.3181 212 ASN A ND2 
1543  N N   . ASN A 213 ? 0.6675 0.5795 1.5822 -0.0366 0.1596  -0.1185 213 ASN A N   
1544  C CA  . ASN A 213 ? 0.6366 0.5491 1.6161 -0.0242 0.1835  -0.0690 213 ASN A CA  
1545  C C   . ASN A 213 ? 0.5916 0.5046 1.5261 -0.0099 0.1819  -0.0073 213 ASN A C   
1546  O O   . ASN A 213 ? 0.6140 0.5319 1.5733 0.0007  0.1970  0.0283  213 ASN A O   
1547  C CB  . ASN A 213 ? 0.6303 0.5506 1.6799 -0.0249 0.1941  -0.0649 213 ASN A CB  
1548  C CG  . ASN A 213 ? 0.6490 0.5735 1.7570 -0.0369 0.2001  -0.1226 213 ASN A CG  
1549  O OD1 . ASN A 213 ? 0.6700 0.5943 1.8074 -0.0396 0.2111  -0.1469 213 ASN A OD1 
1550  N ND2 . ASN A 213 ? 0.6420 0.5730 1.7635 -0.0452 0.1918  -0.1478 213 ASN A ND2 
1551  N N   . TYR A 214 ? 0.5062 0.4186 1.3740 -0.0101 0.1633  0.0046  214 TYR A N   
1552  C CA  . TYR A 214 ? 0.4496 0.3685 1.2690 0.0036  0.1606  0.0596  214 TYR A CA  
1553  C C   . TYR A 214 ? 0.4550 0.3650 1.2203 0.0080  0.1532  0.0564  214 TYR A C   
1554  O O   . TYR A 214 ? 0.4626 0.3835 1.2154 0.0208  0.1587  0.0989  214 TYR A O   
1555  C CB  . TYR A 214 ? 0.4067 0.3295 1.1731 0.0022  0.1446  0.0728  214 TYR A CB  
1556  C CG  . TYR A 214 ? 0.3806 0.3197 1.0977 0.0179  0.1431  0.1290  214 TYR A CG  
1557  C CD1 . TYR A 214 ? 0.4003 0.3659 1.1497 0.0301  0.1583  0.1776  214 TYR A CD1 
1558  C CD2 . TYR A 214 ? 0.3730 0.3080 1.0102 0.0226  0.1260  0.1307  214 TYR A CD2 
1559  C CE1 . TYR A 214 ? 0.3924 0.3848 1.0912 0.0437  0.1555  0.2226  214 TYR A CE1 
1560  C CE2 . TYR A 214 ? 0.3847 0.3436 0.9742 0.0375  0.1231  0.1766  214 TYR A CE2 
1561  C CZ  . TYR A 214 ? 0.4007 0.3907 1.0189 0.0463  0.1375  0.2201  214 TYR A CZ  
1562  O OH  . TYR A 214 ? 0.4068 0.4311 0.9746 0.0591  0.1338  0.2579  214 TYR A OH  
1563  N N   . ILE A 215 ? 0.4646 0.3605 1.1978 -0.0022 0.1402  0.0043  215 ILE A N   
1564  C CA  . ILE A 215 ? 0.5033 0.3903 1.1795 0.0036  0.1317  -0.0034 215 ILE A CA  
1565  C C   . ILE A 215 ? 0.5482 0.4317 1.2613 0.0018  0.1454  -0.0259 215 ILE A C   
1566  O O   . ILE A 215 ? 0.5739 0.4513 1.2464 0.0057  0.1405  -0.0378 215 ILE A O   
1567  C CB  . ILE A 215 ? 0.5345 0.4270 1.1313 -0.0034 0.1068  -0.0429 215 ILE A CB  
1568  C CG1 . ILE A 215 ? 0.5805 0.4727 1.2013 -0.0207 0.1028  -0.1041 215 ILE A CG1 
1569  C CG2 . ILE A 215 ? 0.4928 0.4060 1.0365 -0.0001 0.0919  -0.0151 215 ILE A CG2 
1570  C CD1 . ILE A 215 ? 0.6233 0.5131 1.2271 -0.0245 0.1017  -0.1511 215 ILE A CD1 
1571  N N   . HIS A 216 ? 0.5497 0.4388 1.3436 -0.0028 0.1643  -0.0294 216 HIS A N   
1572  C CA  . HIS A 216 ? 0.5661 0.4530 1.4040 -0.0060 0.1794  -0.0533 216 HIS A CA  
1573  C C   . HIS A 216 ? 0.5385 0.4235 1.3593 0.0057  0.1851  -0.0196 216 HIS A C   
1574  O O   . HIS A 216 ? 0.4521 0.3306 1.2629 0.0038  0.1870  -0.0459 216 HIS A O   
1575  C CB  . HIS A 216 ? 0.6291 0.5245 1.5683 -0.0092 0.2024  -0.0516 216 HIS A CB  
1576  C CG  . HIS A 216 ? 0.7159 0.6102 1.7108 -0.0133 0.2206  -0.0766 216 HIS A CG  
1577  N ND1 . HIS A 216 ? 0.7428 0.6401 1.7826 -0.0044 0.2400  -0.0382 216 HIS A ND1 
1578  C CD2 . HIS A 216 ? 0.7471 0.6418 1.7586 -0.0253 0.2224  -0.1359 216 HIS A CD2 
1579  C CE1 . HIS A 216 ? 0.7589 0.6536 1.8453 -0.0113 0.2543  -0.0726 216 HIS A CE1 
1580  N NE2 . HIS A 216 ? 0.7675 0.6613 1.8363 -0.0239 0.2440  -0.1328 216 HIS A NE2 
1581  N N   . ASN A 217 ? 0.5312 0.4271 1.3456 0.0179  0.1869  0.0382  217 ASN A N   
1582  C CA  . ASN A 217 ? 0.5755 0.4780 1.3763 0.0292  0.1911  0.0737  217 ASN A CA  
1583  C C   . ASN A 217 ? 0.6036 0.4979 1.3210 0.0343  0.1725  0.0633  217 ASN A C   
1584  O O   . ASN A 217 ? 0.6248 0.5232 1.3322 0.0419  0.1753  0.0807  217 ASN A O   
1585  C CB  . ASN A 217 ? 0.5880 0.5163 1.3971 0.0408  0.1957  0.1361  217 ASN A CB  
1586  C CG  . ASN A 217 ? 0.6027 0.5471 1.4017 0.0518  0.1995  0.1736  217 ASN A CG  
1587  O OD1 . ASN A 217 ? 0.6140 0.5594 1.4698 0.0518  0.2172  0.1771  217 ASN A OD1 
1588  N ND2 . ASN A 217 ? 0.5955 0.5556 1.3240 0.0610  0.1827  0.2000  217 ASN A ND2 
1589  N N   . SER A 218 ? 0.5889 0.4742 1.2506 0.0307  0.1544  0.0348  218 SER A N   
1590  C CA  . SER A 218 ? 0.5350 0.4165 1.1230 0.0377  0.1383  0.0259  218 SER A CA  
1591  C C   . SER A 218 ? 0.5279 0.3977 1.0975 0.0294  0.1354  -0.0329 218 SER A C   
1592  O O   . SER A 218 ? 0.5401 0.4110 1.0503 0.0348  0.1239  -0.0449 218 SER A O   
1593  C CB  . SER A 218 ? 0.4824 0.3722 1.0128 0.0420  0.1195  0.0398  218 SER A CB  
1594  O OG  . SER A 218 ? 0.4639 0.3540 0.9740 0.0280  0.1090  -0.0022 218 SER A OG  
1595  N N   . LEU A 219 ? 0.5068 0.3738 1.1261 0.0165  0.1465  -0.0687 219 LEU A N   
1596  C CA  . LEU A 219 ? 0.4878 0.3563 1.0832 0.0063  0.1413  -0.1285 219 LEU A CA  
1597  C C   . LEU A 219 ? 0.4913 0.3590 1.0513 0.0123  0.1427  -0.1405 219 LEU A C   
1598  O O   . LEU A 219 ? 0.4751 0.3510 0.9826 0.0093  0.1325  -0.1782 219 LEU A O   
1599  C CB  . LEU A 219 ? 0.4921 0.3658 1.1563 -0.0077 0.1546  -0.1619 219 LEU A CB  
1600  C CG  . LEU A 219 ? 0.4933 0.3745 1.1819 -0.0177 0.1492  -0.1751 219 LEU A CG  
1601  C CD1 . LEU A 219 ? 0.5074 0.3966 1.2768 -0.0286 0.1658  -0.2036 219 LEU A CD1 
1602  C CD2 . LEU A 219 ? 0.4996 0.3921 1.1185 -0.0238 0.1260  -0.2112 219 LEU A CD2 
1603  N N   . ASP A 220 ? 0.5305 0.3936 1.1193 0.0206  0.1557  -0.1077 220 ASP A N   
1604  C CA  . ASP A 220 ? 0.5845 0.4471 1.1445 0.0267  0.1581  -0.1161 220 ASP A CA  
1605  C C   . ASP A 220 ? 0.4823 0.3489 0.9700 0.0387  0.1420  -0.1006 220 ASP A C   
1606  O O   . ASP A 220 ? 0.4646 0.3360 0.9067 0.0405  0.1381  -0.1258 220 ASP A O   
1607  C CB  . ASP A 220 ? 0.7054 0.5651 1.3206 0.0317  0.1762  -0.0847 220 ASP A CB  
1608  C CG  . ASP A 220 ? 0.7924 0.6577 1.4412 0.0385  0.1793  -0.0274 220 ASP A CG  
1609  O OD1 . ASP A 220 ? 0.8081 0.6778 1.4322 0.0406  0.1669  -0.0103 220 ASP A OD1 
1610  O OD2 . ASP A 220 ? 0.8125 0.6817 1.5129 0.0417  0.1950  0.0009  220 ASP A OD2 
1611  N N   . VAL A 221 ? 0.4464 0.3159 0.9248 0.0467  0.1335  -0.0591 221 VAL A N   
1612  C CA  . VAL A 221 ? 0.4244 0.3113 0.8270 0.0525  0.1140  -0.0412 221 VAL A CA  
1613  C C   . VAL A 221 ? 0.4371 0.3359 0.7771 0.0428  0.0977  -0.0772 221 VAL A C   
1614  O O   . VAL A 221 ? 0.4190 0.3299 0.7013 0.0452  0.0881  -0.0823 221 VAL A O   
1615  C CB  . VAL A 221 ? 0.4090 0.3084 0.8065 0.0584  0.1054  0.0078  221 VAL A CB  
1616  C CG1 . VAL A 221 ? 0.3238 0.2445 0.6450 0.0615  0.0853  0.0208  221 VAL A CG1 
1617  C CG2 . VAL A 221 ? 0.3809 0.2781 0.8402 0.0696  0.1207  0.0494  221 VAL A CG2 
1618  N N   . LEU A 222 ? 0.3705 0.2683 0.7263 0.0325  0.0953  -0.0991 222 LEU A N   
1619  C CA  . LEU A 222 ? 0.3882 0.3032 0.6908 0.0239  0.0792  -0.1300 222 LEU A CA  
1620  C C   . LEU A 222 ? 0.4514 0.3754 0.7293 0.0207  0.0810  -0.1741 222 LEU A C   
1621  O O   . LEU A 222 ? 0.4835 0.4285 0.6990 0.0204  0.0672  -0.1834 222 LEU A O   
1622  C CB  . LEU A 222 ? 0.4120 0.3263 0.7504 0.0130  0.0778  -0.1462 222 LEU A CB  
1623  C CG  . LEU A 222 ? 0.4062 0.3184 0.7616 0.0156  0.0752  -0.1043 222 LEU A CG  
1624  C CD1 . LEU A 222 ? 0.4047 0.3177 0.7974 0.0038  0.0745  -0.1245 222 LEU A CD1 
1625  C CD2 . LEU A 222 ? 0.4080 0.3374 0.6922 0.0214  0.0574  -0.0792 222 LEU A CD2 
1626  N N   . HIS A 223 ? 0.5278 0.4378 0.8577 0.0189  0.0998  -0.2006 223 HIS A N   
1627  C CA  . HIS A 223 ? 0.6042 0.5258 0.9160 0.0161  0.1054  -0.2468 223 HIS A CA  
1628  C C   . HIS A 223 ? 0.5641 0.4960 0.8188 0.0266  0.1027  -0.2303 223 HIS A C   
1629  O O   . HIS A 223 ? 0.5636 0.5182 0.7711 0.0259  0.0988  -0.2571 223 HIS A O   
1630  C CB  . HIS A 223 ? 0.7052 0.6177 1.0824 0.0096  0.1237  -0.2605 223 HIS A CB  
1631  C CG  . HIS A 223 ? 0.8362 0.7685 1.1939 0.0047  0.1279  -0.3003 223 HIS A CG  
1632  N ND1 . HIS A 223 ? 0.8904 0.8529 1.2214 -0.0057 0.1176  -0.3405 223 HIS A ND1 
1633  C CD2 . HIS A 223 ? 0.8844 0.8139 1.2468 0.0094  0.1414  -0.3038 223 HIS A CD2 
1634  C CE1 . HIS A 223 ? 0.9219 0.9001 1.2402 -0.0065 0.1248  -0.3665 223 HIS A CE1 
1635  N NE2 . HIS A 223 ? 0.9193 0.8758 1.2564 0.0023  0.1399  -0.3460 223 HIS A NE2 
1636  N N   . ASP A 224 ? 0.5287 0.4483 0.7887 0.0365  0.1045  -0.1851 224 ASP A N   
1637  C CA  . ASP A 224 ? 0.5217 0.4481 0.7441 0.0460  0.1050  -0.1688 224 ASP A CA  
1638  C C   . ASP A 224 ? 0.4657 0.4067 0.6297 0.0491  0.0858  -0.1392 224 ASP A C   
1639  O O   . ASP A 224 ? 0.4688 0.4141 0.6100 0.0564  0.0855  -0.1198 224 ASP A O   
1640  C CB  . ASP A 224 ? 0.5566 0.4654 0.8273 0.0554  0.1195  -0.1399 224 ASP A CB  
1641  C CG  . ASP A 224 ? 0.5696 0.4618 0.9060 0.0540  0.1422  -0.1643 224 ASP A CG  
1642  O OD1 . ASP A 224 ? 0.6233 0.5238 0.9541 0.0441  0.1452  -0.2056 224 ASP A OD1 
1643  O OD2 . ASP A 224 ? 0.5308 0.4125 0.9140 0.0586  0.1510  -0.1323 224 ASP A OD2 
1644  N N   . LEU A 225 ? 0.4579 0.4066 0.6033 0.0432  0.0712  -0.1368 225 LEU A N   
1645  C CA  . LEU A 225 ? 0.4386 0.4002 0.5346 0.0456  0.0547  -0.1118 225 LEU A CA  
1646  C C   . LEU A 225 ? 0.4369 0.4164 0.4827 0.0489  0.0519  -0.1202 225 LEU A C   
1647  O O   . LEU A 225 ? 0.4775 0.4701 0.5105 0.0466  0.0560  -0.1513 225 LEU A O   
1648  C CB  . LEU A 225 ? 0.4236 0.3926 0.5106 0.0387  0.0417  -0.1141 225 LEU A CB  
1649  C CG  . LEU A 225 ? 0.4292 0.3872 0.5512 0.0370  0.0405  -0.0920 225 LEU A CG  
1650  C CD1 . LEU A 225 ? 0.4537 0.4233 0.5577 0.0308  0.0273  -0.0959 225 LEU A CD1 
1651  C CD2 . LEU A 225 ? 0.4117 0.3682 0.5286 0.0450  0.0386  -0.0534 225 LEU A CD2 
1652  N N   . VAL A 226 ? 0.4060 0.3892 0.4264 0.0545  0.0460  -0.0925 226 VAL A N   
1653  C CA  . VAL A 226 ? 0.4113 0.4109 0.3899 0.0588  0.0445  -0.0908 226 VAL A CA  
1654  C C   . VAL A 226 ? 0.3917 0.4022 0.3399 0.0579  0.0298  -0.0751 226 VAL A C   
1655  O O   . VAL A 226 ? 0.3716 0.3738 0.3302 0.0565  0.0227  -0.0575 226 VAL A O   
1656  C CB  . VAL A 226 ? 0.4876 0.4811 0.4746 0.0658  0.0531  -0.0725 226 VAL A CB  
1657  C CG1 . VAL A 226 ? 0.5440 0.5512 0.4972 0.0700  0.0503  -0.0590 226 VAL A CG1 
1658  C CG2 . VAL A 226 ? 0.4832 0.4717 0.4935 0.0683  0.0702  -0.0916 226 VAL A CG2 
1659  N N   . TYR A 227 ? 0.4277 0.4595 0.3410 0.0594  0.0263  -0.0805 227 TYR A N   
1660  C CA  . TYR A 227 ? 0.4252 0.4682 0.3164 0.0594  0.0140  -0.0657 227 TYR A CA  
1661  C C   . TYR A 227 ? 0.4650 0.5183 0.3347 0.0665  0.0162  -0.0446 227 TYR A C   
1662  O O   . TYR A 227 ? 0.5189 0.5810 0.3791 0.0718  0.0262  -0.0454 227 TYR A O   
1663  C CB  . TYR A 227 ? 0.4077 0.4731 0.2837 0.0555  0.0062  -0.0851 227 TYR A CB  
1664  C CG  . TYR A 227 ? 0.4239 0.4803 0.3281 0.0470  0.0038  -0.1062 227 TYR A CG  
1665  C CD1 . TYR A 227 ? 0.4382 0.4856 0.3573 0.0426  -0.0045 -0.0963 227 TYR A CD1 
1666  C CD2 . TYR A 227 ? 0.4753 0.5321 0.3964 0.0433  0.0123  -0.1368 227 TYR A CD2 
1667  C CE1 . TYR A 227 ? 0.4787 0.5178 0.4308 0.0350  -0.0044 -0.1128 227 TYR A CE1 
1668  C CE2 . TYR A 227 ? 0.5288 0.5755 0.4862 0.0350  0.0127  -0.1567 227 TYR A CE2 
1669  C CZ  . TYR A 227 ? 0.5373 0.5750 0.5112 0.0309  0.0044  -0.1428 227 TYR A CZ  
1670  O OH  . TYR A 227 ? 0.5886 0.6163 0.6060 0.0225  0.0069  -0.1603 227 TYR A OH  
1671  N N   . THR A 228 ? 0.4360 0.4888 0.3022 0.0670  0.0088  -0.0261 228 THR A N   
1672  C CA  . THR A 228 ? 0.4092 0.4705 0.2653 0.0732  0.0125  -0.0058 228 THR A CA  
1673  C C   . THR A 228 ? 0.3959 0.4668 0.2448 0.0733  0.0034  0.0043  228 THR A C   
1674  O O   . THR A 228 ? 0.4204 0.4844 0.2766 0.0678  -0.0052 -0.0014 228 THR A O   
1675  C CB  . THR A 228 ? 0.4660 0.5096 0.3432 0.0737  0.0176  0.0073  228 THR A CB  
1676  O OG1 . THR A 228 ? 0.5096 0.5604 0.3864 0.0794  0.0253  0.0248  228 THR A OG1 
1677  C CG2 . THR A 228 ? 0.4317 0.4635 0.3228 0.0687  0.0088  0.0111  228 THR A CG2 
1678  N N   . PRO A 229 ? 0.3865 0.4751 0.2247 0.0804  0.0068  0.0217  229 PRO A N   
1679  C CA  . PRO A 229 ? 0.3861 0.4861 0.2227 0.0820  -0.0005 0.0339  229 PRO A CA  
1680  C C   . PRO A 229 ? 0.3637 0.4420 0.2228 0.0780  -0.0034 0.0403  229 PRO A C   
1681  O O   . PRO A 229 ? 0.3637 0.4252 0.2399 0.0771  0.0024  0.0449  229 PRO A O   
1682  C CB  . PRO A 229 ? 0.3917 0.5128 0.2222 0.0925  0.0086  0.0581  229 PRO A CB  
1683  C CG  . PRO A 229 ? 0.3970 0.5300 0.2111 0.0957  0.0170  0.0501  229 PRO A CG  
1684  C CD  . PRO A 229 ? 0.3818 0.4856 0.2104 0.0885  0.0189  0.0328  229 PRO A CD  
1685  N N   . LEU A 230 ? 0.3558 0.4388 0.2153 0.0756  -0.0125 0.0387  230 LEU A N   
1686  C CA  . LEU A 230 ? 0.3521 0.4198 0.2301 0.0724  -0.0143 0.0421  230 LEU A CA  
1687  C C   . LEU A 230 ? 0.3602 0.4373 0.2483 0.0786  -0.0114 0.0611  230 LEU A C   
1688  O O   . LEU A 230 ? 0.3990 0.4987 0.2778 0.0831  -0.0157 0.0691  230 LEU A O   
1689  C CB  . LEU A 230 ? 0.3947 0.4595 0.2727 0.0656  -0.0236 0.0285  230 LEU A CB  
1690  C CG  . LEU A 230 ? 0.4001 0.4554 0.2924 0.0624  -0.0258 0.0297  230 LEU A CG  
1691  C CD1 . LEU A 230 ? 0.3670 0.4077 0.2695 0.0603  -0.0210 0.0281  230 LEU A CD1 
1692  C CD2 . LEU A 230 ? 0.3569 0.4144 0.2506 0.0568  -0.0332 0.0198  230 LEU A CD2 
1693  N N   . THR A 231 ? 0.3439 0.4067 0.2554 0.0790  -0.0037 0.0678  231 THR A N   
1694  C CA  . THR A 231 ? 0.3179 0.3850 0.2506 0.0847  0.0021  0.0849  231 THR A CA  
1695  C C   . THR A 231 ? 0.3226 0.3752 0.2747 0.0793  0.0016  0.0744  231 THR A C   
1696  O O   . THR A 231 ? 0.3333 0.3743 0.2846 0.0724  -0.0005 0.0578  231 THR A O   
1697  C CB  . THR A 231 ? 0.3304 0.3961 0.2843 0.0913  0.0164  0.1032  231 THR A CB  
1698  O OG1 . THR A 231 ? 0.3306 0.3786 0.2950 0.0855  0.0210  0.0907  231 THR A OG1 
1699  C CG2 . THR A 231 ? 0.3587 0.4490 0.2919 0.0999  0.0185  0.1202  231 THR A CG2 
1700  N N   . ILE A 232 ? 0.3441 0.4023 0.3139 0.0836  0.0042  0.0853  232 ILE A N   
1701  C CA  . ILE A 232 ? 0.3249 0.3752 0.3105 0.0798  0.0043  0.0748  232 ILE A CA  
1702  C C   . ILE A 232 ? 0.3128 0.3559 0.3396 0.0841  0.0185  0.0833  232 ILE A C   
1703  O O   . ILE A 232 ? 0.3365 0.3887 0.3797 0.0931  0.0248  0.1071  232 ILE A O   
1704  C CB  . ILE A 232 ? 0.3191 0.3838 0.2933 0.0806  -0.0054 0.0775  232 ILE A CB  
1705  C CG1 . ILE A 232 ? 0.2686 0.3399 0.2116 0.0756  -0.0175 0.0669  232 ILE A CG1 
1706  C CG2 . ILE A 232 ? 0.3341 0.3924 0.3242 0.0772  -0.0032 0.0671  232 ILE A CG2 
1707  C CD1 . ILE A 232 ? 0.2332 0.2903 0.1690 0.0676  -0.0193 0.0489  232 ILE A CD1 
1708  N N   . SER A 233 ? 0.3042 0.3341 0.3510 0.0781  0.0245  0.0640  233 SER A N   
1709  C CA  . SER A 233 ? 0.3138 0.3348 0.4090 0.0809  0.0403  0.0661  233 SER A CA  
1710  C C   . SER A 233 ? 0.3311 0.3566 0.4428 0.0851  0.0431  0.0715  233 SER A C   
1711  O O   . SER A 233 ? 0.3397 0.3750 0.4246 0.0840  0.0320  0.0693  233 SER A O   
1712  C CB  . SER A 233 ? 0.3350 0.3458 0.4484 0.0717  0.0454  0.0368  233 SER A CB  
1713  O OG  . SER A 233 ? 0.3541 0.3705 0.4499 0.0660  0.0386  0.0149  233 SER A OG  
1714  N N   . LYS A 234 ? 0.3588 0.3765 0.5214 0.0898  0.0597  0.0782  234 LYS A N   
1715  C CA  . LYS A 234 ? 0.4343 0.4557 0.6215 0.0950  0.0653  0.0845  234 LYS A CA  
1716  C C   . LYS A 234 ? 0.4094 0.4296 0.5851 0.0868  0.0621  0.0531  234 LYS A C   
1717  O O   . LYS A 234 ? 0.3831 0.4100 0.5651 0.0902  0.0626  0.0569  234 LYS A O   
1718  C CB  . LYS A 234 ? 0.5374 0.5486 0.7917 0.1024  0.0872  0.0989  234 LYS A CB  
1719  C CG  . LYS A 234 ? 0.6431 0.6650 0.9049 0.1140  0.0902  0.1406  234 LYS A CG  
1720  C CD  . LYS A 234 ? 0.7309 0.7428 1.0546 0.1161  0.1125  0.1579  234 LYS A CD  
1721  C CE  . LYS A 234 ? 0.7875 0.8186 1.1003 0.1214  0.1138  0.1962  234 LYS A CE  
1722  N NZ  . LYS A 234 ? 0.7985 0.8304 1.0753 0.1213  0.1055  0.1927  234 LYS A NZ  
1723  N N   . GLN A 235 ? 0.4150 0.4318 0.5711 0.0770  0.0579  0.0249  235 GLN A N   
1724  C CA  . GLN A 235 ? 0.4129 0.4364 0.5533 0.0705  0.0552  -0.0021 235 GLN A CA  
1725  C C   . GLN A 235 ? 0.3760 0.4113 0.4647 0.0679  0.0379  0.0014  235 GLN A C   
1726  O O   . GLN A 235 ? 0.3547 0.3998 0.4267 0.0641  0.0354  -0.0137 235 GLN A O   
1727  C CB  . GLN A 235 ? 0.4606 0.4830 0.6112 0.0618  0.0601  -0.0350 235 GLN A CB  
1728  C CG  . GLN A 235 ? 0.5771 0.5885 0.7877 0.0616  0.0796  -0.0499 235 GLN A CG  
1729  C CD  . GLN A 235 ? 0.7098 0.7230 0.9449 0.0650  0.0910  -0.0577 235 GLN A CD  
1730  O OE1 . GLN A 235 ? 0.7594 0.7871 0.9637 0.0631  0.0851  -0.0694 235 GLN A OE1 
1731  N NE2 . GLN A 235 ? 0.7611 0.7602 1.0563 0.0710  0.1094  -0.0489 235 GLN A NE2 
1732  N N   . GLY A 236 ? 0.3675 0.4040 0.4347 0.0706  0.0279  0.0221  236 GLY A N   
1733  C CA  . GLY A 236 ? 0.3207 0.3659 0.3493 0.0679  0.0136  0.0248  236 GLY A CA  
1734  C C   . GLY A 236 ? 0.3182 0.3632 0.3206 0.0621  0.0064  0.0145  236 GLY A C   
1735  O O   . GLY A 236 ? 0.3254 0.3766 0.3045 0.0594  -0.0021 0.0143  236 GLY A O   
1736  N N   . GLU A 237 ? 0.3286 0.3669 0.3406 0.0604  0.0107  0.0079  237 GLU A N   
1737  C CA  . GLU A 237 ? 0.3237 0.3642 0.3166 0.0556  0.0043  -0.0003 237 GLU A CA  
1738  C C   . GLU A 237 ? 0.3251 0.3612 0.3026 0.0576  -0.0011 0.0136  237 GLU A C   
1739  O O   . GLU A 237 ? 0.3293 0.3620 0.3144 0.0627  0.0023  0.0280  237 GLU A O   
1740  C CB  . GLU A 237 ? 0.3343 0.3740 0.3492 0.0517  0.0110  -0.0180 237 GLU A CB  
1741  C CG  . GLU A 237 ? 0.3367 0.3847 0.3678 0.0486  0.0175  -0.0397 237 GLU A CG  
1742  C CD  . GLU A 237 ? 0.4064 0.4481 0.4775 0.0455  0.0284  -0.0560 237 GLU A CD  
1743  O OE1 . GLU A 237 ? 0.4484 0.4744 0.5498 0.0501  0.0383  -0.0417 237 GLU A OE1 
1744  O OE2 . GLU A 237 ? 0.4275 0.4828 0.5032 0.0387  0.0277  -0.0821 237 GLU A OE2 
1745  N N   . TYR A 238 ? 0.3108 0.3503 0.2689 0.0545  -0.0082 0.0099  238 TYR A N   
1746  C CA  . TYR A 238 ? 0.3351 0.3710 0.2793 0.0558  -0.0120 0.0181  238 TYR A CA  
1747  C C   . TYR A 238 ? 0.3398 0.3713 0.2932 0.0555  -0.0076 0.0168  238 TYR A C   
1748  O O   . TYR A 238 ? 0.3165 0.3522 0.2766 0.0517  -0.0081 0.0060  238 TYR A O   
1749  C CB  . TYR A 238 ? 0.3287 0.3688 0.2570 0.0532  -0.0191 0.0166  238 TYR A CB  
1750  C CG  . TYR A 238 ? 0.3061 0.3504 0.2305 0.0529  -0.0224 0.0193  238 TYR A CG  
1751  C CD1 . TYR A 238 ? 0.3129 0.3574 0.2336 0.0542  -0.0256 0.0241  238 TYR A CD1 
1752  C CD2 . TYR A 238 ? 0.3089 0.3617 0.2342 0.0513  -0.0223 0.0165  238 TYR A CD2 
1753  C CE1 . TYR A 238 ? 0.3449 0.3952 0.2680 0.0529  -0.0290 0.0253  238 TYR A CE1 
1754  C CE2 . TYR A 238 ? 0.2857 0.3428 0.2124 0.0510  -0.0237 0.0207  238 TYR A CE2 
1755  C CZ  . TYR A 238 ? 0.3275 0.3818 0.2556 0.0513  -0.0273 0.0246  238 TYR A CZ  
1756  O OH  . TYR A 238 ? 0.3709 0.4311 0.3059 0.0500  -0.0292 0.0274  238 TYR A OH  
1757  N N   . PHE A 239 ? 0.3507 0.3785 0.3050 0.0600  -0.0034 0.0283  239 PHE A N   
1758  C CA  . PHE A 239 ? 0.3397 0.3635 0.3064 0.0609  0.0034  0.0311  239 PHE A CA  
1759  C C   . PHE A 239 ? 0.3311 0.3567 0.2794 0.0642  0.0030  0.0386  239 PHE A C   
1760  O O   . PHE A 239 ? 0.3520 0.3840 0.2836 0.0678  0.0005  0.0450  239 PHE A O   
1761  C CB  . PHE A 239 ? 0.3188 0.3391 0.3143 0.0649  0.0151  0.0413  239 PHE A CB  
1762  C CG  . PHE A 239 ? 0.3439 0.3604 0.3695 0.0603  0.0198  0.0276  239 PHE A CG  
1763  C CD1 . PHE A 239 ? 0.3513 0.3688 0.3822 0.0604  0.0198  0.0235  239 PHE A CD1 
1764  C CD2 . PHE A 239 ? 0.3637 0.3782 0.4143 0.0552  0.0243  0.0152  239 PHE A CD2 
1765  C CE1 . PHE A 239 ? 0.3381 0.3543 0.3978 0.0558  0.0257  0.0053  239 PHE A CE1 
1766  C CE2 . PHE A 239 ? 0.3423 0.3574 0.4226 0.0494  0.0285  -0.0049 239 PHE A CE2 
1767  C CZ  . PHE A 239 ? 0.3177 0.3334 0.4015 0.0499  0.0297  -0.0108 239 PHE A CZ  
1768  N N   . ILE A 240 ? 0.3531 0.3762 0.3068 0.0631  0.0059  0.0361  240 ILE A N   
1769  C CA  . ILE A 240 ? 0.3446 0.3698 0.2869 0.0674  0.0103  0.0429  240 ILE A CA  
1770  C C   . ILE A 240 ? 0.3785 0.4017 0.3437 0.0696  0.0218  0.0511  240 ILE A C   
1771  O O   . ILE A 240 ? 0.3925 0.4116 0.3852 0.0658  0.0245  0.0469  240 ILE A O   
1772  C CB  . ILE A 240 ? 0.3358 0.3597 0.2667 0.0651  0.0056  0.0337  240 ILE A CB  
1773  C CG1 . ILE A 240 ? 0.3147 0.3374 0.2631 0.0607  0.0034  0.0278  240 ILE A CG1 
1774  C CG2 . ILE A 240 ? 0.3480 0.3734 0.2627 0.0632  -0.0028 0.0275  240 ILE A CG2 
1775  C CD1 . ILE A 240 ? 0.2999 0.3228 0.2473 0.0606  0.0018  0.0252  240 ILE A CD1 
1776  N N   . GLN A 241 ? 0.3732 0.4018 0.3291 0.0754  0.0293  0.0607  241 GLN A N   
1777  C CA  . GLN A 241 ? 0.3661 0.3948 0.3457 0.0788  0.0429  0.0731  241 GLN A CA  
1778  C C   . GLN A 241 ? 0.3744 0.4005 0.3602 0.0767  0.0452  0.0660  241 GLN A C   
1779  O O   . GLN A 241 ? 0.3722 0.4020 0.3361 0.0790  0.0448  0.0621  241 GLN A O   
1780  C CB  . GLN A 241 ? 0.4097 0.4528 0.3769 0.0890  0.0527  0.0941  241 GLN A CB  
1781  C CG  . GLN A 241 ? 0.4741 0.5203 0.4644 0.0944  0.0697  0.1116  241 GLN A CG  
1782  C CD  . GLN A 241 ? 0.4822 0.5157 0.5230 0.0906  0.0778  0.1161  241 GLN A CD  
1783  O OE1 . GLN A 241 ? 0.4749 0.5014 0.5312 0.0871  0.0735  0.1113  241 GLN A OE1 
1784  N NE2 . GLN A 241 ? 0.4964 0.5277 0.5674 0.0910  0.0907  0.1231  241 GLN A NE2 
1785  N N   . VAL A 242 ? 0.3505 0.3720 0.3703 0.0718  0.0479  0.0622  242 VAL A N   
1786  C CA  . VAL A 242 ? 0.3266 0.3494 0.3610 0.0703  0.0510  0.0588  242 VAL A CA  
1787  C C   . VAL A 242 ? 0.3540 0.3776 0.4207 0.0736  0.0681  0.0734  242 VAL A C   
1788  O O   . VAL A 242 ? 0.3646 0.3850 0.4688 0.0697  0.0728  0.0738  242 VAL A O   
1789  C CB  . VAL A 242 ? 0.3056 0.3310 0.3568 0.0617  0.0392  0.0425  242 VAL A CB  
1790  C CG1 . VAL A 242 ? 0.3128 0.3439 0.3851 0.0608  0.0420  0.0416  242 VAL A CG1 
1791  C CG2 . VAL A 242 ? 0.3045 0.3316 0.3270 0.0602  0.0254  0.0339  242 VAL A CG2 
1792  N N   . ASN A 243 ? 0.3136 0.3424 0.3701 0.0806  0.0790  0.0843  243 ASN A N   
1793  C CA  . ASN A 243 ? 0.3319 0.3642 0.4185 0.0854  0.0980  0.1026  243 ASN A CA  
1794  C C   . ASN A 243 ? 0.3298 0.3602 0.4596 0.0789  0.1002  0.0954  243 ASN A C   
1795  O O   . ASN A 243 ? 0.2988 0.3288 0.4725 0.0784  0.1136  0.1060  243 ASN A O   
1796  C CB  . ASN A 243 ? 0.3787 0.4231 0.4349 0.0960  0.1098  0.1152  243 ASN A CB  
1797  C CG  . ASN A 243 ? 0.4597 0.5169 0.4881 0.1047  0.1139  0.1320  243 ASN A CG  
1798  O OD1 . ASN A 243 ? 0.4787 0.5326 0.5129 0.1034  0.1086  0.1366  243 ASN A OD1 
1799  N ND2 . ASN A 243 ? 0.5074 0.5835 0.5064 0.1141  0.1238  0.1408  243 ASN A ND2 
1800  N N   . ALA A 244 ? 0.3612 0.3930 0.4827 0.0743  0.0872  0.0787  244 ALA A N   
1801  C CA  . ALA A 244 ? 0.2905 0.3278 0.4501 0.0683  0.0853  0.0711  244 ALA A CA  
1802  C C   . ALA A 244 ? 0.3252 0.3691 0.4731 0.0636  0.0665  0.0553  244 ALA A C   
1803  O O   . ALA A 244 ? 0.2648 0.3057 0.3768 0.0668  0.0597  0.0530  244 ALA A O   
1804  C CB  . ALA A 244 ? 0.2749 0.3159 0.4470 0.0748  0.1019  0.0840  244 ALA A CB  
1805  N N   . ILE A 245 ? 0.3519 0.4085 0.5344 0.0562  0.0585  0.0453  245 ILE A N   
1806  C CA  . ILE A 245 ? 0.3058 0.3775 0.4846 0.0545  0.0436  0.0382  245 ILE A CA  
1807  C C   . ILE A 245 ? 0.3243 0.4045 0.5327 0.0573  0.0513  0.0455  245 ILE A C   
1808  O O   . ILE A 245 ? 0.2720 0.3616 0.5226 0.0525  0.0552  0.0434  245 ILE A O   
1809  C CB  . ILE A 245 ? 0.2972 0.3888 0.4902 0.0451  0.0264  0.0213  245 ILE A CB  
1810  C CG1 . ILE A 245 ? 0.3245 0.4069 0.4955 0.0423  0.0225  0.0130  245 ILE A CG1 
1811  C CG2 . ILE A 245 ? 0.2568 0.3707 0.4419 0.0465  0.0114  0.0216  245 ILE A CG2 
1812  C CD1 . ILE A 245 ? 0.3304 0.4330 0.5206 0.0320  0.0102  -0.0092 245 ILE A CD1 
1813  N N   . ARG A 246 ? 0.3382 0.4156 0.5301 0.0648  0.0539  0.0527  246 ARG A N   
1814  C CA  . ARG A 246 ? 0.2881 0.3718 0.5082 0.0691  0.0640  0.0607  246 ARG A CA  
1815  C C   . ARG A 246 ? 0.2783 0.3858 0.5207 0.0678  0.0494  0.0603  246 ARG A C   
1816  O O   . ARG A 246 ? 0.3189 0.4309 0.5423 0.0697  0.0381  0.0610  246 ARG A O   
1817  C CB  . ARG A 246 ? 0.3162 0.3843 0.5125 0.0789  0.0802  0.0672  246 ARG A CB  
1818  C CG  . ARG A 246 ? 0.3853 0.4593 0.6124 0.0845  0.0938  0.0747  246 ARG A CG  
1819  C CD  . ARG A 246 ? 0.4492 0.5106 0.6540 0.0939  0.1135  0.0762  246 ARG A CD  
1820  N NE  . ARG A 246 ? 0.4835 0.5358 0.6611 0.0965  0.1082  0.0677  246 ARG A NE  
1821  C CZ  . ARG A 246 ? 0.5155 0.5576 0.6599 0.1011  0.1187  0.0597  246 ARG A CZ  
1822  N NH1 . ARG A 246 ? 0.4885 0.5222 0.6181 0.1018  0.1140  0.0494  246 ARG A NH1 
1823  N NH2 . ARG A 246 ? 0.5672 0.6113 0.6955 0.1051  0.1344  0.0623  246 ARG A NH2 
1824  N N   . VAL A 247 ? 0.2665 0.3925 0.5530 0.0650  0.0502  0.0617  247 VAL A N   
1825  C CA  . VAL A 247 ? 0.2804 0.4362 0.5950 0.0658  0.0382  0.0660  247 VAL A CA  
1826  C C   . VAL A 247 ? 0.2562 0.4111 0.6035 0.0727  0.0549  0.0781  247 VAL A C   
1827  O O   . VAL A 247 ? 0.2704 0.4296 0.6521 0.0691  0.0640  0.0775  247 VAL A O   
1828  C CB  . VAL A 247 ? 0.2749 0.4652 0.6204 0.0547  0.0204  0.0530  247 VAL A CB  
1829  C CG1 . VAL A 247 ? 0.2231 0.4525 0.5963 0.0573  0.0070  0.0612  247 VAL A CG1 
1830  C CG2 . VAL A 247 ? 0.2110 0.4046 0.5275 0.0473  0.0059  0.0369  247 VAL A CG2 
1831  N N   . ASN A 248 ? 0.2633 0.4127 0.6057 0.0826  0.0610  0.0887  248 ASN A N   
1832  C CA  . ASN A 248 ? 0.2893 0.4322 0.6580 0.0907  0.0818  0.0980  248 ASN A CA  
1833  C C   . ASN A 248 ? 0.3039 0.4241 0.6601 0.0917  0.1041  0.0955  248 ASN A C   
1834  O O   . ASN A 248 ? 0.3241 0.4228 0.6381 0.0946  0.1116  0.0909  248 ASN A O   
1835  C CB  . ASN A 248 ? 0.3284 0.5034 0.7527 0.0892  0.0766  0.1053  248 ASN A CB  
1836  C CG  . ASN A 248 ? 0.3598 0.5640 0.8001 0.0929  0.0588  0.1155  248 ASN A CG  
1837  O OD1 . ASN A 248 ? 0.3541 0.5487 0.7726 0.0995  0.0576  0.1218  248 ASN A OD1 
1838  N ND2 . ASN A 248 ? 0.3746 0.6186 0.8572 0.0889  0.0452  0.1187  248 ASN A ND2 
1839  N N   . LYS A 249 ? 0.3173 0.4462 0.7117 0.0897  0.1148  0.1000  249 LYS A N   
1840  C CA  . LYS A 249 ? 0.3230 0.4359 0.7085 0.0923  0.1376  0.1039  249 LYS A CA  
1841  C C   . LYS A 249 ? 0.2984 0.4126 0.6989 0.0829  0.1353  0.1021  249 LYS A C   
1842  O O   . LYS A 249 ? 0.2811 0.3887 0.6921 0.0853  0.1558  0.1120  249 LYS A O   
1843  C CB  . LYS A 249 ? 0.3354 0.4507 0.7508 0.0987  0.1596  0.1143  249 LYS A CB  
1844  C CG  . LYS A 249 ? 0.3363 0.4474 0.7449 0.1062  0.1632  0.1141  249 LYS A CG  
1845  C CD  . LYS A 249 ? 0.3703 0.4757 0.7908 0.1100  0.1848  0.1206  249 LYS A CD  
1846  C CE  . LYS A 249 ? 0.4399 0.5469 0.8797 0.1139  0.1852  0.1219  249 LYS A CE  
1847  N NZ  . LYS A 249 ? 0.4961 0.5965 0.9440 0.1186  0.2089  0.1261  249 LYS A NZ  
1848  N N   . HIS A 250 ? 0.2886 0.4123 0.6909 0.0729  0.1120  0.0898  250 HIS A N   
1849  C CA  . HIS A 250 ? 0.2659 0.3893 0.6873 0.0630  0.1096  0.0827  250 HIS A CA  
1850  C C   . HIS A 250 ? 0.2816 0.3879 0.6531 0.0623  0.1029  0.0767  250 HIS A C   
1851  O O   . HIS A 250 ? 0.2708 0.3819 0.6143 0.0602  0.0836  0.0667  250 HIS A O   
1852  C CB  . HIS A 250 ? 0.2525 0.4056 0.7186 0.0512  0.0890  0.0677  250 HIS A CB  
1853  C CG  . HIS A 250 ? 0.2422 0.4158 0.7643 0.0512  0.0951  0.0740  250 HIS A CG  
1854  N ND1 . HIS A 250 ? 0.2329 0.4429 0.7972 0.0422  0.0755  0.0619  250 HIS A ND1 
1855  C CD2 . HIS A 250 ? 0.2410 0.4067 0.7821 0.0592  0.1183  0.0910  250 HIS A CD2 
1856  C CE1 . HIS A 250 ? 0.2317 0.4497 0.8340 0.0437  0.0848  0.0713  250 HIS A CE1 
1857  N NE2 . HIS A 250 ? 0.2443 0.4311 0.8279 0.0532  0.1104  0.0887  250 HIS A NE2 
1858  N N   . LEU A 251 ? 0.2949 0.3852 0.6607 0.0641  0.1186  0.0849  251 LEU A N   
1859  C CA  . LEU A 251 ? 0.2809 0.3571 0.6024 0.0647  0.1133  0.0819  251 LEU A CA  
1860  C C   . LEU A 251 ? 0.2694 0.3433 0.6194 0.0554  0.1106  0.0741  251 LEU A C   
1861  O O   . LEU A 251 ? 0.3002 0.3695 0.6889 0.0551  0.1283  0.0851  251 LEU A O   
1862  C CB  . LEU A 251 ? 0.2959 0.3599 0.5800 0.0766  0.1322  0.0989  251 LEU A CB  
1863  C CG  . LEU A 251 ? 0.3219 0.3856 0.5697 0.0848  0.1334  0.0977  251 LEU A CG  
1864  C CD1 . LEU A 251 ? 0.3178 0.3881 0.5909 0.0913  0.1529  0.1083  251 LEU A CD1 
1865  C CD2 . LEU A 251 ? 0.3378 0.3937 0.5317 0.0917  0.1373  0.0995  251 LEU A CD2 
1866  N N   . VAL A 252 ? 0.2409 0.3179 0.5722 0.0487  0.0904  0.0560  252 VAL A N   
1867  C CA  . VAL A 252 ? 0.2666 0.3426 0.6224 0.0391  0.0858  0.0413  252 VAL A CA  
1868  C C   . VAL A 252 ? 0.2726 0.3294 0.5945 0.0449  0.0925  0.0512  252 VAL A C   
1869  O O   . VAL A 252 ? 0.2927 0.3461 0.5632 0.0491  0.0825  0.0504  252 VAL A O   
1870  C CB  . VAL A 252 ? 0.2307 0.3277 0.5828 0.0293  0.0606  0.0146  252 VAL A CB  
1871  C CG1 . VAL A 252 ? 0.2333 0.3315 0.6158 0.0185  0.0580  -0.0069 252 VAL A CG1 
1872  C CG2 . VAL A 252 ? 0.2268 0.3508 0.6100 0.0252  0.0517  0.0080  252 VAL A CG2 
1873  N N   . ILE A 253 ? 0.3103 0.3564 0.6668 0.0456  0.1105  0.0628  253 ILE A N   
1874  C CA  . ILE A 253 ? 0.3478 0.3804 0.6779 0.0536  0.1195  0.0797  253 ILE A CA  
1875  C C   . ILE A 253 ? 0.4075 0.4346 0.7580 0.0453  0.1132  0.0624  253 ILE A C   
1876  O O   . ILE A 253 ? 0.4395 0.4639 0.8519 0.0384  0.1232  0.0564  253 ILE A O   
1877  C CB  . ILE A 253 ? 0.3600 0.3880 0.7163 0.0631  0.1467  0.1119  253 ILE A CB  
1878  C CG1 . ILE A 253 ? 0.3565 0.3931 0.7090 0.0700  0.1578  0.1262  253 ILE A CG1 
1879  C CG2 . ILE A 253 ? 0.4022 0.4255 0.7216 0.0736  0.1527  0.1326  253 ILE A CG2 
1880  C CD1 . ILE A 253 ? 0.3648 0.4060 0.6537 0.0761  0.1474  0.1221  253 ILE A CD1 
1881  N N   . PRO A 254 ? 0.4321 0.4580 0.7357 0.0454  0.0976  0.0519  254 PRO A N   
1882  C CA  . PRO A 254 ? 0.4832 0.5054 0.8006 0.0383  0.0916  0.0331  254 PRO A CA  
1883  C C   . PRO A 254 ? 0.5659 0.5733 0.9138 0.0437  0.1111  0.0525  254 PRO A C   
1884  O O   . PRO A 254 ? 0.5744 0.5783 0.9166 0.0550  0.1265  0.0846  254 PRO A O   
1885  C CB  . PRO A 254 ? 0.4173 0.4426 0.6710 0.0406  0.0734  0.0263  254 PRO A CB  
1886  C CG  . PRO A 254 ? 0.3929 0.4251 0.6125 0.0453  0.0674  0.0335  254 PRO A CG  
1887  C CD  . PRO A 254 ? 0.4010 0.4292 0.6397 0.0521  0.0863  0.0561  254 PRO A CD  
1888  N N   . THR A 255 ? 0.6635 0.6660 1.0445 0.0361  0.1108  0.0327  255 THR A N   
1889  C CA  . THR A 255 ? 0.7400 0.7279 1.1601 0.0398  0.1282  0.0457  255 THR A CA  
1890  C C   . THR A 255 ? 0.7844 0.7666 1.2933 0.0313  0.1454  0.0360  255 THR A C   
1891  O O   . THR A 255 ? 0.7943 0.7862 1.3306 0.0172  0.1357  -0.0012 255 THR A O   
1892  C CB  . THR A 255 ? 1.0884 1.0719 1.4860 0.0569  0.1426  0.0918  255 THR A CB  
1893  O OG1 . THR A 255 ? 1.1148 1.1019 1.5313 0.0631  0.1585  0.1182  255 THR A OG1 
1894  C CG2 . THR A 255 ? 1.0655 1.0565 1.3808 0.0639  0.1256  0.0971  255 THR A CG2 
1895  N N   . GLU A 272 ? 0.7852 0.9218 0.8506 0.1383  0.0913  0.2449  272 GLU A N   
1896  C CA  . GLU A 272 ? 0.7345 0.8301 0.8334 0.1320  0.0974  0.2339  272 GLU A CA  
1897  C C   . GLU A 272 ? 0.6674 0.7429 0.7349 0.1219  0.0793  0.1988  272 GLU A C   
1898  O O   . GLU A 272 ? 0.6464 0.7316 0.6671 0.1190  0.0672  0.1842  272 GLU A O   
1899  C CB  . GLU A 272 ? 0.7382 0.8255 0.8629 0.1328  0.1139  0.2423  272 GLU A CB  
1900  C CG  . GLU A 272 ? 0.8007 0.9034 0.9760 0.1393  0.1355  0.2710  272 GLU A CG  
1901  C CD  . GLU A 272 ? 0.8652 0.9463 1.1032 0.1341  0.1471  0.2716  272 GLU A CD  
1902  O OE1 . GLU A 272 ? 0.8685 0.9192 1.1143 0.1253  0.1392  0.2450  272 GLU A OE1 
1903  O OE2 . GLU A 272 ? 0.9152 1.0119 1.1991 0.1392  0.1652  0.2964  272 GLU A OE2 
1904  N N   . ILE A 273 ? 0.6173 0.6690 0.7146 0.1131  0.0784  0.1782  273 ILE A N   
1905  C CA  . ILE A 273 ? 0.5916 0.6301 0.6652 0.1003  0.0628  0.1410  273 ILE A CA  
1906  C C   . ILE A 273 ? 0.5476 0.5763 0.6171 0.0929  0.0626  0.1237  273 ILE A C   
1907  O O   . ILE A 273 ? 0.5454 0.5666 0.6518 0.0931  0.0763  0.1301  273 ILE A O   
1908  C CB  . ILE A 273 ? 0.4343 0.4570 0.5415 0.0939  0.0643  0.1234  273 ILE A CB  
1909  C CG1 . ILE A 273 ? 0.5072 0.5398 0.6215 0.1017  0.0647  0.1408  273 ILE A CG1 
1910  C CG2 . ILE A 273 ? 0.3882 0.4053 0.4680 0.0829  0.0492  0.0905  273 ILE A CG2 
1911  C CD1 . ILE A 273 ? 0.5413 0.5605 0.6843 0.0962  0.0668  0.1214  273 ILE A CD1 
1912  N N   . GLY A 274 ? 0.4886 0.5181 0.5197 0.0867  0.0481  0.1034  274 GLY A N   
1913  C CA  . GLY A 274 ? 0.4178 0.4407 0.4463 0.0806  0.0466  0.0885  274 GLY A CA  
1914  C C   . GLY A 274 ? 0.3693 0.3806 0.4364 0.0723  0.0498  0.0714  274 GLY A C   
1915  O O   . GLY A 274 ? 0.3726 0.3795 0.4591 0.0695  0.0503  0.0631  274 GLY A O   
1916  N N   . GLY A 275 ? 0.3564 0.3657 0.4356 0.0680  0.0519  0.0635  275 GLY A N   
1917  C CA  . GLY A 275 ? 0.3572 0.3623 0.4763 0.0592  0.0541  0.0441  275 GLY A CA  
1918  C C   . GLY A 275 ? 0.3737 0.3865 0.4753 0.0507  0.0385  0.0184  275 GLY A C   
1919  O O   . GLY A 275 ? 0.3731 0.3905 0.5023 0.0427  0.0373  -0.0030 275 GLY A O   
1920  N N   . ALA A 276 ? 0.3676 0.3259 0.3634 0.0140  0.0728  -0.0252 276 ALA A N   
1921  C CA  . ALA A 276 ? 0.3863 0.3446 0.3790 0.0149  0.0658  -0.0311 276 ALA A CA  
1922  C C   . ALA A 276 ? 0.3658 0.3217 0.3446 0.0155  0.0624  -0.0301 276 ALA A C   
1923  O O   . ALA A 276 ? 0.3703 0.3237 0.3414 0.0162  0.0633  -0.0274 276 ALA A O   
1924  C CB  . ALA A 276 ? 0.3425 0.3041 0.3395 0.0174  0.0653  -0.0321 276 ALA A CB  
1925  N N   . LEU A 277 ? 0.3535 0.3149 0.3312 0.0149  0.0586  -0.0341 277 LEU A N   
1926  C CA  . LEU A 277 ? 0.3372 0.3039 0.3034 0.0153  0.0566  -0.0320 277 LEU A CA  
1927  C C   . LEU A 277 ? 0.3500 0.3218 0.3138 0.0155  0.0520  -0.0234 277 LEU A C   
1928  O O   . LEU A 277 ? 0.3632 0.3404 0.3338 0.0164  0.0481  -0.0220 277 LEU A O   
1929  C CB  . LEU A 277 ? 0.3233 0.3022 0.2898 0.0153  0.0552  -0.0424 277 LEU A CB  
1930  C CG  . LEU A 277 ? 0.3336 0.3291 0.2874 0.0160  0.0543  -0.0409 277 LEU A CG  
1931  C CD1 . LEU A 277 ? 0.2988 0.2880 0.2504 0.0168  0.0590  -0.0377 277 LEU A CD1 
1932  C CD2 . LEU A 277 ? 0.3420 0.3586 0.2961 0.0167  0.0525  -0.0575 277 LEU A CD2 
1933  N N   . ILE A 278 ? 0.3666 0.3374 0.3258 0.0146  0.0521  -0.0158 278 ILE A N   
1934  C CA  . ILE A 278 ? 0.3196 0.2964 0.2833 0.0140  0.0478  -0.0024 278 ILE A CA  
1935  C C   . ILE A 278 ? 0.3419 0.3393 0.2950 0.0126  0.0477  0.0043  278 ILE A C   
1936  O O   . ILE A 278 ? 0.3737 0.3728 0.3207 0.0116  0.0518  0.0005  278 ILE A O   
1937  C CB  . ILE A 278 ? 0.3161 0.2777 0.2916 0.0126  0.0482  0.0012  278 ILE A CB  
1938  C CG1 . ILE A 278 ? 0.3248 0.2743 0.3079 0.0149  0.0502  -0.0105 278 ILE A CG1 
1939  C CG2 . ILE A 278 ? 0.3322 0.2961 0.3240 0.0117  0.0436  0.0182  278 ILE A CG2 
1940  C CD1 . ILE A 278 ? 0.3463 0.2859 0.3404 0.0137  0.0507  -0.0162 278 ILE A CD1 
1941  N N   . THR A 279 ? 0.3329 0.3518 0.2840 0.0131  0.0432  0.0147  279 THR A N   
1942  C CA  . THR A 279 ? 0.3402 0.3902 0.2777 0.0122  0.0441  0.0198  279 THR A CA  
1943  C C   . THR A 279 ? 0.3732 0.4477 0.3133 0.0118  0.0389  0.0451  279 THR A C   
1944  O O   . THR A 279 ? 0.3934 0.4624 0.3463 0.0135  0.0330  0.0545  279 THR A O   
1945  C CB  . THR A 279 ? 0.3457 0.4135 0.2717 0.0143  0.0445  -0.0023 279 THR A CB  
1946  O OG1 . THR A 279 ? 0.3582 0.4629 0.2701 0.0144  0.0466  -0.0018 279 THR A OG1 
1947  C CG2 . THR A 279 ? 0.3609 0.4378 0.2901 0.0156  0.0373  -0.0057 279 THR A CG2 
1948  N N   . THR A 280 ? 0.3827 0.4878 0.3133 0.0098  0.0415  0.0589  280 THR A N   
1949  C CA  . THR A 280 ? 0.3514 0.4881 0.2851 0.0092  0.0369  0.0905  280 THR A CA  
1950  C C   . THR A 280 ? 0.3436 0.5361 0.2516 0.0110  0.0357  0.0877  280 THR A C   
1951  O O   . THR A 280 ? 0.3581 0.5896 0.2634 0.0107  0.0322  0.1172  280 THR A O   
1952  C CB  . THR A 280 ? 0.3740 0.5104 0.3238 0.0040  0.0409  0.1195  280 THR A CB  
1953  O OG1 . THR A 280 ? 0.4026 0.5516 0.3389 0.0017  0.0494  0.1084  280 THR A OG1 
1954  C CG2 . THR A 280 ? 0.3276 0.4155 0.3094 0.0018  0.0395  0.1226  280 THR A CG2 
1955  N N   . THR A 281 ? 0.3472 0.5471 0.2392 0.0131  0.0381  0.0526  281 THR A N   
1956  C CA  . THR A 281 ? 0.4115 0.6691 0.2800 0.0149  0.0381  0.0406  281 THR A CA  
1957  C C   . THR A 281 ? 0.4250 0.7067 0.2867 0.0174  0.0282  0.0232  281 THR A C   
1958  O O   . THR A 281 ? 0.4080 0.7401 0.2510 0.0190  0.0270  0.0030  281 THR A O   
1959  C CB  . THR A 281 ? 0.4566 0.7167 0.3179 0.0162  0.0475  0.0085  281 THR A CB  
1960  O OG1 . THR A 281 ? 0.4904 0.7033 0.3660 0.0174  0.0478  -0.0188 281 THR A OG1 
1961  C CG2 . THR A 281 ? 0.4580 0.7141 0.3234 0.0136  0.0565  0.0281  281 THR A CG2 
1962  N N   . HIS A 282 ? 0.4259 0.6767 0.3046 0.0178  0.0209  0.0288  282 HIS A N   
1963  C CA  . HIS A 282 ? 0.4262 0.7082 0.3028 0.0197  0.0092  0.0262  282 HIS A CA  
1964  C C   . HIS A 282 ? 0.4118 0.6698 0.3110 0.0210  0.0028  0.0582  282 HIS A C   
1965  O O   . HIS A 282 ? 0.4159 0.6226 0.3344 0.0205  0.0076  0.0636  282 HIS A O   
1966  C CB  . HIS A 282 ? 0.4074 0.6812 0.2884 0.0194  0.0067  -0.0174 282 HIS A CB  
1967  C CG  . HIS A 282 ? 0.3542 0.5657 0.2571 0.0182  0.0118  -0.0295 282 HIS A CG  
1968  N ND1 . HIS A 282 ? 0.3658 0.5448 0.2877 0.0188  0.0091  -0.0140 282 HIS A ND1 
1969  C CD2 . HIS A 282 ? 0.3499 0.5313 0.2600 0.0172  0.0197  -0.0545 282 HIS A CD2 
1970  C CE1 . HIS A 282 ? 0.3432 0.4791 0.2783 0.0175  0.0157  -0.0287 282 HIS A CE1 
1971  N NE2 . HIS A 282 ? 0.3216 0.4573 0.2507 0.0164  0.0217  -0.0506 282 HIS A NE2 
1972  N N   . PRO A 283 ? 0.3867 0.6862 0.2854 0.0236  -0.0082 0.0795  283 PRO A N   
1973  C CA  . PRO A 283 ? 0.3675 0.6461 0.2951 0.0265  -0.0140 0.1140  283 PRO A CA  
1974  C C   . PRO A 283 ? 0.3683 0.6045 0.3195 0.0285  -0.0162 0.0950  283 PRO A C   
1975  O O   . PRO A 283 ? 0.3927 0.5839 0.3698 0.0299  -0.0127 0.1048  283 PRO A O   
1976  C CB  . PRO A 283 ? 0.3974 0.7417 0.3174 0.0296  -0.0260 0.1435  283 PRO A CB  
1977  C CG  . PRO A 283 ? 0.4067 0.8024 0.2939 0.0282  -0.0288 0.1099  283 PRO A CG  
1978  C CD  . PRO A 283 ? 0.3607 0.7339 0.2339 0.0245  -0.0156 0.0779  283 PRO A CD  
1979  N N   . TYR A 284 ? 0.3623 0.6157 0.3072 0.0282  -0.0217 0.0661  284 TYR A N   
1980  C CA  . TYR A 284 ? 0.3486 0.5725 0.3186 0.0297  -0.0240 0.0533  284 TYR A CA  
1981  C C   . TYR A 284 ? 0.3700 0.5498 0.3428 0.0259  -0.0132 0.0221  284 TYR A C   
1982  O O   . TYR A 284 ? 0.4130 0.5897 0.3688 0.0225  -0.0064 0.0044  284 TYR A O   
1983  C CB  . TYR A 284 ? 0.3531 0.6218 0.3245 0.0307  -0.0374 0.0444  284 TYR A CB  
1984  C CG  . TYR A 284 ? 0.3478 0.6675 0.3160 0.0353  -0.0492 0.0809  284 TYR A CG  
1985  C CD1 . TYR A 284 ? 0.3751 0.6788 0.3698 0.0409  -0.0512 0.1208  284 TYR A CD1 
1986  C CD2 . TYR A 284 ? 0.3730 0.7599 0.3155 0.0343  -0.0588 0.0760  284 TYR A CD2 
1987  C CE1 . TYR A 284 ? 0.4024 0.7531 0.4003 0.0455  -0.0622 0.1618  284 TYR A CE1 
1988  C CE2 . TYR A 284 ? 0.4062 0.8482 0.3447 0.0389  -0.0701 0.1157  284 TYR A CE2 
1989  C CZ  . TYR A 284 ? 0.4207 0.8431 0.3882 0.0445  -0.0718 0.1618  284 TYR A CZ  
1990  O OH  . TYR A 284 ? 0.4392 0.9170 0.4085 0.0493  -0.0834 0.2078  284 TYR A OH  
1991  N N   . THR A 285 ? 0.3624 0.5112 0.3594 0.0274  -0.0113 0.0182  285 THR A N   
1992  C CA  . THR A 285 ? 0.3507 0.4627 0.3530 0.0241  -0.0009 -0.0041 285 THR A CA  
1993  C C   . THR A 285 ? 0.3459 0.4716 0.3498 0.0194  -0.0031 -0.0324 285 THR A C   
1994  O O   . THR A 285 ? 0.3461 0.4978 0.3612 0.0192  -0.0125 -0.0378 285 THR A O   
1995  C CB  . THR A 285 ? 0.3447 0.4278 0.3719 0.0276  0.0031  0.0020  285 THR A CB  
1996  O OG1 . THR A 285 ? 0.3565 0.4237 0.3884 0.0312  0.0052  0.0225  285 THR A OG1 
1997  C CG2 . THR A 285 ? 0.3331 0.3881 0.3635 0.0242  0.0141  -0.0165 285 THR A CG2 
1998  N N   . VAL A 286 ? 0.3497 0.4588 0.3470 0.0156  0.0049  -0.0505 286 VAL A N   
1999  C CA  . VAL A 286 ? 0.3460 0.4649 0.3522 0.0107  0.0033  -0.0792 286 VAL A CA  
2000  C C   . VAL A 286 ? 0.3571 0.4409 0.3862 0.0075  0.0120  -0.0851 286 VAL A C   
2001  O O   . VAL A 286 ? 0.3664 0.4214 0.3917 0.0087  0.0217  -0.0750 286 VAL A O   
2002  C CB  . VAL A 286 ? 0.3349 0.4667 0.3240 0.0098  0.0054  -0.0961 286 VAL A CB  
2003  C CG1 . VAL A 286 ? 0.3239 0.4595 0.3327 0.0050  0.0043  -0.1296 286 VAL A CG1 
2004  C CG2 . VAL A 286 ? 0.3262 0.5042 0.2911 0.0124  -0.0025 -0.0886 286 VAL A CG2 
2005  N N   . LEU A 287 ? 0.3691 0.4608 0.4236 0.0031  0.0081  -0.0988 287 LEU A N   
2006  C CA  . LEU A 287 ? 0.3658 0.4318 0.4478 -0.0014 0.0167  -0.1017 287 LEU A CA  
2007  C C   . LEU A 287 ? 0.3805 0.4482 0.4876 -0.0085 0.0153  -0.1279 287 LEU A C   
2008  O O   . LEU A 287 ? 0.3779 0.4744 0.4894 -0.0110 0.0047  -0.1495 287 LEU A O   
2009  C CB  . LEU A 287 ? 0.3239 0.3959 0.4261 -0.0014 0.0154  -0.0927 287 LEU A CB  
2010  C CG  . LEU A 287 ? 0.3066 0.3789 0.3974 0.0066  0.0153  -0.0715 287 LEU A CG  
2011  C CD1 . LEU A 287 ? 0.3005 0.3864 0.4190 0.0071  0.0127  -0.0688 287 LEU A CD1 
2012  C CD2 . LEU A 287 ? 0.3131 0.3565 0.3926 0.0095  0.0277  -0.0599 287 LEU A CD2 
2013  N N   . SER A 288 ? 0.4175 0.4567 0.5442 -0.0117 0.0256  -0.1261 288 SER A N   
2014  C CA  . SER A 288 ? 0.4683 0.5022 0.6320 -0.0186 0.0251  -0.1486 288 SER A CA  
2015  C C   . SER A 288 ? 0.4364 0.4870 0.6336 -0.0259 0.0183  -0.1592 288 SER A C   
2016  O O   . SER A 288 ? 0.4359 0.4944 0.6309 -0.0250 0.0182  -0.1429 288 SER A O   
2017  C CB  . SER A 288 ? 0.5355 0.5363 0.7212 -0.0204 0.0375  -0.1349 288 SER A CB  
2018  O OG  . SER A 288 ? 0.5539 0.5477 0.7534 -0.0231 0.0449  -0.1119 288 SER A OG  
2019  N N   . HIS A 289 ? 0.4253 0.4831 0.6575 -0.0328 0.0122  -0.1891 289 HIS A N   
2020  C CA  . HIS A 289 ? 0.4605 0.5410 0.7273 -0.0410 0.0026  -0.2060 289 HIS A CA  
2021  C C   . HIS A 289 ? 0.4948 0.5642 0.7941 -0.0468 0.0100  -0.1831 289 HIS A C   
2022  O O   . HIS A 289 ? 0.4894 0.5832 0.7954 -0.0485 0.0035  -0.1814 289 HIS A O   
2023  C CB  . HIS A 289 ? 0.4656 0.5491 0.7751 -0.0488 -0.0033 -0.2455 289 HIS A CB  
2024  C CG  . HIS A 289 ? 0.4604 0.5693 0.8119 -0.0590 -0.0147 -0.2678 289 HIS A CG  
2025  N ND1 . HIS A 289 ? 0.4573 0.6134 0.7881 -0.0578 -0.0301 -0.2828 289 HIS A ND1 
2026  C CD2 . HIS A 289 ? 0.5071 0.6037 0.9229 -0.0710 -0.0132 -0.2745 289 HIS A CD2 
2027  C CE1 . HIS A 289 ? 0.4856 0.6585 0.8650 -0.0687 -0.0387 -0.3019 289 HIS A CE1 
2028  N NE2 . HIS A 289 ? 0.5241 0.6590 0.9518 -0.0748 -0.0268 -0.2931 289 HIS A NE2 
2029  N N   . SER A 290 ? 0.5219 0.5599 0.8437 -0.0496 0.0238  -0.1645 290 SER A N   
2030  C CA  . SER A 290 ? 0.5278 0.5627 0.8802 -0.0554 0.0329  -0.1411 290 SER A CA  
2031  C C   . SER A 290 ? 0.4270 0.4734 0.7404 -0.0468 0.0371  -0.1177 290 SER A C   
2032  O O   . SER A 290 ? 0.4108 0.4754 0.7414 -0.0492 0.0371  -0.1118 290 SER A O   
2033  C CB  . SER A 290 ? 0.6122 0.6176 0.9939 -0.0594 0.0471  -0.1198 290 SER A CB  
2034  O OG  . SER A 290 ? 0.6695 0.6596 1.0075 -0.0496 0.0550  -0.1007 290 SER A OG  
2035  N N   . ILE A 291 ? 0.4034 0.4403 0.6688 -0.0366 0.0402  -0.1071 291 ILE A N   
2036  C CA  . ILE A 291 ? 0.3601 0.4051 0.5946 -0.0278 0.0434  -0.0899 291 ILE A CA  
2037  C C   . ILE A 291 ? 0.3820 0.4540 0.6077 -0.0239 0.0294  -0.1000 291 ILE A C   
2038  O O   . ILE A 291 ? 0.3823 0.4681 0.6120 -0.0199 0.0299  -0.0901 291 ILE A O   
2039  C CB  . ILE A 291 ? 0.3583 0.3865 0.5506 -0.0194 0.0486  -0.0789 291 ILE A CB  
2040  C CG1 . ILE A 291 ? 0.3522 0.3599 0.5519 -0.0219 0.0613  -0.0649 291 ILE A CG1 
2041  C CG2 . ILE A 291 ? 0.3451 0.3804 0.5141 -0.0106 0.0505  -0.0668 291 ILE A CG2 
2042  C CD1 . ILE A 291 ? 0.3210 0.3157 0.4820 -0.0143 0.0649  -0.0562 291 ILE A CD1 
2043  N N   . PHE A 292 ? 0.3536 0.4374 0.5676 -0.0241 0.0168  -0.1188 292 PHE A N   
2044  C CA  . PHE A 292 ? 0.3433 0.4608 0.5482 -0.0205 0.0018  -0.1251 292 PHE A CA  
2045  C C   . PHE A 292 ? 0.4034 0.5444 0.6479 -0.0263 -0.0042 -0.1311 292 PHE A C   
2046  O O   . PHE A 292 ? 0.3828 0.5431 0.6285 -0.0204 -0.0087 -0.1194 292 PHE A O   
2047  C CB  . PHE A 292 ? 0.3315 0.4675 0.5201 -0.0214 -0.0097 -0.1478 292 PHE A CB  
2048  C CG  . PHE A 292 ? 0.3197 0.5007 0.4994 -0.0187 -0.0266 -0.1534 292 PHE A CG  
2049  C CD1 . PHE A 292 ? 0.3243 0.5182 0.4720 -0.0087 -0.0307 -0.1310 292 PHE A CD1 
2050  C CD2 . PHE A 292 ? 0.3591 0.5725 0.5652 -0.0263 -0.0393 -0.1804 292 PHE A CD2 
2051  C CE1 . PHE A 292 ? 0.3465 0.5868 0.4873 -0.0054 -0.0469 -0.1296 292 PHE A CE1 
2052  C CE2 . PHE A 292 ? 0.3757 0.6390 0.5714 -0.0233 -0.0566 -0.1839 292 PHE A CE2 
2053  C CZ  . PHE A 292 ? 0.3529 0.6307 0.5147 -0.0124 -0.0603 -0.1558 292 PHE A CZ  
2054  N N   . GLU A 293 ? 0.4384 0.5764 0.7224 -0.0378 -0.0034 -0.1481 293 GLU A N   
2055  C CA  . GLU A 293 ? 0.4783 0.6412 0.8062 -0.0457 -0.0101 -0.1570 293 GLU A CA  
2056  C C   . GLU A 293 ? 0.4210 0.5819 0.7627 -0.0428 0.0017  -0.1316 293 GLU A C   
2057  O O   . GLU A 293 ? 0.3967 0.5862 0.7536 -0.0407 -0.0054 -0.1295 293 GLU A O   
2058  C CB  . GLU A 293 ? 0.5898 0.7446 0.9665 -0.0602 -0.0102 -0.1799 293 GLU A CB  
2059  C CG  . GLU A 293 ? 0.7157 0.9095 1.1244 -0.0684 -0.0286 -0.2099 293 GLU A CG  
2060  C CD  . GLU A 293 ? 0.8303 1.0547 1.2001 -0.0624 -0.0454 -0.2323 293 GLU A CD  
2061  O OE1 . GLU A 293 ? 0.8752 1.0872 1.2322 -0.0626 -0.0448 -0.2509 293 GLU A OE1 
2062  O OE2 . GLU A 293 ? 0.8678 1.1318 1.2200 -0.0565 -0.0586 -0.2286 293 GLU A OE2 
2063  N N   . VAL A 294 ? 0.4002 0.5323 0.7352 -0.0415 0.0196  -0.1126 294 VAL A N   
2064  C CA  . VAL A 294 ? 0.3799 0.5161 0.7262 -0.0384 0.0331  -0.0919 294 VAL A CA  
2065  C C   . VAL A 294 ? 0.3736 0.5194 0.6904 -0.0238 0.0304  -0.0829 294 VAL A C   
2066  O O   . VAL A 294 ? 0.4076 0.5760 0.7453 -0.0201 0.0299  -0.0788 294 VAL A O   
2067  C CB  . VAL A 294 ? 0.4040 0.5153 0.7452 -0.0399 0.0524  -0.0735 294 VAL A CB  
2068  C CG1 . VAL A 294 ? 0.3786 0.5031 0.7235 -0.0348 0.0670  -0.0555 294 VAL A CG1 
2069  C CG2 . VAL A 294 ? 0.4216 0.5230 0.8052 -0.0540 0.0562  -0.0754 294 VAL A CG2 
2070  N N   . PHE A 295 ? 0.3149 0.4446 0.5897 -0.0156 0.0282  -0.0802 295 PHE A N   
2071  C CA  . PHE A 295 ? 0.2983 0.4317 0.5528 -0.0024 0.0259  -0.0701 295 PHE A CA  
2072  C C   . PHE A 295 ? 0.2924 0.4577 0.5600 0.0019  0.0085  -0.0725 295 PHE A C   
2073  O O   . PHE A 295 ? 0.2906 0.4677 0.5721 0.0111  0.0086  -0.0632 295 PHE A O   
2074  C CB  . PHE A 295 ? 0.3220 0.4325 0.5344 0.0032  0.0260  -0.0658 295 PHE A CB  
2075  C CG  . PHE A 295 ? 0.3100 0.4232 0.5092 0.0155  0.0207  -0.0549 295 PHE A CG  
2076  C CD1 . PHE A 295 ? 0.3215 0.4258 0.5259 0.0237  0.0314  -0.0476 295 PHE A CD1 
2077  C CD2 . PHE A 295 ? 0.2891 0.4171 0.4753 0.0190  0.0053  -0.0518 295 PHE A CD2 
2078  C CE1 . PHE A 295 ? 0.3092 0.4120 0.5133 0.0351  0.0264  -0.0385 295 PHE A CE1 
2079  C CE2 . PHE A 295 ? 0.2995 0.4286 0.4828 0.0300  0.0006  -0.0358 295 PHE A CE2 
2080  C CZ  . PHE A 295 ? 0.2826 0.3957 0.4785 0.0380  0.0109  -0.0299 295 PHE A CZ  
2081  N N   . THR A 296 ? 0.2899 0.4733 0.5549 -0.0036 -0.0070 -0.0856 296 THR A N   
2082  C CA  . THR A 296 ? 0.3091 0.5308 0.5826 0.0013  -0.0252 -0.0844 296 THR A CA  
2083  C C   . THR A 296 ? 0.3251 0.5727 0.6448 -0.0012 -0.0273 -0.0867 296 THR A C   
2084  O O   . THR A 296 ? 0.3027 0.5765 0.6359 0.0080  -0.0369 -0.0760 296 THR A O   
2085  C CB  . THR A 296 ? 0.3418 0.5893 0.5994 -0.0041 -0.0422 -0.1015 296 THR A CB  
2086  O OG1 . THR A 296 ? 0.4114 0.6587 0.6929 -0.0180 -0.0416 -0.1271 296 THR A OG1 
2087  C CG2 . THR A 296 ? 0.2911 0.5220 0.5043 0.0002  -0.0404 -0.0964 296 THR A CG2 
2088  N N   . GLN A 297 ? 0.3414 0.5840 0.6910 -0.0134 -0.0185 -0.0978 297 GLN A N   
2089  C CA  . GLN A 297 ? 0.3414 0.6111 0.7386 -0.0166 -0.0189 -0.0984 297 GLN A CA  
2090  C C   . GLN A 297 ? 0.3322 0.5961 0.7378 -0.0054 -0.0033 -0.0803 297 GLN A C   
2091  O O   . GLN A 297 ? 0.3449 0.6367 0.7771 0.0021  -0.0087 -0.0750 297 GLN A O   
2092  C CB  . GLN A 297 ? 0.3683 0.6360 0.8033 -0.0342 -0.0130 -0.1122 297 GLN A CB  
2093  C CG  . GLN A 297 ? 0.6333 0.9352 1.1246 -0.0405 -0.0148 -0.1143 297 GLN A CG  
2094  C CD  . GLN A 297 ? 0.6538 1.0010 1.1588 -0.0389 -0.0398 -0.1263 297 GLN A CD  
2095  O OE1 . GLN A 297 ? 0.6790 1.0400 1.1779 -0.0459 -0.0566 -0.1475 297 GLN A OE1 
2096  N NE2 . GLN A 297 ? 0.6483 1.0235 1.1743 -0.0291 -0.0424 -0.1138 297 GLN A NE2 
2097  N N   . VAL A 298 ? 0.3368 0.5686 0.7215 -0.0036 0.0155  -0.0726 298 VAL A N   
2098  C CA  . VAL A 298 ? 0.3212 0.5500 0.7092 0.0077  0.0313  -0.0618 298 VAL A CA  
2099  C C   . VAL A 298 ? 0.3237 0.5589 0.7065 0.0242  0.0207  -0.0553 298 VAL A C   
2100  O O   . VAL A 298 ? 0.3309 0.5823 0.7415 0.0344  0.0249  -0.0518 298 VAL A O   
2101  C CB  . VAL A 298 ? 0.3093 0.5068 0.6659 0.0077  0.0491  -0.0570 298 VAL A CB  
2102  C CG1 . VAL A 298 ? 0.3007 0.4961 0.6512 0.0223  0.0609  -0.0529 298 VAL A CG1 
2103  C CG2 . VAL A 298 ? 0.2938 0.4911 0.6676 -0.0062 0.0632  -0.0546 298 VAL A CG2 
2104  N N   . PHE A 299 ? 0.3294 0.5541 0.6812 0.0269  0.0072  -0.0526 299 PHE A N   
2105  C CA  . PHE A 299 ? 0.3012 0.5328 0.6525 0.0412  -0.0047 -0.0401 299 PHE A CA  
2106  C C   . PHE A 299 ? 0.2866 0.5601 0.6749 0.0443  -0.0204 -0.0372 299 PHE A C   
2107  O O   . PHE A 299 ? 0.2602 0.5442 0.6757 0.0579  -0.0220 -0.0267 299 PHE A O   
2108  C CB  . PHE A 299 ? 0.3332 0.5530 0.6444 0.0410  -0.0155 -0.0342 299 PHE A CB  
2109  C CG  . PHE A 299 ? 0.3611 0.5837 0.6738 0.0551  -0.0253 -0.0141 299 PHE A CG  
2110  C CD1 . PHE A 299 ? 0.3608 0.6212 0.6882 0.0600  -0.0452 -0.0015 299 PHE A CD1 
2111  C CD2 . PHE A 299 ? 0.3588 0.5491 0.6632 0.0633  -0.0155 -0.0065 299 PHE A CD2 
2112  C CE1 . PHE A 299 ? 0.3384 0.6027 0.6741 0.0732  -0.0544 0.0236  299 PHE A CE1 
2113  C CE2 . PHE A 299 ? 0.3523 0.5424 0.6686 0.0756  -0.0246 0.0145  299 PHE A CE2 
2114  C CZ  . PHE A 299 ? 0.3496 0.5760 0.6828 0.0808  -0.0437 0.0323  299 PHE A CZ  
2115  N N   . ALA A 300 ? 0.3136 0.6127 0.7072 0.0323  -0.0327 -0.0482 300 ALA A N   
2116  C CA  . ALA A 300 ? 0.3167 0.6626 0.7455 0.0336  -0.0500 -0.0477 300 ALA A CA  
2117  C C   . ALA A 300 ? 0.3484 0.7067 0.8251 0.0376  -0.0388 -0.0472 300 ALA A C   
2118  O O   . ALA A 300 ? 0.4101 0.8011 0.9202 0.0471  -0.0498 -0.0387 300 ALA A O   
2119  C CB  . ALA A 300 ? 0.3101 0.6810 0.7396 0.0175  -0.0634 -0.0677 300 ALA A CB  
2120  N N   . ASN A 301 ? 0.3358 0.6725 0.8170 0.0309  -0.0165 -0.0543 301 ASN A N   
2121  C CA  . ASN A 301 ? 0.3239 0.6767 0.8477 0.0345  -0.0015 -0.0541 301 ASN A CA  
2122  C C   . ASN A 301 ? 0.3427 0.6896 0.8761 0.0547  0.0069  -0.0456 301 ASN A C   
2123  O O   . ASN A 301 ? 0.3744 0.7447 0.9491 0.0617  0.0159  -0.0469 301 ASN A O   
2124  C CB  . ASN A 301 ? 0.2940 0.6314 0.8168 0.0219  0.0215  -0.0596 301 ASN A CB  
2125  C CG  . ASN A 301 ? 0.2882 0.6340 0.8258 0.0018  0.0162  -0.0687 301 ASN A CG  
2126  O OD1 . ASN A 301 ? 0.2746 0.6462 0.8303 -0.0035 -0.0042 -0.0766 301 ASN A OD1 
2127  N ND2 . ASN A 301 ? 0.2865 0.6133 0.8206 -0.0099 0.0340  -0.0678 301 ASN A ND2 
2128  N N   . ASN A 302 ? 0.3195 0.6359 0.8197 0.0638  0.0053  -0.0391 302 ASN A N   
2129  C CA  . ASN A 302 ? 0.2942 0.6010 0.8106 0.0827  0.0117  -0.0343 302 ASN A CA  
2130  C C   . ASN A 302 ? 0.3442 0.6619 0.8763 0.0959  -0.0108 -0.0161 302 ASN A C   
2131  O O   . ASN A 302 ? 0.3759 0.6747 0.9165 0.1105  -0.0102 -0.0078 302 ASN A O   
2132  C CB  . ASN A 302 ? 0.2562 0.5223 0.7351 0.0838  0.0274  -0.0397 302 ASN A CB  
2133  C CG  . ASN A 302 ? 0.2345 0.5016 0.7099 0.0769  0.0520  -0.0531 302 ASN A CG  
2134  O OD1 . ASN A 302 ? 0.2377 0.5134 0.7346 0.0873  0.0675  -0.0621 302 ASN A OD1 
2135  N ND2 . ASN A 302 ? 0.2337 0.4959 0.6850 0.0598  0.0557  -0.0540 302 ASN A ND2 
2136  N N   . MET A 303 ? 0.3071 0.6590 0.8475 0.0905  -0.0310 -0.0094 303 MET A N   
2137  C CA  . MET A 303 ? 0.3110 0.6856 0.8649 0.1017  -0.0544 0.0130  303 MET A CA  
2138  C C   . MET A 303 ? 0.3136 0.7415 0.9100 0.1019  -0.0693 0.0145  303 MET A C   
2139  O O   . MET A 303 ? 0.2983 0.7431 0.9041 0.0884  -0.0645 -0.0035 303 MET A O   
2140  C CB  . MET A 303 ? 0.2682 0.6393 0.7726 0.0938  -0.0690 0.0220  303 MET A CB  
2141  C CG  . MET A 303 ? 0.4476 0.7718 0.9155 0.0958  -0.0588 0.0270  303 MET A CG  
2142  S SD  . MET A 303 ? 0.4879 0.7962 0.9873 0.1177  -0.0626 0.0554  303 MET A SD  
2143  C CE  . MET A 303 ? 0.3519 0.7023 0.8397 0.1193  -0.0917 0.0886  303 MET A CE  
2144  N N   . PRO A 304 ? 0.3873 0.8443 1.0131 0.1166  -0.0886 0.0382  304 PRO A N   
2145  C CA  . PRO A 304 ? 0.4126 0.9253 1.0714 0.1148  -0.1055 0.0388  304 PRO A CA  
2146  C C   . PRO A 304 ? 0.4089 0.9513 1.0367 0.0957  -0.1219 0.0269  304 PRO A C   
2147  O O   . PRO A 304 ? 0.3752 0.9317 0.9688 0.0949  -0.1393 0.0393  304 PRO A O   
2148  C CB  . PRO A 304 ? 0.4390 0.9639 1.1088 0.1332  -0.1210 0.0685  304 PRO A CB  
2149  C CG  . PRO A 304 ? 0.4269 0.9142 1.0692 0.1395  -0.1201 0.0875  304 PRO A CG  
2150  C CD  . PRO A 304 ? 0.4149 0.8550 1.0475 0.1345  -0.0947 0.0658  304 PRO A CD  
2151  N N   . LYS A 305 ? 0.4299 0.9851 1.0731 0.0803  -0.1155 0.0016  305 LYS A N   
2152  C CA  . LYS A 305 ? 0.4297 1.0002 1.0473 0.0597  -0.1252 -0.0199 305 LYS A CA  
2153  C C   . LYS A 305 ? 0.4427 1.0736 1.0583 0.0590  -0.1569 -0.0154 305 LYS A C   
2154  O O   . LYS A 305 ? 0.4557 1.0992 1.0396 0.0446  -0.1671 -0.0343 305 LYS A O   
2155  C CB  . LYS A 305 ? 0.3999 0.9748 1.0525 0.0437  -0.1121 -0.0440 305 LYS A CB  
2156  C CG  . LYS A 305 ? 0.3880 1.0096 1.0827 0.0439  -0.1228 -0.0411 305 LYS A CG  
2157  C CD  . LYS A 305 ? 0.3700 0.9879 1.0904 0.0266  -0.1067 -0.0583 305 LYS A CD  
2158  C CE  . LYS A 305 ? 0.3716 1.0224 1.1332 0.0339  -0.1069 -0.0484 305 LYS A CE  
2159  N NZ  . LYS A 305 ? 0.3618 0.9903 1.1323 0.0533  -0.0866 -0.0348 305 LYS A NZ  
2160  N N   . GLN A 306 ? 0.4346 1.1059 1.0852 0.0741  -0.1721 0.0079  306 GLN A N   
2161  C CA  . GLN A 306 ? 0.4219 1.1393 1.0606 0.0718  -0.2008 0.0160  306 GLN A CA  
2162  C C   . GLN A 306 ? 0.4002 1.1161 1.0064 0.0886  -0.2122 0.0475  306 GLN A C   
2163  O O   . GLN A 306 ? 0.4083 1.1557 1.0169 0.0960  -0.2314 0.0639  306 GLN A O   
2164  C CB  . GLN A 306 ? 0.4169 1.1692 1.1058 0.0707  -0.2113 0.0172  306 GLN A CB  
2165  C CG  . GLN A 306 ? 0.4291 1.2231 1.0969 0.0569  -0.2355 0.0040  306 GLN A CG  
2166  C CD  . GLN A 306 ? 0.4062 1.1996 1.0742 0.0321  -0.2273 -0.0330 306 GLN A CD  
2167  O OE1 . GLN A 306 ? 0.3788 1.1480 1.0734 0.0263  -0.2050 -0.0439 306 GLN A OE1 
2168  N NE2 . GLN A 306 ? 0.4243 1.2388 1.0592 0.0184  -0.2431 -0.0556 306 GLN A NE2 
2169  N N   . ALA A 307 ? 0.4078 1.0846 0.9864 0.0940  -0.1983 0.0602  307 ALA A N   
2170  C CA  . ALA A 307 ? 0.4573 1.1267 1.0017 0.1051  -0.2061 0.0937  307 ALA A CA  
2171  C C   . ALA A 307 ? 0.4601 1.1362 0.9441 0.0927  -0.2102 0.0861  307 ALA A C   
2172  O O   . ALA A 307 ? 0.5156 1.1894 0.9651 0.0987  -0.2149 0.1136  307 ALA A O   
2173  C CB  . ALA A 307 ? 0.4720 1.0862 1.0332 0.1205  -0.1871 0.1154  307 ALA A CB  
2174  N N   . GLN A 308 ? 0.4034 1.0836 0.8770 0.0756  -0.2052 0.0472  308 GLN A N   
2175  C CA  . GLN A 308 ? 0.3847 1.0661 0.8042 0.0635  -0.2056 0.0284  308 GLN A CA  
2176  C C   . GLN A 308 ? 0.4233 1.1512 0.8079 0.0586  -0.2264 0.0282  308 GLN A C   
2177  O O   . GLN A 308 ? 0.4253 1.1882 0.8315 0.0578  -0.2411 0.0263  308 GLN A O   
2178  C CB  . GLN A 308 ? 0.3641 1.0157 0.7862 0.0454  -0.1912 -0.0170 308 GLN A CB  
2179  C CG  . GLN A 308 ? 0.3587 0.9451 0.8050 0.0478  -0.1645 -0.0163 308 GLN A CG  
2180  C CD  . GLN A 308 ? 0.3927 0.9469 0.8428 0.0303  -0.1483 -0.0519 308 GLN A CD  
2181  O OE1 . GLN A 308 ? 0.4368 1.0098 0.8753 0.0158  -0.1566 -0.0806 308 GLN A OE1 
2182  N NE2 . GLN A 308 ? 0.3669 0.8744 0.8361 0.0317  -0.1248 -0.0501 308 GLN A NE2 
2183  N N   . VAL A 309 ? 0.4582 1.1891 0.7886 0.0558  -0.2263 0.0299  309 VAL A N   
2184  C CA  . VAL A 309 ? 0.5009 1.2797 0.7919 0.0507  -0.2413 0.0248  309 VAL A CA  
2185  C C   . VAL A 309 ? 0.5207 1.2917 0.7719 0.0372  -0.2330 -0.0145 309 VAL A C   
2186  O O   . VAL A 309 ? 0.4618 1.1899 0.7128 0.0346  -0.2176 -0.0252 309 VAL A O   
2187  C CB  . VAL A 309 ? 0.5236 1.3204 0.7879 0.0634  -0.2467 0.0732  309 VAL A CB  
2188  C CG1 . VAL A 309 ? 0.4813 1.2727 0.7925 0.0788  -0.2519 0.1124  309 VAL A CG1 
2189  C CG2 . VAL A 309 ? 0.5364 1.2988 0.7682 0.0657  -0.2316 0.0888  309 VAL A CG2 
2190  N N   . LYS A 310 ? 0.5856 1.3984 0.8059 0.0294  -0.2424 -0.0377 310 LYS A N   
2191  C CA  . LYS A 310 ? 0.6071 1.4148 0.7909 0.0187  -0.2337 -0.0769 310 LYS A CA  
2192  C C   . LYS A 310 ? 0.5739 1.3534 0.7234 0.0243  -0.2197 -0.0564 310 LYS A C   
2193  O O   . LYS A 310 ? 0.5670 1.3602 0.6948 0.0347  -0.2208 -0.0124 310 LYS A O   
2194  C CB  . LYS A 310 ? 0.6667 1.5331 0.8195 0.0146  -0.2443 -0.0967 310 LYS A CB  
2195  C CG  . LYS A 310 ? 0.6811 1.5446 0.8081 0.0045  -0.2347 -0.1457 310 LYS A CG  
2196  C CD  . LYS A 310 ? 0.7440 1.6742 0.8463 0.0028  -0.2447 -0.1645 310 LYS A CD  
2197  C CE  . LYS A 310 ? 0.7770 1.7513 0.8437 0.0143  -0.2488 -0.1154 310 LYS A CE  
2198  N NZ  . LYS A 310 ? 0.8385 1.8855 0.8759 0.0130  -0.2550 -0.1344 310 LYS A NZ  
2199  N N   . ALA A 311 ? 0.5496 1.2874 0.6996 0.0166  -0.2061 -0.0871 311 ALA A N   
2200  C CA  . ALA A 311 ? 0.5313 1.2389 0.6522 0.0200  -0.1923 -0.0748 311 ALA A CA  
2201  C C   . ALA A 311 ? 0.6034 1.3469 0.6730 0.0223  -0.1918 -0.0656 311 ALA A C   
2202  O O   . ALA A 311 ? 0.6673 1.4509 0.7200 0.0170  -0.1965 -0.0939 311 ALA A O   
2203  C CB  . ALA A 311 ? 0.4902 1.1548 0.6206 0.0097  -0.1796 -0.1166 311 ALA A CB  
2204  N N   . VAL A 312 ? 0.6223 1.3515 0.6711 0.0300  -0.1839 -0.0268 312 VAL A N   
2205  C CA  . VAL A 312 ? 0.6700 1.4358 0.6769 0.0330  -0.1810 -0.0062 312 VAL A CA  
2206  C C   . VAL A 312 ? 0.6960 1.4290 0.6786 0.0321  -0.1647 -0.0069 312 VAL A C   
2207  O O   . VAL A 312 ? 0.7003 1.3833 0.6991 0.0339  -0.1585 0.0016  312 VAL A O   
2208  C CB  . VAL A 312 ? 0.6740 1.4579 0.6880 0.0436  -0.1877 0.0546  312 VAL A CB  
2209  C CG1 . VAL A 312 ? 0.7140 1.5201 0.6934 0.0464  -0.1786 0.0877  312 VAL A CG1 
2210  C CG2 . VAL A 312 ? 0.6954 1.5252 0.7264 0.0448  -0.2048 0.0545  312 VAL A CG2 
2211  N N   . GLY A 313 ? 0.7211 1.4856 0.6682 0.0296  -0.1571 -0.0194 313 GLY A N   
2212  C CA  . GLY A 313 ? 0.6981 1.4360 0.6232 0.0290  -0.1411 -0.0190 313 GLY A CA  
2213  C C   . GLY A 313 ? 0.6400 1.3330 0.5749 0.0221  -0.1342 -0.0685 313 GLY A C   
2214  O O   . GLY A 313 ? 0.6700 1.3682 0.6204 0.0158  -0.1383 -0.1139 313 GLY A O   
2215  N N   . PRO A 314 ? 0.5615 1.2076 0.4923 0.0231  -0.1234 -0.0581 314 PRO A N   
2216  C CA  . PRO A 314 ? 0.5104 1.1069 0.4515 0.0174  -0.1149 -0.0958 314 PRO A CA  
2217  C C   . PRO A 314 ? 0.4919 1.0291 0.4750 0.0156  -0.1123 -0.0957 314 PRO A C   
2218  O O   . PRO A 314 ? 0.4813 0.9615 0.4804 0.0105  -0.0990 -0.1191 314 PRO A O   
2219  C CB  . PRO A 314 ? 0.5003 1.0640 0.4200 0.0208  -0.0994 -0.0694 314 PRO A CB  
2220  C CG  . PRO A 314 ? 0.4900 1.0678 0.4090 0.0284  -0.1048 -0.0110 314 PRO A CG  
2221  C CD  . PRO A 314 ? 0.5178 1.1570 0.4355 0.0299  -0.1179 -0.0038 314 PRO A CD  
2222  N N   . PHE A 315 ? 0.5090 1.0603 0.5116 0.0207  -0.1230 -0.0659 315 PHE A N   
2223  C CA  . PHE A 315 ? 0.4862 0.9845 0.5289 0.0213  -0.1178 -0.0587 315 PHE A CA  
2224  C C   . PHE A 315 ? 0.5197 1.0343 0.5948 0.0138  -0.1272 -0.0938 315 PHE A C   
2225  O O   . PHE A 315 ? 0.5764 1.1537 0.6456 0.0102  -0.1433 -0.1168 315 PHE A O   
2226  C CB  . PHE A 315 ? 0.4659 0.9668 0.5206 0.0322  -0.1226 -0.0078 315 PHE A CB  
2227  C CG  . PHE A 315 ? 0.4620 0.9477 0.4942 0.0380  -0.1142 0.0285  315 PHE A CG  
2228  C CD1 . PHE A 315 ? 0.4531 0.8737 0.4820 0.0363  -0.0952 0.0261  315 PHE A CD1 
2229  C CD2 . PHE A 315 ? 0.4819 1.0219 0.4993 0.0445  -0.1258 0.0674  315 PHE A CD2 
2230  C CE1 . PHE A 315 ? 0.4424 0.8497 0.4559 0.0401  -0.0881 0.0576  315 PHE A CE1 
2231  C CE2 . PHE A 315 ? 0.4662 0.9922 0.4702 0.0483  -0.1175 0.1036  315 PHE A CE2 
2232  C CZ  . PHE A 315 ? 0.4563 0.9147 0.4596 0.0456  -0.0987 0.0968  315 PHE A CZ  
2233  N N   . GLY A 316 ? 0.4940 0.9559 0.6043 0.0109  -0.1167 -0.0989 316 GLY A N   
2234  C CA  . GLY A 316 ? 0.4864 0.9554 0.6358 0.0021  -0.1222 -0.1287 316 GLY A CA  
2235  C C   . GLY A 316 ? 0.5074 0.9856 0.6940 0.0066  -0.1288 -0.1088 316 GLY A C   
2236  O O   . GLY A 316 ? 0.5654 1.0697 0.7853 -0.0003 -0.1385 -0.1304 316 GLY A O   
2237  N N   . LEU A 317 ? 0.4405 0.8978 0.6274 0.0183  -0.1233 -0.0694 317 LEU A N   
2238  C CA  . LEU A 317 ? 0.3771 0.8396 0.6037 0.0251  -0.1272 -0.0508 317 LEU A CA  
2239  C C   . LEU A 317 ? 0.3946 0.8798 0.6146 0.0396  -0.1367 -0.0078 317 LEU A C   
2240  O O   . LEU A 317 ? 0.4325 0.8788 0.6434 0.0470  -0.1253 0.0167  317 LEU A O   
2241  C CB  . LEU A 317 ? 0.3106 0.7119 0.5605 0.0249  -0.1056 -0.0507 317 LEU A CB  
2242  C CG  . LEU A 317 ? 0.3061 0.7047 0.6008 0.0317  -0.1029 -0.0379 317 LEU A CG  
2243  C CD1 . LEU A 317 ? 0.3111 0.7539 0.6415 0.0244  -0.1160 -0.0566 317 LEU A CD1 
2244  C CD2 . LEU A 317 ? 0.2889 0.6312 0.5920 0.0305  -0.0786 -0.0418 317 LEU A CD2 
2245  N N   . CYS A 318 ? 0.3962 0.9460 0.6247 0.0433  -0.1583 0.0024  318 CYS A N   
2246  C CA  . CYS A 318 ? 0.4128 0.9917 0.6394 0.0572  -0.1696 0.0491  318 CYS A CA  
2247  C C   . CYS A 318 ? 0.4664 1.0711 0.7420 0.0667  -0.1815 0.0684  318 CYS A C   
2248  O O   . CYS A 318 ? 0.4597 1.0875 0.7613 0.0607  -0.1884 0.0427  318 CYS A O   
2249  C CB  . CYS A 318 ? 0.4172 1.0641 0.6031 0.0552  -0.1863 0.0533  318 CYS A CB  
2250  S SG  . CYS A 318 ? 0.5268 1.1456 0.6601 0.0468  -0.1707 0.0336  318 CYS A SG  
2251  N N   . TYR A 319 ? 0.5155 1.1156 0.8098 0.0818  -0.1839 0.1140  319 TYR A N   
2252  C CA  . TYR A 319 ? 0.5309 1.1455 0.8764 0.0936  -0.1930 0.1355  319 TYR A CA  
2253  C C   . TYR A 319 ? 0.5721 1.2074 0.9091 0.1026  -0.2048 0.1770  319 TYR A C   
2254  O O   . TYR A 319 ? 0.5892 1.2234 0.8897 0.1019  -0.2028 0.1991  319 TYR A O   
2255  C CB  . TYR A 319 ? 0.5102 1.0624 0.8976 0.1029  -0.1741 0.1414  319 TYR A CB  
2256  C CG  . TYR A 319 ? 0.4832 0.9915 0.8748 0.0923  -0.1542 0.0982  319 TYR A CG  
2257  C CD1 . TYR A 319 ? 0.4922 0.9566 0.8444 0.0810  -0.1373 0.0753  319 TYR A CD1 
2258  C CD2 . TYR A 319 ? 0.4458 0.9593 0.8843 0.0941  -0.1516 0.0845  319 TYR A CD2 
2259  C CE1 . TYR A 319 ? 0.4854 0.9139 0.8442 0.0718  -0.1193 0.0429  319 TYR A CE1 
2260  C CE2 . TYR A 319 ? 0.4392 0.9186 0.8834 0.0841  -0.1325 0.0514  319 TYR A CE2 
2261  C CZ  . TYR A 319 ? 0.4737 0.9109 0.8779 0.0729  -0.1166 0.0324  319 TYR A CZ  
2262  O OH  . TYR A 319 ? 0.4790 0.8867 0.8912 0.0632  -0.0979 0.0058  319 TYR A OH  
2263  N N   . ASP A 320 ? 0.5834 1.2396 0.9563 0.1105  -0.2158 0.1889  320 ASP A N   
2264  C CA  . ASP A 320 ? 0.6247 1.2937 1.0026 0.1211  -0.2239 0.2341  320 ASP A CA  
2265  C C   . ASP A 320 ? 0.6041 1.2136 1.0163 0.1331  -0.2095 0.2619  320 ASP A C   
2266  O O   . ASP A 320 ? 0.5537 1.1261 1.0073 0.1392  -0.1990 0.2472  320 ASP A O   
2267  C CB  . ASP A 320 ? 0.6716 1.3827 1.0798 0.1266  -0.2406 0.2380  320 ASP A CB  
2268  C CG  . ASP A 320 ? 0.7225 1.4385 1.1512 0.1398  -0.2461 0.2881  320 ASP A CG  
2269  O OD1 . ASP A 320 ? 0.6928 1.3672 1.1693 0.1521  -0.2377 0.3038  320 ASP A OD1 
2270  O OD2 . ASP A 320 ? 0.7957 1.5581 1.1942 0.1375  -0.2574 0.3111  320 ASP A OD2 
2271  N N   . SER A 321 ? 0.6539 1.2562 1.0513 0.1355  -0.2077 0.3003  321 SER A N   
2272  C CA  . SER A 321 ? 0.6810 1.2243 1.1103 0.1434  -0.1936 0.3245  321 SER A CA  
2273  C C   . SER A 321 ? 0.7304 1.2553 1.2220 0.1574  -0.1943 0.3405  321 SER A C   
2274  O O   . SER A 321 ? 0.7626 1.2318 1.2913 0.1637  -0.1803 0.3364  321 SER A O   
2275  C CB  . SER A 321 ? 0.7103 1.2576 1.1124 0.1392  -0.1915 0.3630  321 SER A CB  
2276  O OG  . SER A 321 ? 0.7133 1.2849 1.0558 0.1270  -0.1905 0.3480  321 SER A OG  
2277  N N   . ARG A 322 ? 0.7225 1.2949 1.2263 0.1621  -0.2103 0.3558  322 ARG A N   
2278  C CA  . ARG A 322 ? 0.7152 1.2736 1.2798 0.1761  -0.2115 0.3729  322 ARG A CA  
2279  C C   . ARG A 322 ? 0.7015 1.2367 1.3024 0.1819  -0.2035 0.3334  322 ARG A C   
2280  O O   . ARG A 322 ? 0.7316 1.2254 1.3809 0.1922  -0.1928 0.3345  322 ARG A O   
2281  C CB  . ARG A 322 ? 0.7267 1.3470 1.2957 0.1802  -0.2315 0.4009  322 ARG A CB  
2282  C CG  . ARG A 322 ? 0.6998 1.3485 1.2997 0.1868  -0.2417 0.3774  322 ARG A CG  
2283  C CD  . ARG A 322 ? 0.7275 1.4445 1.3224 0.1887  -0.2635 0.4021  322 ARG A CD  
2284  N NE  . ARG A 322 ? 0.7057 1.4618 1.3134 0.1889  -0.2758 0.3701  322 ARG A NE  
2285  C CZ  . ARG A 322 ? 0.6812 1.4752 1.2506 0.1757  -0.2843 0.3360  322 ARG A CZ  
2286  N NH1 . ARG A 322 ? 0.6711 1.4691 1.1838 0.1625  -0.2811 0.3283  322 ARG A NH1 
2287  N NH2 . ARG A 322 ? 0.6718 1.4997 1.2633 0.1748  -0.2955 0.3081  322 ARG A NH2 
2288  N N   . LYS A 323 ? 0.6658 1.2263 1.2449 0.1738  -0.2061 0.2963  323 LYS A N   
2289  C CA  . LYS A 323 ? 0.6384 1.1875 1.2539 0.1774  -0.1973 0.2610  323 LYS A CA  
2290  C C   . LYS A 323 ? 0.6488 1.1395 1.2721 0.1765  -0.1734 0.2353  323 LYS A C   
2291  O O   . LYS A 323 ? 0.6591 1.1266 1.3225 0.1842  -0.1606 0.2179  323 LYS A O   
2292  C CB  . LYS A 323 ? 0.5637 1.1653 1.1627 0.1666  -0.2088 0.2312  323 LYS A CB  
2293  C CG  . LYS A 323 ? 0.5765 1.2404 1.1708 0.1668  -0.2330 0.2465  323 LYS A CG  
2294  C CD  . LYS A 323 ? 0.5446 1.2518 1.1357 0.1547  -0.2423 0.2081  323 LYS A CD  
2295  C CE  . LYS A 323 ? 0.5693 1.3386 1.1298 0.1476  -0.2662 0.2150  323 LYS A CE  
2296  N NZ  . LYS A 323 ? 0.5473 1.3437 1.0823 0.1283  -0.2716 0.1731  323 LYS A NZ  
2297  N N   . ILE A 324 ? 0.6447 1.1128 1.2295 0.1675  -0.1665 0.2334  324 ILE A N   
2298  C CA  . ILE A 324 ? 0.6020 1.0186 1.1898 0.1655  -0.1447 0.2079  324 ILE A CA  
2299  C C   . ILE A 324 ? 0.6468 1.0066 1.2524 0.1726  -0.1323 0.2219  324 ILE A C   
2300  O O   . ILE A 324 ? 0.5904 0.9071 1.1949 0.1707  -0.1147 0.1996  324 ILE A O   
2301  C CB  . ILE A 324 ? 0.5352 0.9584 1.0749 0.1511  -0.1431 0.1929  324 ILE A CB  
2302  C CG1 . ILE A 324 ? 0.5360 0.9617 1.0358 0.1473  -0.1508 0.2235  324 ILE A CG1 
2303  C CG2 . ILE A 324 ? 0.5138 0.9945 1.0382 0.1410  -0.1568 0.1759  324 ILE A CG2 
2304  C CD1 . ILE A 324 ? 0.5199 0.8905 1.0119 0.1467  -0.1351 0.2269  324 ILE A CD1 
2305  N N   . SER A 325 ? 0.7507 1.1110 1.3765 0.1798  -0.1410 0.2572  325 SER A N   
2306  C CA  . SER A 325 ? 0.8169 1.1241 1.4665 0.1833  -0.1299 0.2694  325 SER A CA  
2307  C C   . SER A 325 ? 0.8338 1.1064 1.5287 0.1921  -0.1145 0.2385  325 SER A C   
2308  O O   . SER A 325 ? 0.8442 1.0690 1.5589 0.1931  -0.1016 0.2301  325 SER A O   
2309  C CB  . SER A 325 ? 0.8851 1.2035 1.5529 0.1868  -0.1418 0.3172  325 SER A CB  
2310  O OG  . SER A 325 ? 0.9182 1.1873 1.6316 0.1913  -0.1314 0.3242  325 SER A OG  
2311  N N   . GLY A 326 ? 0.8395 1.1415 1.5514 0.1974  -0.1163 0.2207  326 GLY A N   
2312  C CA  . GLY A 326 ? 0.8618 1.1438 1.6029 0.2031  -0.0992 0.1837  326 GLY A CA  
2313  C C   . GLY A 326 ? 0.8816 1.1171 1.6082 0.1977  -0.0786 0.1528  326 GLY A C   
2314  O O   . GLY A 326 ? 0.9556 1.1559 1.7123 0.2033  -0.0669 0.1386  326 GLY A O   
2315  N N   . GLY A 327 ? 0.7947 1.0338 1.4767 0.1866  -0.0748 0.1397  327 GLY A N   
2316  C CA  . GLY A 327 ? 0.7155 0.9183 1.3785 0.1808  -0.0553 0.1080  327 GLY A CA  
2317  C C   . GLY A 327 ? 0.6202 0.8331 1.2382 0.1686  -0.0521 0.0958  327 GLY A C   
2318  O O   . GLY A 327 ? 0.6057 0.8523 1.2189 0.1641  -0.0528 0.0842  327 GLY A O   
2319  N N   . ALA A 328 ? 0.5693 0.7546 1.1585 0.1623  -0.0484 0.0978  328 ALA A N   
2320  C CA  . ALA A 328 ? 0.4999 0.6912 1.0514 0.1514  -0.0429 0.0828  328 ALA A CA  
2321  C C   . ALA A 328 ? 0.4836 0.6483 1.0274 0.1486  -0.0193 0.0440  328 ALA A C   
2322  O O   . ALA A 328 ? 0.5380 0.6750 1.0970 0.1540  -0.0093 0.0306  328 ALA A O   
2323  C CB  . ALA A 328 ? 0.4998 0.6771 1.0085 0.1428  -0.0498 0.1029  328 ALA A CB  
2324  N N   . PRO A 329 ? 0.4236 0.5952 0.9230 0.1338  -0.0099 0.0236  329 PRO A N   
2325  C CA  . PRO A 329 ? 0.4051 0.5609 0.8977 0.1320  0.0124  -0.0079 329 PRO A CA  
2326  C C   . PRO A 329 ? 0.4056 0.5239 0.8652 0.1274  0.0207  -0.0162 329 PRO A C   
2327  O O   . PRO A 329 ? 0.3632 0.4663 0.7965 0.1219  0.0109  0.0016  329 PRO A O   
2328  C CB  . PRO A 329 ? 0.3723 0.5506 0.8362 0.1174  0.0179  -0.0187 329 PRO A CB  
2329  C CG  . PRO A 329 ? 0.3613 0.5509 0.7978 0.1076  -0.0001 -0.0005 329 PRO A CG  
2330  C CD  . PRO A 329 ? 0.3864 0.5851 0.8514 0.1197  -0.0186 0.0264  329 PRO A CD  
2331  N N   . SER A 330 ? 0.4579 0.5674 0.9206 0.1299  0.0388  -0.0440 330 SER A N   
2332  C CA  . SER A 330 ? 0.5293 0.6118 0.9572 0.1237  0.0483  -0.0581 330 SER A CA  
2333  C C   . SER A 330 ? 0.5104 0.5916 0.8785 0.1065  0.0498  -0.0543 330 SER A C   
2334  O O   . SER A 330 ? 0.5274 0.6283 0.8813 0.0992  0.0583  -0.0617 330 SER A O   
2335  C CB  . SER A 330 ? 0.5734 0.6582 0.9990 0.1253  0.0647  -0.0880 330 SER A CB  
2336  O OG  . SER A 330 ? 0.6318 0.7201 1.0967 0.1354  0.0622  -0.0918 330 SER A OG  
2337  N N   . VAL A 331 ? 0.3717 0.6156 0.7385 0.0641  0.0556  -0.0108 331 VAL A N   
2338  C CA  . VAL A 331 ? 0.3291 0.5555 0.6420 0.0524  0.0530  -0.0108 331 VAL A CA  
2339  C C   . VAL A 331 ? 0.3716 0.5666 0.6433 0.0509  0.0634  -0.0116 331 VAL A C   
2340  O O   . VAL A 331 ? 0.4270 0.6103 0.6886 0.0599  0.0566  -0.0029 331 VAL A O   
2341  C CB  . VAL A 331 ? 0.2649 0.4989 0.5614 0.0546  0.0284  0.0005  331 VAL A CB  
2342  C CG1 . VAL A 331 ? 0.2141 0.4287 0.4626 0.0447  0.0272  -0.0024 331 VAL A CG1 
2343  C CG2 . VAL A 331 ? 0.2680 0.5353 0.6005 0.0530  0.0152  -0.0003 331 VAL A CG2 
2344  N N   . ASP A 332 ? 0.3408 0.5236 0.5897 0.0383  0.0788  -0.0206 332 ASP A N   
2345  C CA  . ASP A 332 ? 0.3113 0.4679 0.5229 0.0354  0.0870  -0.0217 332 ASP A CA  
2346  C C   . ASP A 332 ? 0.2552 0.3962 0.4276 0.0236  0.0844  -0.0190 332 ASP A C   
2347  O O   . ASP A 332 ? 0.2525 0.3993 0.4269 0.0126  0.0880  -0.0212 332 ASP A O   
2348  C CB  . ASP A 332 ? 0.3582 0.5136 0.5768 0.0309  0.1095  -0.0348 332 ASP A CB  
2349  C CG  . ASP A 332 ? 0.4311 0.6000 0.6980 0.0432  0.1153  -0.0409 332 ASP A CG  
2350  O OD1 . ASP A 332 ? 0.4592 0.6301 0.7453 0.0568  0.0999  -0.0300 332 ASP A OD1 
2351  O OD2 . ASP A 332 ? 0.4569 0.6342 0.7431 0.0389  0.1361  -0.0565 332 ASP A OD2 
2352  N N   . LEU A 333 ? 0.2545 0.3754 0.3961 0.0256  0.0786  -0.0138 333 LEU A N   
2353  C CA  . LEU A 333 ? 0.2622 0.3662 0.3721 0.0155  0.0766  -0.0107 333 LEU A CA  
2354  C C   . LEU A 333 ? 0.3015 0.3957 0.3916 0.0060  0.0910  -0.0142 333 LEU A C   
2355  O O   . LEU A 333 ? 0.3186 0.4059 0.4005 0.0100  0.0949  -0.0176 333 LEU A O   
2356  C CB  . LEU A 333 ? 0.2496 0.3403 0.3409 0.0219  0.0634  -0.0045 333 LEU A CB  
2357  C CG  . LEU A 333 ? 0.2360 0.3392 0.3396 0.0307  0.0506  -0.0018 333 LEU A CG  
2358  C CD1 . LEU A 333 ? 0.2287 0.3203 0.3122 0.0343  0.0421  0.0019  333 LEU A CD1 
2359  C CD2 . LEU A 333 ? 0.2328 0.3509 0.3512 0.0252  0.0458  -0.0054 333 LEU A CD2 
2360  N N   . ILE A 334 ? 0.3005 0.3951 0.3823 -0.0082 0.0988  -0.0134 334 ILE A N   
2361  C CA  . ILE A 334 ? 0.3275 0.4151 0.3816 -0.0210 0.1113  -0.0143 334 ILE A CA  
2362  C C   . ILE A 334 ? 0.3877 0.4539 0.4095 -0.0251 0.0984  -0.0019 334 ILE A C   
2363  O O   . ILE A 334 ? 0.3773 0.4357 0.4004 -0.0277 0.0882  0.0074  334 ILE A O   
2364  C CB  . ILE A 334 ? 0.3821 0.4802 0.4390 -0.0369 0.1257  -0.0148 334 ILE A CB  
2365  C CG1 . ILE A 334 ? 0.3779 0.5007 0.4793 -0.0326 0.1346  -0.0253 334 ILE A CG1 
2366  C CG2 . ILE A 334 ? 0.4425 0.5391 0.4670 -0.0508 0.1415  -0.0182 334 ILE A CG2 
2367  C CD1 . ILE A 334 ? 0.3624 0.4976 0.4862 -0.0226 0.1457  -0.0398 334 ILE A CD1 
2368  N N   . LEU A 335 ? 0.4295 0.4867 0.4276 -0.0253 0.0980  -0.0029 335 LEU A N   
2369  C CA  . LEU A 335 ? 0.4537 0.4933 0.4292 -0.0256 0.0827  0.0085  335 LEU A CA  
2370  C C   . LEU A 335 ? 0.4945 0.5261 0.4362 -0.0421 0.0827  0.0192  335 LEU A C   
2371  O O   . LEU A 335 ? 0.4948 0.5349 0.4241 -0.0559 0.0970  0.0176  335 LEU A O   
2372  C CB  . LEU A 335 ? 0.4710 0.5063 0.4450 -0.0150 0.0775  0.0027  335 LEU A CB  
2373  C CG  . LEU A 335 ? 0.4748 0.5167 0.4786 0.0004  0.0751  -0.0022 335 LEU A CG  
2374  C CD1 . LEU A 335 ? 0.5129 0.5491 0.5157 0.0081  0.0715  -0.0053 335 LEU A CD1 
2375  C CD2 . LEU A 335 ? 0.4761 0.5158 0.4896 0.0050  0.0630  0.0055  335 LEU A CD2 
2376  N N   . ASP A 336 ? 0.5536 0.5705 0.4822 -0.0405 0.0658  0.0307  336 ASP A N   
2377  C CA  . ASP A 336 ? 0.6194 0.6260 0.5187 -0.0537 0.0568  0.0479  336 ASP A CA  
2378  C C   . ASP A 336 ? 0.6318 0.6493 0.4982 -0.0697 0.0714  0.0426  336 ASP A C   
2379  O O   . ASP A 336 ? 0.6240 0.6506 0.4870 -0.0670 0.0809  0.0243  336 ASP A O   
2380  C CB  . ASP A 336 ? 0.6938 0.6894 0.5914 -0.0452 0.0376  0.0537  336 ASP A CB  
2381  C CG  . ASP A 336 ? 0.8029 0.7876 0.6769 -0.0563 0.0216  0.0757  336 ASP A CG  
2382  O OD1 . ASP A 336 ? 0.8449 0.8164 0.7355 -0.0545 0.0096  0.0913  336 ASP A OD1 
2383  O OD2 . ASP A 336 ? 0.8338 0.8232 0.6752 -0.0665 0.0193  0.0771  336 ASP A OD2 
2384  N N   . LYS A 337 ? 0.6826 0.7003 0.5280 -0.0872 0.0759  0.0568  337 LYS A N   
2385  C CA  . LYS A 337 ? 0.7625 0.7927 0.5685 -0.1064 0.0904  0.0531  337 LYS A CA  
2386  C C   . LYS A 337 ? 0.7529 0.8024 0.5728 -0.1054 0.1164  0.0256  337 LYS A C   
2387  O O   . LYS A 337 ? 0.7938 0.8565 0.5858 -0.1188 0.1321  0.0130  337 LYS A O   
2388  C CB  . LYS A 337 ? 0.8432 0.8711 0.6150 -0.1105 0.0773  0.0543  337 LYS A CB  
2389  C CG  . LYS A 337 ? 0.9426 0.9601 0.6825 -0.1230 0.0564  0.0840  337 LYS A CG  
2390  C CD  . LYS A 337 ? 1.0576 1.0819 0.7630 -0.1472 0.0678  0.0995  337 LYS A CD  
2391  C CE  . LYS A 337 ? 1.1546 1.1666 0.8314 -0.1590 0.0429  0.1353  337 LYS A CE  
2392  N NZ  . LYS A 337 ? 1.2380 1.2652 0.8624 -0.1770 0.0436  0.1334  337 LYS A NZ  
2393  N N   . ASN A 338 ? 0.7429 0.7956 0.6075 -0.0902 0.1207  0.0162  338 ASN A N   
2394  C CA  . ASN A 338 ? 0.7500 0.8203 0.6420 -0.0841 0.1413  -0.0084 338 ASN A CA  
2395  C C   . ASN A 338 ? 0.8298 0.9045 0.7124 -0.0813 0.1486  -0.0297 338 ASN A C   
2396  O O   . ASN A 338 ? 0.8651 0.9557 0.7598 -0.0840 0.1709  -0.0516 338 ASN A O   
2397  C CB  . ASN A 338 ? 0.7427 0.8306 0.6328 -0.1011 0.1648  -0.0125 338 ASN A CB  
2398  C CG  . ASN A 338 ? 0.6999 0.7826 0.5957 -0.1097 0.1595  0.0095  338 ASN A CG  
2399  O OD1 . ASN A 338 ? 0.6035 0.6770 0.5283 -0.0976 0.1448  0.0171  338 ASN A OD1 
2400  N ND2 . ASN A 338 ? 0.7541 0.8429 0.6207 -0.1325 0.1726  0.0191  338 ASN A ND2 
2401  N N   . ASP A 339 ? 0.8312 0.8926 0.6982 -0.0761 0.1310  -0.0256 339 ASP A N   
2402  C CA  . ASP A 339 ? 0.8638 0.9281 0.7259 -0.0746 0.1374  -0.0474 339 ASP A CA  
2403  C C   . ASP A 339 ? 0.8113 0.8747 0.7210 -0.0544 0.1398  -0.0602 339 ASP A C   
2404  O O   . ASP A 339 ? 0.8670 0.9343 0.7897 -0.0517 0.1518  -0.0821 339 ASP A O   
2405  C CB  . ASP A 339 ? 0.9254 0.9779 0.7589 -0.0770 0.1170  -0.0393 339 ASP A CB  
2406  C CG  . ASP A 339 ? 1.0179 1.0697 0.8053 -0.0957 0.1079  -0.0203 339 ASP A CG  
2407  O OD1 . ASP A 339 ? 1.0614 1.1206 0.8093 -0.1118 0.1107  -0.0283 339 ASP A OD1 
2408  O OD2 . ASP A 339 ? 1.0484 1.0920 0.8404 -0.0946 0.0971  0.0030  339 ASP A OD2 
2409  N N   . ALA A 340 ? 0.7003 0.7585 0.6368 -0.0408 0.1279  -0.0460 340 ALA A N   
2410  C CA  . ALA A 340 ? 0.6196 0.6756 0.5944 -0.0223 0.1245  -0.0510 340 ALA A CA  
2411  C C   . ALA A 340 ? 0.5701 0.6341 0.5777 -0.0129 0.1233  -0.0439 340 ALA A C   
2412  O O   . ALA A 340 ? 0.6298 0.6960 0.6300 -0.0195 0.1204  -0.0332 340 ALA A O   
2413  C CB  . ALA A 340 ? 0.5950 0.6364 0.5624 -0.0151 0.1050  -0.0408 340 ALA A CB  
2414  N N   . VAL A 341 ? 0.4747 0.5427 0.5200 0.0018  0.1241  -0.0490 341 VAL A N   
2415  C CA  . VAL A 341 ? 0.3955 0.4754 0.4749 0.0113  0.1209  -0.0433 341 VAL A CA  
2416  C C   . VAL A 341 ? 0.3425 0.4170 0.4398 0.0264  0.1074  -0.0352 341 VAL A C   
2417  O O   . VAL A 341 ? 0.3565 0.4249 0.4662 0.0324  0.1108  -0.0414 341 VAL A O   
2418  C CB  . VAL A 341 ? 0.4143 0.5124 0.5298 0.0123  0.1389  -0.0579 341 VAL A CB  
2419  C CG1 . VAL A 341 ? 0.3518 0.4632 0.5103 0.0257  0.1305  -0.0509 341 VAL A CG1 
2420  C CG2 . VAL A 341 ? 0.4510 0.5593 0.5498 -0.0049 0.1542  -0.0638 341 VAL A CG2 
2421  N N   . TRP A 342 ? 0.3156 0.3929 0.4150 0.0312  0.0933  -0.0223 342 TRP A N   
2422  C CA  . TRP A 342 ? 0.2711 0.3486 0.3856 0.0437  0.0815  -0.0128 342 TRP A CA  
2423  C C   . TRP A 342 ? 0.2768 0.3736 0.4267 0.0509  0.0794  -0.0103 342 TRP A C   
2424  O O   . TRP A 342 ? 0.2947 0.4029 0.4451 0.0483  0.0726  -0.0067 342 TRP A O   
2425  C CB  . TRP A 342 ? 0.2893 0.3606 0.3809 0.0433  0.0677  -0.0027 342 TRP A CB  
2426  C CG  . TRP A 342 ? 0.2907 0.3592 0.3870 0.0524  0.0599  0.0059  342 TRP A CG  
2427  C CD1 . TRP A 342 ? 0.3251 0.3966 0.4468 0.0613  0.0607  0.0101  342 TRP A CD1 
2428  C CD2 . TRP A 342 ? 0.3278 0.3897 0.4058 0.0528  0.0514  0.0121  342 TRP A CD2 
2429  N NE1 . TRP A 342 ? 0.3161 0.3832 0.4324 0.0657  0.0532  0.0211  342 TRP A NE1 
2430  C CE2 . TRP A 342 ? 0.3108 0.3736 0.4001 0.0605  0.0486  0.0209  342 TRP A CE2 
2431  C CE3 . TRP A 342 ? 0.3604 0.4162 0.4181 0.0476  0.0465  0.0114  342 TRP A CE3 
2432  C CZ2 . TRP A 342 ? 0.3132 0.3735 0.3904 0.0614  0.0434  0.0277  342 TRP A CZ2 
2433  C CZ3 . TRP A 342 ? 0.3457 0.3992 0.3964 0.0504  0.0410  0.0157  342 TRP A CZ3 
2434  C CH2 . TRP A 342 ? 0.3595 0.4164 0.4181 0.0566  0.0405  0.0232  342 TRP A CH2 
2435  N N   . ARG A 343 ? 0.2942 0.3949 0.4777 0.0594  0.0851  -0.0132 343 ARG A N   
2436  C CA  . ARG A 343 ? 0.2770 0.3976 0.5022 0.0680  0.0809  -0.0089 343 ARG A CA  
2437  C C   . ARG A 343 ? 0.3287 0.4550 0.5534 0.0756  0.0608  0.0103  343 ARG A C   
2438  O O   . ARG A 343 ? 0.3233 0.4369 0.5360 0.0796  0.0554  0.0198  343 ARG A O   
2439  C CB  . ARG A 343 ? 0.2781 0.3992 0.5465 0.0761  0.0927  -0.0176 343 ARG A CB  
2440  C CG  . ARG A 343 ? 0.2727 0.4156 0.5938 0.0865  0.0872  -0.0121 343 ARG A CG  
2441  C CD  . ARG A 343 ? 0.3277 0.4714 0.6846 0.0881  0.1041  -0.0299 343 ARG A CD  
2442  N NE  . ARG A 343 ? 0.3690 0.5209 0.7117 0.0747  0.1222  -0.0489 343 ARG A NE  
2443  C CZ  . ARG A 343 ? 0.4211 0.5686 0.7651 0.0677  0.1405  -0.0692 343 ARG A CZ  
2444  N NH1 . ARG A 343 ? 0.4458 0.5797 0.8103 0.0734  0.1439  -0.0767 343 ARG A NH1 
2445  N NH2 . ARG A 343 ? 0.4312 0.5881 0.7564 0.0534  0.1556  -0.0817 343 ARG A NH2 
2446  N N   . ILE A 344 ? 0.3323 0.4799 0.5688 0.0758  0.0502  0.0153  344 ILE A N   
2447  C CA  . ILE A 344 ? 0.3239 0.4822 0.5555 0.0807  0.0307  0.0323  344 ILE A CA  
2448  C C   . ILE A 344 ? 0.3395 0.5183 0.6185 0.0913  0.0209  0.0435  344 ILE A C   
2449  O O   . ILE A 344 ? 0.3270 0.5252 0.6370 0.0912  0.0213  0.0370  344 ILE A O   
2450  C CB  . ILE A 344 ? 0.2750 0.4434 0.4797 0.0712  0.0221  0.0288  344 ILE A CB  
2451  C CG1 . ILE A 344 ? 0.2892 0.4361 0.4577 0.0620  0.0315  0.0189  344 ILE A CG1 
2452  C CG2 . ILE A 344 ? 0.2539 0.4352 0.4446 0.0735  0.0038  0.0427  344 ILE A CG2 
2453  C CD1 . ILE A 344 ? 0.3001 0.4524 0.4512 0.0529  0.0255  0.0130  344 ILE A CD1 
2454  N N   . SER A 345 ? 0.3793 0.5538 0.6672 0.1003  0.0116  0.0620  345 SER A N   
2455  C CA  . SER A 345 ? 0.3925 0.5836 0.7289 0.1119  -0.0009 0.0784  345 SER A CA  
2456  C C   . SER A 345 ? 0.3890 0.6107 0.7218 0.1097  -0.0229 0.0896  345 SER A C   
2457  O O   . SER A 345 ? 0.4288 0.6539 0.7157 0.1013  -0.0310 0.0920  345 SER A O   
2458  C CB  . SER A 345 ? 0.3956 0.5701 0.7387 0.1201  -0.0056 0.0993  345 SER A CB  
2459  O OG  . SER A 345 ? 0.3600 0.5473 0.7257 0.1262  -0.0255 0.1222  345 SER A OG  
2460  N N   . SER A 346 ? 0.3869 0.6324 0.7705 0.1169  -0.0327 0.0949  346 SER A N   
2461  C CA  . SER A 346 ? 0.3825 0.6615 0.7677 0.1141  -0.0563 0.1047  346 SER A CA  
2462  C C   . SER A 346 ? 0.3810 0.6652 0.7398 0.1154  -0.0785 0.1330  346 SER A C   
2463  O O   . SER A 346 ? 0.3679 0.6792 0.7092 0.1097  -0.0994 0.1413  346 SER A O   
2464  C CB  . SER A 346 ? 0.4015 0.6965 0.8380 0.1185  -0.0603 0.0987  346 SER A CB  
2465  O OG  . SER A 346 ? 0.4385 0.7225 0.8993 0.1283  -0.0678 0.1142  346 SER A OG  
2466  N N   . GLU A 347 ? 0.4095 0.6660 0.7591 0.1199  -0.0723 0.1453  347 GLU A N   
2467  C CA  . GLU A 347 ? 0.4715 0.7281 0.7901 0.1180  -0.0883 0.1723  347 GLU A CA  
2468  C C   . GLU A 347 ? 0.4449 0.7012 0.7057 0.1083  -0.0833 0.1684  347 GLU A C   
2469  O O   . GLU A 347 ? 0.4534 0.7206 0.6774 0.1027  -0.0959 0.1866  347 GLU A O   
2470  C CB  . GLU A 347 ? 0.5500 0.7755 0.8881 0.1246  -0.0817 0.1857  347 GLU A CB  
2471  C CG  . GLU A 347 ? 0.6479 0.8691 1.0423 0.1333  -0.0818 0.1823  347 GLU A CG  
2472  C CD  . GLU A 347 ? 0.7548 0.9441 1.1739 0.1387  -0.0722 0.1899  347 GLU A CD  
2473  O OE1 . GLU A 347 ? 0.7738 0.9479 1.1669 0.1353  -0.0721 0.2067  347 GLU A OE1 
2474  O OE2 . GLU A 347 ? 0.8112 0.9923 1.2779 0.1453  -0.0642 0.1784  347 GLU A OE2 
2475  N N   . ASN A 348 ? 0.3825 0.6210 0.6275 0.1028  -0.0627 0.1396  348 ASN A N   
2476  C CA  . ASN A 348 ? 0.3776 0.6091 0.5679 0.0913  -0.0556 0.1264  348 ASN A CA  
2477  C C   . ASN A 348 ? 0.3758 0.6301 0.5484 0.0816  -0.0633 0.1099  348 ASN A C   
2478  O O   . ASN A 348 ? 0.4351 0.7021 0.5687 0.0731  -0.0711 0.1102  348 ASN A O   
2479  C CB  . ASN A 348 ? 0.3958 0.5959 0.5794 0.0901  -0.0326 0.1074  348 ASN A CB  
2480  C CG  . ASN A 348 ? 0.4927 0.6842 0.6281 0.0802  -0.0260 0.0955  348 ASN A CG  
2481  O OD1 . ASN A 348 ? 0.5275 0.7307 0.6436 0.0723  -0.0290 0.0813  348 ASN A OD1 
2482  N ND2 . ASN A 348 ? 0.5293 0.7013 0.6507 0.0808  -0.0172 0.1012  348 ASN A ND2 
2483  N N   . PHE A 349 ? 0.3416 0.6028 0.5441 0.0814  -0.0605 0.0944  349 PHE A N   
2484  C CA  . PHE A 349 ? 0.3475 0.6242 0.5340 0.0701  -0.0645 0.0752  349 PHE A CA  
2485  C C   . PHE A 349 ? 0.3684 0.6829 0.5668 0.0674  -0.0881 0.0818  349 PHE A C   
2486  O O   . PHE A 349 ? 0.3797 0.7091 0.5661 0.0566  -0.0932 0.0644  349 PHE A O   
2487  C CB  . PHE A 349 ? 0.3306 0.5947 0.5358 0.0665  -0.0475 0.0534  349 PHE A CB  
2488  C CG  . PHE A 349 ? 0.3242 0.5996 0.5824 0.0728  -0.0456 0.0539  349 PHE A CG  
2489  C CD1 . PHE A 349 ? 0.3447 0.6530 0.6333 0.0716  -0.0616 0.0547  349 PHE A CD1 
2490  C CD2 . PHE A 349 ? 0.3246 0.5797 0.6033 0.0782  -0.0263 0.0493  349 PHE A CD2 
2491  C CE1 . PHE A 349 ? 0.3553 0.6768 0.6999 0.0777  -0.0581 0.0531  349 PHE A CE1 
2492  C CE2 . PHE A 349 ? 0.3367 0.6041 0.6671 0.0834  -0.0207 0.0453  349 PHE A CE2 
2493  C CZ  . PHE A 349 ? 0.3558 0.6568 0.7221 0.0837  -0.0361 0.0475  349 PHE A CZ  
2494  N N   . MET A 350 ? 0.3966 0.7269 0.6230 0.0769  -0.1038 0.1064  350 MET A N   
2495  C CA  . MET A 350 ? 0.3883 0.7578 0.6200 0.0736  -0.1312 0.1172  350 MET A CA  
2496  C C   . MET A 350 ? 0.4222 0.8006 0.6059 0.0691  -0.1447 0.1370  350 MET A C   
2497  O O   . MET A 350 ? 0.4236 0.7853 0.6029 0.0763  -0.1414 0.1593  350 MET A O   
2498  C CB  . MET A 350 ? 0.3818 0.7687 0.6773 0.0862  -0.1447 0.1352  350 MET A CB  
2499  C CG  . MET A 350 ? 0.3502 0.7366 0.6976 0.0890  -0.1305 0.1143  350 MET A CG  
2500  S SD  . MET A 350 ? 0.3024 0.7065 0.6421 0.0720  -0.1287 0.0821  350 MET A SD  
2501  C CE  . MET A 350 ? 0.2883 0.7422 0.6269 0.0659  -0.1673 0.0943  350 MET A CE  
2502  N N   . VAL A 351 ? 0.4758 0.8799 0.6221 0.0555  -0.1574 0.1265  351 VAL A N   
2503  C CA  . VAL A 351 ? 0.5287 0.9470 0.6221 0.0476  -0.1684 0.1421  351 VAL A CA  
2504  C C   . VAL A 351 ? 0.6401 1.0854 0.7330 0.0425  -0.1953 0.1548  351 VAL A C   
2505  O O   . VAL A 351 ? 0.6755 1.1415 0.7918 0.0388  -0.2069 0.1393  351 VAL A O   
2506  C CB  . VAL A 351 ? 0.4923 0.9066 0.5337 0.0331  -0.1548 0.1119  351 VAL A CB  
2507  C CG1 . VAL A 351 ? 0.5123 0.9426 0.4976 0.0240  -0.1612 0.1267  351 VAL A CG1 
2508  C CG2 . VAL A 351 ? 0.4511 0.8238 0.4967 0.0374  -0.1257 0.0944  351 VAL A CG2 
2509  N N   . GLN A 352 ? 0.7220 1.1644 0.7869 0.0409  -0.2038 0.1811  352 GLN A N   
2510  C CA  . GLN A 352 ? 0.8078 1.2710 0.8685 0.0366  -0.2291 0.1970  352 GLN A CA  
2511  C C   . GLN A 352 ? 0.8954 1.3833 0.8931 0.0169  -0.2356 0.1820  352 GLN A C   
2512  O O   . GLN A 352 ? 0.9818 1.4749 0.9390 0.0094  -0.2416 0.2005  352 GLN A O   
2513  C CB  . GLN A 352 ? 0.8286 1.2747 0.8982 0.0454  -0.2342 0.2353  352 GLN A CB  
2514  C CG  . GLN A 352 ? 0.8872 1.3537 0.9590 0.0438  -0.2622 0.2582  352 GLN A CG  
2515  C CD  . GLN A 352 ? 0.8716 1.3501 1.0047 0.0544  -0.2778 0.2541  352 GLN A CD  
2516  O OE1 . GLN A 352 ? 0.8227 1.2823 1.0126 0.0700  -0.2699 0.2582  352 GLN A OE1 
2517  N NE2 . GLN A 352 ? 0.9193 1.4302 1.0428 0.0454  -0.2992 0.2440  352 GLN A NE2 
2518  N N   . ALA A 353 ? 0.8907 1.3922 0.8817 0.0076  -0.2314 0.1461  353 ALA A N   
2519  C CA  . ALA A 353 ? 0.9237 1.4471 0.8626 -0.0117 -0.2345 0.1216  353 ALA A CA  
2520  C C   . ALA A 353 ? 0.9560 1.4999 0.8634 -0.0202 -0.2560 0.1410  353 ALA A C   
2521  O O   . ALA A 353 ? 1.0101 1.5624 0.8612 -0.0340 -0.2507 0.1366  353 ALA A O   
2522  C CB  . ALA A 353 ? 0.9165 1.4549 0.8781 -0.0185 -0.2380 0.0849  353 ALA A CB  
2523  N N   . GLN A 354 ? 0.9031 1.4572 0.8482 -0.0124 -0.2797 0.1605  354 GLN A N   
2524  C CA  . GLN A 354 ? 0.8995 1.4756 0.8180 -0.0198 -0.3034 0.1803  354 GLN A CA  
2525  C C   . GLN A 354 ? 0.8744 1.4465 0.8375 -0.0040 -0.3221 0.2185  354 GLN A C   
2526  O O   . GLN A 354 ? 0.7949 1.3484 0.8151 0.0127  -0.3160 0.2243  354 GLN A O   
2527  C CB  . GLN A 354 ? 0.9189 1.5253 0.8261 -0.0341 -0.3193 0.1505  354 GLN A CB  
2528  C CG  . GLN A 354 ? 0.9727 1.5939 0.8086 -0.0546 -0.3134 0.1337  354 GLN A CG  
2529  C CD  . GLN A 354 ? 0.9899 1.6336 0.8178 -0.0695 -0.3204 0.0932  354 GLN A CD  
2530  O OE1 . GLN A 354 ? 0.9851 1.6400 0.8577 -0.0662 -0.3381 0.0856  354 GLN A OE1 
2531  N NE2 . GLN A 354 ? 1.0172 1.6680 0.7919 -0.0866 -0.3057 0.0653  354 GLN A NE2 
2532  N N   . ASP A 355 ? 0.9508 1.5396 0.8860 -0.0098 -0.3423 0.2440  355 ASP A N   
2533  C CA  . ASP A 355 ? 1.0271 1.6218 1.0022 0.0023  -0.3674 0.2785  355 ASP A CA  
2534  C C   . ASP A 355 ? 1.0037 1.5822 1.0610 0.0242  -0.3668 0.2836  355 ASP A C   
2535  O O   . ASP A 355 ? 1.0141 1.5671 1.1008 0.0377  -0.3588 0.3093  355 ASP A O   
2536  C CB  . ASP A 355 ? 1.1027 1.7363 1.0642 -0.0083 -0.3979 0.2721  355 ASP A CB  
2537  C CG  . ASP A 355 ? 1.1044 1.7531 1.0753 -0.0160 -0.3967 0.2267  355 ASP A CG  
2538  O OD1 . ASP A 355 ? 1.1309 1.7846 1.0508 -0.0330 -0.3835 0.1983  355 ASP A OD1 
2539  O OD2 . ASP A 355 ? 1.0682 1.7224 1.1018 -0.0053 -0.4059 0.2176  355 ASP A OD2 
2540  N N   . GLY A 356 ? 0.9631 1.5584 1.0588 0.0262  -0.3749 0.2573  356 GLY A N   
2541  C CA  . GLY A 356 ? 0.8841 1.4730 1.0593 0.0444  -0.3733 0.2542  356 GLY A CA  
2542  C C   . GLY A 356 ? 0.7829 1.3732 0.9762 0.0404  -0.3575 0.2137  356 GLY A C   
2543  O O   . GLY A 356 ? 0.7586 1.3610 1.0109 0.0478  -0.3619 0.1997  356 GLY A O   
2544  N N   . VAL A 357 ? 0.7151 1.2952 0.8585 0.0278  -0.3383 0.1947  357 VAL A N   
2545  C CA  . VAL A 357 ? 0.6218 1.2003 0.7779 0.0222  -0.3210 0.1582  357 VAL A CA  
2546  C C   . VAL A 357 ? 0.5801 1.1268 0.7324 0.0280  -0.2906 0.1557  357 VAL A C   
2547  O O   . VAL A 357 ? 0.6023 1.1359 0.7034 0.0229  -0.2794 0.1629  357 VAL A O   
2548  C CB  . VAL A 357 ? 0.6376 1.2353 0.7405 0.0002  -0.3242 0.1293  357 VAL A CB  
2549  C CG1 . VAL A 357 ? 0.5962 1.1885 0.7155 -0.0058 -0.3044 0.0931  357 VAL A CG1 
2550  C CG2 . VAL A 357 ? 0.6691 1.3001 0.7735 -0.0079 -0.3553 0.1273  357 VAL A CG2 
2551  N N   . SER A 358 ? 0.5267 1.0630 0.7340 0.0381  -0.2762 0.1443  358 SER A N   
2552  C CA  . SER A 358 ? 0.5100 1.0176 0.7179 0.0441  -0.2480 0.1405  358 SER A CA  
2553  C C   . SER A 358 ? 0.4626 0.9758 0.6780 0.0353  -0.2335 0.1065  358 SER A C   
2554  O O   . SER A 358 ? 0.4328 0.9609 0.6932 0.0340  -0.2369 0.0908  358 SER A O   
2555  C CB  . SER A 358 ? 0.5290 1.0139 0.7919 0.0634  -0.2379 0.1570  358 SER A CB  
2556  O OG  . SER A 358 ? 0.6168 1.0924 0.8710 0.0703  -0.2490 0.1888  358 SER A OG  
2557  N N   . CYS A 359 ? 0.4548 0.9576 0.6259 0.0281  -0.2172 0.0939  359 CYS A N   
2558  C CA  . CYS A 359 ? 0.4075 0.9107 0.5777 0.0178  -0.2027 0.0587  359 CYS A CA  
2559  C C   . CYS A 359 ? 0.3537 0.8106 0.5344 0.0265  -0.1710 0.0525  359 CYS A C   
2560  O O   . CYS A 359 ? 0.3401 0.7736 0.5081 0.0362  -0.1610 0.0707  359 CYS A O   
2561  C CB  . CYS A 359 ? 0.4224 0.9328 0.5312 0.0014  -0.2033 0.0382  359 CYS A CB  
2562  S SG  . CYS A 359 ? 0.5548 1.0978 0.6411 -0.0124 -0.2321 0.0364  359 CYS A SG  
2563  N N   . LEU A 360 ? 0.3464 0.7912 0.5504 0.0215  -0.1560 0.0272  360 LEU A N   
2564  C CA  . LEU A 360 ? 0.3353 0.7381 0.5403 0.0256  -0.1271 0.0188  360 LEU A CA  
2565  C C   . LEU A 360 ? 0.3585 0.7396 0.5099 0.0197  -0.1162 0.0084  360 LEU A C   
2566  O O   . LEU A 360 ? 0.4223 0.8098 0.5535 0.0070  -0.1180 -0.0144 360 LEU A O   
2567  C CB  . LEU A 360 ? 0.3122 0.7104 0.5516 0.0186  -0.1153 -0.0027 360 LEU A CB  
2568  C CG  . LEU A 360 ? 0.3065 0.6641 0.5432 0.0192  -0.0872 -0.0115 360 LEU A CG  
2569  C CD1 . LEU A 360 ? 0.2809 0.6211 0.5336 0.0334  -0.0747 0.0058  360 LEU A CD1 
2570  C CD2 . LEU A 360 ? 0.3320 0.6897 0.5973 0.0075  -0.0785 -0.0311 360 LEU A CD2 
2571  N N   . GLY A 361 ? 0.3122 0.6687 0.4458 0.0288  -0.1046 0.0232  361 GLY A N   
2572  C CA  . GLY A 361 ? 0.3015 0.6433 0.3885 0.0247  -0.0959 0.0173  361 GLY A CA  
2573  C C   . GLY A 361 ? 0.3271 0.6371 0.4066 0.0208  -0.0752 -0.0047 361 GLY A C   
2574  O O   . GLY A 361 ? 0.3406 0.6266 0.4021 0.0252  -0.0620 -0.0006 361 GLY A O   
2575  N N   . PHE A 362 ? 0.3344 0.6448 0.4308 0.0121  -0.0737 -0.0263 362 PHE A N   
2576  C CA  . PHE A 362 ? 0.3270 0.6093 0.4200 0.0065  -0.0580 -0.0466 362 PHE A CA  
2577  C C   . PHE A 362 ? 0.3365 0.6336 0.4202 -0.0066 -0.0647 -0.0727 362 PHE A C   
2578  O O   . PHE A 362 ? 0.3946 0.7203 0.4903 -0.0139 -0.0794 -0.0794 362 PHE A O   
2579  C CB  . PHE A 362 ? 0.2762 0.5407 0.4021 0.0062  -0.0476 -0.0480 362 PHE A CB  
2580  C CG  . PHE A 362 ? 0.2619 0.5105 0.3970 0.0170  -0.0377 -0.0294 362 PHE A CG  
2581  C CD1 . PHE A 362 ? 0.2658 0.5322 0.4210 0.0250  -0.0446 -0.0134 362 PHE A CD1 
2582  C CD2 . PHE A 362 ? 0.2669 0.4835 0.3947 0.0186  -0.0221 -0.0292 362 PHE A CD2 
2583  C CE1 . PHE A 362 ? 0.2694 0.5204 0.4372 0.0343  -0.0335 -0.0011 362 PHE A CE1 
2584  C CE2 . PHE A 362 ? 0.2762 0.4798 0.4108 0.0265  -0.0125 -0.0161 362 PHE A CE2 
2585  C CZ  . PHE A 362 ? 0.2737 0.4940 0.4290 0.0342  -0.0170 -0.0040 362 PHE A CZ  
2586  N N   . VAL A 363 ? 0.3366 0.6149 0.4034 -0.0100 -0.0540 -0.0895 363 VAL A N   
2587  C CA  . VAL A 363 ? 0.3525 0.6450 0.4106 -0.0225 -0.0583 -0.1189 363 VAL A CA  
2588  C C   . VAL A 363 ? 0.3506 0.6143 0.4336 -0.0283 -0.0471 -0.1406 363 VAL A C   
2589  O O   . VAL A 363 ? 0.3611 0.5925 0.4552 -0.0220 -0.0351 -0.1310 363 VAL A O   
2590  C CB  . VAL A 363 ? 0.4731 0.7768 0.4904 -0.0231 -0.0561 -0.1240 363 VAL A CB  
2591  C CG1 . VAL A 363 ? 0.5451 0.8645 0.5518 -0.0368 -0.0573 -0.1597 363 VAL A CG1 
2592  C CG2 . VAL A 363 ? 0.4319 0.7647 0.4260 -0.0196 -0.0696 -0.0982 363 VAL A CG2 
2593  N N   . ASP A 364 ? 0.3473 0.6233 0.4420 -0.0412 -0.0530 -0.1679 364 ASP A N   
2594  C CA  . ASP A 364 ? 0.3598 0.6084 0.4846 -0.0482 -0.0443 -0.1883 364 ASP A CA  
2595  C C   . ASP A 364 ? 0.3728 0.6021 0.4888 -0.0470 -0.0326 -0.2079 364 ASP A C   
2596  O O   . ASP A 364 ? 0.3791 0.6289 0.4768 -0.0535 -0.0343 -0.2329 364 ASP A O   
2597  C CB  . ASP A 364 ? 0.3761 0.6465 0.5225 -0.0636 -0.0555 -0.2121 364 ASP A CB  
2598  C CG  . ASP A 364 ? 0.4110 0.6514 0.5989 -0.0720 -0.0476 -0.2266 364 ASP A CG  
2599  O OD1 . ASP A 364 ? 0.4217 0.6248 0.6186 -0.0666 -0.0346 -0.2229 364 ASP A OD1 
2600  O OD2 . ASP A 364 ? 0.4162 0.6714 0.6305 -0.0846 -0.0559 -0.2396 364 ASP A OD2 
2601  N N   . GLY A 365 ? 0.3737 0.5656 0.5053 -0.0397 -0.0209 -0.1981 365 GLY A N   
2602  C CA  . GLY A 365 ? 0.3528 0.5248 0.4870 -0.0363 -0.0100 -0.2145 365 GLY A CA  
2603  C C   . GLY A 365 ? 0.4167 0.5736 0.5862 -0.0461 -0.0074 -0.2458 365 GLY A C   
2604  O O   . GLY A 365 ? 0.4474 0.5871 0.6305 -0.0434 0.0018  -0.2639 365 GLY A O   
2605  N N   . GLY A 366 ? 0.4158 0.5789 0.6067 -0.0575 -0.0150 -0.2532 366 GLY A N   
2606  C CA  . GLY A 366 ? 0.4379 0.5854 0.6676 -0.0684 -0.0128 -0.2837 366 GLY A CA  
2607  C C   . GLY A 366 ? 0.4820 0.5844 0.7500 -0.0658 -0.0065 -0.2676 366 GLY A C   
2608  O O   . GLY A 366 ? 0.4445 0.5324 0.7053 -0.0578 -0.0050 -0.2330 366 GLY A O   
2609  N N   . VAL A 367 ? 0.5788 0.6596 0.8883 -0.0735 -0.0033 -0.2934 367 VAL A N   
2610  C CA  . VAL A 367 ? 0.6259 0.6631 0.9786 -0.0744 0.0001  -0.2778 367 VAL A CA  
2611  C C   . VAL A 367 ? 0.7000 0.7059 1.0670 -0.0614 0.0069  -0.2728 367 VAL A C   
2612  O O   . VAL A 367 ? 0.7382 0.7077 1.1358 -0.0599 0.0074  -0.2511 367 VAL A O   
2613  C CB  . VAL A 367 ? 0.6146 0.6413 1.0148 -0.0903 -0.0012 -0.3059 367 VAL A CB  
2614  C CG1 . VAL A 367 ? 0.5809 0.6370 0.9758 -0.1040 -0.0093 -0.3061 367 VAL A CG1 
2615  C CG2 . VAL A 367 ? 0.6432 0.6814 1.0467 -0.0884 0.0040  -0.3441 367 VAL A CG2 
2616  N N   . HIS A 368 ? 0.7228 0.7444 1.0707 -0.0532 0.0120  -0.2928 368 HIS A N   
2617  C CA  . HIS A 368 ? 0.7460 0.7439 1.1089 -0.0394 0.0182  -0.2869 368 HIS A CA  
2618  C C   . HIS A 368 ? 0.7006 0.7175 1.0159 -0.0279 0.0196  -0.2654 368 HIS A C   
2619  O O   . HIS A 368 ? 0.7439 0.7648 1.0562 -0.0188 0.0268  -0.2765 368 HIS A O   
2620  C CB  . HIS A 368 ? 0.8052 0.8054 1.1965 -0.0383 0.0269  -0.3249 368 HIS A CB  
2621  C CG  . HIS A 368 ? 0.8648 0.8493 1.3026 -0.0462 0.0264  -0.3347 368 HIS A CG  
2622  N ND1 . HIS A 368 ? 0.8853 0.8309 1.3664 -0.0434 0.0231  -0.3099 368 HIS A ND1 
2623  C CD2 . HIS A 368 ? 0.9138 0.9170 1.3608 -0.0569 0.0283  -0.3648 368 HIS A CD2 
2624  C CE1 . HIS A 368 ? 0.9353 0.8754 1.4523 -0.0516 0.0240  -0.3252 368 HIS A CE1 
2625  N NE2 . HIS A 368 ? 0.9437 0.9177 1.4421 -0.0597 0.0274  -0.3600 368 HIS A NE2 
2626  N N   . ALA A 369 ? 0.6232 0.6515 0.9056 -0.0286 0.0137  -0.2355 369 ALA A N   
2627  C CA  . ALA A 369 ? 0.5501 0.5927 0.7925 -0.0183 0.0146  -0.2135 369 ALA A CA  
2628  C C   . ALA A 369 ? 0.5833 0.5967 0.8398 -0.0071 0.0165  -0.1917 369 ALA A C   
2629  O O   . ALA A 369 ? 0.5914 0.5740 0.8780 -0.0082 0.0132  -0.1770 369 ALA A O   
2630  C CB  . ALA A 369 ? 0.4736 0.5321 0.6876 -0.0212 0.0086  -0.1885 369 ALA A CB  
2631  N N   . ARG A 370 ? 0.5995 0.6247 0.8330 0.0025  0.0206  -0.1874 370 ARG A N   
2632  C CA  . ARG A 370 ? 0.6276 0.6328 0.8746 0.0134  0.0214  -0.1713 370 ARG A CA  
2633  C C   . ARG A 370 ? 0.5724 0.5599 0.8099 0.0137  0.0138  -0.1333 370 ARG A C   
2634  O O   . ARG A 370 ? 0.5917 0.5518 0.8543 0.0162  0.0090  -0.1175 370 ARG A O   
2635  C CB  . ARG A 370 ? 0.7228 0.7514 0.9441 0.0206  0.0287  -0.1769 370 ARG A CB  
2636  C CG  . ARG A 370 ? 0.8182 0.8355 1.0469 0.0317  0.0291  -0.1592 370 ARG A CG  
2637  C CD  . ARG A 370 ? 0.9168 0.9118 1.1984 0.0374  0.0297  -0.1712 370 ARG A CD  
2638  N NE  . ARG A 370 ? 0.9501 0.9370 1.2435 0.0477  0.0271  -0.1535 370 ARG A NE  
2639  C CZ  . ARG A 370 ? 0.9689 0.9335 1.2696 0.0504  0.0148  -0.1224 370 ARG A CZ  
2640  N NH1 . ARG A 370 ? 0.9720 0.9195 1.2674 0.0431  0.0064  -0.1041 370 ARG A NH1 
2641  N NH2 . ARG A 370 ? 0.9724 0.9343 1.2851 0.0591  0.0109  -0.1097 370 ARG A NH2 
2642  N N   . ALA A 371 ? 0.5093 0.5136 0.7122 0.0102  0.0126  -0.1196 371 ALA A N   
2643  C CA  . ALA A 371 ? 0.4324 0.4258 0.6224 0.0081  0.0088  -0.0891 371 ALA A CA  
2644  C C   . ALA A 371 ? 0.4074 0.4162 0.5857 -0.0010 0.0087  -0.0874 371 ALA A C   
2645  O O   . ALA A 371 ? 0.4429 0.4745 0.6173 -0.0043 0.0088  -0.1064 371 ALA A O   
2646  C CB  . ALA A 371 ? 0.4075 0.4060 0.5709 0.0164  0.0095  -0.0719 371 ALA A CB  
2647  N N   . GLY A 372 ? 0.3758 0.3746 0.5496 -0.0061 0.0084  -0.0652 372 GLY A N   
2648  C CA  . GLY A 372 ? 0.3612 0.3761 0.5307 -0.0145 0.0100  -0.0632 372 GLY A CA  
2649  C C   . GLY A 372 ? 0.3464 0.3903 0.4921 -0.0090 0.0106  -0.0639 372 GLY A C   
2650  O O   . GLY A 372 ? 0.3666 0.4326 0.5164 -0.0135 0.0086  -0.0733 372 GLY A O   
2651  N N   . ILE A 373 ? 0.3490 0.3926 0.4737 0.0004  0.0123  -0.0527 373 ILE A N   
2652  C CA  . ILE A 373 ? 0.3200 0.3862 0.4252 0.0071  0.0126  -0.0498 373 ILE A CA  
2653  C C   . ILE A 373 ? 0.3316 0.3981 0.4240 0.0159  0.0129  -0.0524 373 ILE A C   
2654  O O   . ILE A 373 ? 0.3409 0.3889 0.4333 0.0194  0.0142  -0.0452 373 ILE A O   
2655  C CB  . ILE A 373 ? 0.2892 0.3545 0.3850 0.0081  0.0172  -0.0321 373 ILE A CB  
2656  C CG1 . ILE A 373 ? 0.2875 0.3556 0.3976 -0.0019 0.0204  -0.0298 373 ILE A CG1 
2657  C CG2 . ILE A 373 ? 0.2596 0.3451 0.3442 0.0161  0.0168  -0.0287 373 ILE A CG2 
2658  C CD1 . ILE A 373 ? 0.2897 0.3564 0.3921 -0.0032 0.0287  -0.0166 373 ILE A CD1 
2659  N N   . ALA A 374 ? 0.2914 0.3804 0.3729 0.0184  0.0113  -0.0611 374 ALA A N   
2660  C CA  . ALA A 374 ? 0.2831 0.3754 0.3507 0.0253  0.0143  -0.0605 374 ALA A CA  
2661  C C   . ALA A 374 ? 0.3171 0.4286 0.3668 0.0293  0.0131  -0.0482 374 ALA A C   
2662  O O   . ALA A 374 ? 0.3539 0.4886 0.3962 0.0266  0.0083  -0.0525 374 ALA A O   
2663  C CB  . ALA A 374 ? 0.2833 0.3834 0.3538 0.0233  0.0161  -0.0825 374 ALA A CB  
2664  N N   . LEU A 375 ? 0.3018 0.4038 0.3469 0.0349  0.0162  -0.0323 375 LEU A N   
2665  C CA  . LEU A 375 ? 0.3166 0.4318 0.3524 0.0393  0.0152  -0.0186 375 LEU A CA  
2666  C C   . LEU A 375 ? 0.3446 0.4718 0.3654 0.0409  0.0170  -0.0185 375 LEU A C   
2667  O O   . LEU A 375 ? 0.3707 0.4874 0.3910 0.0426  0.0228  -0.0211 375 LEU A O   
2668  C CB  . LEU A 375 ? 0.3111 0.4106 0.3507 0.0434  0.0194  -0.0056 375 LEU A CB  
2669  C CG  . LEU A 375 ? 0.3118 0.4002 0.3614 0.0396  0.0211  -0.0057 375 LEU A CG  
2670  C CD1 . LEU A 375 ? 0.2743 0.3480 0.3220 0.0412  0.0266  0.0021  375 LEU A CD1 
2671  C CD2 . LEU A 375 ? 0.2837 0.3897 0.3448 0.0377  0.0180  -0.0058 375 LEU A CD2 
2672  N N   . GLY A 376 ? 0.3390 0.4895 0.3481 0.0396  0.0118  -0.0139 376 GLY A N   
2673  C CA  . GLY A 376 ? 0.3256 0.4916 0.3150 0.0376  0.0147  -0.0142 376 GLY A CA  
2674  C C   . GLY A 376 ? 0.3306 0.4996 0.3136 0.0418  0.0148  0.0096  376 GLY A C   
2675  O O   . GLY A 376 ? 0.3252 0.4787 0.3231 0.0475  0.0151  0.0221  376 GLY A O   
2676  N N   . ALA A 377 ? 0.3067 0.4956 0.2681 0.0377  0.0156  0.0154  377 ALA A N   
2677  C CA  . ALA A 377 ? 0.3094 0.4996 0.2656 0.0399  0.0166  0.0407  377 ALA A CA  
2678  C C   . ALA A 377 ? 0.3227 0.5148 0.2921 0.0453  0.0047  0.0625  377 ALA A C   
2679  O O   . ALA A 377 ? 0.3482 0.5255 0.3336 0.0511  0.0065  0.0795  377 ALA A O   
2680  C CB  . ALA A 377 ? 0.3235 0.5388 0.2493 0.0314  0.0199  0.0440  377 ALA A CB  
2681  N N   . HIS A 378 ? 0.3096 0.5197 0.2779 0.0433  -0.0075 0.0595  378 HIS A N   
2682  C CA  . HIS A 378 ? 0.2871 0.5040 0.2740 0.0488  -0.0203 0.0792  378 HIS A CA  
2683  C C   . HIS A 378 ? 0.2812 0.4735 0.3016 0.0573  -0.0148 0.0786  378 HIS A C   
2684  O O   . HIS A 378 ? 0.2882 0.4747 0.3308 0.0645  -0.0175 0.0967  378 HIS A O   
2685  C CB  . HIS A 378 ? 0.2995 0.5421 0.2837 0.0440  -0.0344 0.0705  378 HIS A CB  
2686  C CG  . HIS A 378 ? 0.3428 0.6031 0.3437 0.0485  -0.0517 0.0938  378 HIS A CG  
2687  N ND1 . HIS A 378 ? 0.3810 0.6652 0.3613 0.0449  -0.0651 0.1166  378 HIS A ND1 
2688  C CD2 . HIS A 378 ? 0.3460 0.6050 0.3856 0.0562  -0.0582 0.0990  378 HIS A CD2 
2689  C CE1 . HIS A 378 ? 0.3741 0.6698 0.3827 0.0516  -0.0817 0.1368  378 HIS A CE1 
2690  N NE2 . HIS A 378 ? 0.3321 0.6133 0.3795 0.0589  -0.0768 0.1247  378 HIS A NE2 
2691  N N   . HIS A 379 ? 0.2846 0.4622 0.3088 0.0557  -0.0066 0.0572  379 HIS A N   
2692  C CA  . HIS A 379 ? 0.2694 0.4257 0.3170 0.0605  0.0005  0.0540  379 HIS A CA  
2693  C C   . HIS A 379 ? 0.3188 0.4560 0.3709 0.0647  0.0088  0.0636  379 HIS A C   
2694  O O   . HIS A 379 ? 0.3473 0.4740 0.4221 0.0702  0.0115  0.0694  379 HIS A O   
2695  C CB  . HIS A 379 ? 0.2699 0.4144 0.3149 0.0557  0.0066  0.0335  379 HIS A CB  
2696  C CG  . HIS A 379 ? 0.2830 0.4088 0.3443 0.0576  0.0142  0.0306  379 HIS A CG  
2697  N ND1 . HIS A 379 ? 0.2959 0.4269 0.3767 0.0575  0.0140  0.0277  379 HIS A ND1 
2698  C CD2 . HIS A 379 ? 0.3100 0.4150 0.3698 0.0582  0.0227  0.0289  379 HIS A CD2 
2699  C CE1 . HIS A 379 ? 0.2626 0.3768 0.3498 0.0572  0.0239  0.0239  379 HIS A CE1 
2700  N NE2 . HIS A 379 ? 0.3052 0.4035 0.3784 0.0575  0.0279  0.0247  379 HIS A NE2 
2701  N N   . LEU A 380 ? 0.3445 0.4787 0.3780 0.0615  0.0137  0.0634  380 LEU A N   
2702  C CA  . LEU A 380 ? 0.3408 0.4573 0.3798 0.0634  0.0219  0.0696  380 LEU A CA  
2703  C C   . LEU A 380 ? 0.3198 0.4376 0.3696 0.0670  0.0195  0.0928  380 LEU A C   
2704  O O   . LEU A 380 ? 0.3373 0.4372 0.4042 0.0697  0.0254  0.0973  380 LEU A O   
2705  C CB  . LEU A 380 ? 0.3514 0.4682 0.3728 0.0584  0.0284  0.0615  380 LEU A CB  
2706  C CG  . LEU A 380 ? 0.3325 0.4439 0.3503 0.0558  0.0305  0.0405  380 LEU A CG  
2707  C CD1 . LEU A 380 ? 0.3282 0.4457 0.3354 0.0519  0.0368  0.0313  380 LEU A CD1 
2708  C CD2 . LEU A 380 ? 0.3468 0.4366 0.3781 0.0578  0.0332  0.0364  380 LEU A CD2 
2709  N N   . GLU A 381 ? 0.3379 0.4768 0.3783 0.0660  0.0099  0.1080  381 GLU A N   
2710  C CA  . GLU A 381 ? 0.3229 0.4648 0.3719 0.0683  0.0048  0.1364  381 GLU A CA  
2711  C C   . GLU A 381 ? 0.3339 0.4601 0.4238 0.0777  0.0032  0.1455  381 GLU A C   
2712  O O   . GLU A 381 ? 0.3392 0.4672 0.4482 0.0825  -0.0001 0.1359  381 GLU A O   
2713  C CB  . GLU A 381 ? 0.3118 0.4831 0.3413 0.0647  -0.0093 0.1516  381 GLU A CB  
2714  C CG  . GLU A 381 ? 0.3328 0.5211 0.3213 0.0538  -0.0048 0.1467  381 GLU A CG  
2715  C CD  . GLU A 381 ? 0.3699 0.5912 0.3314 0.0472  -0.0187 0.1510  381 GLU A CD  
2716  O OE1 . GLU A 381 ? 0.3903 0.6224 0.3674 0.0518  -0.0345 0.1609  381 GLU A OE1 
2717  O OE2 . GLU A 381 ? 0.3733 0.6119 0.2994 0.0369  -0.0134 0.1420  381 GLU A OE2 
2718  N N   . GLU A 382 ? 0.2772 0.3884 0.3833 0.0794  0.0073  0.1626  382 GLU A N   
2719  C CA  . GLU A 382 ? 0.3365 0.4289 0.4877 0.0881  0.0084  0.1695  382 GLU A CA  
2720  C C   . GLU A 382 ? 0.3193 0.3941 0.4859 0.0901  0.0198  0.1409  382 GLU A C   
2721  O O   . GLU A 382 ? 0.3709 0.4358 0.5744 0.0970  0.0221  0.1370  382 GLU A O   
2722  C CB  . GLU A 382 ? 0.3566 0.4629 0.5343 0.0961  -0.0066 0.1881  382 GLU A CB  
2723  C CG  . GLU A 382 ? 0.3737 0.4966 0.5372 0.0933  -0.0203 0.2229  382 GLU A CG  
2724  C CD  . GLU A 382 ? 0.4232 0.5284 0.5914 0.0901  -0.0138 0.2442  382 GLU A CD  
2725  O OE1 . GLU A 382 ? 0.4160 0.4948 0.6228 0.0954  -0.0054 0.2416  382 GLU A OE1 
2726  O OE2 . GLU A 382 ? 0.4776 0.5962 0.6112 0.0809  -0.0161 0.2628  382 GLU A OE2 
2727  N N   . ASN A 383 ? 0.3117 0.3832 0.4510 0.0833  0.0272  0.1212  383 ASN A N   
2728  C CA  . ASN A 383 ? 0.3197 0.3746 0.4657 0.0822  0.0371  0.0976  383 ASN A CA  
2729  C C   . ASN A 383 ? 0.3216 0.3636 0.4573 0.0762  0.0440  0.0933  383 ASN A C   
2730  O O   . ASN A 383 ? 0.3636 0.4139 0.4788 0.0718  0.0431  0.1008  383 ASN A O   
2731  C CB  . ASN A 383 ? 0.3187 0.3819 0.4456 0.0792  0.0369  0.0788  383 ASN A CB  
2732  C CG  . ASN A 383 ? 0.3357 0.4113 0.4807 0.0840  0.0325  0.0779  383 ASN A CG  
2733  O OD1 . ASN A 383 ? 0.3296 0.3985 0.5036 0.0883  0.0381  0.0717  383 ASN A OD1 
2734  N ND2 . ASN A 383 ? 0.3672 0.4624 0.4976 0.0824  0.0235  0.0810  383 ASN A ND2 
2735  N N   . LEU A 384 ? 0.3139 0.3381 0.4654 0.0751  0.0514  0.0797  384 LEU A N   
2736  C CA  . LEU A 384 ? 0.2989 0.3138 0.4417 0.0683  0.0559  0.0715  384 LEU A CA  
2737  C C   . LEU A 384 ? 0.3388 0.3548 0.4596 0.0639  0.0558  0.0516  384 LEU A C   
2738  O O   . LEU A 384 ? 0.3372 0.3483 0.4608 0.0634  0.0585  0.0376  384 LEU A O   
2739  C CB  . LEU A 384 ? 0.3259 0.3217 0.4979 0.0674  0.0622  0.0675  384 LEU A CB  
2740  C CG  . LEU A 384 ? 0.3424 0.3311 0.5083 0.0590  0.0650  0.0567  384 LEU A CG  
2741  C CD1 . LEU A 384 ? 0.3129 0.3086 0.4738 0.0557  0.0649  0.0737  384 LEU A CD1 
2742  C CD2 . LEU A 384 ? 0.3635 0.3336 0.5576 0.0561  0.0710  0.0439  384 LEU A CD2 
2743  N N   . VAL A 385 ? 0.3358 0.3593 0.4363 0.0603  0.0531  0.0512  385 VAL A N   
2744  C CA  . VAL A 385 ? 0.2796 0.3041 0.3624 0.0567  0.0502  0.0377  385 VAL A CA  
2745  C C   . VAL A 385 ? 0.2782 0.2982 0.3607 0.0517  0.0495  0.0322  385 VAL A C   
2746  O O   . VAL A 385 ? 0.2651 0.2920 0.3490 0.0511  0.0504  0.0377  385 VAL A O   
2747  C CB  . VAL A 385 ? 0.2346 0.2729 0.3022 0.0580  0.0462  0.0399  385 VAL A CB  
2748  C CG1 . VAL A 385 ? 0.2297 0.2653 0.2855 0.0547  0.0426  0.0285  385 VAL A CG1 
2749  C CG2 . VAL A 385 ? 0.2232 0.2699 0.2944 0.0623  0.0445  0.0462  385 VAL A CG2 
2750  N N   . VAL A 386 ? 0.2936 0.3045 0.3743 0.0472  0.0478  0.0207  386 VAL A N   
2751  C CA  . VAL A 386 ? 0.2821 0.2905 0.3664 0.0419  0.0440  0.0154  386 VAL A CA  
2752  C C   . VAL A 386 ? 0.3210 0.3327 0.3919 0.0398  0.0351  0.0115  386 VAL A C   
2753  O O   . VAL A 386 ? 0.3676 0.3759 0.4233 0.0369  0.0314  0.0071  386 VAL A O   
2754  C CB  . VAL A 386 ? 0.2781 0.2763 0.3692 0.0361  0.0452  0.0047  386 VAL A CB  
2755  C CG1 . VAL A 386 ? 0.3034 0.3027 0.3985 0.0297  0.0380  -0.0007 386 VAL A CG1 
2756  C CG2 . VAL A 386 ? 0.2864 0.2772 0.4004 0.0385  0.0540  0.0083  386 VAL A CG2 
2757  N N   . PHE A 387 ? 0.2910 0.3098 0.3706 0.0408  0.0321  0.0136  387 PHE A N   
2758  C CA  . PHE A 387 ? 0.2677 0.2884 0.3445 0.0402  0.0221  0.0114  387 PHE A CA  
2759  C C   . PHE A 387 ? 0.3260 0.3451 0.4107 0.0346  0.0130  0.0076  387 PHE A C   
2760  O O   . PHE A 387 ? 0.3329 0.3584 0.4386 0.0342  0.0133  0.0069  387 PHE A O   
2761  C CB  . PHE A 387 ? 0.2456 0.2766 0.3336 0.0452  0.0247  0.0124  387 PHE A CB  
2762  C CG  . PHE A 387 ? 0.2900 0.3252 0.3666 0.0488  0.0307  0.0139  387 PHE A CG  
2763  C CD1 . PHE A 387 ? 0.2750 0.3155 0.3483 0.0499  0.0395  0.0196  387 PHE A CD1 
2764  C CD2 . PHE A 387 ? 0.3041 0.3382 0.3754 0.0503  0.0261  0.0109  387 PHE A CD2 
2765  C CE1 . PHE A 387 ? 0.2693 0.3171 0.3316 0.0523  0.0419  0.0216  387 PHE A CE1 
2766  C CE2 . PHE A 387 ? 0.3194 0.3593 0.3817 0.0522  0.0304  0.0100  387 PHE A CE2 
2767  C CZ  . PHE A 387 ? 0.3078 0.3562 0.3642 0.0531  0.0376  0.0151  387 PHE A CZ  
2768  N N   . ASP A 388 ? 0.3515 0.3643 0.4185 0.0285  0.0054  0.0048  388 ASP A N   
2769  C CA  . ASP A 388 ? 0.3485 0.3624 0.4176 0.0209  -0.0061 0.0006  388 ASP A CA  
2770  C C   . ASP A 388 ? 0.3897 0.4073 0.4617 0.0212  -0.0228 0.0076  388 ASP A C   
2771  O O   . ASP A 388 ? 0.4496 0.4631 0.4993 0.0165  -0.0319 0.0123  388 ASP A O   
2772  C CB  . ASP A 388 ? 0.3853 0.3933 0.4306 0.0118  -0.0052 -0.0077 388 ASP A CB  
2773  C CG  . ASP A 388 ? 0.4463 0.4578 0.4915 0.0015  -0.0165 -0.0157 388 ASP A CG  
2774  O OD1 . ASP A 388 ? 0.4866 0.5056 0.5509 0.0018  -0.0287 -0.0120 388 ASP A OD1 
2775  O OD2 . ASP A 388 ? 0.4724 0.4809 0.5008 -0.0074 -0.0131 -0.0280 388 ASP A OD2 
2776  N N   . LEU A 389 ? 0.3222 0.3481 0.4246 0.0261  -0.0265 0.0090  389 LEU A N   
2777  C CA  . LEU A 389 ? 0.3147 0.3440 0.4325 0.0296  -0.0415 0.0158  389 LEU A CA  
2778  C C   . LEU A 389 ? 0.3651 0.3970 0.4783 0.0214  -0.0626 0.0197  389 LEU A C   
2779  O O   . LEU A 389 ? 0.4110 0.4418 0.5262 0.0218  -0.0795 0.0305  389 LEU A O   
2780  C CB  . LEU A 389 ? 0.3076 0.3482 0.4650 0.0373  -0.0362 0.0124  389 LEU A CB  
2781  C CG  . LEU A 389 ? 0.3247 0.3666 0.4791 0.0421  -0.0150 0.0082  389 LEU A CG  
2782  C CD1 . LEU A 389 ? 0.3490 0.4057 0.5369 0.0457  -0.0059 0.0028  389 LEU A CD1 
2783  C CD2 . LEU A 389 ? 0.2991 0.3343 0.4416 0.0469  -0.0140 0.0102  389 LEU A CD2 
2784  N N   . GLU A 390 ? 0.3462 0.3816 0.4543 0.0131  -0.0625 0.0113  390 GLU A N   
2785  C CA  . GLU A 390 ? 0.3678 0.4095 0.4685 0.0028  -0.0834 0.0121  390 GLU A CA  
2786  C C   . GLU A 390 ? 0.3947 0.4300 0.4487 -0.0069 -0.0915 0.0176  390 GLU A C   
2787  O O   . GLU A 390 ? 0.4117 0.4528 0.4543 -0.0144 -0.1139 0.0269  390 GLU A O   
2788  C CB  . GLU A 390 ? 0.4042 0.4515 0.5157 -0.0046 -0.0786 -0.0026 390 GLU A CB  
2789  C CG  . GLU A 390 ? 0.4999 0.5557 0.5997 -0.0180 -0.0984 -0.0074 390 GLU A CG  
2790  C CD  . GLU A 390 ? 0.5749 0.6309 0.6810 -0.0266 -0.0884 -0.0263 390 GLU A CD  
2791  O OE1 . GLU A 390 ? 0.6807 0.7324 0.7537 -0.0378 -0.0866 -0.0382 390 GLU A OE1 
2792  O OE2 . GLU A 390 ? 0.5075 0.5675 0.6529 -0.0228 -0.0802 -0.0301 390 GLU A OE2 
2793  N N   . ARG A 391 ? 0.4055 0.4310 0.4334 -0.0074 -0.0736 0.0132  391 ARG A N   
2794  C CA  . ARG A 391 ? 0.4404 0.4618 0.4247 -0.0175 -0.0762 0.0175  391 ARG A CA  
2795  C C   . ARG A 391 ? 0.4346 0.4471 0.4144 -0.0107 -0.0711 0.0306  391 ARG A C   
2796  O O   . ARG A 391 ? 0.4660 0.4749 0.4129 -0.0190 -0.0695 0.0358  391 ARG A O   
2797  C CB  . ARG A 391 ? 0.4672 0.4867 0.4278 -0.0256 -0.0585 -0.0010 391 ARG A CB  
2798  C CG  . ARG A 391 ? 0.5158 0.5420 0.4816 -0.0343 -0.0622 -0.0178 391 ARG A CG  
2799  C CD  . ARG A 391 ? 0.6103 0.6341 0.5539 -0.0442 -0.0459 -0.0393 391 ARG A CD  
2800  N NE  . ARG A 391 ? 0.7691 0.7949 0.6678 -0.0551 -0.0443 -0.0385 391 ARG A NE  
2801  C CZ  . ARG A 391 ? 0.8912 0.9193 0.7650 -0.0670 -0.0310 -0.0597 391 ARG A CZ  
2802  N NH1 . ARG A 391 ? 0.9011 0.9270 0.7942 -0.0687 -0.0199 -0.0838 391 ARG A NH1 
2803  N NH2 . ARG A 391 ? 0.9505 0.9832 0.7823 -0.0782 -0.0275 -0.0575 391 ARG A NH2 
2804  N N   . SER A 392 ? 0.3807 0.3911 0.3940 0.0026  -0.0673 0.0340  392 SER A N   
2805  C CA  . SER A 392 ? 0.3611 0.3635 0.3771 0.0091  -0.0620 0.0421  392 SER A CA  
2806  C C   . SER A 392 ? 0.3919 0.3896 0.3821 0.0059  -0.0440 0.0364  392 SER A C   
2807  O O   . SER A 392 ? 0.4024 0.3949 0.3725 0.0002  -0.0448 0.0451  392 SER A O   
2808  C CB  . SER A 392 ? 0.3664 0.3637 0.3794 0.0058  -0.0819 0.0612  392 SER A CB  
2809  O OG  . SER A 392 ? 0.3543 0.3427 0.3855 0.0138  -0.0785 0.0672  392 SER A OG  
2810  N N   . ARG A 393 ? 0.3785 0.3789 0.3735 0.0094  -0.0280 0.0233  393 ARG A N   
2811  C CA  . ARG A 393 ? 0.3742 0.3728 0.3543 0.0080  -0.0117 0.0172  393 ARG A CA  
2812  C C   . ARG A 393 ? 0.3487 0.3495 0.3498 0.0180  0.0012  0.0111  393 ARG A C   
2813  O O   . ARG A 393 ? 0.3249 0.3287 0.3454 0.0224  0.0005  0.0092  393 ARG A O   
2814  C CB  . ARG A 393 ? 0.3943 0.3945 0.3497 -0.0035 -0.0069 0.0072  393 ARG A CB  
2815  C CG  . ARG A 393 ? 0.4032 0.4055 0.3705 -0.0043 -0.0047 -0.0058 393 ARG A CG  
2816  C CD  . ARG A 393 ? 0.4168 0.4213 0.3588 -0.0177 -0.0012 -0.0196 393 ARG A CD  
2817  N NE  . ARG A 393 ? 0.4282 0.4325 0.3866 -0.0191 0.0028  -0.0353 393 ARG A NE  
2818  C CZ  . ARG A 393 ? 0.4428 0.4477 0.3904 -0.0288 0.0116  -0.0550 393 ARG A CZ  
2819  N NH1 . ARG A 393 ? 0.4724 0.4812 0.3888 -0.0387 0.0188  -0.0622 393 ARG A NH1 
2820  N NH2 . ARG A 393 ? 0.4457 0.4480 0.4155 -0.0298 0.0145  -0.0691 393 ARG A NH2 
2821  N N   . VAL A 394 ? 0.3597 0.3607 0.3573 0.0204  0.0125  0.0095  394 VAL A N   
2822  C CA  . VAL A 394 ? 0.3720 0.3767 0.3859 0.0286  0.0229  0.0071  394 VAL A CA  
2823  C C   . VAL A 394 ? 0.3778 0.3817 0.3902 0.0264  0.0340  -0.0012 394 VAL A C   
2824  O O   . VAL A 394 ? 0.3767 0.3807 0.3747 0.0204  0.0383  -0.0054 394 VAL A O   
2825  C CB  . VAL A 394 ? 0.3891 0.3980 0.4067 0.0340  0.0251  0.0114  394 VAL A CB  
2826  C CG1 . VAL A 394 ? 0.4064 0.4221 0.4368 0.0411  0.0326  0.0119  394 VAL A CG1 
2827  C CG2 . VAL A 394 ? 0.3981 0.4070 0.4226 0.0365  0.0168  0.0150  394 VAL A CG2 
2828  N N   . GLY A 395 ? 0.3640 0.3670 0.3945 0.0307  0.0397  -0.0037 395 GLY A N   
2829  C CA  . GLY A 395 ? 0.3575 0.3581 0.3978 0.0310  0.0506  -0.0122 395 GLY A CA  
2830  C C   . GLY A 395 ? 0.3233 0.3275 0.3844 0.0408  0.0558  -0.0040 395 GLY A C   
2831  O O   . GLY A 395 ? 0.2814 0.2893 0.3479 0.0458  0.0518  0.0070  395 GLY A O   
2832  N N   . PHE A 396 ? 0.3467 0.3520 0.4201 0.0432  0.0643  -0.0094 396 PHE A N   
2833  C CA  . PHE A 396 ? 0.3564 0.3668 0.4535 0.0529  0.0659  0.0011  396 PHE A CA  
2834  C C   . PHE A 396 ? 0.3494 0.3555 0.4756 0.0562  0.0759  -0.0076 396 PHE A C   
2835  O O   . PHE A 396 ? 0.3802 0.3832 0.5036 0.0501  0.0845  -0.0258 396 PHE A O   
2836  C CB  . PHE A 396 ? 0.3270 0.3504 0.4166 0.0555  0.0620  0.0077  396 PHE A CB  
2837  C CG  . PHE A 396 ? 0.3320 0.3590 0.4118 0.0495  0.0673  -0.0032 396 PHE A CG  
2838  C CD1 . PHE A 396 ? 0.3362 0.3684 0.4366 0.0514  0.0770  -0.0111 396 PHE A CD1 
2839  C CD2 . PHE A 396 ? 0.3328 0.3587 0.3862 0.0416  0.0631  -0.0045 396 PHE A CD2 
2840  C CE1 . PHE A 396 ? 0.3296 0.3675 0.4205 0.0439  0.0846  -0.0214 396 PHE A CE1 
2841  C CE2 . PHE A 396 ? 0.3123 0.3414 0.3548 0.0339  0.0688  -0.0111 396 PHE A CE2 
2842  C CZ  . PHE A 396 ? 0.3035 0.3396 0.3627 0.0342  0.0806  -0.0201 396 PHE A CZ  
2843  N N   . ASN A 397 ? 0.3379 0.3445 0.4930 0.0655  0.0749  0.0054  397 ASN A N   
2844  C CA  . ASN A 397 ? 0.3441 0.3456 0.5377 0.0709  0.0834  -0.0014 397 ASN A CA  
2845  C C   . ASN A 397 ? 0.3357 0.3494 0.5370 0.0721  0.0901  -0.0125 397 ASN A C   
2846  O O   . ASN A 397 ? 0.3424 0.3705 0.5369 0.0746  0.0838  -0.0026 397 ASN A O   
2847  C CB  . ASN A 397 ? 0.3461 0.3454 0.5711 0.0808  0.0775  0.0213  397 ASN A CB  
2848  C CG  . ASN A 397 ? 0.3025 0.3184 0.5140 0.0847  0.0656  0.0426  397 ASN A CG  
2849  O OD1 . ASN A 397 ? 0.2945 0.3153 0.4740 0.0800  0.0599  0.0485  397 ASN A OD1 
2850  N ND2 . ASN A 397 ? 0.3244 0.3506 0.5636 0.0933  0.0615  0.0529  397 ASN A ND2 
2851  N N   . SER A 398 ? 0.3434 0.3526 0.5599 0.0689  0.1042  -0.0354 398 SER A N   
2852  C CA  . SER A 398 ? 0.3800 0.4026 0.6053 0.0676  0.1153  -0.0502 398 SER A CA  
2853  C C   . SER A 398 ? 0.3831 0.4122 0.6649 0.0809  0.1183  -0.0467 398 SER A C   
2854  O O   . SER A 398 ? 0.3872 0.4310 0.6824 0.0808  0.1249  -0.0552 398 SER A O   
2855  C CB  . SER A 398 ? 0.3861 0.4052 0.5968 0.0555  0.1314  -0.0794 398 SER A CB  
2856  O OG  . SER A 398 ? 0.4074 0.4120 0.6459 0.0569  0.1390  -0.0940 398 SER A OG  
2857  N N   . ASN A 399 ? 0.3559 0.3734 0.6669 0.0896  0.1104  -0.0316 399 ASN A N   
2858  C CA  . ASN A 399 ? 0.3719 0.3943 0.7223 0.0985  0.1021  -0.0177 399 ASN A CA  
2859  C C   . ASN A 399 ? 0.3883 0.4113 0.7370 0.1056  0.0843  0.0158  399 ASN A C   
2860  O O   . ASN A 399 ? 0.4096 0.4242 0.7347 0.1034  0.0820  0.0240  399 ASN A O   
2861  C CB  . ASN A 399 ? 0.3419 0.3491 0.7295 0.0981  0.1098  -0.0310 399 ASN A CB  
2862  C CG  . ASN A 399 ? 0.3490 0.3580 0.7331 0.0887  0.1286  -0.0658 399 ASN A CG  
2863  O OD1 . ASN A 399 ? 0.3426 0.3669 0.7365 0.0882  0.1350  -0.0759 399 ASN A OD1 
2864  N ND2 . ASN A 399 ? 0.3793 0.3745 0.7489 0.0798  0.1376  -0.0846 399 ASN A ND2 
2865  N N   . SER A 400 ? 0.3827 0.4172 0.7546 0.1130  0.0716  0.0352  400 SER A N   
2866  C CA  . SER A 400 ? 0.3534 0.3925 0.7177 0.1173  0.0541  0.0680  400 SER A CA  
2867  C C   . SER A 400 ? 0.3401 0.3573 0.7135 0.1163  0.0533  0.0808  400 SER A C   
2868  O O   . SER A 400 ? 0.3483 0.3491 0.7517 0.1154  0.0614  0.0689  400 SER A O   
2869  C CB  . SER A 400 ? 0.3087 0.3660 0.6971 0.1239  0.0393  0.0853  400 SER A CB  
2870  O OG  . SER A 400 ? 0.3474 0.3936 0.7794 0.1278  0.0394  0.0872  400 SER A OG  
2871  N N   . LEU A 401 ? 0.3546 0.3732 0.7037 0.1152  0.0444  0.1048  401 LEU A N   
2872  C CA  . LEU A 401 ? 0.4029 0.4026 0.7616 0.1124  0.0441  0.1203  401 LEU A CA  
2873  C C   . LEU A 401 ? 0.3611 0.3559 0.7613 0.1161  0.0370  0.1354  401 LEU A C   
2874  O O   . LEU A 401 ? 0.3591 0.3343 0.7885 0.1140  0.0428  0.1336  401 LEU A O   
2875  C CB  . LEU A 401 ? 0.4182 0.4254 0.7425 0.1096  0.0361  0.1467  401 LEU A CB  
2876  C CG  . LEU A 401 ? 0.3840 0.3945 0.6620 0.1015  0.0420  0.1324  401 LEU A CG  
2877  C CD1 . LEU A 401 ? 0.3803 0.3960 0.6307 0.0951  0.0371  0.1559  401 LEU A CD1 
2878  C CD2 . LEU A 401 ? 0.3707 0.3616 0.6542 0.0964  0.0559  0.1043  401 LEU A CD2 
2879  N N   . LYS A 402 ? 0.3556 0.3701 0.7607 0.1214  0.0239  0.1495  402 LYS A N   
2880  C CA  . LYS A 402 ? 0.3988 0.4138 0.8432 0.1261  0.0133  0.1682  402 LYS A CA  
2881  C C   . LYS A 402 ? 0.3666 0.3682 0.8594 0.1292  0.0250  0.1434  402 LYS A C   
2882  O O   . LYS A 402 ? 0.4054 0.3970 0.9394 0.1318  0.0218  0.1547  402 LYS A O   
2883  C CB  . LYS A 402 ? 0.4354 0.4783 0.8693 0.1301  -0.0044 0.1848  402 LYS A CB  
2884  C CG  . LYS A 402 ? 0.5137 0.5638 0.9853 0.1358  -0.0191 0.2047  402 LYS A CG  
2885  C CD  . LYS A 402 ? 0.5795 0.6608 1.0255 0.1366  -0.0368 0.2172  402 LYS A CD  
2886  C CE  . LYS A 402 ? 0.6548 0.7502 1.1357 0.1427  -0.0546 0.2351  402 LYS A CE  
2887  N NZ  . LYS A 402 ? 0.6849 0.8070 1.1272 0.1386  -0.0761 0.2606  402 LYS A NZ  
2888  N N   . SER A 403 ? 0.3555 0.3579 0.8432 0.1279  0.0395  0.1096  403 SER A N   
2889  C CA  . SER A 403 ? 0.3950 0.3860 0.9225 0.1280  0.0541  0.0818  403 SER A CA  
2890  C C   . SER A 403 ? 0.4718 0.4376 1.0124 0.1220  0.0650  0.0718  403 SER A C   
2891  O O   . SER A 403 ? 0.5378 0.4932 1.1178 0.1213  0.0757  0.0516  403 SER A O   
2892  C CB  . SER A 403 ? 0.3680 0.3696 0.8797 0.1252  0.0679  0.0485  403 SER A CB  
2893  O OG  . SER A 403 ? 0.3459 0.3371 0.8249 0.1168  0.0808  0.0277  403 SER A OG  
2894  N N   . TYR A 404 ? 0.4485 0.4059 0.9582 0.1168  0.0632  0.0836  404 TYR A N   
2895  C CA  . TYR A 404 ? 0.4291 0.3642 0.9540 0.1104  0.0713  0.0776  404 TYR A CA  
2896  C C   . TYR A 404 ? 0.4507 0.3781 1.0017 0.1117  0.0605  0.1123  404 TYR A C   
2897  O O   . TYR A 404 ? 0.4637 0.3735 1.0348 0.1063  0.0658  0.1122  404 TYR A O   
2898  C CB  . TYR A 404 ? 0.4252 0.3558 0.9063 0.1029  0.0769  0.0685  404 TYR A CB  
2899  C CG  . TYR A 404 ? 0.4361 0.3732 0.8900 0.0996  0.0880  0.0347  404 TYR A CG  
2900  C CD1 . TYR A 404 ? 0.4474 0.3745 0.9128 0.0928  0.1025  0.0000  404 TYR A CD1 
2901  C CD2 . TYR A 404 ? 0.4335 0.3886 0.8494 0.1018  0.0840  0.0374  404 TYR A CD2 
2902  C CE1 . TYR A 404 ? 0.4593 0.3948 0.8944 0.0875  0.1126  -0.0292 404 TYR A CE1 
2903  C CE2 . TYR A 404 ? 0.4411 0.4031 0.8315 0.0973  0.0944  0.0091  404 TYR A CE2 
2904  C CZ  . TYR A 404 ? 0.4578 0.4103 0.8557 0.0898  0.1087  -0.0233 404 TYR A CZ  
2905  O OH  . TYR A 404 ? 0.4429 0.4045 0.8100 0.0831  0.1191  -0.0496 404 TYR A OH  
2906  N N   . GLY A 405 ? 0.4674 0.4097 1.0179 0.1178  0.0447  0.1422  405 GLY A N   
2907  C CA  . GLY A 405 ? 0.5021 0.4421 1.0666 0.1178  0.0320  0.1805  405 GLY A CA  
2908  C C   . GLY A 405 ? 0.5380 0.4811 1.0562 0.1109  0.0282  0.2020  405 GLY A C   
2909  O O   . GLY A 405 ? 0.5569 0.4949 1.0829 0.1072  0.0226  0.2305  405 GLY A O   
2910  N N   . LYS A 406 ? 0.4911 0.4440 0.9626 0.1090  0.0318  0.1890  406 LYS A N   
2911  C CA  . LYS A 406 ? 0.4314 0.3879 0.8600 0.1021  0.0317  0.2034  406 LYS A CA  
2912  C C   . LYS A 406 ? 0.4361 0.4186 0.8210 0.1035  0.0203  0.2193  406 LYS A C   
2913  O O   . LYS A 406 ? 0.3679 0.3651 0.7513 0.1096  0.0145  0.2108  406 LYS A O   
2914  C CB  . LYS A 406 ? 0.4125 0.3579 0.8249 0.0975  0.0465  0.1735  406 LYS A CB  
2915  C CG  . LYS A 406 ? 0.4655 0.3886 0.9155 0.0945  0.0585  0.1483  406 LYS A CG  
2916  C CD  . LYS A 406 ? 0.5511 0.4599 1.0261 0.0886  0.0591  0.1672  406 LYS A CD  
2917  C CE  . LYS A 406 ? 0.6255 0.5147 1.1467 0.0862  0.0695  0.1415  406 LYS A CE  
2918  N NZ  . LYS A 406 ? 0.6342 0.5195 1.1404 0.0829  0.0810  0.1008  406 LYS A NZ  
2919  N N   . THR A 407 ? 0.4493 0.4388 0.7988 0.0964  0.0185  0.2396  407 THR A N   
2920  C CA  . THR A 407 ? 0.4369 0.4519 0.7368 0.0947  0.0114  0.2489  407 THR A CA  
2921  C C   . THR A 407 ? 0.4197 0.4317 0.6876 0.0878  0.0230  0.2435  407 THR A C   
2922  O O   . THR A 407 ? 0.4132 0.4041 0.6984 0.0837  0.0342  0.2363  407 THR A O   
2923  C CB  . THR A 407 ? 0.4542 0.4893 0.7361 0.0907  -0.0042 0.2833  407 THR A CB  
2924  O OG1 . THR A 407 ? 0.4735 0.5023 0.7469 0.0809  0.0001  0.3044  407 THR A OG1 
2925  C CG2 . THR A 407 ? 0.4246 0.4595 0.7459 0.0974  -0.0163 0.2928  407 THR A CG2 
2926  N N   . CYS A 408 ? 0.3756 0.4100 0.5971 0.0845  0.0208  0.2414  408 CYS A N   
2927  C CA  . CYS A 408 ? 0.3762 0.4126 0.5644 0.0736  0.0324  0.2272  408 CYS A CA  
2928  C C   . CYS A 408 ? 0.4019 0.4384 0.5830 0.0640  0.0361  0.2560  408 CYS A C   
2929  O O   . CYS A 408 ? 0.3999 0.4330 0.5707 0.0554  0.0481  0.2456  408 CYS A O   
2930  C CB  . CYS A 408 ? 0.3493 0.4104 0.4923 0.0701  0.0303  0.2096  408 CYS A CB  
2931  S SG  . CYS A 408 ? 0.3975 0.4508 0.5413 0.0736  0.0358  0.1681  408 CYS A SG  
2932  N N   . SER A 409 ? 0.4471 0.4892 0.6351 0.0639  0.0257  0.2897  409 SER A N   
2933  C CA  . SER A 409 ? 0.4881 0.5320 0.6676 0.0517  0.0295  0.3129  409 SER A CA  
2934  C C   . SER A 409 ? 0.4968 0.5112 0.7236 0.0506  0.0370  0.3139  409 SER A C   
2935  O O   . SER A 409 ? 0.4940 0.5050 0.7176 0.0398  0.0467  0.3231  409 SER A O   
2936  C CB  . SER A 409 ? 0.5330 0.5960 0.6980 0.0486  0.0136  0.3403  409 SER A CB  
2937  O OG  . SER A 409 ? 0.5614 0.6545 0.6809 0.0468  0.0059  0.3374  409 SER A OG  
2938  N N   . ASN A 410 ? 0.4977 0.4927 0.7698 0.0607  0.0336  0.3020  410 ASN A N   
2939  C CA  . ASN A 410 ? 0.4924 0.4615 0.8118 0.0590  0.0398  0.3009  410 ASN A CA  
2940  C C   . ASN A 410 ? 0.4679 0.4146 0.8159 0.0622  0.0512  0.2654  410 ASN A C   
2941  O O   . ASN A 410 ? 0.4835 0.4099 0.8718 0.0598  0.0568  0.2589  410 ASN A O   
2942  C CB  . ASN A 410 ? 0.5309 0.4963 0.8861 0.0646  0.0273  0.3192  410 ASN A CB  
2943  C CG  . ASN A 410 ? 0.5389 0.5056 0.9139 0.0770  0.0203  0.3017  410 ASN A CG  
2944  O OD1 . ASN A 410 ? 0.5428 0.5010 0.9260 0.0817  0.0284  0.2696  410 ASN A OD1 
2945  N ND2 . ASN A 410 ? 0.5600 0.5395 0.9407 0.0813  0.0048  0.3228  410 ASN A ND2 
2946  N N   . LEU A 411 ? 0.4520 0.4035 0.7775 0.0662  0.0545  0.2420  411 LEU A N   
2947  C CA  . LEU A 411 ? 0.4483 0.3812 0.7918 0.0672  0.0646  0.2069  411 LEU A CA  
2948  C C   . LEU A 411 ? 0.4979 0.4178 0.8497 0.0555  0.0751  0.2049  411 LEU A C   
2949  O O   . LEU A 411 ? 0.5226 0.4235 0.9067 0.0525  0.0814  0.1829  411 LEU A O   
2950  C CB  . LEU A 411 ? 0.4223 0.3702 0.7291 0.0703  0.0642  0.1822  411 LEU A CB  
2951  C CG  . LEU A 411 ? 0.3945 0.3317 0.7087 0.0698  0.0712  0.1422  411 LEU A CG  
2952  C CD1 . LEU A 411 ? 0.4083 0.3289 0.7690 0.0784  0.0729  0.1330  411 LEU A CD1 
2953  C CD2 . LEU A 411 ? 0.3680 0.3249 0.6383 0.0699  0.0686  0.1223  411 LEU A CD2 
2954  N N   . PHE A 412 ? 0.4927 0.4268 0.8152 0.0469  0.0774  0.2262  412 PHE A N   
2955  C CA  . PHE A 412 ? 0.4695 0.3979 0.8005 0.0337  0.0877  0.2276  412 PHE A CA  
2956  C C   . PHE A 412 ? 0.4739 0.4124 0.8003 0.0266  0.0865  0.2625  412 PHE A C   
2957  O O   . PHE A 412 ? 0.5139 0.4700 0.8144 0.0296  0.0777  0.2840  412 PHE A O   
2958  C CB  . PHE A 412 ? 0.4467 0.3967 0.7393 0.0271  0.0924  0.2038  412 PHE A CB  
2959  C CG  . PHE A 412 ? 0.3981 0.3483 0.6810 0.0330  0.0888  0.1670  412 PHE A CG  
2960  C CD1 . PHE A 412 ? 0.4016 0.3344 0.7106 0.0304  0.0916  0.1404  412 PHE A CD1 
2961  C CD2 . PHE A 412 ? 0.3492 0.3169 0.5971 0.0399  0.0824  0.1595  412 PHE A CD2 
2962  C CE1 . PHE A 412 ? 0.3466 0.2812 0.6415 0.0338  0.0880  0.1096  412 PHE A CE1 
2963  C CE2 . PHE A 412 ? 0.3475 0.3147 0.5863 0.0438  0.0795  0.1295  412 PHE A CE2 
2964  C CZ  . PHE A 412 ? 0.3486 0.2998 0.6085 0.0406  0.0823  0.1059  412 PHE A CZ  
2965  N N   . ASP A 413 ? 0.4588 0.3875 0.8091 0.0162  0.0942  0.2664  413 ASP A N   
2966  C CA  . ASP A 413 ? 0.5011 0.4389 0.8440 0.0075  0.0944  0.2984  413 ASP A CA  
2967  C C   . ASP A 413 ? 0.5163 0.4817 0.8113 -0.0027 0.1026  0.3048  413 ASP A C   
2968  O O   . ASP A 413 ? 0.5123 0.4808 0.8097 -0.0113 0.1149  0.2888  413 ASP A O   
2969  C CB  . ASP A 413 ? 0.5326 0.4503 0.9202 -0.0005 0.1009  0.2985  413 ASP A CB  
2970  C CG  . ASP A 413 ? 0.6050 0.5261 0.9916 -0.0084 0.0994  0.3347  413 ASP A CG  
2971  O OD1 . ASP A 413 ? 0.6315 0.5758 0.9730 -0.0145 0.0994  0.3552  413 ASP A OD1 
2972  O OD2 . ASP A 413 ? 0.6501 0.5512 1.0808 -0.0093 0.0984  0.3418  413 ASP A OD2 
2973  N N   . LEU A 414 ? 0.5449 0.5330 0.7984 -0.0026 0.0961  0.3251  414 LEU A N   
2974  C CA  . LEU A 414 ? 0.5440 0.5625 0.7497 -0.0131 0.1055  0.3260  414 LEU A CA  
2975  C C   . LEU A 414 ? 0.6439 0.6730 0.8326 -0.0265 0.1088  0.3533  414 LEU A C   
2976  O O   . LEU A 414 ? 0.6582 0.7152 0.8001 -0.0352 0.1137  0.3578  414 LEU A O   
2977  C CB  . LEU A 414 ? 0.5010 0.5426 0.6637 -0.0062 0.0975  0.3222  414 LEU A CB  
2978  C CG  . LEU A 414 ? 0.4613 0.4946 0.6331 0.0064  0.0947  0.2973  414 LEU A CG  
2979  C CD1 . LEU A 414 ? 0.4441 0.5013 0.5746 0.0126  0.0847  0.2919  414 LEU A CD1 
2980  C CD2 . LEU A 414 ? 0.4665 0.5000 0.6453 0.0024  0.1066  0.2631  414 LEU A CD2 
2981  N N   . ASN A 415 ? 0.7431 0.7499 0.9686 -0.0283 0.1058  0.3708  415 ASN A N   
2982  C CA  . ASN A 415 ? 0.8375 0.8495 1.0517 -0.0426 0.1105  0.3983  415 ASN A CA  
2983  C C   . ASN A 415 ? 0.8578 0.8672 1.0884 -0.0564 0.1296  0.3883  415 ASN A C   
2984  O O   . ASN A 415 ? 0.8307 0.8178 1.1095 -0.0537 0.1328  0.3720  415 ASN A O   
2985  C CB  . ASN A 415 ? 0.9181 0.9079 1.1678 -0.0378 0.0972  0.4247  415 ASN A CB  
2986  C CG  . ASN A 415 ? 0.9669 0.9608 1.2097 -0.0243 0.0774  0.4344  415 ASN A CG  
2987  O OD1 . ASN A 415 ? 1.0139 1.0334 1.2085 -0.0251 0.0712  0.4398  415 ASN A OD1 
2988  N ND2 . ASN A 415 ? 0.9642 0.9344 1.2586 -0.0123 0.0678  0.4337  415 ASN A ND2 
2989  N N   . ASN A 416 ? 0.9219 0.9562 1.1128 -0.0719 0.1422  0.3959  416 ASN A N   
2990  C CA  . ASN A 416 ? 1.0145 1.0472 1.2109 -0.0894 0.1548  0.4141  416 ASN A CA  
2991  C C   . ASN A 416 ? 1.0019 1.0029 1.2564 -0.0907 0.1541  0.4231  416 ASN A C   
2992  O O   . ASN A 416 ? 1.0233 1.0083 1.2919 -0.0895 0.1440  0.4513  416 ASN A O   
2993  C CB  . ASN A 416 ? 1.1503 1.1989 1.2977 -0.0972 0.1497  0.4459  416 ASN A CB  
2994  C CG  . ASN A 416 ? 1.2028 1.2875 1.2893 -0.1018 0.1565  0.4315  416 ASN A CG  
2995  O OD1 . ASN A 416 ? 1.2876 1.3867 1.3329 -0.1003 0.1450  0.4454  416 ASN A OD1 
2996  N ND2 . ASN A 416 ? 1.1506 1.2516 1.2345 -0.1091 0.1763  0.4023  416 ASN A ND2 
2997  N N   . LYS B 11  ? 0.8125 0.9734 1.4909 -0.2008 -0.0999 -0.0498 11  LYS B N   
2998  C CA  . LYS B 11  ? 0.7870 0.9385 1.3981 -0.1879 -0.1212 -0.0611 11  LYS B CA  
2999  C C   . LYS B 11  ? 0.6946 0.8844 1.3009 -0.1714 -0.1305 -0.0560 11  LYS B C   
3000  O O   . LYS B 11  ? 0.7003 0.9168 1.3348 -0.1721 -0.1531 -0.0620 11  LYS B O   
3001  C CB  . LYS B 11  ? 0.8498 0.9727 1.4252 -0.1945 -0.1593 -0.0878 11  LYS B CB  
3002  C CG  . LYS B 11  ? 0.8460 0.9542 1.3473 -0.1773 -0.1780 -0.0982 11  LYS B CG  
3003  C CD  . LYS B 11  ? 0.8606 0.9140 1.3039 -0.1795 -0.1871 -0.1144 11  LYS B CD  
3004  C CE  . LYS B 11  ? 0.7914 0.8185 1.2276 -0.1819 -0.1520 -0.1014 11  LYS B CE  
3005  N NZ  . LYS B 11  ? 0.7597 0.7357 1.1267 -0.1750 -0.1580 -0.1137 11  LYS B NZ  
3006  N N   . PRO B 12  ? 0.5633 0.7553 1.1356 -0.1564 -0.1118 -0.0440 12  PRO B N   
3007  C CA  . PRO B 12  ? 0.5110 0.7357 1.0771 -0.1395 -0.1112 -0.0353 12  PRO B CA  
3008  C C   . PRO B 12  ? 0.5521 0.7822 1.0788 -0.1285 -0.1478 -0.0517 12  PRO B C   
3009  O O   . PRO B 12  ? 0.5988 0.7994 1.0772 -0.1275 -0.1694 -0.0687 12  PRO B O   
3010  C CB  . PRO B 12  ? 0.3768 0.5916 0.9114 -0.1291 -0.0818 -0.0210 12  PRO B CB  
3011  C CG  . PRO B 12  ? 0.3565 0.5333 0.8614 -0.1367 -0.0836 -0.0302 12  PRO B CG  
3012  C CD  . PRO B 12  ? 0.4461 0.6067 0.9823 -0.1546 -0.0904 -0.0388 12  PRO B CD  
3013  N N   . ASN B 13  ? 0.5142 0.7788 1.0584 -0.1180 -0.1516 -0.0451 13  ASN B N   
3014  C CA  . ASN B 13  ? 0.4925 0.7634 0.9988 -0.1034 -0.1802 -0.0559 13  ASN B CA  
3015  C C   . ASN B 13  ? 0.4624 0.7420 0.9357 -0.0844 -0.1645 -0.0448 13  ASN B C   
3016  O O   . ASN B 13  ? 0.4749 0.7574 0.9118 -0.0687 -0.1819 -0.0505 13  ASN B O   
3017  C CB  . ASN B 13  ? 0.5007 0.8034 1.0493 -0.1039 -0.1995 -0.0577 13  ASN B CB  
3018  C CG  . ASN B 13  ? 0.6031 0.8898 1.1471 -0.1135 -0.2353 -0.0788 13  ASN B CG  
3019  O OD1 . ASN B 13  ? 0.6633 0.9284 1.1490 -0.1026 -0.2601 -0.0931 13  ASN B OD1 
3020  N ND2 . ASN B 13  ? 0.6322 0.9257 1.2350 -0.1327 -0.2373 -0.0809 13  ASN B ND2 
3021  N N   . LEU B 14  ? 0.3788 0.6607 0.8636 -0.0845 -0.1305 -0.0283 14  LEU B N   
3022  C CA  . LEU B 14  ? 0.3234 0.6123 0.7795 -0.0672 -0.1141 -0.0176 14  LEU B CA  
3023  C C   . LEU B 14  ? 0.2655 0.5335 0.7016 -0.0677 -0.0788 -0.0046 14  LEU B C   
3024  O O   . LEU B 14  ? 0.2243 0.4963 0.7045 -0.0779 -0.0572 0.0071  14  LEU B O   
3025  C CB  . LEU B 14  ? 0.3105 0.6327 0.7946 -0.0563 -0.1046 -0.0047 14  LEU B CB  
3026  C CG  . LEU B 14  ? 0.2814 0.6103 0.7320 -0.0357 -0.0945 0.0032  14  LEU B CG  
3027  C CD1 . LEU B 14  ? 0.2726 0.5940 0.6775 -0.0232 -0.1242 -0.0117 14  LEU B CD1 
3028  C CD2 . LEU B 14  ? 0.3031 0.6589 0.7866 -0.0269 -0.0747 0.0195  14  LEU B CD2 
3029  N N   . LEU B 15  ? 0.2346 0.4775 0.6006 -0.0550 -0.0719 -0.0060 15  LEU B N   
3030  C CA  . LEU B 15  ? 0.2144 0.4338 0.5457 -0.0516 -0.0436 0.0040  15  LEU B CA  
3031  C C   . LEU B 15  ? 0.2135 0.4342 0.5085 -0.0351 -0.0279 0.0125  15  LEU B C   
3032  O O   . LEU B 15  ? 0.2104 0.4370 0.4842 -0.0253 -0.0401 0.0066  15  LEU B O   
3033  C CB  . LEU B 15  ? 0.2035 0.3896 0.4891 -0.0535 -0.0521 -0.0070 15  LEU B CB  
3034  C CG  . LEU B 15  ? 0.2378 0.4138 0.5477 -0.0690 -0.0715 -0.0195 15  LEU B CG  
3035  C CD1 . LEU B 15  ? 0.2519 0.3914 0.5080 -0.0663 -0.0786 -0.0301 15  LEU B CD1 
3036  C CD2 . LEU B 15  ? 0.2314 0.4104 0.5937 -0.0833 -0.0534 -0.0094 15  LEU B CD2 
3037  N N   . VAL B 16  ? 0.2383 0.4482 0.5199 -0.0309 -0.0010 0.0255  16  VAL B N   
3038  C CA  . VAL B 16  ? 0.2008 0.4089 0.4494 -0.0163 0.0134  0.0323  16  VAL B CA  
3039  C C   . VAL B 16  ? 0.1919 0.3721 0.3904 -0.0109 0.0247  0.0339  16  VAL B C   
3040  O O   . VAL B 16  ? 0.2454 0.4115 0.4427 -0.0131 0.0382  0.0412  16  VAL B O   
3041  C CB  . VAL B 16  ? 0.2688 0.4934 0.5510 -0.0110 0.0363  0.0488  16  VAL B CB  
3042  C CG1 . VAL B 16  ? 0.2325 0.4491 0.4742 0.0047  0.0500  0.0537  16  VAL B CG1 
3043  C CG2 . VAL B 16  ? 0.1711 0.4302 0.5145 -0.0159 0.0237  0.0488  16  VAL B CG2 
3044  N N   . LEU B 17  ? 0.1996 0.3722 0.3588 -0.0028 0.0190  0.0274  17  LEU B N   
3045  C CA  . LEU B 17  ? 0.2646 0.4155 0.3811 0.0027  0.0248  0.0271  17  LEU B CA  
3046  C C   . LEU B 17  ? 0.2809 0.4276 0.3723 0.0133  0.0352  0.0301  17  LEU B C   
3047  O O   . LEU B 17  ? 0.3019 0.4523 0.3836 0.0170  0.0289  0.0238  17  LEU B O   
3048  C CB  . LEU B 17  ? 0.2614 0.4038 0.3579 0.0010  0.0086  0.0155  17  LEU B CB  
3049  C CG  . LEU B 17  ? 0.3030 0.4291 0.3664 0.0055  0.0093  0.0138  17  LEU B CG  
3050  C CD1 . LEU B 17  ? 0.3287 0.4422 0.3873 0.0045  0.0153  0.0203  17  LEU B CD1 
3051  C CD2 . LEU B 17  ? 0.2670 0.3892 0.3205 0.0056  -0.0024 0.0044  17  LEU B CD2 
3052  N N   . PRO B 18  ? 0.2934 0.4268 0.3694 0.0197  0.0527  0.0399  18  PRO B N   
3053  C CA  . PRO B 18  ? 0.3331 0.4531 0.3754 0.0305  0.0621  0.0410  18  PRO B CA  
3054  C C   . PRO B 18  ? 0.3711 0.4758 0.3772 0.0311  0.0489  0.0294  18  PRO B C   
3055  O O   . PRO B 18  ? 0.3477 0.4449 0.3445 0.0284  0.0405  0.0268  18  PRO B O   
3056  C CB  . PRO B 18  ? 0.3355 0.4382 0.3649 0.0388  0.0841  0.0546  18  PRO B CB  
3057  C CG  . PRO B 18  ? 0.3425 0.4594 0.4179 0.0311  0.0908  0.0635  18  PRO B CG  
3058  C CD  . PRO B 18  ? 0.3239 0.4505 0.4130 0.0189  0.0679  0.0517  18  PRO B CD  
3059  N N   . VAL B 19  ? 0.3809 0.4812 0.3707 0.0349  0.0481  0.0234  19  VAL B N   
3060  C CA  . VAL B 19  ? 0.3705 0.4592 0.3375 0.0335  0.0361  0.0118  19  VAL B CA  
3061  C C   . VAL B 19  ? 0.4100 0.4762 0.3418 0.0412  0.0439  0.0099  19  VAL B C   
3062  O O   . VAL B 19  ? 0.4219 0.4848 0.3501 0.0485  0.0600  0.0173  19  VAL B O   
3063  C CB  . VAL B 19  ? 0.3559 0.4566 0.3398 0.0290  0.0279  0.0042  19  VAL B CB  
3064  C CG1 . VAL B 19  ? 0.3081 0.4243 0.3183 0.0235  0.0200  0.0050  19  VAL B CG1 
3065  C CG2 . VAL B 19  ? 0.3762 0.4800 0.3620 0.0348  0.0380  0.0062  19  VAL B CG2 
3066  N N   . GLN B 20  ? 0.4263 0.4763 0.3336 0.0401  0.0317  -0.0001 20  GLN B N   
3067  C CA  . GLN B 20  ? 0.4474 0.4690 0.3145 0.0468  0.0346  -0.0054 20  GLN B CA  
3068  C C   . GLN B 20  ? 0.4252 0.4413 0.2921 0.0394  0.0216  -0.0204 20  GLN B C   
3069  O O   . GLN B 20  ? 0.3789 0.4085 0.2685 0.0310  0.0067  -0.0266 20  GLN B O   
3070  C CB  . GLN B 20  ? 0.5044 0.5037 0.3341 0.0547  0.0301  -0.0039 20  GLN B CB  
3071  C CG  . GLN B 20  ? 0.6063 0.5677 0.3826 0.0654  0.0345  -0.0086 20  GLN B CG  
3072  C CD  . GLN B 20  ? 0.7010 0.6356 0.4315 0.0780  0.0312  -0.0051 20  GLN B CD  
3073  O OE1 . GLN B 20  ? 0.7238 0.6329 0.4141 0.0818  0.0126  -0.0176 20  GLN B OE1 
3074  N NE2 . GLN B 20  ? 0.7335 0.6726 0.4707 0.0849  0.0479  0.0115  20  GLN B NE2 
3075  N N   . GLU B 21  ? 0.4389 0.4334 0.2825 0.0430  0.0298  -0.0254 21  GLU B N   
3076  C CA  . GLU B 21  ? 0.4460 0.4294 0.2901 0.0350  0.0200  -0.0403 21  GLU B CA  
3077  C C   . GLU B 21  ? 0.4680 0.4300 0.2844 0.0329  -0.0018 -0.0535 21  GLU B C   
3078  O O   . GLU B 21  ? 0.4866 0.4232 0.2578 0.0433  -0.0020 -0.0526 21  GLU B O   
3079  C CB  . GLU B 21  ? 0.4397 0.4039 0.2682 0.0400  0.0386  -0.0408 21  GLU B CB  
3080  C CG  . GLU B 21  ? 0.4545 0.4130 0.2996 0.0305  0.0363  -0.0525 21  GLU B CG  
3081  C CD  . GLU B 21  ? 0.5312 0.4538 0.3451 0.0265  0.0270  -0.0687 21  GLU B CD  
3082  O OE1 . GLU B 21  ? 0.5878 0.4879 0.3597 0.0334  0.0203  -0.0713 21  GLU B OE1 
3083  O OE2 . GLU B 21  ? 0.5381 0.4512 0.3673 0.0172  0.0267  -0.0791 21  GLU B OE2 
3084  N N   . ASP B 22  ? 0.4351 0.4064 0.2786 0.0209  -0.0205 -0.0651 22  ASP B N   
3085  C CA  . ASP B 22  ? 0.4619 0.4156 0.2854 0.0181  -0.0460 -0.0799 22  ASP B CA  
3086  C C   . ASP B 22  ? 0.4904 0.4168 0.3028 0.0114  -0.0471 -0.0954 22  ASP B C   
3087  O O   . ASP B 22  ? 0.4840 0.4207 0.3369 -0.0002 -0.0433 -0.1001 22  ASP B O   
3088  C CB  . ASP B 22  ? 0.4503 0.4320 0.3167 0.0091  -0.0675 -0.0833 22  ASP B CB  
3089  C CG  . ASP B 22  ? 0.5114 0.4801 0.3654 0.0058  -0.0985 -0.0996 22  ASP B CG  
3090  O OD1 . ASP B 22  ? 0.5770 0.5240 0.3801 0.0179  -0.1089 -0.1004 22  ASP B OD1 
3091  O OD2 . ASP B 22  ? 0.5251 0.5031 0.4193 -0.0079 -0.1128 -0.1117 22  ASP B OD2 
3092  N N   . ALA B 23  ? 0.5519 0.4384 0.3062 0.0198  -0.0504 -0.1029 23  ALA B N   
3093  C CA  . ALA B 23  ? 0.5988 0.4504 0.3327 0.0156  -0.0458 -0.1167 23  ALA B CA  
3094  C C   . ALA B 23  ? 0.6338 0.4893 0.4065 -0.0036 -0.0700 -0.1360 23  ALA B C   
3095  O O   . ALA B 23  ? 0.6542 0.4999 0.4481 -0.0137 -0.0589 -0.1429 23  ALA B O   
3096  C CB  . ALA B 23  ? 0.6587 0.4605 0.3150 0.0301  -0.0473 -0.1225 23  ALA B CB  
3097  N N   . SER B 24  ? 0.5939 0.4621 0.3767 -0.0075 -0.1026 -0.1443 24  SER B N   
3098  C CA  . SER B 24  ? 0.6361 0.5138 0.4655 -0.0259 -0.1296 -0.1622 24  SER B CA  
3099  C C   . SER B 24  ? 0.5639 0.4780 0.4726 -0.0399 -0.1144 -0.1555 24  SER B C   
3100  O O   . SER B 24  ? 0.5772 0.4847 0.5219 -0.0553 -0.1157 -0.1678 24  SER B O   
3101  C CB  . SER B 24  ? 0.7254 0.6161 0.5534 -0.0236 -0.1675 -0.1686 24  SER B CB  
3102  O OG  . SER B 24  ? 0.7815 0.6912 0.6715 -0.0424 -0.1929 -0.1837 24  SER B OG  
3103  N N   . THR B 25  ? 0.5208 0.4696 0.4564 -0.0343 -0.1005 -0.1367 25  THR B N   
3104  C CA  . THR B 25  ? 0.4881 0.4659 0.4905 -0.0436 -0.0857 -0.1294 25  THR B CA  
3105  C C   . THR B 25  ? 0.4629 0.4352 0.4608 -0.0378 -0.0489 -0.1168 25  THR B C   
3106  O O   . THR B 25  ? 0.4393 0.4200 0.4802 -0.0440 -0.0322 -0.1134 25  THR B O   
3107  C CB  . THR B 25  ? 0.4355 0.4518 0.4721 -0.0403 -0.0925 -0.1171 25  THR B CB  
3108  O OG1 . THR B 25  ? 0.4335 0.4528 0.4339 -0.0258 -0.0796 -0.1020 25  THR B OG1 
3109  C CG2 . THR B 25  ? 0.4383 0.4654 0.4856 -0.0435 -0.1295 -0.1273 25  THR B CG2 
3110  N N   . GLY B 26  ? 0.4430 0.4006 0.3902 -0.0243 -0.0354 -0.1087 26  GLY B N   
3111  C CA  . GLY B 26  ? 0.4168 0.3731 0.3606 -0.0163 -0.0046 -0.0961 26  GLY B CA  
3112  C C   . GLY B 26  ? 0.3978 0.3861 0.3653 -0.0105 0.0034  -0.0804 26  GLY B C   
3113  O O   . GLY B 26  ? 0.3873 0.3794 0.3590 -0.0037 0.0244  -0.0703 26  GLY B O   
3114  N N   . LEU B 27  ? 0.3719 0.3808 0.3529 -0.0123 -0.0149 -0.0791 27  LEU B N   
3115  C CA  . LEU B 27  ? 0.3164 0.3501 0.3150 -0.0073 -0.0094 -0.0661 27  LEU B CA  
3116  C C   . LEU B 27  ? 0.3433 0.3791 0.3104 0.0022  -0.0100 -0.0577 27  LEU B C   
3117  O O   . LEU B 27  ? 0.3795 0.3983 0.3116 0.0062  -0.0150 -0.0609 27  LEU B O   
3118  C CB  . LEU B 27  ? 0.3238 0.3774 0.3603 -0.0138 -0.0243 -0.0674 27  LEU B CB  
3119  C CG  . LEU B 27  ? 0.3398 0.3930 0.4187 -0.0239 -0.0207 -0.0741 27  LEU B CG  
3120  C CD1 . LEU B 27  ? 0.3541 0.4300 0.4765 -0.0292 -0.0352 -0.0739 27  LEU B CD1 
3121  C CD2 . LEU B 27  ? 0.3235 0.3717 0.4108 -0.0191 0.0075  -0.0657 27  LEU B CD2 
3122  N N   . HIS B 28  ? 0.3537 0.4074 0.3329 0.0065  -0.0035 -0.0469 28  HIS B N   
3123  C CA  . HIS B 28  ? 0.3435 0.4015 0.3045 0.0136  -0.0011 -0.0377 28  HIS B CA  
3124  C C   . HIS B 28  ? 0.3389 0.4113 0.3129 0.0124  -0.0120 -0.0337 28  HIS B C   
3125  O O   . HIS B 28  ? 0.3224 0.4055 0.3225 0.0086  -0.0157 -0.0345 28  HIS B O   
3126  C CB  . HIS B 28  ? 0.3301 0.3946 0.2945 0.0193  0.0148  -0.0294 28  HIS B CB  
3127  C CG  . HIS B 28  ? 0.3166 0.3657 0.2641 0.0240  0.0282  -0.0305 28  HIS B CG  
3128  N ND1 . HIS B 28  ? 0.3320 0.3761 0.2607 0.0323  0.0388  -0.0234 28  HIS B ND1 
3129  C CD2 . HIS B 28  ? 0.3188 0.3535 0.2662 0.0222  0.0350  -0.0371 28  HIS B CD2 
3130  C CE1 . HIS B 28  ? 0.3294 0.3567 0.2440 0.0367  0.0512  -0.0255 28  HIS B CE1 
3131  N NE2 . HIS B 28  ? 0.3319 0.3517 0.2561 0.0301  0.0489  -0.0344 28  HIS B NE2 
3132  N N   . TRP B 29  ? 0.3515 0.4207 0.3057 0.0174  -0.0141 -0.0282 29  TRP B N   
3133  C CA  . TRP B 29  ? 0.3215 0.3991 0.2822 0.0182  -0.0226 -0.0234 29  TRP B CA  
3134  C C   . TRP B 29  ? 0.3792 0.4556 0.3294 0.0234  -0.0118 -0.0123 29  TRP B C   
3135  O O   . TRP B 29  ? 0.3867 0.4555 0.3227 0.0277  0.0002  -0.0084 29  TRP B O   
3136  C CB  . TRP B 29  ? 0.3113 0.3812 0.2580 0.0197  -0.0407 -0.0295 29  TRP B CB  
3137  C CG  . TRP B 29  ? 0.3423 0.3881 0.2443 0.0277  -0.0409 -0.0309 29  TRP B CG  
3138  C CD1 . TRP B 29  ? 0.3706 0.3975 0.2503 0.0277  -0.0411 -0.0400 29  TRP B CD1 
3139  C CD2 . TRP B 29  ? 0.3978 0.4297 0.2672 0.0389  -0.0375 -0.0221 29  TRP B CD2 
3140  N NE1 . TRP B 29  ? 0.4186 0.4191 0.2498 0.0393  -0.0388 -0.0378 29  TRP B NE1 
3141  C CE2 . TRP B 29  ? 0.4196 0.4231 0.2443 0.0470  -0.0352 -0.0259 29  TRP B CE2 
3142  C CE3 . TRP B 29  ? 0.4070 0.4433 0.2784 0.0439  -0.0335 -0.0108 29  TRP B CE3 
3143  C CZ2 . TRP B 29  ? 0.4790 0.4581 0.2594 0.0618  -0.0278 -0.0174 29  TRP B CZ2 
3144  C CZ3 . TRP B 29  ? 0.4340 0.4479 0.2662 0.0570  -0.0255 -0.0023 29  TRP B CZ3 
3145  C CH2 . TRP B 29  ? 0.4764 0.4619 0.2628 0.0667  -0.0222 -0.0050 29  TRP B CH2 
3146  N N   . ALA B 30  ? 0.3972 0.4801 0.3576 0.0234  -0.0141 -0.0063 30  ALA B N   
3147  C CA  . ALA B 30  ? 0.3556 0.4361 0.3135 0.0264  -0.0025 0.0043  30  ALA B CA  
3148  C C   . ALA B 30  ? 0.3700 0.4429 0.3176 0.0311  -0.0062 0.0101  30  ALA B C   
3149  O O   . ALA B 30  ? 0.3722 0.4495 0.3262 0.0305  -0.0185 0.0068  30  ALA B O   
3150  C CB  . ALA B 30  ? 0.2957 0.3905 0.2829 0.0202  0.0027  0.0064  30  ALA B CB  
3151  N N   . ASN B 31  ? 0.3844 0.4448 0.3167 0.0376  0.0068  0.0203  31  ASN B N   
3152  C CA  . ASN B 31  ? 0.4110 0.4619 0.3360 0.0429  0.0090  0.0287  31  ASN B CA  
3153  C C   . ASN B 31  ? 0.4073 0.4683 0.3669 0.0335  0.0151  0.0324  31  ASN B C   
3154  O O   . ASN B 31  ? 0.4369 0.5024 0.4163 0.0283  0.0276  0.0367  31  ASN B O   
3155  C CB  . ASN B 31  ? 0.4526 0.4801 0.3461 0.0554  0.0257  0.0403  31  ASN B CB  
3156  C CG  . ASN B 31  ? 0.4840 0.4909 0.3289 0.0692  0.0150  0.0368  31  ASN B CG  
3157  O OD1 . ASN B 31  ? 0.5225 0.5321 0.3603 0.0713  -0.0058 0.0301  31  ASN B OD1 
3158  N ND2 . ASN B 31  ? 0.4944 0.4788 0.3048 0.0800  0.0287  0.0416  31  ASN B ND2 
3159  N N   . ILE B 32  ? 0.3713 0.4350 0.3394 0.0318  0.0059  0.0303  32  ILE B N   
3160  C CA  . ILE B 32  ? 0.3382 0.4030 0.3305 0.0240  0.0107  0.0322  32  ILE B CA  
3161  C C   . ILE B 32  ? 0.3478 0.3946 0.3295 0.0303  0.0211  0.0433  32  ILE B C   
3162  O O   . ILE B 32  ? 0.3709 0.4087 0.3289 0.0418  0.0166  0.0470  32  ILE B O   
3163  C CB  . ILE B 32  ? 0.3535 0.4257 0.3579 0.0204  -0.0010 0.0243  32  ILE B CB  
3164  C CG1 . ILE B 32  ? 0.3398 0.4251 0.3515 0.0166  -0.0075 0.0150  32  ILE B CG1 
3165  C CG2 . ILE B 32  ? 0.3271 0.3931 0.3478 0.0132  0.0026  0.0238  32  ILE B CG2 
3166  C CD1 . ILE B 32  ? 0.3640 0.4552 0.3906 0.0095  -0.0035 0.0126  32  ILE B CD1 
3167  N N   . HIS B 33  ? 0.3445 0.3855 0.3456 0.0233  0.0348  0.0487  33  HIS B N   
3168  C CA  . HIS B 33  ? 0.3479 0.3675 0.3421 0.0285  0.0493  0.0603  33  HIS B CA  
3169  C C   . HIS B 33  ? 0.3786 0.3920 0.3825 0.0239  0.0442  0.0570  33  HIS B C   
3170  O O   . HIS B 33  ? 0.3718 0.3909 0.4000 0.0109  0.0389  0.0483  33  HIS B O   
3171  C CB  . HIS B 33  ? 0.3743 0.3883 0.3913 0.0222  0.0703  0.0691  33  HIS B CB  
3172  C CG  . HIS B 33  ? 0.4254 0.4380 0.4282 0.0311  0.0828  0.0766  33  HIS B CG  
3173  N ND1 . HIS B 33  ? 0.4584 0.4893 0.4654 0.0286  0.0751  0.0695  33  HIS B ND1 
3174  C CD2 . HIS B 33  ? 0.4575 0.4476 0.4381 0.0444  0.1055  0.0918  33  HIS B CD2 
3175  C CE1 . HIS B 33  ? 0.4508 0.4706 0.4389 0.0396  0.0921  0.0794  33  HIS B CE1 
3176  N NE2 . HIS B 33  ? 0.4660 0.4602 0.4364 0.0499  0.1110  0.0931  33  HIS B NE2 
3177  N N   . LYS B 34  ? 0.3847 0.3841 0.3658 0.0367  0.0449  0.0638  34  LYS B N   
3178  C CA  . LYS B 34  ? 0.3939 0.3836 0.3794 0.0361  0.0427  0.0626  34  LYS B CA  
3179  C C   . LYS B 34  ? 0.3832 0.3472 0.3501 0.0487  0.0570  0.0764  34  LYS B C   
3180  O O   . LYS B 34  ? 0.4455 0.3997 0.3892 0.0616  0.0656  0.0871  34  LYS B O   
3181  C CB  . LYS B 34  ? 0.4313 0.4372 0.4144 0.0409  0.0248  0.0553  34  LYS B CB  
3182  C CG  . LYS B 34  ? 0.4206 0.4476 0.4178 0.0312  0.0138  0.0432  34  LYS B CG  
3183  C CD  . LYS B 34  ? 0.4294 0.4649 0.4332 0.0329  0.0040  0.0370  34  LYS B CD  
3184  C CE  . LYS B 34  ? 0.4555 0.4726 0.4627 0.0305  0.0101  0.0365  34  LYS B CE  
3185  N NZ  . LYS B 34  ? 0.4655 0.4859 0.4742 0.0397  0.0065  0.0375  34  LYS B NZ  
3186  N N   . ARG B 35  ? 0.3709 0.3191 0.3435 0.0467  0.0614  0.0767  35  ARG B N   
3187  C CA  . ARG B 35  ? 0.4180 0.3402 0.3712 0.0612  0.0749  0.0901  35  ARG B CA  
3188  C C   . ARG B 35  ? 0.4315 0.3254 0.3844 0.0596  0.1003  0.1013  35  ARG B C   
3189  O O   . ARG B 35  ? 0.4965 0.3937 0.4672 0.0482  0.1086  0.1006  35  ARG B O   
3190  C CB  . ARG B 35  ? 0.4566 0.3870 0.3815 0.0835  0.0650  0.0980  35  ARG B CB  
3191  C CG  . ARG B 35  ? 0.4224 0.3806 0.3572 0.0848  0.0421  0.0886  35  ARG B CG  
3192  C CD  . ARG B 35  ? 0.4308 0.4039 0.3470 0.1019  0.0254  0.0918  35  ARG B CD  
3193  N NE  . ARG B 35  ? 0.4253 0.4287 0.3637 0.0958  0.0052  0.0800  35  ARG B NE  
3194  C CZ  . ARG B 35  ? 0.4521 0.4752 0.3885 0.1055  -0.0156 0.0779  35  ARG B CZ  
3195  N NH1 . ARG B 35  ? 0.5074 0.5223 0.4132 0.1240  -0.0225 0.0859  35  ARG B NH1 
3196  N NH2 . ARG B 35  ? 0.4136 0.4623 0.3782 0.0974  -0.0296 0.0676  35  ARG B NH2 
3197  N N   . THR B 36  ? 0.4662 0.3316 0.4023 0.0720  0.1150  0.1132  36  THR B N   
3198  C CA  . THR B 36  ? 0.5343 0.3673 0.4656 0.0753  0.1442  0.1277  36  THR B CA  
3199  C C   . THR B 36  ? 0.5459 0.3608 0.4324 0.1055  0.1528  0.1457  36  THR B C   
3200  O O   . THR B 36  ? 0.5597 0.3659 0.4303 0.1194  0.1495  0.1503  36  THR B O   
3201  C CB  . THR B 36  ? 0.5241 0.3278 0.4773 0.0605  0.1600  0.1258  36  THR B CB  
3202  O OG1 . THR B 36  ? 0.5953 0.4141 0.5854 0.0343  0.1466  0.1072  36  THR B OG1 
3203  C CG2 . THR B 36  ? 0.5636 0.3361 0.5215 0.0608  0.1925  0.1407  36  THR B CG2 
3204  N N   . PRO B 37  ? 0.5690 0.3769 0.4319 0.1184  0.1634  0.1564  37  PRO B N   
3205  C CA  . PRO B 37  ? 0.5599 0.3757 0.4381 0.1073  0.1721  0.1551  37  PRO B CA  
3206  C C   . PRO B 37  ? 0.5650 0.4199 0.4543 0.0973  0.1439  0.1386  37  PRO B C   
3207  O O   . PRO B 37  ? 0.5560 0.4305 0.4299 0.1051  0.1179  0.1309  37  PRO B O   
3208  C CB  . PRO B 37  ? 0.6239 0.4119 0.4532 0.1349  0.1915  0.1741  37  PRO B CB  
3209  C CG  . PRO B 37  ? 0.6536 0.4375 0.4383 0.1611  0.1736  0.1783  37  PRO B CG  
3210  C CD  . PRO B 37  ? 0.6421 0.4285 0.4532 0.1510  0.1689  0.1732  37  PRO B CD  
3211  N N   . LEU B 38  ? 0.5482 0.4148 0.4692 0.0798  0.1505  0.1338  38  LEU B N   
3212  C CA  . LEU B 38  ? 0.5360 0.4368 0.4710 0.0691  0.1279  0.1189  38  LEU B CA  
3213  C C   . LEU B 38  ? 0.5380 0.4425 0.4297 0.0883  0.1177  0.1207  38  LEU B C   
3214  O O   . LEU B 38  ? 0.5658 0.4458 0.4229 0.1063  0.1354  0.1345  38  LEU B O   
3215  C CB  . LEU B 38  ? 0.5050 0.4159 0.4857 0.0489  0.1398  0.1163  38  LEU B CB  
3216  C CG  . LEU B 38  ? 0.4628 0.4070 0.4774 0.0298  0.1185  0.0988  38  LEU B CG  
3217  C CD1 . LEU B 38  ? 0.3737 0.3226 0.4030 0.0181  0.1006  0.0853  38  LEU B CD1 
3218  C CD2 . LEU B 38  ? 0.5066 0.4570 0.5660 0.0155  0.1349  0.1022  38  LEU B CD2 
3219  N N   . MET B 39  ? 0.5366 0.4675 0.4277 0.0853  0.0897  0.1065  39  MET B N   
3220  C CA  . MET B 39  ? 0.5652 0.4999 0.4203 0.0989  0.0757  0.1036  39  MET B CA  
3221  C C   . MET B 39  ? 0.5169 0.4825 0.3947 0.0842  0.0552  0.0868  39  MET B C   
3222  O O   . MET B 39  ? 0.5009 0.4844 0.4163 0.0672  0.0499  0.0782  39  MET B O   
3223  C CB  . MET B 39  ? 0.6237 0.5501 0.4403 0.1203  0.0592  0.1067  39  MET B CB  
3224  C CG  . MET B 39  ? 0.5913 0.5338 0.4314 0.1163  0.0437  0.1017  39  MET B CG  
3225  S SD  . MET B 39  ? 0.7396 0.7211 0.6103 0.1019  0.0140  0.0823  39  MET B SD  
3226  C CE  . MET B 39  ? 0.7394 0.7224 0.5699 0.1209  -0.0111 0.0790  39  MET B CE  
3227  N N   . GLN B 40  ? 0.5204 0.4875 0.3703 0.0924  0.0437  0.0819  40  GLN B N   
3228  C CA  . GLN B 40  ? 0.4852 0.4762 0.3532 0.0799  0.0284  0.0673  40  GLN B CA  
3229  C C   . GLN B 40  ? 0.4666 0.4738 0.3342 0.0811  0.0004  0.0559  40  GLN B C   
3230  O O   . GLN B 40  ? 0.5100 0.5081 0.3452 0.0962  -0.0137 0.0563  40  GLN B O   
3231  C CB  . GLN B 40  ? 0.5260 0.5060 0.3674 0.0861  0.0357  0.0678  40  GLN B CB  
3232  C CG  . GLN B 40  ? 0.6155 0.5874 0.4709 0.0828  0.0642  0.0787  40  GLN B CG  
3233  C CD  . GLN B 40  ? 0.7392 0.6970 0.5637 0.0924  0.0735  0.0806  40  GLN B CD  
3234  O OE1 . GLN B 40  ? 0.7534 0.7259 0.6016 0.0827  0.0782  0.0767  40  GLN B OE1 
3235  N NE2 . GLN B 40  ? 0.8272 0.7533 0.5933 0.1141  0.0755  0.0865  40  GLN B NE2 
3236  N N   . VAL B 41  ? 0.4124 0.4428 0.3163 0.0662  -0.0080 0.0458  41  VAL B N   
3237  C CA  . VAL B 41  ? 0.3956 0.4438 0.3112 0.0650  -0.0304 0.0357  41  VAL B CA  
3238  C C   . VAL B 41  ? 0.3496 0.4089 0.2745 0.0550  -0.0354 0.0241  41  VAL B C   
3239  O O   . VAL B 41  ? 0.3461 0.4123 0.2917 0.0443  -0.0252 0.0222  41  VAL B O   
3240  C CB  . VAL B 41  ? 0.3798 0.4403 0.3285 0.0596  -0.0314 0.0359  41  VAL B CB  
3241  C CG1 . VAL B 41  ? 0.3420 0.4205 0.3074 0.0616  -0.0507 0.0296  41  VAL B CG1 
3242  C CG2 . VAL B 41  ? 0.4163 0.4609 0.3569 0.0678  -0.0202 0.0481  41  VAL B CG2 
3243  N N   . PRO B 42  ? 0.3652 0.4237 0.2727 0.0593  -0.0520 0.0160  42  PRO B N   
3244  C CA  . PRO B 42  ? 0.3474 0.4131 0.2646 0.0495  -0.0553 0.0047  42  PRO B CA  
3245  C C   . PRO B 42  ? 0.3426 0.4302 0.3025 0.0392  -0.0620 -0.0021 42  PRO B C   
3246  O O   . PRO B 42  ? 0.3363 0.4346 0.3124 0.0414  -0.0770 -0.0040 42  PRO B O   
3247  C CB  . PRO B 42  ? 0.3681 0.4194 0.2496 0.0578  -0.0721 -0.0028 42  PRO B CB  
3248  C CG  . PRO B 42  ? 0.3883 0.4370 0.2566 0.0699  -0.0873 0.0011  42  PRO B CG  
3249  C CD  . PRO B 42  ? 0.3976 0.4433 0.2699 0.0743  -0.0684 0.0162  42  PRO B CD  
3250  N N   . LEU B 43  ? 0.3244 0.4177 0.3024 0.0302  -0.0496 -0.0040 43  LEU B N   
3251  C CA  . LEU B 43  ? 0.2985 0.4055 0.3106 0.0236  -0.0491 -0.0078 43  LEU B CA  
3252  C C   . LEU B 43  ? 0.2777 0.3853 0.2957 0.0172  -0.0434 -0.0150 43  LEU B C   
3253  O O   . LEU B 43  ? 0.2725 0.3731 0.2741 0.0170  -0.0349 -0.0147 43  LEU B O   
3254  C CB  . LEU B 43  ? 0.2630 0.3701 0.2864 0.0230  -0.0378 -0.0013 43  LEU B CB  
3255  C CG  . LEU B 43  ? 0.2931 0.3959 0.3135 0.0291  -0.0382 0.0071  43  LEU B CG  
3256  C CD1 . LEU B 43  ? 0.2944 0.3903 0.3211 0.0265  -0.0269 0.0104  43  LEU B CD1 
3257  C CD2 . LEU B 43  ? 0.2820 0.3947 0.3184 0.0346  -0.0501 0.0079  43  LEU B CD2 
3258  N N   . LEU B 44  ? 0.2902 0.4057 0.3346 0.0132  -0.0457 -0.0199 44  LEU B N   
3259  C CA  . LEU B 44  ? 0.2629 0.3754 0.3132 0.0088  -0.0367 -0.0253 44  LEU B CA  
3260  C C   . LEU B 44  ? 0.2590 0.3689 0.3069 0.0107  -0.0216 -0.0207 44  LEU B C   
3261  O O   . LEU B 44  ? 0.2669 0.3780 0.3223 0.0132  -0.0181 -0.0160 44  LEU B O   
3262  C CB  . LEU B 44  ? 0.2764 0.3964 0.3614 0.0043  -0.0393 -0.0298 44  LEU B CB  
3263  C CG  . LEU B 44  ? 0.2714 0.3848 0.3664 0.0002  -0.0269 -0.0346 44  LEU B CG  
3264  C CD1 . LEU B 44  ? 0.2693 0.3731 0.3497 -0.0049 -0.0358 -0.0447 44  LEU B CD1 
3265  C CD2 . LEU B 44  ? 0.2465 0.3675 0.3848 -0.0020 -0.0204 -0.0331 44  LEU B CD2 
3266  N N   . LEU B 45  ? 0.2695 0.3736 0.3044 0.0109  -0.0138 -0.0226 45  LEU B N   
3267  C CA  . LEU B 45  ? 0.2824 0.3846 0.3152 0.0144  -0.0032 -0.0199 45  LEU B CA  
3268  C C   . LEU B 45  ? 0.2647 0.3617 0.3101 0.0166  0.0063  -0.0213 45  LEU B C   
3269  O O   . LEU B 45  ? 0.2694 0.3612 0.3191 0.0148  0.0121  -0.0252 45  LEU B O   
3270  C CB  . LEU B 45  ? 0.3223 0.4224 0.3392 0.0165  0.0021  -0.0193 45  LEU B CB  
3271  C CG  . LEU B 45  ? 0.3275 0.4276 0.3422 0.0223  0.0098  -0.0172 45  LEU B CG  
3272  C CD1 . LEU B 45  ? 0.3333 0.4383 0.3515 0.0234  0.0041  -0.0145 45  LEU B CD1 
3273  C CD2 . LEU B 45  ? 0.3267 0.4271 0.3312 0.0259  0.0162  -0.0153 45  LEU B CD2 
3274  N N   . ASP B 46  ? 0.2614 0.3552 0.3104 0.0213  0.0102  -0.0178 46  ASP B N   
3275  C CA  . ASP B 46  ? 0.2428 0.3264 0.3000 0.0271  0.0240  -0.0161 46  ASP B CA  
3276  C C   . ASP B 46  ? 0.2758 0.3462 0.3089 0.0377  0.0298  -0.0140 46  ASP B C   
3277  O O   . ASP B 46  ? 0.2728 0.3364 0.2969 0.0421  0.0271  -0.0124 46  ASP B O   
3278  C CB  . ASP B 46  ? 0.2560 0.3424 0.3371 0.0268  0.0252  -0.0128 46  ASP B CB  
3279  C CG  . ASP B 46  ? 0.2590 0.3328 0.3535 0.0341  0.0452  -0.0086 46  ASP B CG  
3280  O OD1 . ASP B 46  ? 0.2930 0.3539 0.3757 0.0393  0.0581  -0.0087 46  ASP B OD1 
3281  O OD2 . ASP B 46  ? 0.2787 0.3542 0.3960 0.0363  0.0505  -0.0035 46  ASP B OD2 
3282  N N   . LEU B 47  ? 0.2881 0.3016 0.3168 -0.0002 0.0693  -0.0166 47  LEU B N   
3283  C CA  . LEU B 47  ? 0.2777 0.2888 0.3227 0.0126  0.0584  -0.0098 47  LEU B CA  
3284  C C   . LEU B 47  ? 0.2654 0.2701 0.2995 0.0175  0.0412  -0.0152 47  LEU B C   
3285  O O   . LEU B 47  ? 0.3089 0.3157 0.3570 0.0247  0.0200  -0.0113 47  LEU B O   
3286  C CB  . LEU B 47  ? 0.3129 0.3066 0.3484 0.0211  0.0756  -0.0076 47  LEU B CB  
3287  C CG  . LEU B 47  ? 0.2823 0.2698 0.3308 0.0375  0.0606  -0.0010 47  LEU B CG  
3288  C CD1 . LEU B 47  ? 0.2267 0.2355 0.3244 0.0396  0.0472  0.0101  47  LEU B CD1 
3289  C CD2 . LEU B 47  ? 0.2625 0.2288 0.2940 0.0473  0.0801  0.0010  47  LEU B CD2 
3290  N N   . ASN B 48  ? 0.2778 0.2712 0.2876 0.0137  0.0513  -0.0243 48  ASN B N   
3291  C CA  . ASN B 48  ? 0.2984 0.2769 0.2924 0.0213  0.0427  -0.0278 48  ASN B CA  
3292  C C   . ASN B 48  ? 0.2766 0.2691 0.2786 0.0141  0.0319  -0.0310 48  ASN B C   
3293  O O   . ASN B 48  ? 0.2713 0.2487 0.2590 0.0202  0.0295  -0.0337 48  ASN B O   
3294  C CB  . ASN B 48  ? 0.3570 0.3101 0.3247 0.0240  0.0659  -0.0337 48  ASN B CB  
3295  C CG  . ASN B 48  ? 0.3718 0.3043 0.3249 0.0357  0.0756  -0.0294 48  ASN B CG  
3296  O OD1 . ASN B 48  ? 0.3877 0.3099 0.3366 0.0505  0.0590  -0.0233 48  ASN B OD1 
3297  N ND2 . ASN B 48  ? 0.3888 0.3143 0.3354 0.0293  0.1005  -0.0330 48  ASN B ND2 
3298  N N   . GLY B 49  ? 0.2709 0.2875 0.2918 0.0031  0.0277  -0.0300 49  GLY B N   
3299  C CA  . GLY B 49  ? 0.2529 0.2833 0.2820 -0.0023 0.0174  -0.0320 49  GLY B CA  
3300  C C   . GLY B 49  ? 0.2533 0.2796 0.2858 0.0059  -0.0018 -0.0277 49  GLY B C   
3301  O O   . GLY B 49  ? 0.2796 0.3050 0.3225 0.0110  -0.0142 -0.0219 49  GLY B O   
3302  N N   . LYS B 50  ? 0.2457 0.2685 0.2731 0.0072  -0.0043 -0.0308 50  LYS B N   
3303  C CA  . LYS B 50  ? 0.2791 0.2885 0.3002 0.0161  -0.0208 -0.0285 50  LYS B CA  
3304  C C   . LYS B 50  ? 0.2527 0.2810 0.2964 0.0112  -0.0371 -0.0233 50  LYS B C   
3305  O O   . LYS B 50  ? 0.2833 0.3004 0.3273 0.0168  -0.0540 -0.0214 50  LYS B O   
3306  C CB  . LYS B 50  ? 0.2984 0.2912 0.3035 0.0213  -0.0119 -0.0322 50  LYS B CB  
3307  C CG  . LYS B 50  ? 0.3402 0.3018 0.3174 0.0302  0.0069  -0.0355 50  LYS B CG  
3308  C CD  . LYS B 50  ? 0.3996 0.3392 0.3628 0.0377  0.0201  -0.0367 50  LYS B CD  
3309  C CE  . LYS B 50  ? 0.4625 0.3685 0.4006 0.0464  0.0478  -0.0387 50  LYS B CE  
3310  N NZ  . LYS B 50  ? 0.5299 0.4167 0.4637 0.0533  0.0658  -0.0379 50  LYS B NZ  
3311  N N   . HIS B 51  ? 0.2251 0.2770 0.2841 0.0016  -0.0322 -0.0215 51  HIS B N   
3312  C CA  . HIS B 51  ? 0.1993 0.2643 0.2755 -0.0014 -0.0424 -0.0150 51  HIS B CA  
3313  C C   . HIS B 51  ? 0.2111 0.2912 0.2913 -0.0086 -0.0335 -0.0120 51  HIS B C   
3314  O O   . HIS B 51  ? 0.2224 0.3036 0.2917 -0.0126 -0.0225 -0.0170 51  HIS B O   
3315  C CB  . HIS B 51  ? 0.2346 0.2990 0.3087 0.0011  -0.0496 -0.0155 51  HIS B CB  
3316  C CG  . HIS B 51  ? 0.2564 0.3310 0.3283 -0.0018 -0.0410 -0.0201 51  HIS B CG  
3317  N ND1 . HIS B 51  ? 0.2345 0.2974 0.2993 0.0027  -0.0326 -0.0252 51  HIS B ND1 
3318  C CD2 . HIS B 51  ? 0.2292 0.3226 0.3078 -0.0078 -0.0406 -0.0205 51  HIS B CD2 
3319  C CE1 . HIS B 51  ? 0.2536 0.3335 0.3324 -0.0023 -0.0272 -0.0285 51  HIS B CE1 
3320  N NE2 . HIS B 51  ? 0.2420 0.3407 0.3273 -0.0087 -0.0354 -0.0267 51  HIS B NE2 
3321  N N   . LEU B 52  ? 0.1888 0.2744 0.2806 -0.0093 -0.0375 -0.0039 52  LEU B N   
3322  C CA  . LEU B 52  ? 0.2044 0.2943 0.2871 -0.0125 -0.0290 0.0000  52  LEU B CA  
3323  C C   . LEU B 52  ? 0.2539 0.3509 0.3250 -0.0128 -0.0370 -0.0034 52  LEU B C   
3324  O O   . LEU B 52  ? 0.2985 0.3982 0.3781 -0.0095 -0.0465 -0.0014 52  LEU B O   
3325  C CB  . LEU B 52  ? 0.2054 0.2920 0.3047 -0.0109 -0.0241 0.0121  52  LEU B CB  
3326  C CG  . LEU B 52  ? 0.2409 0.3195 0.3212 -0.0102 -0.0098 0.0191  52  LEU B CG  
3327  C CD1 . LEU B 52  ? 0.2539 0.3260 0.3601 -0.0086 0.0054  0.0311  52  LEU B CD1 
3328  C CD2 . LEU B 52  ? 0.2646 0.3419 0.3308 -0.0072 -0.0169 0.0227  52  LEU B CD2 
3329  N N   . TRP B 53  ? 0.2336 0.3323 0.2865 -0.0161 -0.0351 -0.0089 53  TRP B N   
3330  C CA  . TRP B 53  ? 0.2281 0.3356 0.2759 -0.0152 -0.0476 -0.0115 53  TRP B CA  
3331  C C   . TRP B 53  ? 0.3080 0.4059 0.3256 -0.0145 -0.0491 -0.0104 53  TRP B C   
3332  O O   . TRP B 53  ? 0.3331 0.4172 0.3309 -0.0170 -0.0381 -0.0121 53  TRP B O   
3333  C CB  . TRP B 53  ? 0.2173 0.3363 0.2785 -0.0191 -0.0518 -0.0227 53  TRP B CB  
3334  C CG  . TRP B 53  ? 0.2520 0.3680 0.3076 -0.0267 -0.0443 -0.0333 53  TRP B CG  
3335  C CD1 . TRP B 53  ? 0.2678 0.3761 0.3266 -0.0287 -0.0304 -0.0368 53  TRP B CD1 
3336  C CD2 . TRP B 53  ? 0.2510 0.3682 0.2955 -0.0329 -0.0519 -0.0426 53  TRP B CD2 
3337  N NE1 . TRP B 53  ? 0.2522 0.3572 0.3048 -0.0364 -0.0249 -0.0468 53  TRP B NE1 
3338  C CE2 . TRP B 53  ? 0.2661 0.3765 0.3109 -0.0401 -0.0394 -0.0517 53  TRP B CE2 
3339  C CE3 . TRP B 53  ? 0.2397 0.3591 0.2704 -0.0319 -0.0703 -0.0448 53  TRP B CE3 
3340  C CZ2 . TRP B 53  ? 0.3092 0.4155 0.3446 -0.0487 -0.0445 -0.0640 53  TRP B CZ2 
3341  C CZ3 . TRP B 53  ? 0.2776 0.3919 0.2956 -0.0391 -0.0794 -0.0575 53  TRP B CZ3 
3342  C CH2 . TRP B 53  ? 0.3173 0.4254 0.3394 -0.0486 -0.0664 -0.0676 53  TRP B CH2 
3343  N N   . VAL B 54  ? 0.3159 0.4160 0.3249 -0.0089 -0.0622 -0.0069 54  VAL B N   
3344  C CA  . VAL B 54  ? 0.3391 0.4219 0.3076 -0.0040 -0.0679 -0.0053 54  VAL B CA  
3345  C C   . VAL B 54  ? 0.3569 0.4520 0.3249 -0.0005 -0.0935 -0.0109 54  VAL B C   
3346  O O   . VAL B 54  ? 0.3398 0.4560 0.3416 0.0007  -0.1015 -0.0103 54  VAL B O   
3347  C CB  A VAL B 54  ? 0.3354 0.3966 0.2838 0.0055  -0.0553 0.0108  54  VAL B CB  
3348  C CB  B VAL B 54  ? 0.3269 0.3879 0.2763 0.0052  -0.0541 0.0110  54  VAL B CB  
3349  C CG1 A VAL B 54  ? 0.3740 0.4020 0.2708 0.0100  -0.0448 0.0128  54  VAL B CG1 
3350  C CG1 B VAL B 54  ? 0.3324 0.3835 0.2929 0.0022  -0.0295 0.0173  54  VAL B CG1 
3351  C CG2 A VAL B 54  ? 0.3075 0.3722 0.2903 0.0034  -0.0387 0.0194  54  VAL B CG2 
3352  C CG2 B VAL B 54  ? 0.2565 0.3278 0.2291 0.0106  -0.0600 0.0195  54  VAL B CG2 
3353  N N   . THR B 55  ? 0.4392 0.5183 0.3681 0.0022  -0.1071 -0.0165 55  THR B N   
3354  C CA  . THR B 55  ? 0.5154 0.6017 0.4390 0.0092  -0.1363 -0.0195 55  THR B CA  
3355  C C   . THR B 55  ? 0.5879 0.6581 0.4870 0.0245  -0.1338 -0.0027 55  THR B C   
3356  O O   . THR B 55  ? 0.6538 0.6888 0.5051 0.0319  -0.1187 0.0064  55  THR B O   
3357  C CB  . THR B 55  ? 0.5445 0.6103 0.4246 0.0089  -0.1564 -0.0318 55  THR B CB  
3358  O OG1 . THR B 55  ? 0.5170 0.5932 0.4195 -0.0064 -0.1545 -0.0472 55  THR B OG1 
3359  C CG2 . THR B 55  ? 0.6036 0.6796 0.4851 0.0170  -0.1932 -0.0359 55  THR B CG2 
3360  N N   . CYS B 56  ? 0.5690 0.6600 0.4984 0.0304  -0.1455 0.0023  56  CYS B N   
3361  C CA  . CYS B 56  ? 0.5865 0.6602 0.4951 0.0448  -0.1398 0.0189  56  CYS B CA  
3362  C C   . CYS B 56  ? 0.6734 0.7401 0.5539 0.0597  -0.1676 0.0206  56  CYS B C   
3363  O O   . CYS B 56  ? 0.7559 0.7949 0.5975 0.0748  -0.1627 0.0344  56  CYS B O   
3364  C CB  . CYS B 56  ? 0.4605 0.5532 0.4160 0.0434  -0.1284 0.0262  56  CYS B CB  
3365  S SG  . CYS B 56  ? 0.4399 0.5295 0.4162 0.0316  -0.1003 0.0276  56  CYS B SG  
3366  N N   . SER B 57  ? 0.6850 0.7752 0.5872 0.0563  -0.1971 0.0069  57  SER B N   
3367  C CA  . SER B 57  ? 0.8110 0.9001 0.7045 0.0646  -0.2172 0.0090  57  SER B CA  
3368  C C   . SER B 57  ? 0.9326 0.9727 0.7438 0.0785  -0.2229 0.0130  57  SER B C   
3369  O O   . SER B 57  ? 0.9934 1.0252 0.7874 0.0895  -0.2395 0.0164  57  SER B O   
3370  C CB  . SER B 57  ? 0.8309 0.9519 0.7724 0.0510  -0.2339 -0.0059 57  SER B CB  
3371  O OG  . SER B 57  ? 0.8709 0.9760 0.7847 0.0415  -0.2389 -0.0199 57  SER B OG  
3372  N N   . GLN B 58  ? 0.9769 0.9811 0.7354 0.0794  -0.2065 0.0134  58  GLN B N   
3373  C CA  . GLN B 58  ? 1.1093 1.0553 0.7818 0.0941  -0.1993 0.0200  58  GLN B CA  
3374  C C   . GLN B 58  ? 1.1867 1.0957 0.8144 0.1151  -0.1834 0.0406  58  GLN B C   
3375  O O   . GLN B 58  ? 1.2490 1.1720 0.8971 0.1234  -0.1939 0.0476  58  GLN B O   
3376  C CB  . GLN B 58  ? 1.1683 1.0838 0.8024 0.0896  -0.1738 0.0192  58  GLN B CB  
3377  C CG  . GLN B 58  ? 1.1625 1.1200 0.8635 0.0662  -0.1666 0.0065  58  GLN B CG  
3378  C CD  . GLN B 58  ? 1.2466 1.1745 0.9170 0.0596  -0.1374 0.0050  58  GLN B CD  
3379  O OE1 . GLN B 58  ? 1.3365 1.2196 0.9362 0.0664  -0.1422 -0.0003 58  GLN B OE1 
3380  N NE2 . GLN B 58  ? 1.2129 1.1613 0.9327 0.0480  -0.1074 0.0100  58  GLN B NE2 
3381  N N   . HIS B 59  ? 1.1761 1.0336 0.7421 0.1235  -0.1527 0.0507  59  HIS B N   
3382  C CA  . HIS B 59  ? 1.1670 0.9766 0.6844 0.1425  -0.1245 0.0711  59  HIS B CA  
3383  C C   . HIS B 59  ? 1.0650 0.8887 0.6295 0.1378  -0.0897 0.0871  59  HIS B C   
3384  O O   . HIS B 59  ? 1.1593 0.9453 0.7019 0.1430  -0.0488 0.1022  59  HIS B O   
3385  C CB  . HIS B 59  ? 1.2188 0.9650 0.6606 0.1509  -0.0992 0.0733  59  HIS B CB  
3386  C CG  . HIS B 59  ? 1.2517 0.9814 0.6541 0.1508  -0.1291 0.0543  59  HIS B CG  
3387  N ND1 . HIS B 59  ? 1.3101 1.0316 0.6903 0.1621  -0.1607 0.0490  59  HIS B ND1 
3388  C CD2 . HIS B 59  ? 1.2615 0.9765 0.6410 0.1418  -0.1307 0.0402  59  HIS B CD2 
3389  C CE1 . HIS B 59  ? 1.3630 1.0662 0.7102 0.1596  -0.1830 0.0322  59  HIS B CE1 
3390  N NE2 . HIS B 59  ? 1.3331 1.0314 0.6788 0.1470  -0.1648 0.0264  59  HIS B NE2 
3391  N N   . TYR B 60  ? 0.8517 0.7328 0.4978 0.1229  -0.1006 0.0812  60  TYR B N   
3392  C CA  . TYR B 60  ? 0.6868 0.5852 0.3922 0.1110  -0.0688 0.0897  60  TYR B CA  
3393  C C   . TYR B 60  ? 0.6625 0.5310 0.3533 0.1259  -0.0466 0.1102  60  TYR B C   
3394  O O   . TYR B 60  ? 0.6300 0.5100 0.3326 0.1341  -0.0616 0.1145  60  TYR B O   
3395  C CB  . TYR B 60  ? 0.5895 0.5449 0.3710 0.0950  -0.0861 0.0784  60  TYR B CB  
3396  C CG  . TYR B 60  ? 0.5074 0.4801 0.3464 0.0798  -0.0617 0.0806  60  TYR B CG  
3397  C CD1 . TYR B 60  ? 0.4788 0.4379 0.3352 0.0827  -0.0389 0.0952  60  TYR B CD1 
3398  C CD2 . TYR B 60  ? 0.4177 0.4172 0.2925 0.0629  -0.0633 0.0674  60  TYR B CD2 
3399  C CE1 . TYR B 60  ? 0.4618 0.4353 0.3722 0.0686  -0.0236 0.0951  60  TYR B CE1 
3400  C CE2 . TYR B 60  ? 0.3884 0.4006 0.3107 0.0513  -0.0471 0.0685  60  TYR B CE2 
3401  C CZ  . TYR B 60  ? 0.4137 0.4138 0.3550 0.0538  -0.0300 0.0815  60  TYR B CZ  
3402  O OH  . TYR B 60  ? 0.4262 0.4376 0.4168 0.0420  -0.0202 0.0807  60  TYR B OH  
3403  N N   . SER B 61  ? 0.6441 0.4733 0.3145 0.1294  -0.0072 0.1237  61  SER B N   
3404  C CA  . SER B 61  ? 0.6635 0.4575 0.3213 0.1431  0.0214  0.1444  61  SER B CA  
3405  C C   . SER B 61  ? 0.6752 0.4839 0.4075 0.1265  0.0540  0.1508  61  SER B C   
3406  O O   . SER B 61  ? 0.6847 0.4857 0.4304 0.1185  0.0788  0.1521  61  SER B O   
3407  C CB  . SER B 61  ? 0.7613 0.4849 0.3260 0.1659  0.0435  0.1575  61  SER B CB  
3408  O OG  . SER B 61  ? 0.8424 0.5530 0.3443 0.1799  0.0069  0.1471  61  SER B OG  
3409  N N   . SER B 62  ? 0.6220 0.4504 0.4043 0.1219  0.0524  0.1546  62  SER B N   
3410  C CA  . SER B 62  ? 0.5543 0.3969 0.4108 0.1052  0.0747  0.1577  62  SER B CA  
3411  C C   . SER B 62  ? 0.5551 0.3982 0.4433 0.1062  0.0763  0.1650  62  SER B C   
3412  O O   . SER B 62  ? 0.5732 0.4342 0.4575 0.1103  0.0493  0.1595  62  SER B O   
3413  C CB  . SER B 62  ? 0.4769 0.3667 0.3859 0.0844  0.0551  0.1394  62  SER B CB  
3414  O OG  . SER B 62  ? 0.4592 0.3618 0.4386 0.0694  0.0687  0.1407  62  SER B OG  
3415  N N   . SER B 63  ? 0.5426 0.3632 0.4645 0.1031  0.1105  0.1784  63  SER B N   
3416  C CA  . SER B 63  ? 0.5566 0.3740 0.5158 0.1008  0.1151  0.1842  63  SER B CA  
3417  C C   . SER B 63  ? 0.5212 0.3776 0.5568 0.0778  0.0975  0.1695  63  SER B C   
3418  O O   . SER B 63  ? 0.5076 0.3624 0.5794 0.0722  0.0966  0.1701  63  SER B O   
3419  C CB  . SER B 63  ? 0.6086 0.3797 0.5727 0.1077  0.1612  0.2052  63  SER B CB  
3420  O OG  . SER B 63  ? 0.6209 0.3964 0.6435 0.0928  0.1851  0.2067  63  SER B OG  
3421  N N   . THR B 64  ? 0.5002 0.3865 0.5547 0.0658  0.0827  0.1558  64  THR B N   
3422  C CA  . THR B 64  ? 0.4810 0.3972 0.5980 0.0470  0.0643  0.1419  64  THR B CA  
3423  C C   . THR B 64  ? 0.4596 0.4076 0.5647 0.0436  0.0297  0.1242  64  THR B C   
3424  O O   . THR B 64  ? 0.4688 0.4361 0.6116 0.0308  0.0142  0.1119  64  THR B O   
3425  C CB  . THR B 64  ? 0.3803 0.3040 0.5495 0.0339  0.0787  0.1415  64  THR B CB  
3426  O OG1 . THR B 64  ? 0.4194 0.3392 0.5520 0.0401  0.0910  0.1441  64  THR B OG1 
3427  C CG2 . THR B 64  ? 0.4394 0.3398 0.6567 0.0305  0.1094  0.1558  64  THR B CG2 
3428  N N   . TYR B 65  ? 0.4199 0.3710 0.4745 0.0559  0.0175  0.1229  65  TYR B N   
3429  C CA  . TYR B 65  ? 0.3442 0.3249 0.3955 0.0527  -0.0102 0.1074  65  TYR B CA  
3430  C C   . TYR B 65  ? 0.3455 0.3331 0.4131 0.0525  -0.0251 0.1023  65  TYR B C   
3431  O O   . TYR B 65  ? 0.4073 0.3781 0.4660 0.0618  -0.0201 0.1117  65  TYR B O   
3432  C CB  . TYR B 65  ? 0.3616 0.3454 0.3640 0.0649  -0.0209 0.1067  65  TYR B CB  
3433  C CG  . TYR B 65  ? 0.3462 0.3603 0.3552 0.0629  -0.0467 0.0930  65  TYR B CG  
3434  C CD1 . TYR B 65  ? 0.3328 0.3680 0.3553 0.0517  -0.0544 0.0795  65  TYR B CD1 
3435  C CD2 . TYR B 65  ? 0.3245 0.3443 0.3291 0.0734  -0.0598 0.0947  65  TYR B CD2 
3436  C CE1 . TYR B 65  ? 0.3509 0.4101 0.3834 0.0502  -0.0719 0.0683  65  TYR B CE1 
3437  C CE2 . TYR B 65  ? 0.2980 0.3443 0.3176 0.0721  -0.0776 0.0840  65  TYR B CE2 
3438  C CZ  . TYR B 65  ? 0.3600 0.4253 0.3938 0.0602  -0.0826 0.0708  65  TYR B CZ  
3439  O OH  . TYR B 65  ? 0.3932 0.4820 0.4457 0.0594  -0.0953 0.0613  65  TYR B OH  
3440  N N   . GLN B 66  ? 0.3580 0.3650 0.4443 0.0439  -0.0408 0.0883  66  GLN B N   
3441  C CA  . GLN B 66  ? 0.4180 0.4271 0.5081 0.0470  -0.0531 0.0829  66  GLN B CA  
3442  C C   . GLN B 66  ? 0.3901 0.4210 0.4797 0.0448  -0.0665 0.0700  66  GLN B C   
3443  O O   . GLN B 66  ? 0.3505 0.3913 0.4470 0.0359  -0.0683 0.0619  66  GLN B O   
3444  C CB  . GLN B 66  ? 0.5038 0.4940 0.6195 0.0392  -0.0529 0.0803  66  GLN B CB  
3445  C CG  . GLN B 66  ? 0.6383 0.6038 0.7603 0.0421  -0.0385 0.0930  66  GLN B CG  
3446  C CD  . GLN B 66  ? 0.7143 0.6604 0.8684 0.0312  -0.0418 0.0878  66  GLN B CD  
3447  O OE1 . GLN B 66  ? 0.7538 0.6932 0.9059 0.0294  -0.0568 0.0767  66  GLN B OE1 
3448  N NE2 . GLN B 66  ? 0.7404 0.6735 0.9244 0.0244  -0.0272 0.0955  66  GLN B NE2 
3449  N N   . ALA B 67  ? 0.4005 0.4370 0.4852 0.0537  -0.0730 0.0691  67  ALA B N   
3450  C CA  . ALA B 67  ? 0.3934 0.4446 0.4845 0.0524  -0.0795 0.0581  67  ALA B CA  
3451  C C   . ALA B 67  ? 0.3707 0.4003 0.4642 0.0539  -0.0783 0.0543  67  ALA B C   
3452  O O   . ALA B 67  ? 0.3639 0.3826 0.4544 0.0639  -0.0754 0.0606  67  ALA B O   
3453  C CB  . ALA B 67  ? 0.4173 0.4909 0.5089 0.0619  -0.0859 0.0597  67  ALA B CB  
3454  N N   . PRO B 68  ? 0.3065 0.3245 0.4001 0.0459  -0.0810 0.0442  68  PRO B N   
3455  C CA  . PRO B 68  ? 0.3122 0.2982 0.3951 0.0488  -0.0824 0.0391  68  PRO B CA  
3456  C C   . PRO B 68  ? 0.3432 0.3241 0.4173 0.0614  -0.0745 0.0398  68  PRO B C   
3457  O O   . PRO B 68  ? 0.3414 0.3467 0.4250 0.0641  -0.0702 0.0391  68  PRO B O   
3458  C CB  . PRO B 68  ? 0.2597 0.2373 0.3383 0.0410  -0.0898 0.0278  68  PRO B CB  
3459  C CG  . PRO B 68  ? 0.2459 0.2465 0.3427 0.0313  -0.0911 0.0298  68  PRO B CG  
3460  C CD  . PRO B 68  ? 0.2456 0.2728 0.3447 0.0353  -0.0838 0.0378  68  PRO B CD  
3461  N N   . PHE B 69  ? 0.3618 0.3089 0.4211 0.0688  -0.0711 0.0411  69  PHE B N   
3462  C CA  . PHE B 69  ? 0.3889 0.3276 0.4427 0.0826  -0.0583 0.0441  69  PHE B CA  
3463  C C   . PHE B 69  ? 0.4129 0.3301 0.4472 0.0851  -0.0520 0.0345  69  PHE B C   
3464  O O   . PHE B 69  ? 0.4319 0.3284 0.4468 0.0781  -0.0617 0.0250  69  PHE B O   
3465  C CB  . PHE B 69  ? 0.4444 0.3491 0.4844 0.0921  -0.0527 0.0504  69  PHE B CB  
3466  C CG  . PHE B 69  ? 0.4549 0.3095 0.4661 0.0874  -0.0607 0.0417  69  PHE B CG  
3467  C CD1 . PHE B 69  ? 0.4808 0.2912 0.4557 0.0940  -0.0576 0.0326  69  PHE B CD1 
3468  C CD2 . PHE B 69  ? 0.4230 0.2690 0.4423 0.0780  -0.0706 0.0428  69  PHE B CD2 
3469  C CE1 . PHE B 69  ? 0.5105 0.2696 0.4540 0.0905  -0.0714 0.0225  69  PHE B CE1 
3470  C CE2 . PHE B 69  ? 0.4473 0.2477 0.4481 0.0723  -0.0827 0.0329  69  PHE B CE2 
3471  C CZ  . PHE B 69  ? 0.4880 0.2450 0.4490 0.0786  -0.0862 0.0219  69  PHE B CZ  
3472  N N   . CYS B 70  ? 0.3830 0.3042 0.4248 0.0963  -0.0348 0.0380  70  CYS B N   
3473  C CA  . CYS B 70  ? 0.4071 0.3026 0.4285 0.1017  -0.0209 0.0314  70  CYS B CA  
3474  C C   . CYS B 70  ? 0.4332 0.2623 0.4002 0.1086  -0.0207 0.0252  70  CYS B C   
3475  O O   . CYS B 70  ? 0.4813 0.2827 0.4338 0.1155  -0.0191 0.0291  70  CYS B O   
3476  C CB  . CYS B 70  ? 0.4360 0.3464 0.4860 0.1136  0.0027  0.0387  70  CYS B CB  
3477  S SG  . CYS B 70  ? 0.4887 0.3853 0.5326 0.1167  0.0253  0.0324  70  CYS B SG  
3478  N N   . HIS B 71  ? 0.2936 0.2897 0.3351 0.0505  0.0428  -0.0003 71  HIS B N   
3479  C CA  . HIS B 71  ? 0.3604 0.3245 0.3709 0.0434  0.0504  -0.0001 71  HIS B CA  
3480  C C   . HIS B 71  ? 0.3667 0.3132 0.3588 0.0406  0.0425  -0.0006 71  HIS B C   
3481  O O   . HIS B 71  ? 0.4061 0.3267 0.3735 0.0352  0.0451  -0.0032 71  HIS B O   
3482  C CB  . HIS B 71  ? 0.3947 0.3442 0.3969 0.0491  0.0698  -0.0002 71  HIS B CB  
3483  C CG  . HIS B 71  ? 0.3982 0.3673 0.4306 0.0525  0.0825  -0.0009 71  HIS B CG  
3484  N ND1 . HIS B 71  ? 0.3943 0.3839 0.4581 0.0662  0.0895  -0.0006 71  HIS B ND1 
3485  C CD2 . HIS B 71  ? 0.3955 0.3662 0.4361 0.0440  0.0912  -0.0024 71  HIS B CD2 
3486  C CE1 . HIS B 71  ? 0.3525 0.3603 0.4500 0.0648  0.1012  -0.0037 71  HIS B CE1 
3487  N NE2 . HIS B 71  ? 0.4028 0.3970 0.4851 0.0505  0.1050  -0.0048 71  HIS B NE2 
3488  N N   . SER B 72  ? 0.3319 0.2901 0.3360 0.0431  0.0337  0.0003  72  SER B N   
3489  C CA  . SER B 72  ? 0.3124 0.2553 0.3094 0.0389  0.0305  -0.0012 72  SER B CA  
3490  C C   . SER B 72  ? 0.3588 0.2983 0.3566 0.0265  0.0188  -0.0042 72  SER B C   
3491  O O   . SER B 72  ? 0.3958 0.3416 0.3937 0.0230  0.0140  -0.0031 72  SER B O   
3492  C CB  . SER B 72  ? 0.2963 0.2463 0.3017 0.0455  0.0296  0.0013  72  SER B CB  
3493  O OG  . SER B 72  ? 0.3075 0.2763 0.3263 0.0426  0.0202  0.0009  72  SER B OG  
3494  N N   . THR B 73  ? 0.3685 0.2966 0.3688 0.0205  0.0149  -0.0083 73  THR B N   
3495  C CA  . THR B 73  ? 0.3343 0.2638 0.3443 0.0114  -0.0005 -0.0114 73  THR B CA  
3496  C C   . THR B 73  ? 0.2974 0.2453 0.3304 0.0120  -0.0046 -0.0079 73  THR B C   
3497  O O   . THR B 73  ? 0.2841 0.2361 0.3226 0.0085  -0.0158 -0.0067 73  THR B O   
3498  C CB  . THR B 73  ? 0.3410 0.2594 0.3616 0.0043  -0.0036 -0.0193 73  THR B CB  
3499  O OG1 . THR B 73  ? 0.3528 0.2701 0.3882 0.0076  0.0118  -0.0186 73  THR B OG1 
3500  C CG2 . THR B 73  ? 0.3226 0.2183 0.3155 0.0012  -0.0021 -0.0255 73  THR B CG2 
3501  N N   . GLN B 74  ? 0.3032 0.2575 0.3443 0.0175  0.0050  -0.0061 74  GLN B N   
3502  C CA  . GLN B 74  ? 0.2860 0.2527 0.3419 0.0176  0.0033  -0.0046 74  GLN B CA  
3503  C C   . GLN B 74  ? 0.2958 0.2742 0.3490 0.0174  -0.0013 -0.0028 74  GLN B C   
3504  O O   . GLN B 74  ? 0.3039 0.2872 0.3690 0.0135  -0.0058 -0.0024 74  GLN B O   
3505  C CB  . GLN B 74  ? 0.2957 0.2602 0.3469 0.0250  0.0140  -0.0036 74  GLN B CB  
3506  C CG  . GLN B 74  ? 0.3007 0.2475 0.3557 0.0246  0.0263  -0.0047 74  GLN B CG  
3507  C CD  . GLN B 74  ? 0.3837 0.3152 0.4189 0.0315  0.0360  -0.0028 74  GLN B CD  
3508  O OE1 . GLN B 74  ? 0.4274 0.3613 0.4533 0.0329  0.0318  -0.0025 74  GLN B OE1 
3509  N NE2 . GLN B 74  ? 0.4637 0.3748 0.4887 0.0372  0.0525  -0.0005 74  GLN B NE2 
3510  N N   . CYS B 75  ? 0.3382 0.3199 0.3800 0.0218  0.0029  -0.0020 75  CYS B N   
3511  C CA  . CYS B 75  ? 0.3324 0.3245 0.3784 0.0200  0.0037  -0.0019 75  CYS B CA  
3512  C C   . CYS B 75  ? 0.3169 0.2951 0.3521 0.0138  0.0016  0.0007  75  CYS B C   
3513  O O   . CYS B 75  ? 0.3021 0.2822 0.3430 0.0102  0.0032  0.0019  75  CYS B O   
3514  C CB  . CYS B 75  ? 0.3583 0.3595 0.4046 0.0270  0.0110  -0.0026 75  CYS B CB  
3515  S SG  . CYS B 75  ? 0.4274 0.4439 0.4801 0.0386  0.0072  -0.0042 75  CYS B SG  
3516  N N   . SER B 76  ? 0.3335 0.2934 0.3490 0.0130  -0.0018 0.0012  76  SER B N   
3517  C CA  . SER B 76  ? 0.3389 0.2795 0.3333 0.0098  -0.0087 0.0041  76  SER B CA  
3518  C C   . SER B 76  ? 0.3188 0.2633 0.3297 0.0081  -0.0215 0.0065  76  SER B C   
3519  O O   . SER B 76  ? 0.3639 0.2990 0.3663 0.0080  -0.0225 0.0117  76  SER B O   
3520  C CB  . SER B 76  ? 0.3772 0.2971 0.3452 0.0090  -0.0148 0.0010  76  SER B CB  
3521  O OG  . SER B 76  ? 0.4648 0.3615 0.4020 0.0080  -0.0256 0.0037  76  SER B OG  
3522  N N   . ARG B 77  ? 0.3145 0.2700 0.3502 0.0076  -0.0278 0.0032  77  ARG B N   
3523  C CA  . ARG B 77  ? 0.3068 0.2674 0.3668 0.0072  -0.0372 0.0049  77  ARG B CA  
3524  C C   . ARG B 77  ? 0.3069 0.2738 0.3777 0.0072  -0.0286 0.0079  77  ARG B C   
3525  O O   . ARG B 77  ? 0.3287 0.2897 0.4050 0.0083  -0.0337 0.0126  77  ARG B O   
3526  C CB  . ARG B 77  ? 0.2880 0.2578 0.3777 0.0058  -0.0370 -0.0005 77  ARG B CB  
3527  C CG  . ARG B 77  ? 0.3192 0.2951 0.4428 0.0058  -0.0454 0.0000  77  ARG B CG  
3528  C CD  . ARG B 77  ? 0.3291 0.3118 0.4882 0.0032  -0.0386 -0.0063 77  ARG B CD  
3529  N NE  . ARG B 77  ? 0.3532 0.3437 0.5524 0.0045  -0.0448 -0.0056 77  ARG B NE  
3530  C CZ  . ARG B 77  ? 0.3242 0.3202 0.5642 0.0029  -0.0326 -0.0096 77  ARG B CZ  
3531  N NH1 . ARG B 77  ? 0.3617 0.3518 0.6013 0.0000  -0.0124 -0.0141 77  ARG B NH1 
3532  N NH2 . ARG B 77  ? 0.3284 0.3324 0.6085 0.0058  -0.0381 -0.0082 77  ARG B NH2 
3533  N N   . ALA B 78  ? 0.2780 0.2554 0.3512 0.0065  -0.0165 0.0044  78  ALA B N   
3534  C CA  . ALA B 78  ? 0.2451 0.2296 0.3289 0.0042  -0.0087 0.0027  78  ALA B CA  
3535  C C   . ALA B 78  ? 0.2976 0.2747 0.3705 0.0015  -0.0021 0.0054  78  ALA B C   
3536  O O   . ALA B 78  ? 0.2969 0.2775 0.3816 -0.0028 0.0058  0.0027  78  ALA B O   
3537  C CB  . ALA B 78  ? 0.2124 0.2109 0.3000 0.0054  -0.0034 -0.0040 78  ALA B CB  
3538  N N   . ASN B 79  ? 0.3601 0.3236 0.4090 0.0032  -0.0025 0.0095  79  ASN B N   
3539  C CA  . ASN B 79  ? 0.3948 0.3413 0.4254 0.0014  0.0092  0.0135  79  ASN B CA  
3540  C C   . ASN B 79  ? 0.4108 0.3746 0.4617 -0.0030 0.0251  0.0066  79  ASN B C   
3541  O O   . ASN B 79  ? 0.4065 0.3648 0.4651 -0.0084 0.0389  0.0061  79  ASN B O   
3542  C CB  . ASN B 79  ? 0.4375 0.3641 0.4613 0.0017  0.0085  0.0210  79  ASN B CB  
3543  C CG  . ASN B 79  ? 0.5585 0.4522 0.5462 0.0024  0.0212  0.0286  79  ASN B CG  
3544  O OD1 . ASN B 79  ? 0.6131 0.4930 0.5722 0.0039  0.0253  0.0293  79  ASN B OD1 
3545  N ND2 . ASN B 79  ? 0.5937 0.4689 0.5789 0.0017  0.0309  0.0346  79  ASN B ND2 
3546  N N   . THR B 80  ? 0.4046 0.3893 0.4673 -0.0002 0.0230  0.0007  80  THR B N   
3547  C CA  . THR B 80  ? 0.4226 0.4283 0.5100 -0.0019 0.0330  -0.0067 80  THR B CA  
3548  C C   . THR B 80  ? 0.5346 0.5393 0.6126 0.0044  0.0386  -0.0056 80  THR B C   
3549  O O   . THR B 80  ? 0.5536 0.5578 0.6196 0.0109  0.0296  -0.0041 80  THR B O   
3550  C CB  . THR B 80  ? 0.3477 0.3811 0.4604 -0.0013 0.0225  -0.0157 80  THR B CB  
3551  O OG1 . THR B 80  ? 0.3987 0.4566 0.5375 0.0003  0.0254  -0.0234 80  THR B OG1 
3552  C CG2 . THR B 80  ? 0.2757 0.3089 0.3745 0.0064  0.0103  -0.0137 80  THR B CG2 
3553  N N   . HIS B 81  ? 0.5825 0.5828 0.6660 0.0025  0.0571  -0.0063 81  HIS B N   
3554  C CA  . HIS B 81  ? 0.6427 0.6397 0.7192 0.0094  0.0664  -0.0056 81  HIS B CA  
3555  C C   . HIS B 81  ? 0.6724 0.7013 0.7971 0.0112  0.0762  -0.0134 81  HIS B C   
3556  O O   . HIS B 81  ? 0.7176 0.7451 0.8489 0.0164  0.0916  -0.0136 81  HIS B O   
3557  C CB  . HIS B 81  ? 0.7337 0.6888 0.7666 0.0078  0.0823  0.0008  81  HIS B CB  
3558  C CG  . HIS B 81  ? 0.8390 0.7670 0.8278 0.0082  0.0657  0.0064  81  HIS B CG  
3559  N ND1 . HIS B 81  ? 0.8953 0.8098 0.8708 0.0046  0.0565  0.0111  81  HIS B ND1 
3560  C CD2 . HIS B 81  ? 0.8436 0.7580 0.8054 0.0119  0.0552  0.0067  81  HIS B CD2 
3561  C CE1 . HIS B 81  ? 0.9034 0.8008 0.8490 0.0070  0.0385  0.0140  81  HIS B CE1 
3562  N NE2 . HIS B 81  ? 0.8827 0.7800 0.8203 0.0099  0.0375  0.0101  81  HIS B NE2 
3563  N N   . GLN B 82  ? 0.6352 0.6930 0.7957 0.0069  0.0659  -0.0213 82  GLN B N   
3564  C CA  . GLN B 82  ? 0.5590 0.6560 0.7744 0.0080  0.0654  -0.0324 82  GLN B CA  
3565  C C   . GLN B 82  ? 0.4369 0.5603 0.6602 0.0212  0.0406  -0.0352 82  GLN B C   
3566  O O   . GLN B 82  ? 0.4168 0.5387 0.6208 0.0218  0.0227  -0.0353 82  GLN B O   
3567  C CB  . GLN B 82  ? 0.6068 0.7171 0.8541 -0.0058 0.0665  -0.0426 82  GLN B CB  
3568  C CG  . GLN B 82  ? 0.6501 0.8073 0.9529 -0.0044 0.0511  -0.0579 82  GLN B CG  
3569  C CD  . GLN B 82  ? 0.6866 0.8574 1.0234 -0.0204 0.0506  -0.0721 82  GLN B CD  
3570  O OE1 . GLN B 82  ? 0.7330 0.8756 1.0539 -0.0323 0.0668  -0.0689 82  GLN B OE1 
3571  N NE2 . GLN B 82  ? 0.6563 0.8689 1.0395 -0.0200 0.0308  -0.0885 82  GLN B NE2 
3572  N N   . CYS B 83  ? 0.3835 0.5272 0.6329 0.0332  0.0415  -0.0367 83  CYS B N   
3573  C CA  . CYS B 83  ? 0.3423 0.5042 0.5909 0.0501  0.0183  -0.0364 83  CYS B CA  
3574  C C   . CYS B 83  ? 0.3237 0.5229 0.6066 0.0511  -0.0066 -0.0494 83  CYS B C   
3575  O O   . CYS B 83  ? 0.3300 0.5546 0.6613 0.0404  -0.0042 -0.0619 83  CYS B O   
3576  C CB  . CYS B 83  ? 0.3229 0.4899 0.5857 0.0660  0.0276  -0.0318 83  CYS B CB  
3577  S SG  . CYS B 83  ? 0.4392 0.5559 0.6463 0.0670  0.0503  -0.0187 83  CYS B SG  
3578  N N   . PHE B 84  ? 0.2919 0.4906 0.5467 0.0641  -0.0295 -0.0472 84  PHE B N   
3579  C CA  . PHE B 84  ? 0.2454 0.4687 0.5122 0.0659  -0.0571 -0.0595 84  PHE B CA  
3580  C C   . PHE B 84  ? 0.3029 0.5548 0.5907 0.0885  -0.0790 -0.0612 84  PHE B C   
3581  O O   . PHE B 84  ? 0.3237 0.5607 0.5864 0.1073  -0.0772 -0.0480 84  PHE B O   
3582  C CB  . PHE B 84  ? 0.2435 0.4365 0.4527 0.0647  -0.0652 -0.0556 84  PHE B CB  
3583  C CG  . PHE B 84  ? 0.2636 0.4703 0.4701 0.0638  -0.0909 -0.0696 84  PHE B CG  
3584  C CD1 . PHE B 84  ? 0.2870 0.4964 0.4677 0.0840  -0.1162 -0.0696 84  PHE B CD1 
3585  C CD2 . PHE B 84  ? 0.2513 0.4618 0.4736 0.0436  -0.0890 -0.0827 84  PHE B CD2 
3586  C CE1 . PHE B 84  ? 0.2979 0.5145 0.4658 0.0835  -0.1420 -0.0841 84  PHE B CE1 
3587  C CE2 . PHE B 84  ? 0.2577 0.4763 0.4727 0.0413  -0.1120 -0.0981 84  PHE B CE2 
3588  C CZ  . PHE B 84  ? 0.3061 0.5274 0.4914 0.0609  -0.1396 -0.0994 84  PHE B CZ  
3589  N N   . THR B 85  ? 0.3498 0.6428 0.6871 0.0868  -0.1004 -0.0782 85  THR B N   
3590  C CA  . THR B 85  ? 0.3988 0.7242 0.7602 0.1097  -0.1300 -0.0822 85  THR B CA  
3591  C C   . THR B 85  ? 0.3909 0.7314 0.7419 0.1098  -0.1674 -0.0980 85  THR B C   
3592  O O   . THR B 85  ? 0.3890 0.7437 0.7682 0.0875  -0.1691 -0.1154 85  THR B O   
3593  C CB  . THR B 85  ? 0.4380 0.8029 0.8803 0.1089  -0.1210 -0.0888 85  THR B CB  
3594  O OG1 . THR B 85  ? 0.4267 0.7737 0.8722 0.1124  -0.0864 -0.0755 85  THR B OG1 
3595  C CG2 . THR B 85  ? 0.5073 0.8949 0.9622 0.1293  -0.1497 -0.0873 85  THR B CG2 
3596  N N   . CYS B 86  ? 0.4294 0.7546 0.7270 0.1336  -0.1925 -0.0901 86  CYS B N   
3597  C CA  . CYS B 86  ? 0.5174 0.8399 0.7810 0.1346  -0.2252 -0.1016 86  CYS B CA  
3598  C C   . CYS B 86  ? 0.5751 0.9333 0.8826 0.1392  -0.2501 -0.1108 86  CYS B C   
3599  O O   . CYS B 86  ? 0.5366 0.9020 0.8495 0.1613  -0.2586 -0.0988 86  CYS B O   
3600  C CB  . CYS B 86  ? 0.5791 0.8570 0.7522 0.1576  -0.2364 -0.0874 86  CYS B CB  
3601  S SG  . CYS B 86  ? 0.5327 0.7912 0.6456 0.1541  -0.2677 -0.1031 86  CYS B SG  
3602  N N   . THR B 87  ? 0.6652 1.0445 1.0044 0.1182  -0.2615 -0.1326 87  THR B N   
3603  C CA  . THR B 87  ? 0.7429 1.1597 1.1305 0.1182  -0.2869 -0.1464 87  THR B CA  
3604  C C   . THR B 87  ? 0.8402 1.2473 1.1796 0.1201  -0.3240 -0.1601 87  THR B C   
3605  O O   . THR B 87  ? 0.9165 1.3551 1.2968 0.1142  -0.3474 -0.1774 87  THR B O   
3606  C CB  . THR B 87  ? 0.7022 1.1516 1.1745 0.0906  -0.2672 -0.1632 87  THR B CB  
3607  O OG1 . THR B 87  ? 0.6926 1.1238 1.1496 0.0657  -0.2550 -0.1760 87  THR B OG1 
3608  C CG2 . THR B 87  ? 0.6456 1.1020 1.1636 0.0898  -0.2296 -0.1502 87  THR B CG2 
3609  N N   . ASP B 88  ? 0.8359 1.1974 1.0876 0.1281  -0.3281 -0.1534 88  ASP B N   
3610  C CA  . ASP B 88  ? 0.8846 1.2247 1.0733 0.1325  -0.3593 -0.1639 88  ASP B CA  
3611  C C   . ASP B 88  ? 0.9388 1.2566 1.0663 0.1657  -0.3816 -0.1471 88  ASP B C   
3612  O O   . ASP B 88  ? 0.9972 1.3443 1.1546 0.1782  -0.4084 -0.1495 88  ASP B O   
3613  C CB  . ASP B 88  ? 0.8859 1.1824 1.0110 0.1192  -0.3456 -0.1684 88  ASP B CB  
3614  C CG  . ASP B 88  ? 0.8570 1.1712 1.0364 0.0856  -0.3279 -0.1880 88  ASP B CG  
3615  O OD1 . ASP B 88  ? 0.8830 1.2376 1.1339 0.0718  -0.3351 -0.2037 88  ASP B OD1 
3616  O OD2 . ASP B 88  ? 0.8132 1.0991 0.9649 0.0732  -0.3050 -0.1875 88  ASP B OD2 
3617  N N   . SER B 89  ? 0.9401 1.2034 0.9804 0.1802  -0.3703 -0.1305 89  SER B N   
3618  C CA  . SER B 89  ? 1.0402 1.2723 1.0167 0.2121  -0.3832 -0.1116 89  SER B CA  
3619  C C   . SER B 89  ? 1.0428 1.3020 1.0758 0.2264  -0.3725 -0.0949 89  SER B C   
3620  O O   . SER B 89  ? 1.0095 1.2942 1.1059 0.2116  -0.3476 -0.0953 89  SER B O   
3621  C CB  . SER B 89  ? 1.0742 1.2362 0.9489 0.2215  -0.3623 -0.0967 89  SER B CB  
3622  O OG  . SER B 89  ? 1.1284 1.2547 0.9500 0.2513  -0.3585 -0.0731 89  SER B OG  
3623  N N   . THR B 90  ? 1.0768 1.3299 1.0897 0.2544  -0.3891 -0.0808 90  THR B N   
3624  C CA  . THR B 90  ? 1.0475 1.3137 1.1018 0.2690  -0.3713 -0.0618 90  THR B CA  
3625  C C   . THR B 90  ? 1.0755 1.2788 1.0455 0.2911  -0.3503 -0.0368 90  THR B C   
3626  O O   . THR B 90  ? 1.0771 1.2774 1.0619 0.3075  -0.3356 -0.0188 90  THR B O   
3627  C CB  . THR B 90  ? 0.9928 1.3062 1.1100 0.2841  -0.3985 -0.0620 90  THR B CB  
3628  O OG1 . THR B 90  ? 0.9344 1.2692 1.1147 0.2884  -0.3725 -0.0488 90  THR B OG1 
3629  C CG2 . THR B 90  ? 1.0789 1.3626 1.1275 0.3149  -0.4269 -0.0504 90  THR B CG2 
3630  N N   . THR B 91  ? 1.0977 1.2481 0.9804 0.2905  -0.3456 -0.0364 91  THR B N   
3631  C CA  . THR B 91  ? 1.0957 1.1807 0.9002 0.3049  -0.3150 -0.0147 91  THR B CA  
3632  C C   . THR B 91  ? 1.0080 1.0677 0.7911 0.2843  -0.2846 -0.0172 91  THR B C   
3633  O O   . THR B 91  ? 0.9656 1.0437 0.7650 0.2627  -0.2932 -0.0363 91  THR B O   
3634  C CB  . THR B 91  ? 1.2004 1.2316 0.9100 0.3271  -0.3288 -0.0072 91  THR B CB  
3635  O OG1 . THR B 91  ? 1.2144 1.1790 0.8534 0.3385  -0.2916 0.0132  91  THR B OG1 
3636  C CG2 . THR B 91  ? 1.2330 1.2523 0.9011 0.3141  -0.3481 -0.0264 91  THR B CG2 
3637  N N   . THR B 92  ? 0.9739 0.9893 0.7200 0.2910  -0.2489 0.0016  92  THR B N   
3638  C CA  . THR B 92  ? 0.9066 0.9045 0.6457 0.2726  -0.2201 0.0012  92  THR B CA  
3639  C C   . THR B 92  ? 0.9082 0.8503 0.5658 0.2678  -0.2092 -0.0002 92  THR B C   
3640  O O   . THR B 92  ? 0.9650 0.8551 0.5484 0.2834  -0.2055 0.0084  92  THR B O   
3641  C CB  . THR B 92  ? 0.8976 0.8725 0.6406 0.2780  -0.1828 0.0210  92  THR B CB  
3642  O OG1 . THR B 92  ? 0.9761 0.8856 0.6420 0.2955  -0.1624 0.0384  92  THR B OG1 
3643  C CG2 . THR B 92  ? 0.8686 0.8902 0.6870 0.2827  -0.1865 0.0231  92  THR B CG2 
3644  N N   . ARG B 93  ? 0.8136 0.7642 0.4904 0.2436  -0.1973 -0.0107 93  ARG B N   
3645  C CA  . ARG B 93  ? 0.7964 0.7009 0.4173 0.2293  -0.1783 -0.0157 93  ARG B CA  
3646  C C   . ARG B 93  ? 0.6908 0.6162 0.3735 0.1949  -0.1508 -0.0236 93  ARG B C   
3647  O O   . ARG B 93  ? 0.5756 0.5507 0.3341 0.1839  -0.1539 -0.0276 93  ARG B O   
3648  C CB  . ARG B 93  ? 0.8903 0.7958 0.4749 0.2314  -0.2144 -0.0342 93  ARG B CB  
3649  C CG  . ARG B 93  ? 0.8880 0.8648 0.5548 0.2152  -0.2457 -0.0565 93  ARG B CG  
3650  C CD  . ARG B 93  ? 0.9867 0.9610 0.6321 0.2017  -0.2659 -0.0789 93  ARG B CD  
3651  N NE  . ARG B 93  ? 1.0065 1.0489 0.7418 0.1824  -0.2889 -0.1006 93  ARG B NE  
3652  C CZ  . ARG B 93  ? 1.0047 1.0691 0.7850 0.1561  -0.2792 -0.1167 93  ARG B CZ  
3653  N NH1 . ARG B 93  ? 0.9566 0.9811 0.7135 0.1409  -0.2377 -0.1085 93  ARG B NH1 
3654  N NH2 . ARG B 93  ? 1.0159 1.1381 0.8814 0.1380  -0.2939 -0.1349 93  ARG B NH2 
3655  N N   . PRO B 94  ? 0.7003 0.5858 0.3507 0.1794  -0.1229 -0.0255 94  PRO B N   
3656  C CA  . PRO B 94  ? 0.5827 0.4877 0.2898 0.1493  -0.1017 -0.0336 94  PRO B CA  
3657  C C   . PRO B 94  ? 0.5458 0.5045 0.3107 0.1331  -0.1272 -0.0534 94  PRO B C   
3658  O O   . PRO B 94  ? 0.5852 0.5462 0.3259 0.1345  -0.1531 -0.0690 94  PRO B O   
3659  C CB  . PRO B 94  ? 0.6234 0.4752 0.2761 0.1425  -0.0772 -0.0355 94  PRO B CB  
3660  C CG  . PRO B 94  ? 0.6946 0.4907 0.2698 0.1671  -0.0664 -0.0201 94  PRO B CG  
3661  C CD  . PRO B 94  ? 0.7403 0.5560 0.2990 0.1913  -0.1059 -0.0185 94  PRO B CD  
3662  N N   . GLY B 95  ? 0.4786 0.4755 0.3150 0.1176  -0.1189 -0.0539 95  GLY B N   
3663  C CA  . GLY B 95  ? 0.4746 0.5182 0.3699 0.1011  -0.1355 -0.0716 95  GLY B CA  
3664  C C   . GLY B 95  ? 0.4535 0.5445 0.3940 0.1115  -0.1618 -0.0756 95  GLY B C   
3665  O O   . GLY B 95  ? 0.4462 0.5787 0.4490 0.0969  -0.1694 -0.0892 95  GLY B O   
3666  N N   . CYS B 96  ? 0.4978 0.5808 0.4100 0.1376  -0.1730 -0.0633 96  CYS B N   
3667  C CA  . CYS B 96  ? 0.4914 0.6189 0.4483 0.1524  -0.1990 -0.0660 96  CYS B CA  
3668  C C   . CYS B 96  ? 0.4851 0.6029 0.4392 0.1727  -0.1855 -0.0447 96  CYS B C   
3669  O O   . CYS B 96  ? 0.5112 0.5992 0.4098 0.1985  -0.1938 -0.0325 96  CYS B O   
3670  C CB  . CYS B 96  ? 0.5331 0.6674 0.4587 0.1698  -0.2423 -0.0782 96  CYS B CB  
3671  S SG  . CYS B 96  ? 0.9825 1.1696 0.9677 0.1879  -0.2740 -0.0805 96  CYS B SG  
3672  N N   . HIS B 97  ? 0.4082 0.5447 0.4160 0.1613  -0.1627 -0.0403 97  HIS B N   
3673  C CA  . HIS B 97  ? 0.4774 0.6102 0.4936 0.1785  -0.1502 -0.0242 97  HIS B CA  
3674  C C   . HIS B 97  ? 0.4362 0.6140 0.5318 0.1695  -0.1442 -0.0301 97  HIS B C   
3675  O O   . HIS B 97  ? 0.3605 0.5673 0.5021 0.1482  -0.1448 -0.0450 97  HIS B O   
3676  C CB  . HIS B 97  ? 0.4667 0.5512 0.4434 0.1742  -0.1152 -0.0085 97  HIS B CB  
3677  C CG  . HIS B 97  ? 0.4761 0.5129 0.3838 0.1762  -0.1095 -0.0041 97  HIS B CG  
3678  N ND1 . HIS B 97  ? 0.4524 0.4783 0.3518 0.1546  -0.1006 -0.0126 97  HIS B ND1 
3679  C CD2 . HIS B 97  ? 0.5361 0.5293 0.3792 0.1981  -0.1076 0.0083  97  HIS B CD2 
3680  C CE1 . HIS B 97  ? 0.4712 0.4503 0.3074 0.1620  -0.0919 -0.0067 97  HIS B CE1 
3681  N NE2 . HIS B 97  ? 0.5490 0.5054 0.3470 0.1880  -0.0952 0.0062  97  HIS B NE2 
3682  N N   . ASN B 98  ? 0.4875 0.6658 0.5970 0.1864  -0.1343 -0.0181 98  ASN B N   
3683  C CA  . ASN B 98  ? 0.5134 0.7188 0.6866 0.1780  -0.1161 -0.0204 98  ASN B CA  
3684  C C   . ASN B 98  ? 0.4719 0.6362 0.6161 0.1692  -0.0803 -0.0078 98  ASN B C   
3685  O O   . ASN B 98  ? 0.4202 0.5431 0.5080 0.1756  -0.0727 0.0032  98  ASN B O   
3686  C CB  . ASN B 98  ? 0.6224 0.8591 0.8386 0.2035  -0.1298 -0.0183 98  ASN B CB  
3687  C CG  . ASN B 98  ? 0.7059 0.9908 0.9696 0.2036  -0.1638 -0.0345 98  ASN B CG  
3688  O OD1 . ASN B 98  ? 0.5949 0.9007 0.8845 0.1814  -0.1696 -0.0514 98  ASN B OD1 
3689  N ND2 . ASN B 98  ? 0.9347 1.2295 1.2048 0.2233  -0.1826 -0.0281 98  ASN B ND2 
3690  N N   . ASN B 99  ? 0.4834 0.6562 0.6641 0.1536  -0.0579 -0.0107 99  ASN B N   
3691  C CA  . ASN B 99  ? 0.5429 0.6775 0.6945 0.1432  -0.0289 -0.0024 99  ASN B CA  
3692  C C   . ASN B 99  ? 0.4757 0.5815 0.5858 0.1262  -0.0254 -0.0020 99  ASN B C   
3693  O O   . ASN B 99  ? 0.4593 0.5306 0.5370 0.1233  -0.0096 0.0055  99  ASN B O   
3694  C CB  . ASN B 99  ? 0.7138 0.8208 0.8385 0.1642  -0.0185 0.0110  99  ASN B CB  
3695  C CG  . ASN B 99  ? 0.8573 0.9307 0.9645 0.1531  0.0111  0.0154  99  ASN B CG  
3696  O OD1 . ASN B 99  ? 0.9006 0.9786 1.0264 0.1361  0.0241  0.0095  99  ASN B OD1 
3697  N ND2 . ASN B 99  ? 0.9168 0.9515 0.9833 0.1616  0.0220  0.0248  99  ASN B ND2 
3698  N N   . THR B 100 ? 0.4102 0.5308 0.5271 0.1142  -0.0391 -0.0114 100 THR B N   
3699  C CA  . THR B 100 ? 0.3481 0.4461 0.4386 0.0977  -0.0335 -0.0121 100 THR B CA  
3700  C C   . THR B 100 ? 0.2885 0.3983 0.4089 0.0773  -0.0245 -0.0190 100 THR B C   
3701  O O   . THR B 100 ? 0.2474 0.3736 0.4003 0.0761  -0.0164 -0.0212 100 THR B O   
3702  C CB  . THR B 100 ? 0.3525 0.4480 0.4195 0.1005  -0.0510 -0.0168 100 THR B CB  
3703  O OG1 . THR B 100 ? 0.3179 0.4493 0.4150 0.1042  -0.0727 -0.0283 100 THR B OG1 
3704  C CG2 . THR B 100 ? 0.3610 0.4266 0.3808 0.1198  -0.0519 -0.0064 100 THR B CG2 
3705  N N   . CYS B 101 ? 0.3366 0.4344 0.4461 0.0624  -0.0226 -0.0214 101 CYS B N   
3706  C CA  . CYS B 101 ? 0.3175 0.4218 0.4512 0.0457  -0.0135 -0.0263 101 CYS B CA  
3707  C C   . CYS B 101 ? 0.2618 0.3771 0.4083 0.0349  -0.0219 -0.0367 101 CYS B C   
3708  O O   . CYS B 101 ? 0.2682 0.3755 0.3939 0.0362  -0.0314 -0.0389 101 CYS B O   
3709  C CB  A CYS B 101 ? 0.3397 0.4150 0.4518 0.0375  0.0004  -0.0183 101 CYS B CB  
3710  C CB  B CYS B 101 ? 0.3390 0.4139 0.4502 0.0374  -0.0002 -0.0184 101 CYS B CB  
3711  S SG  A CYS B 101 ? 0.3640 0.4122 0.4425 0.0384  -0.0019 -0.0122 101 CYS B SG  
3712  S SG  B CYS B 101 ? 0.3141 0.3630 0.3925 0.0471  0.0040  -0.0090 101 CYS B SG  
3713  N N   . GLY B 102 ? 0.2670 0.3968 0.4475 0.0235  -0.0145 -0.0439 102 GLY B N   
3714  C CA  . GLY B 102 ? 0.2805 0.4214 0.4803 0.0114  -0.0198 -0.0565 102 GLY B CA  
3715  C C   . GLY B 102 ? 0.2722 0.3877 0.4599 -0.0017 -0.0063 -0.0528 102 GLY B C   
3716  O O   . GLY B 102 ? 0.2628 0.3593 0.4420 -0.0049 0.0089  -0.0433 102 GLY B O   
3717  N N   . LEU B 103 ? 0.2790 0.3916 0.4629 -0.0080 -0.0129 -0.0608 103 LEU B N   
3718  C CA  . LEU B 103 ? 0.3286 0.4172 0.5035 -0.0177 -0.0016 -0.0573 103 LEU B CA  
3719  C C   . LEU B 103 ? 0.2943 0.3910 0.4920 -0.0305 -0.0017 -0.0736 103 LEU B C   
3720  O O   . LEU B 103 ? 0.2724 0.3811 0.4682 -0.0296 -0.0174 -0.0864 103 LEU B O   
3721  C CB  . LEU B 103 ? 0.4057 0.4732 0.5476 -0.0108 -0.0052 -0.0491 103 LEU B CB  
3722  C CG  . LEU B 103 ? 0.4725 0.5153 0.6078 -0.0156 0.0051  -0.0410 103 LEU B CG  
3723  C CD1 . LEU B 103 ? 0.5333 0.5662 0.6696 -0.0169 0.0144  -0.0307 103 LEU B CD1 
3724  C CD2 . LEU B 103 ? 0.4739 0.5033 0.5891 -0.0077 0.0022  -0.0343 103 LEU B CD2 
3725  N N   . LEU B 104 ? 0.2813 0.3667 0.4959 -0.0423 0.0161  -0.0737 104 LEU B N   
3726  C CA  . LEU B 104 ? 0.2542 0.3426 0.4929 -0.0570 0.0204  -0.0903 104 LEU B CA  
3727  C C   . LEU B 104 ? 0.2659 0.3285 0.4814 -0.0596 0.0223  -0.0905 104 LEU B C   
3728  O O   . LEU B 104 ? 0.2943 0.3300 0.4937 -0.0567 0.0342  -0.0756 104 LEU B O   
3729  C CB  . LEU B 104 ? 0.2919 0.3714 0.5567 -0.0684 0.0450  -0.0893 104 LEU B CB  
3730  C CG  . LEU B 104 ? 0.3953 0.4890 0.7031 -0.0861 0.0507  -0.1117 104 LEU B CG  
3731  C CD1 . LEU B 104 ? 0.4009 0.5410 0.7504 -0.0868 0.0330  -0.1296 104 LEU B CD1 
3732  C CD2 . LEU B 104 ? 0.4571 0.5244 0.7795 -0.0978 0.0836  -0.1073 104 LEU B CD2 
3733  N N   . SER B 105 ? 0.2886 0.3581 0.5018 -0.0638 0.0097  -0.1078 105 SER B N   
3734  C CA  . SER B 105 ? 0.2668 0.3091 0.4585 -0.0671 0.0152  -0.1113 105 SER B CA  
3735  C C   . SER B 105 ? 0.2873 0.3251 0.5025 -0.0853 0.0244  -0.1309 105 SER B C   
3736  O O   . SER B 105 ? 0.3050 0.3689 0.5471 -0.0945 0.0136  -0.1501 105 SER B O   
3737  C CB  . SER B 105 ? 0.2804 0.3214 0.4373 -0.0578 -0.0021 -0.1170 105 SER B CB  
3738  O OG  . SER B 105 ? 0.3439 0.3853 0.4806 -0.0422 -0.0070 -0.1000 105 SER B OG  
3739  N N   . SER B 106 ? 0.3464 0.3517 0.5543 -0.0903 0.0431  -0.1279 106 SER B N   
3740  C CA  . SER B 106 ? 0.3510 0.3446 0.5804 -0.1088 0.0570  -0.1464 106 SER B CA  
3741  C C   . SER B 106 ? 0.3667 0.3342 0.5705 -0.1123 0.0594  -0.1588 106 SER B C   
3742  O O   . SER B 106 ? 0.3798 0.3246 0.5576 -0.1009 0.0660  -0.1448 106 SER B O   
3743  C CB  A SER B 106 ? 0.3875 0.3565 0.6330 -0.1126 0.0852  -0.1319 106 SER B CB  
3744  C CB  B SER B 106 ? 0.3875 0.3573 0.6336 -0.1127 0.0850  -0.1321 106 SER B CB  
3745  O OG  A SER B 106 ? 0.3988 0.3834 0.6644 -0.1124 0.0894  -0.1237 106 SER B OG  
3746  O OG  B SER B 106 ? 0.4354 0.3679 0.6664 -0.1107 0.1016  -0.1250 106 SER B OG  
3747  N N   . ASN B 107 ? 0.2506 0.3741 0.4069 -0.0341 -0.0248 -0.0584 107 ASN B N   
3748  C CA  . ASN B 107 ? 0.2458 0.3588 0.3900 -0.0374 -0.0324 -0.0655 107 ASN B CA  
3749  C C   . ASN B 107 ? 0.2939 0.3885 0.4437 -0.0479 -0.0164 -0.0638 107 ASN B C   
3750  O O   . ASN B 107 ? 0.2578 0.3592 0.4386 -0.0580 -0.0085 -0.0688 107 ASN B O   
3751  C CB  . ASN B 107 ? 0.2542 0.3872 0.4186 -0.0398 -0.0495 -0.0819 107 ASN B CB  
3752  C CG  . ASN B 107 ? 0.3215 0.4430 0.4695 -0.0424 -0.0581 -0.0922 107 ASN B CG  
3753  O OD1 . ASN B 107 ? 0.2902 0.3906 0.4293 -0.0477 -0.0475 -0.0908 107 ASN B OD1 
3754  N ND2 . ASN B 107 ? 0.2802 0.4157 0.4245 -0.0380 -0.0776 -0.1033 107 ASN B ND2 
3755  N N   . PRO B 108 ? 0.3133 0.3846 0.4351 -0.0450 -0.0103 -0.0552 108 PRO B N   
3756  C CA  . PRO B 108 ? 0.3205 0.3704 0.4427 -0.0518 0.0053  -0.0491 108 PRO B CA  
3757  C C   . PRO B 108 ? 0.3745 0.4161 0.5129 -0.0618 0.0049  -0.0617 108 PRO B C   
3758  O O   . PRO B 108 ? 0.3940 0.4187 0.5422 -0.0696 0.0187  -0.0581 108 PRO B O   
3759  C CB  . PRO B 108 ? 0.3486 0.3813 0.4377 -0.0426 0.0065  -0.0378 108 PRO B CB  
3760  C CG  . PRO B 108 ? 0.3280 0.3689 0.4023 -0.0351 -0.0083 -0.0432 108 PRO B CG  
3761  C CD  . PRO B 108 ? 0.3090 0.3737 0.3988 -0.0342 -0.0179 -0.0495 108 PRO B CD  
3762  N N   . VAL B 109 ? 0.3453 0.3975 0.4850 -0.0612 -0.0110 -0.0765 109 VAL B N   
3763  C CA  . VAL B 109 ? 0.3392 0.3854 0.4937 -0.0704 -0.0148 -0.0928 109 VAL B CA  
3764  C C   . VAL B 109 ? 0.3452 0.4096 0.5423 -0.0826 -0.0155 -0.1041 109 VAL B C   
3765  O O   . VAL B 109 ? 0.3867 0.4403 0.6078 -0.0951 -0.0064 -0.1099 109 VAL B O   
3766  C CB  . VAL B 109 ? 0.3785 0.4287 0.5116 -0.0636 -0.0324 -0.1052 109 VAL B CB  
3767  C CG1 . VAL B 109 ? 0.4240 0.4709 0.5740 -0.0737 -0.0391 -0.1268 109 VAL B CG1 
3768  C CG2 . VAL B 109 ? 0.3456 0.3774 0.4417 -0.0529 -0.0282 -0.0946 109 VAL B CG2 
3769  N N   . THR B 110 ? 0.3445 0.4371 0.5542 -0.0791 -0.0266 -0.1075 110 THR B N   
3770  C CA  . THR B 110 ? 0.3228 0.4385 0.5787 -0.0899 -0.0287 -0.1192 110 THR B CA  
3771  C C   . THR B 110 ? 0.3562 0.4763 0.6326 -0.0935 -0.0088 -0.1059 110 THR B C   
3772  O O   . THR B 110 ? 0.3591 0.4957 0.6788 -0.1046 -0.0035 -0.1132 110 THR B O   
3773  C CB  . THR B 110 ? 0.3112 0.4578 0.5755 -0.0831 -0.0521 -0.1306 110 THR B CB  
3774  O OG1 . THR B 110 ? 0.3091 0.4644 0.5569 -0.0699 -0.0521 -0.1162 110 THR B OG1 
3775  C CG2 . THR B 110 ? 0.3087 0.4502 0.5452 -0.0779 -0.0710 -0.1426 110 THR B CG2 
3776  N N   . GLN B 111 ? 0.3630 0.4700 0.6091 -0.0843 0.0020  -0.0877 111 GLN B N   
3777  C CA  . GLN B 111 ? 0.4223 0.5321 0.6782 -0.0852 0.0210  -0.0749 111 GLN B CA  
3778  C C   . GLN B 111 ? 0.4351 0.5775 0.7163 -0.0809 0.0151  -0.0794 111 GLN B C   
3779  O O   . GLN B 111 ? 0.4153 0.5646 0.7123 -0.0827 0.0316  -0.0726 111 GLN B O   
3780  C CB  . GLN B 111 ? 0.4902 0.5879 0.7726 -0.1004 0.0413  -0.0734 111 GLN B CB  
3781  C CG  . GLN B 111 ? 0.5995 0.6610 0.8570 -0.1027 0.0521  -0.0640 111 GLN B CG  
3782  C CD  . GLN B 111 ? 0.7638 0.8080 0.9816 -0.0917 0.0617  -0.0444 111 GLN B CD  
3783  O OE1 . GLN B 111 ? 0.8013 0.8356 0.9858 -0.0811 0.0518  -0.0405 111 GLN B OE1 
3784  N NE2 . GLN B 111 ? 0.8378 0.8804 1.0595 -0.0940 0.0810  -0.0326 111 GLN B NE2 
3785  N N   . GLU B 112 ? 0.4276 0.5892 0.7118 -0.0744 -0.0080 -0.0904 112 GLU B N   
3786  C CA  . GLU B 112 ? 0.3820 0.5727 0.6848 -0.0659 -0.0176 -0.0932 112 GLU B CA  
3787  C C   . GLU B 112 ? 0.2899 0.4731 0.5623 -0.0524 -0.0122 -0.0784 112 GLU B C   
3788  O O   . GLU B 112 ? 0.2678 0.4289 0.5003 -0.0466 -0.0126 -0.0695 112 GLU B O   
3789  C CB  . GLU B 112 ? 0.4304 0.6378 0.7323 -0.0593 -0.0457 -0.1055 112 GLU B CB  
3790  C CG  . GLU B 112 ? 0.4818 0.7075 0.8204 -0.0700 -0.0590 -0.1252 112 GLU B CG  
3791  C CD  . GLU B 112 ? 0.5379 0.7691 0.8540 -0.0615 -0.0871 -0.1353 112 GLU B CD  
3792  O OE1 . GLU B 112 ? 0.5146 0.7235 0.7827 -0.0533 -0.0897 -0.1277 112 GLU B OE1 
3793  O OE2 . GLU B 112 ? 0.5733 0.8324 0.9197 -0.0622 -0.1064 -0.1505 112 GLU B OE2 
3794  N N   . SER B 113 ? 0.2298 0.4325 0.5237 -0.0471 -0.0079 -0.0772 113 SER B N   
3795  C CA  . SER B 113 ? 0.3373 0.5339 0.6044 -0.0333 -0.0072 -0.0668 113 SER B CA  
3796  C C   . SER B 113 ? 0.2687 0.4919 0.5590 -0.0226 -0.0204 -0.0720 113 SER B C   
3797  O O   . SER B 113 ? 0.2328 0.4825 0.5651 -0.0263 -0.0265 -0.0829 113 SER B O   
3798  C CB  . SER B 113 ? 0.3358 0.5192 0.5937 -0.0349 0.0174  -0.0566 113 SER B CB  
3799  O OG  . SER B 113 ? 0.3709 0.5749 0.6695 -0.0400 0.0309  -0.0612 113 SER B OG  
3800  N N   . GLY B 114 ? 0.2419 0.4576 0.5064 -0.0090 -0.0260 -0.0644 114 GLY B N   
3801  C CA  . GLY B 114 ? 0.2600 0.4962 0.5432 0.0036  -0.0384 -0.0669 114 GLY B CA  
3802  C C   . GLY B 114 ? 0.2443 0.4661 0.5039 0.0155  -0.0322 -0.0571 114 GLY B C   
3803  O O   . GLY B 114 ? 0.2700 0.4663 0.4925 0.0152  -0.0270 -0.0488 114 GLY B O   
3804  N N   . LEU B 115 ? 0.2565 0.4944 0.5396 0.0262  -0.0337 -0.0589 115 LEU B N   
3805  C CA  . LEU B 115 ? 0.2992 0.5216 0.5621 0.0374  -0.0279 -0.0516 115 LEU B CA  
3806  C C   . LEU B 115 ? 0.3193 0.5299 0.5569 0.0489  -0.0469 -0.0448 115 LEU B C   
3807  O O   . LEU B 115 ? 0.3478 0.5743 0.6016 0.0581  -0.0641 -0.0466 115 LEU B O   
3808  C CB  . LEU B 115 ? 0.2803 0.5218 0.5791 0.0451  -0.0185 -0.0567 115 LEU B CB  
3809  C CG  . LEU B 115 ? 0.2704 0.4931 0.5492 0.0547  -0.0077 -0.0523 115 LEU B CG  
3810  C CD1 . LEU B 115 ? 0.2710 0.4762 0.5272 0.0454  0.0146  -0.0505 115 LEU B CD1 
3811  C CD2 . LEU B 115 ? 0.2834 0.5268 0.6001 0.0665  -0.0049 -0.0583 115 LEU B CD2 
3812  N N   . GLY B 116 ? 0.2941 0.4773 0.4929 0.0484  -0.0436 -0.0365 116 GLY B N   
3813  C CA  . GLY B 116 ? 0.2903 0.4593 0.4644 0.0577  -0.0573 -0.0282 116 GLY B CA  
3814  C C   . GLY B 116 ? 0.2895 0.4446 0.4582 0.0673  -0.0515 -0.0237 116 GLY B C   
3815  O O   . GLY B 116 ? 0.2743 0.4311 0.4555 0.0673  -0.0374 -0.0283 116 GLY B O   
3816  N N   . GLU B 117 ? 0.3074 0.4473 0.4567 0.0756  -0.0615 -0.0149 117 GLU B N   
3817  C CA  . GLU B 117 ? 0.2476 0.3703 0.3920 0.0845  -0.0576 -0.0106 117 GLU B CA  
3818  C C   . GLU B 117 ? 0.2582 0.3547 0.3704 0.0785  -0.0530 -0.0038 117 GLU B C   
3819  O O   . GLU B 117 ? 0.2708 0.3608 0.3633 0.0750  -0.0596 0.0028  117 GLU B O   
3820  C CB  . GLU B 117 ? 0.2622 0.3870 0.4145 0.0995  -0.0724 -0.0044 117 GLU B CB  
3821  C CG  . GLU B 117 ? 0.2750 0.3828 0.4308 0.1106  -0.0686 -0.0012 117 GLU B CG  
3822  C CD  . GLU B 117 ? 0.2942 0.3984 0.4519 0.1260  -0.0838 0.0089  117 GLU B CD  
3823  O OE1 . GLU B 117 ? 0.3868 0.4817 0.5200 0.1258  -0.0932 0.0194  117 GLU B OE1 
3824  O OE2 . GLU B 117 ? 0.3675 0.4776 0.5503 0.1393  -0.0860 0.0071  117 GLU B OE2 
3825  N N   . LEU B 118 ? 0.2669 0.3490 0.3741 0.0773  -0.0419 -0.0063 118 LEU B N   
3826  C CA  . LEU B 118 ? 0.2837 0.3430 0.3656 0.0717  -0.0393 -0.0011 118 LEU B CA  
3827  C C   . LEU B 118 ? 0.3044 0.3482 0.3773 0.0783  -0.0481 0.0098  118 LEU B C   
3828  O O   . LEU B 118 ? 0.3224 0.3634 0.4069 0.0896  -0.0528 0.0125  118 LEU B O   
3829  C CB  . LEU B 118 ? 0.2879 0.3355 0.3666 0.0703  -0.0283 -0.0082 118 LEU B CB  
3830  C CG  . LEU B 118 ? 0.3007 0.3287 0.3576 0.0632  -0.0268 -0.0056 118 LEU B CG  
3831  C CD1 . LEU B 118 ? 0.2808 0.3138 0.3245 0.0529  -0.0253 -0.0039 118 LEU B CD1 
3832  C CD2 . LEU B 118 ? 0.2694 0.2848 0.3229 0.0642  -0.0198 -0.0143 118 LEU B CD2 
3833  N N   . ALA B 119 ? 0.2629 0.2963 0.3160 0.0718  -0.0493 0.0171  119 ALA B N   
3834  C CA  . ALA B 119 ? 0.2775 0.2961 0.3200 0.0765  -0.0547 0.0293  119 ALA B CA  
3835  C C   . ALA B 119 ? 0.3315 0.3315 0.3617 0.0684  -0.0485 0.0330  119 ALA B C   
3836  O O   . ALA B 119 ? 0.3191 0.3211 0.3451 0.0593  -0.0433 0.0269  119 ALA B O   
3837  C CB  . ALA B 119 ? 0.2804 0.3089 0.3123 0.0783  -0.0631 0.0355  119 ALA B CB  
3838  N N   . GLN B 120 ? 0.3464 0.3286 0.3720 0.0720  -0.0493 0.0436  120 GLN B N   
3839  C CA  . GLN B 120 ? 0.3634 0.3289 0.3836 0.0641  -0.0436 0.0477  120 GLN B CA  
3840  C C   . GLN B 120 ? 0.3611 0.3158 0.3691 0.0662  -0.0438 0.0638  120 GLN B C   
3841  O O   . GLN B 120 ? 0.4019 0.3498 0.4089 0.0764  -0.0479 0.0726  120 GLN B O   
3842  C CB  . GLN B 120 ? 0.4228 0.3724 0.4559 0.0651  -0.0407 0.0417  120 GLN B CB  
3843  C CG  . GLN B 120 ? 0.4881 0.4211 0.5220 0.0562  -0.0363 0.0433  120 GLN B CG  
3844  C CD  . GLN B 120 ? 0.5387 0.4541 0.5855 0.0576  -0.0349 0.0354  120 GLN B CD  
3845  O OE1 . GLN B 120 ? 0.5142 0.4337 0.5638 0.0565  -0.0344 0.0207  120 GLN B OE1 
3846  N NE2 . GLN B 120 ? 0.6027 0.4965 0.6562 0.0601  -0.0334 0.0449  120 GLN B NE2 
3847  N N   . ASP B 121 ? 0.3564 0.3101 0.3545 0.0577  -0.0388 0.0683  121 ASP B N   
3848  C CA  . ASP B 121 ? 0.3920 0.3349 0.3763 0.0590  -0.0351 0.0842  121 ASP B CA  
3849  C C   . ASP B 121 ? 0.3867 0.3289 0.3702 0.0476  -0.0263 0.0853  121 ASP B C   
3850  O O   . ASP B 121 ? 0.3541 0.3043 0.3468 0.0401  -0.0257 0.0742  121 ASP B O   
3851  C CB  . ASP B 121 ? 0.3906 0.3445 0.3556 0.0672  -0.0417 0.0895  121 ASP B CB  
3852  C CG  . ASP B 121 ? 0.4313 0.3699 0.3786 0.0750  -0.0405 0.1080  121 ASP B CG  
3853  O OD1 . ASP B 121 ? 0.4522 0.3729 0.3991 0.0706  -0.0302 0.1188  121 ASP B OD1 
3854  O OD2 . ASP B 121 ? 0.4688 0.4131 0.4024 0.0858  -0.0501 0.1123  121 ASP B OD2 
3855  N N   . VAL B 122 ? 0.4062 0.3399 0.3780 0.0474  -0.0193 0.0991  122 VAL B N   
3856  C CA  . VAL B 122 ? 0.3893 0.3253 0.3633 0.0376  -0.0096 0.1006  122 VAL B CA  
3857  C C   . VAL B 122 ? 0.4132 0.3676 0.3759 0.0362  -0.0106 0.0933  122 VAL B C   
3858  O O   . VAL B 122 ? 0.4214 0.3822 0.3647 0.0428  -0.0150 0.0944  122 VAL B O   
3859  C CB  . VAL B 122 ? 0.3833 0.3047 0.3475 0.0379  0.0019  0.1187  122 VAL B CB  
3860  C CG1 . VAL B 122 ? 0.3721 0.3001 0.3412 0.0288  0.0133  0.1194  122 VAL B CG1 
3861  C CG2 . VAL B 122 ? 0.4087 0.3082 0.3884 0.0369  0.0056  0.1267  122 VAL B CG2 
3862  N N   . LEU B 123 ? 0.4072 0.3697 0.3830 0.0278  -0.0078 0.0851  123 LEU B N   
3863  C CA  . LEU B 123 ? 0.3703 0.3456 0.3379 0.0260  -0.0050 0.0810  123 LEU B CA  
3864  C C   . LEU B 123 ? 0.3641 0.3383 0.3430 0.0193  0.0064  0.0862  123 LEU B C   
3865  O O   . LEU B 123 ? 0.3593 0.3291 0.3598 0.0132  0.0078  0.0857  123 LEU B O   
3866  C CB  . LEU B 123 ? 0.3373 0.3242 0.3116 0.0239  -0.0121 0.0673  123 LEU B CB  
3867  C CG  . LEU B 123 ? 0.3683 0.3657 0.3377 0.0220  -0.0096 0.0621  123 LEU B CG  
3868  C CD1 . LEU B 123 ? 0.3451 0.3503 0.3112 0.0233  -0.0169 0.0521  123 LEU B CD1 
3869  C CD2 . LEU B 123 ? 0.3781 0.3784 0.3648 0.0159  -0.0057 0.0602  123 LEU B CD2 
3870  N N   . ALA B 124 ? 0.3799 0.3585 0.3459 0.0204  0.0149  0.0902  124 ALA B N   
3871  C CA  . ALA B 124 ? 0.3726 0.3540 0.3525 0.0147  0.0279  0.0945  124 ALA B CA  
3872  C C   . ALA B 124 ? 0.3569 0.3518 0.3365 0.0147  0.0301  0.0861  124 ALA B C   
3873  O O   . ALA B 124 ? 0.3683 0.3667 0.3286 0.0196  0.0251  0.0803  124 ALA B O   
3874  C CB  . ALA B 124 ? 0.3856 0.3565 0.3513 0.0168  0.0418  0.1099  124 ALA B CB  
3875  N N   . ILE B 125 ? 0.3297 0.3323 0.3335 0.0093  0.0369  0.0851  125 ILE B N   
3876  C CA  . ILE B 125 ? 0.3266 0.3412 0.3352 0.0104  0.0392  0.0777  125 ILE B CA  
3877  C C   . ILE B 125 ? 0.3515 0.3739 0.3849 0.0065  0.0530  0.0820  125 ILE B C   
3878  O O   . ILE B 125 ? 0.3621 0.3834 0.4187 0.0001  0.0561  0.0871  125 ILE B O   
3879  C CB  . ILE B 125 ? 0.3177 0.3384 0.3372 0.0095  0.0251  0.0668  125 ILE B CB  
3880  C CG1 . ILE B 125 ? 0.3198 0.3483 0.3384 0.0129  0.0268  0.0604  125 ILE B CG1 
3881  C CG2 . ILE B 125 ? 0.2877 0.3114 0.3358 0.0033  0.0196  0.0656  125 ILE B CG2 
3882  C CD1 . ILE B 125 ? 0.2886 0.3201 0.3123 0.0133  0.0147  0.0524  125 ILE B CD1 
3883  N N   . HIS B 126 ? 0.3307 0.3609 0.3620 0.0101  0.0620  0.0793  126 HIS B N   
3884  C CA  . HIS B 126 ? 0.3394 0.3798 0.3968 0.0077  0.0772  0.0828  126 HIS B CA  
3885  C C   . HIS B 126 ? 0.3176 0.3708 0.4153 0.0026  0.0688  0.0778  126 HIS B C   
3886  O O   . HIS B 126 ? 0.2769 0.3339 0.3770 0.0047  0.0542  0.0694  126 HIS B O   
3887  C CB  . HIS B 126 ? 0.2971 0.3428 0.3431 0.0145  0.0885  0.0787  126 HIS B CB  
3888  C CG  . HIS B 126 ? 0.3792 0.4155 0.3900 0.0190  0.1029  0.0848  126 HIS B CG  
3889  N ND1 . HIS B 126 ? 0.4401 0.4758 0.4540 0.0172  0.1234  0.0960  126 HIS B ND1 
3890  C CD2 . HIS B 126 ? 0.3647 0.3917 0.3352 0.0253  0.0994  0.0812  126 HIS B CD2 
3891  C CE1 . HIS B 126 ? 0.4574 0.4826 0.4293 0.0234  0.1319  0.0998  126 HIS B CE1 
3892  N NE2 . HIS B 126 ? 0.4261 0.4468 0.3718 0.0284  0.1162  0.0901  126 HIS B NE2 
3893  N N   . SER B 127 ? 0.3596 0.4193 0.4888 -0.0042 0.0783  0.0833  127 SER B N   
3894  C CA  . SER B 127 ? 0.3474 0.4248 0.5203 -0.0081 0.0728  0.0778  127 SER B CA  
3895  C C   . SER B 127 ? 0.3417 0.4342 0.5308 -0.0034 0.0881  0.0775  127 SER B C   
3896  O O   . SER B 127 ? 0.3217 0.4089 0.4829 0.0037  0.0996  0.0786  127 SER B O   
3897  C CB  . SER B 127 ? 0.3300 0.4085 0.5356 -0.0192 0.0743  0.0817  127 SER B CB  
3898  O OG  . SER B 127 ? 0.3752 0.4479 0.5810 -0.0226 0.0970  0.0938  127 SER B OG  
3899  N N   . THR B 128 ? 0.3723 0.4844 0.6077 -0.0066 0.0870  0.0745  128 THR B N   
3900  C CA  . THR B 128 ? 0.3603 0.4893 0.6202 -0.0021 0.1036  0.0745  128 THR B CA  
3901  C C   . THR B 128 ? 0.3306 0.4748 0.6380 -0.0115 0.1190  0.0800  128 THR B C   
3902  O O   . THR B 128 ? 0.3089 0.4551 0.6422 -0.0218 0.1104  0.0802  128 THR B O   
3903  C CB  . THR B 128 ? 0.3234 0.4666 0.6016 0.0059  0.0889  0.0653  128 THR B CB  
3904  O OG1 . THR B 128 ? 0.2749 0.4318 0.5897 0.0005  0.0699  0.0609  128 THR B OG1 
3905  C CG2 . THR B 128 ? 0.2431 0.3699 0.4781 0.0133  0.0759  0.0610  128 THR B CG2 
3906  N N   . HIS B 129 ? 0.3564 0.5106 0.6758 -0.0081 0.1431  0.0836  129 HIS B N   
3907  C CA  . HIS B 129 ? 0.3846 0.5561 0.7542 -0.0169 0.1611  0.0888  129 HIS B CA  
3908  C C   . HIS B 129 ? 0.3626 0.5586 0.7662 -0.0090 0.1732  0.0841  129 HIS B C   
3909  O O   . HIS B 129 ? 0.3411 0.5334 0.7218 -0.0008 0.1948  0.0864  129 HIS B O   
3910  C CB  . HIS B 129 ? 0.4738 0.6296 0.8231 -0.0227 0.1875  0.1029  129 HIS B CB  
3911  C CG  . HIS B 129 ? 0.5354 0.7069 0.9401 -0.0346 0.2064  0.1094  129 HIS B CG  
3912  N ND1 . HIS B 129 ? 0.5509 0.7321 1.0036 -0.0472 0.1918  0.1058  129 HIS B ND1 
3913  C CD2 . HIS B 129 ? 0.5902 0.7686 1.0088 -0.0358 0.2366  0.1167  129 HIS B CD2 
3914  C CE1 . HIS B 129 ? 0.5969 0.7877 1.0877 -0.0557 0.2096  0.1097  129 HIS B CE1 
3915  N NE2 . HIS B 129 ? 0.6188 0.8062 1.0855 -0.0484 0.2353  0.1160  129 HIS B NE2 
3916  N N   . GLY B 130 ? 0.3715 0.5925 0.8290 -0.0104 0.1582  0.0766  130 GLY B N   
3917  C CA  . GLY B 130 ? 0.4187 0.6642 0.9118 -0.0003 0.1644  0.0710  130 GLY B CA  
3918  C C   . GLY B 130 ? 0.4635 0.6957 0.9133 0.0149  0.1557  0.0655  130 GLY B C   
3919  O O   . GLY B 130 ? 0.4989 0.7191 0.9240 0.0170  0.1299  0.0614  130 GLY B O   
3920  N N   . SER B 131 ? 0.4299 0.6627 0.8700 0.0250  0.1785  0.0649  131 SER B N   
3921  C CA  . SER B 131 ? 0.3968 0.6148 0.7983 0.0388  0.1731  0.0585  131 SER B CA  
3922  C C   . SER B 131 ? 0.3885 0.5762 0.7215 0.0395  0.1806  0.0604  131 SER B C   
3923  O O   . SER B 131 ? 0.3676 0.5414 0.6681 0.0491  0.1764  0.0539  131 SER B O   
3924  C CB  . SER B 131 ? 0.3929 0.6274 0.8230 0.0511  0.1919  0.0536  131 SER B CB  
3925  O OG  . SER B 131 ? 0.4166 0.6470 0.8301 0.0511  0.2254  0.0572  131 SER B OG  
3926  N N   . LYS B 132 ? 0.4093 0.5866 0.7219 0.0296  0.1905  0.0693  132 LYS B N   
3927  C CA  . LYS B 132 ? 0.4244 0.5754 0.6731 0.0315  0.1963  0.0716  132 LYS B CA  
3928  C C   . LYS B 132 ? 0.3971 0.5315 0.6193 0.0244  0.1738  0.0745  132 LYS B C   
3929  O O   . LYS B 132 ? 0.3545 0.4962 0.6054 0.0174  0.1562  0.0747  132 LYS B O   
3930  C CB  . LYS B 132 ? 0.4663 0.6141 0.7010 0.0293  0.2279  0.0810  132 LYS B CB  
3931  C CG  . LYS B 132 ? 0.5228 0.6845 0.7744 0.0381  0.2552  0.0771  132 LYS B CG  
3932  C CD  . LYS B 132 ? 0.5991 0.7457 0.8012 0.0419  0.2835  0.0824  132 LYS B CD  
3933  C CE  . LYS B 132 ? 0.8422 0.9988 1.0684 0.0357  0.3091  0.0911  132 LYS B CE  
3934  N NZ  . LYS B 132 ? 0.8531 1.0141 1.0739 0.0441  0.3306  0.0842  132 LYS B NZ  
3935  N N   . LEU B 133 ? 0.4398 0.5527 0.6075 0.0268  0.1735  0.0755  133 LEU B N   
3936  C CA  . LEU B 133 ? 0.4616 0.5594 0.6056 0.0204  0.1571  0.0801  133 LEU B CA  
3937  C C   . LEU B 133 ? 0.4997 0.5970 0.6592 0.0103  0.1679  0.0928  133 LEU B C   
3938  O O   . LEU B 133 ? 0.5207 0.6188 0.6792 0.0097  0.1930  0.1013  133 LEU B O   
3939  C CB  . LEU B 133 ? 0.4598 0.5376 0.5459 0.0261  0.1549  0.0785  133 LEU B CB  
3940  C CG  . LEU B 133 ? 0.4208 0.4940 0.4898 0.0333  0.1405  0.0656  133 LEU B CG  
3941  C CD1 . LEU B 133 ? 0.4380 0.4938 0.4541 0.0370  0.1381  0.0634  133 LEU B CD1 
3942  C CD2 . LEU B 133 ? 0.3882 0.4642 0.4768 0.0299  0.1165  0.0620  133 LEU B CD2 
3943  N N   . GLY B 134 ? 0.4737 0.5677 0.6460 0.0025  0.1502  0.0942  134 GLY B N   
3944  C CA  . GLY B 134 ? 0.4625 0.5530 0.6532 -0.0080 0.1586  0.1052  134 GLY B CA  
3945  C C   . GLY B 134 ? 0.4791 0.5454 0.6258 -0.0079 0.1531  0.1124  134 GLY B C   
3946  O O   . GLY B 134 ? 0.4589 0.5148 0.5627 0.0003  0.1458  0.1089  134 GLY B O   
3947  N N   . PRO B 135 ? 0.4901 0.5474 0.6504 -0.0170 0.1559  0.1219  135 PRO B N   
3948  C CA  . PRO B 135 ? 0.4893 0.5226 0.6131 -0.0163 0.1518  0.1310  135 PRO B CA  
3949  C C   . PRO B 135 ? 0.4357 0.4624 0.5408 -0.0127 0.1248  0.1212  135 PRO B C   
3950  O O   . PRO B 135 ? 0.4077 0.4455 0.5347 -0.0144 0.1082  0.1091  135 PRO B O   
3951  C CB  . PRO B 135 ? 0.5006 0.5281 0.6590 -0.0284 0.1598  0.1407  135 PRO B CB  
3952  C CG  . PRO B 135 ? 0.4895 0.5403 0.7044 -0.0363 0.1560  0.1306  135 PRO B CG  
3953  C CD  . PRO B 135 ? 0.4790 0.5489 0.6954 -0.0287 0.1626  0.1239  135 PRO B CD  
3954  N N   . MET B 136 ? 0.4307 0.4398 0.4944 -0.0070 0.1209  0.1270  136 MET B N   
3955  C CA  . MET B 136 ? 0.4247 0.4273 0.4740 -0.0041 0.0982  0.1192  136 MET B CA  
3956  C C   . MET B 136 ? 0.3850 0.3833 0.4644 -0.0125 0.0885  0.1178  136 MET B C   
3957  O O   . MET B 136 ? 0.4192 0.4094 0.5168 -0.0193 0.0994  0.1276  136 MET B O   
3958  C CB  . MET B 136 ? 0.4792 0.4655 0.4835 0.0040  0.0961  0.1267  136 MET B CB  
3959  C CG  . MET B 136 ? 0.5248 0.5120 0.4926 0.0126  0.1054  0.1280  136 MET B CG  
3960  S SD  . MET B 136 ? 0.6034 0.6019 0.5574 0.0186  0.0898  0.1093  136 MET B SD  
3961  C CE  . MET B 136 ? 0.6269 0.6165 0.5606 0.0226  0.0681  0.1065  136 MET B CE  
3962  N N   . VAL B 137 ? 0.3342 0.3369 0.4191 -0.0123 0.0690  0.1051  137 VAL B N   
3963  C CA  . VAL B 137 ? 0.3423 0.3376 0.4469 -0.0185 0.0580  0.1015  137 VAL B CA  
3964  C C   . VAL B 137 ? 0.3333 0.3179 0.4105 -0.0119 0.0435  0.0973  137 VAL B C   
3965  O O   . VAL B 137 ? 0.3392 0.3289 0.3929 -0.0048 0.0379  0.0928  137 VAL B O   
3966  C CB  . VAL B 137 ? 0.3316 0.3429 0.4712 -0.0246 0.0479  0.0890  137 VAL B CB  
3967  C CG1 . VAL B 137 ? 0.3487 0.3714 0.5257 -0.0326 0.0622  0.0933  137 VAL B CG1 
3968  C CG2 . VAL B 137 ? 0.3074 0.3315 0.4349 -0.0180 0.0377  0.0792  137 VAL B CG2 
3969  N N   . LYS B 138 ? 0.3326 0.3026 0.4154 -0.0142 0.0381  0.0982  138 LYS B N   
3970  C CA  . LYS B 138 ? 0.3291 0.2896 0.3886 -0.0067 0.0273  0.0959  138 LYS B CA  
3971  C C   . LYS B 138 ? 0.3373 0.2986 0.4079 -0.0084 0.0124  0.0815  138 LYS B C   
3972  O O   . LYS B 138 ? 0.3508 0.3110 0.4472 -0.0163 0.0099  0.0757  138 LYS B O   
3973  C CB  . LYS B 138 ? 0.3928 0.3323 0.4432 -0.0039 0.0335  0.1096  138 LYS B CB  
3974  C CG  . LYS B 138 ? 0.4665 0.4007 0.4955 0.0002  0.0482  0.1260  138 LYS B CG  
3975  C CD  . LYS B 138 ? 0.5404 0.4503 0.5602 0.0038  0.0530  0.1415  138 LYS B CD  
3976  C CE  . LYS B 138 ? 0.6010 0.5038 0.5936 0.0089  0.0682  0.1597  138 LYS B CE  
3977  N NZ  . LYS B 138 ? 0.6659 0.5435 0.6452 0.0146  0.0716  0.1769  138 LYS B NZ  
3978  N N   . VAL B 139 ? 0.3367 0.3000 0.3873 -0.0012 0.0031  0.0753  139 VAL B N   
3979  C CA  . VAL B 139 ? 0.3304 0.2894 0.3830 0.0001  -0.0080 0.0643  139 VAL B CA  
3980  C C   . VAL B 139 ? 0.3656 0.3100 0.4068 0.0072  -0.0079 0.0709  139 VAL B C   
3981  O O   . VAL B 139 ? 0.3973 0.3458 0.4194 0.0149  -0.0098 0.0735  139 VAL B O   
3982  C CB  . VAL B 139 ? 0.3000 0.2718 0.3404 0.0036  -0.0160 0.0539  139 VAL B CB  
3983  C CG1 . VAL B 139 ? 0.2943 0.2611 0.3355 0.0050  -0.0244 0.0428  139 VAL B CG1 
3984  C CG2 . VAL B 139 ? 0.2848 0.2704 0.3327 -0.0004 -0.0164 0.0500  139 VAL B CG2 
3985  N N   . PRO B 140 ? 0.3797 0.3070 0.4345 0.0049  -0.0063 0.0734  140 PRO B N   
3986  C CA  . PRO B 140 ? 0.3846 0.2960 0.4294 0.0132  -0.0049 0.0836  140 PRO B CA  
3987  C C   . PRO B 140 ? 0.4205 0.3340 0.4565 0.0224  -0.0143 0.0754  140 PRO B C   
3988  O O   . PRO B 140 ? 0.4409 0.3496 0.4649 0.0321  -0.0156 0.0835  140 PRO B O   
3989  C CB  . PRO B 140 ? 0.4190 0.3095 0.4856 0.0072  -0.0006 0.0862  140 PRO B CB  
3990  C CG  . PRO B 140 ? 0.4177 0.3165 0.5061 -0.0054 0.0016  0.0795  140 PRO B CG  
3991  C CD  . PRO B 140 ? 0.3875 0.3081 0.4686 -0.0049 -0.0066 0.0668  140 PRO B CD  
3992  N N   . GLN B 141 ? 0.4048 0.3258 0.4469 0.0200  -0.0205 0.0595  141 GLN B N   
3993  C CA  . GLN B 141 ? 0.4012 0.3260 0.4373 0.0281  -0.0265 0.0510  141 GLN B CA  
3994  C C   . GLN B 141 ? 0.3801 0.3247 0.4071 0.0276  -0.0296 0.0422  141 GLN B C   
3995  O O   . GLN B 141 ? 0.4096 0.3575 0.4379 0.0271  -0.0324 0.0299  141 GLN B O   
3996  C CB  . GLN B 141 ? 0.4864 0.3978 0.5353 0.0278  -0.0287 0.0398  141 GLN B CB  
3997  C CG  . GLN B 141 ? 0.6387 0.5266 0.6983 0.0301  -0.0254 0.0484  141 GLN B CG  
3998  C CD  . GLN B 141 ? 0.7687 0.6414 0.8464 0.0218  -0.0255 0.0382  141 GLN B CD  
3999  O OE1 . GLN B 141 ? 0.7954 0.6735 0.8812 0.0110  -0.0255 0.0343  141 GLN B OE1 
4000  N NE2 . GLN B 141 ? 0.8401 0.6942 0.9262 0.0271  -0.0263 0.0324  141 GLN B NE2 
4001  N N   . PHE B 142 ? 0.3588 0.3147 0.3749 0.0279  -0.0281 0.0488  142 PHE B N   
4002  C CA  . PHE B 142 ? 0.3110 0.2831 0.3192 0.0270  -0.0299 0.0423  142 PHE B CA  
4003  C C   . PHE B 142 ? 0.2992 0.2783 0.3052 0.0339  -0.0333 0.0368  142 PHE B C   
4004  O O   . PHE B 142 ? 0.3226 0.3011 0.3269 0.0409  -0.0356 0.0423  142 PHE B O   
4005  C CB  . PHE B 142 ? 0.3266 0.3059 0.3249 0.0260  -0.0268 0.0498  142 PHE B CB  
4006  C CG  . PHE B 142 ? 0.3300 0.3226 0.3227 0.0242  -0.0277 0.0433  142 PHE B CG  
4007  C CD1 . PHE B 142 ? 0.3015 0.2975 0.2983 0.0186  -0.0266 0.0393  142 PHE B CD1 
4008  C CD2 . PHE B 142 ? 0.3302 0.3313 0.3156 0.0282  -0.0304 0.0410  142 PHE B CD2 
4009  C CE1 . PHE B 142 ? 0.2902 0.2947 0.2817 0.0177  -0.0267 0.0349  142 PHE B CE1 
4010  C CE2 . PHE B 142 ? 0.2993 0.3097 0.2822 0.0255  -0.0300 0.0351  142 PHE B CE2 
4011  C CZ  . PHE B 142 ? 0.3005 0.3111 0.2853 0.0206  -0.0275 0.0329  142 PHE B CZ  
4012  N N   . LEU B 143 ? 0.2713 0.2578 0.2776 0.0322  -0.0335 0.0267  143 LEU B N   
4013  C CA  . LEU B 143 ? 0.2622 0.2577 0.2710 0.0375  -0.0341 0.0210  143 LEU B CA  
4014  C C   . LEU B 143 ? 0.2643 0.2744 0.2690 0.0363  -0.0343 0.0208  143 LEU B C   
4015  O O   . LEU B 143 ? 0.3084 0.3215 0.3068 0.0307  -0.0323 0.0205  143 LEU B O   
4016  C CB  . LEU B 143 ? 0.2836 0.2775 0.2936 0.0366  -0.0315 0.0103  143 LEU B CB  
4017  C CG  . LEU B 143 ? 0.2888 0.2671 0.3041 0.0380  -0.0321 0.0065  143 LEU B CG  
4018  C CD1 . LEU B 143 ? 0.2854 0.2620 0.2955 0.0371  -0.0298 -0.0059 143 LEU B CD1 
4019  C CD2 . LEU B 143 ? 0.2928 0.2658 0.3182 0.0466  -0.0331 0.0096  143 LEU B CD2 
4020  N N   . PHE B 144 ? 0.2741 0.2933 0.2846 0.0420  -0.0375 0.0204  144 PHE B N   
4021  C CA  . PHE B 144 ? 0.2741 0.3073 0.2842 0.0402  -0.0392 0.0184  144 PHE B CA  
4022  C C   . PHE B 144 ? 0.2653 0.3118 0.2903 0.0462  -0.0430 0.0138  144 PHE B C   
4023  O O   . PHE B 144 ? 0.3109 0.3551 0.3455 0.0528  -0.0436 0.0131  144 PHE B O   
4024  C CB  . PHE B 144 ? 0.2971 0.3288 0.2948 0.0401  -0.0428 0.0253  144 PHE B CB  
4025  C CG  . PHE B 144 ? 0.3491 0.3776 0.3433 0.0487  -0.0493 0.0328  144 PHE B CG  
4026  C CD1 . PHE B 144 ? 0.3493 0.3620 0.3398 0.0513  -0.0474 0.0417  144 PHE B CD1 
4027  C CD2 . PHE B 144 ? 0.3426 0.3836 0.3377 0.0542  -0.0580 0.0313  144 PHE B CD2 
4028  C CE1 . PHE B 144 ? 0.3457 0.3524 0.3304 0.0601  -0.0526 0.0513  144 PHE B CE1 
4029  C CE2 . PHE B 144 ? 0.3621 0.3996 0.3505 0.0639  -0.0656 0.0397  144 PHE B CE2 
4030  C CZ  . PHE B 144 ? 0.3659 0.3848 0.3475 0.0674  -0.0621 0.0509  144 PHE B CZ  
4031  N N   . SER B 145 ? 0.2609 0.3217 0.2907 0.0440  -0.0460 0.0098  145 SER B N   
4032  C CA  . SER B 145 ? 0.2603 0.3380 0.3102 0.0489  -0.0506 0.0043  145 SER B CA  
4033  C C   . SER B 145 ? 0.2931 0.3795 0.3410 0.0543  -0.0637 0.0063  145 SER B C   
4034  O O   . SER B 145 ? 0.2961 0.3813 0.3291 0.0503  -0.0668 0.0071  145 SER B O   
4035  C CB  . SER B 145 ? 0.2814 0.3715 0.3454 0.0412  -0.0433 -0.0044 145 SER B CB  
4036  O OG  . SER B 145 ? 0.3009 0.4111 0.3900 0.0446  -0.0480 -0.0107 145 SER B OG  
4037  N N   . CYS B 146 ? 0.3005 0.3947 0.3618 0.0646  -0.0718 0.0072  146 CYS B N   
4038  C CA  . CYS B 146 ? 0.3328 0.4409 0.3963 0.0714  -0.0871 0.0069  146 CYS B CA  
4039  C C   . CYS B 146 ? 0.3086 0.4415 0.4007 0.0673  -0.0896 -0.0058 146 CYS B C   
4040  O O   . CYS B 146 ? 0.3197 0.4657 0.4396 0.0722  -0.0886 -0.0101 146 CYS B O   
4041  C CB  . CYS B 146 ? 0.3702 0.4755 0.4369 0.0862  -0.0961 0.0149  146 CYS B CB  
4042  S SG  . CYS B 146 ? 1.0403 1.1176 1.0726 0.0919  -0.0967 0.0323  146 CYS B SG  
4043  N N   . ALA B 147 ? 0.2933 0.4327 0.3811 0.0584  -0.0920 -0.0123 147 ALA B N   
4044  C CA  . ALA B 147 ? 0.3127 0.4736 0.4303 0.0507  -0.0918 -0.0251 147 ALA B CA  
4045  C C   . ALA B 147 ? 0.3495 0.5335 0.4839 0.0569  -0.1114 -0.0321 147 ALA B C   
4046  O O   . ALA B 147 ? 0.3823 0.5628 0.4943 0.0657  -0.1259 -0.0270 147 ALA B O   
4047  C CB  . ALA B 147 ? 0.3150 0.4684 0.4222 0.0375  -0.0842 -0.0295 147 ALA B CB  
4048  N N   . PRO B 148 ? 0.3398 0.5483 0.5140 0.0525  -0.1120 -0.0436 148 PRO B N   
4049  C CA  . PRO B 148 ? 0.3549 0.5893 0.5498 0.0572  -0.1333 -0.0527 148 PRO B CA  
4050  C C   . PRO B 148 ? 0.3905 0.6221 0.5625 0.0512  -0.1450 -0.0593 148 PRO B C   
4051  O O   . PRO B 148 ? 0.3558 0.5741 0.5166 0.0386  -0.1333 -0.0623 148 PRO B O   
4052  C CB  . PRO B 148 ? 0.3315 0.5917 0.5782 0.0496  -0.1261 -0.0646 148 PRO B CB  
4053  C CG  . PRO B 148 ? 0.3386 0.5830 0.5826 0.0384  -0.1006 -0.0619 148 PRO B CG  
4054  C CD  . PRO B 148 ? 0.3266 0.5416 0.5299 0.0445  -0.0934 -0.0481 148 PRO B CD  
4055  N N   . SER B 149 ? 0.4334 0.6762 0.5966 0.0614  -0.1682 -0.0613 149 SER B N   
4056  C CA  . SER B 149 ? 0.4784 0.7166 0.6115 0.0589  -0.1812 -0.0677 149 SER B CA  
4057  C C   . SER B 149 ? 0.4481 0.6947 0.6004 0.0423  -0.1795 -0.0856 149 SER B C   
4058  O O   . SER B 149 ? 0.4824 0.7135 0.6055 0.0364  -0.1783 -0.0896 149 SER B O   
4059  C CB  . SER B 149 ? 0.5899 0.8445 0.7160 0.0737  -0.2090 -0.0690 149 SER B CB  
4060  O OG  . SER B 149 ? 0.6548 0.8962 0.7573 0.0899  -0.2107 -0.0504 149 SER B OG  
4061  N N   . PHE B 150 ? 0.4208 0.6914 0.6239 0.0347  -0.1785 -0.0968 150 PHE B N   
4062  C CA  . PHE B 150 ? 0.4248 0.7040 0.6523 0.0181  -0.1779 -0.1146 150 PHE B CA  
4063  C C   . PHE B 150 ? 0.4545 0.7059 0.6648 0.0052  -0.1545 -0.1113 150 PHE B C   
4064  O O   . PHE B 150 ? 0.4849 0.7319 0.6983 -0.0069 -0.1543 -0.1240 150 PHE B O   
4065  C CB  . PHE B 150 ? 0.3765 0.6864 0.6668 0.0115  -0.1763 -0.1247 150 PHE B CB  
4066  C CG  . PHE B 150 ? 0.3404 0.6427 0.6505 0.0042  -0.1472 -0.1164 150 PHE B CG  
4067  C CD1 . PHE B 150 ? 0.3182 0.6085 0.6382 -0.0131 -0.1275 -0.1203 150 PHE B CD1 
4068  C CD2 . PHE B 150 ? 0.3000 0.6057 0.6172 0.0154  -0.1395 -0.1048 150 PHE B CD2 
4069  C CE1 . PHE B 150 ? 0.2839 0.5660 0.6157 -0.0185 -0.1010 -0.1115 150 PHE B CE1 
4070  C CE2 . PHE B 150 ? 0.2873 0.5856 0.6176 0.0095  -0.1130 -0.0986 150 PHE B CE2 
4071  C CZ  . PHE B 150 ? 0.2653 0.5520 0.6007 -0.0073 -0.0939 -0.1013 150 PHE B CZ  
4072  N N   . LEU B 151 ? 0.4143 0.6464 0.6073 0.0085  -0.1359 -0.0950 151 LEU B N   
4073  C CA  . LEU B 151 ? 0.3675 0.5774 0.5530 -0.0028 -0.1132 -0.0908 151 LEU B CA  
4074  C C   . LEU B 151 ? 0.3673 0.5557 0.5158 -0.0053 -0.1144 -0.0923 151 LEU B C   
4075  O O   . LEU B 151 ? 0.3840 0.5590 0.5350 -0.0165 -0.1020 -0.0958 151 LEU B O   
4076  C CB  . LEU B 151 ? 0.3296 0.5260 0.5043 0.0025  -0.0962 -0.0744 151 LEU B CB  
4077  C CG  . LEU B 151 ? 0.2832 0.4626 0.4585 -0.0077 -0.0728 -0.0693 151 LEU B CG  
4078  C CD1 . LEU B 151 ? 0.2334 0.4275 0.4513 -0.0201 -0.0636 -0.0787 151 LEU B CD1 
4079  C CD2 . LEU B 151 ? 0.2474 0.4150 0.4080 -0.0007 -0.0605 -0.0555 151 LEU B CD2 
4080  N N   . ALA B 152 ? 0.3801 0.5643 0.4942 0.0059  -0.1283 -0.0891 152 ALA B N   
4081  C CA  . ALA B 152 ? 0.3906 0.5546 0.4664 0.0055  -0.1278 -0.0903 152 ALA B CA  
4082  C C   . ALA B 152 ? 0.4285 0.6013 0.4988 0.0040  -0.1465 -0.1084 152 ALA B C   
4083  O O   . ALA B 152 ? 0.4626 0.6197 0.4994 0.0050  -0.1467 -0.1117 152 ALA B O   
4084  C CB  . ALA B 152 ? 0.3573 0.5071 0.3941 0.0181  -0.1266 -0.0738 152 ALA B CB  
4085  N N   . GLN B 153 ? 0.4575 0.6562 0.5615 0.0018  -0.1621 -0.1215 153 GLN B N   
4086  C CA  . GLN B 153 ? 0.5339 0.7444 0.6333 0.0014  -0.1846 -0.1408 153 GLN B CA  
4087  C C   . GLN B 153 ? 0.4972 0.7001 0.6111 -0.0146 -0.1796 -0.1592 153 GLN B C   
4088  O O   . GLN B 153 ? 0.4921 0.6992 0.5967 -0.0161 -0.1965 -0.1777 153 GLN B O   
4089  C CB  . GLN B 153 ? 0.6183 0.8626 0.7531 0.0055  -0.2062 -0.1493 153 GLN B CB  
4090  C CG  . GLN B 153 ? 0.7255 0.9761 0.8344 0.0248  -0.2213 -0.1361 153 GLN B CG  
4091  C CD  . GLN B 153 ? 0.8095 1.0851 0.9539 0.0284  -0.2339 -0.1378 153 GLN B CD  
4092  O OE1 . GLN B 153 ? 0.8351 1.1283 1.0288 0.0167  -0.2313 -0.1494 153 GLN B OE1 
4093  N NE2 . GLN B 153 ? 0.8494 1.1262 0.9702 0.0444  -0.2463 -0.1253 153 GLN B NE2 
4094  N N   . LYS B 154 ? 0.4685 0.6584 0.6033 -0.0260 -0.1566 -0.1543 154 LYS B N   
4095  C CA  . LYS B 154 ? 0.4647 0.6444 0.6181 -0.0416 -0.1495 -0.1697 154 LYS B CA  
4096  C C   . LYS B 154 ? 0.4378 0.5863 0.5748 -0.0455 -0.1245 -0.1577 154 LYS B C   
4097  O O   . LYS B 154 ? 0.4368 0.5794 0.5760 -0.0437 -0.1084 -0.1398 154 LYS B O   
4098  C CB  . LYS B 154 ? 0.4849 0.6867 0.6981 -0.0545 -0.1488 -0.1792 154 LYS B CB  
4099  C CG  . LYS B 154 ? 0.5736 0.8071 0.8110 -0.0541 -0.1769 -0.1989 154 LYS B CG  
4100  C CD  . LYS B 154 ? 0.6027 0.8620 0.9032 -0.0646 -0.1737 -0.2037 154 LYS B CD  
4101  C CE  . LYS B 154 ? 0.6463 0.9206 0.9663 -0.0685 -0.1908 -0.2196 154 LYS B CE  
4102  N NZ  . LYS B 154 ? 0.6767 0.9374 0.9586 -0.0666 -0.2066 -0.2332 154 LYS B NZ  
4103  N N   . GLY B 155 ? 0.4730 0.6018 0.5935 -0.0501 -0.1223 -0.1688 155 GLY B N   
4104  C CA  . GLY B 155 ? 0.4767 0.5774 0.5921 -0.0553 -0.1002 -0.1609 155 GLY B CA  
4105  C C   . GLY B 155 ? 0.5046 0.5851 0.5766 -0.0441 -0.0911 -0.1468 155 GLY B C   
4106  O O   . GLY B 155 ? 0.5388 0.5964 0.6054 -0.0470 -0.0762 -0.1437 155 GLY B O   
4107  N N   . LEU B 156 ? 0.4838 0.5725 0.5273 -0.0312 -0.0994 -0.1378 156 LEU B N   
4108  C CA  . LEU B 156 ? 0.4376 0.5102 0.4460 -0.0213 -0.0890 -0.1223 156 LEU B CA  
4109  C C   . LEU B 156 ? 0.4873 0.5507 0.4608 -0.0157 -0.0948 -0.1335 156 LEU B C   
4110  O O   . LEU B 156 ? 0.5808 0.6535 0.5521 -0.0170 -0.1110 -0.1517 156 LEU B O   
4111  C CB  . LEU B 156 ? 0.4303 0.5140 0.4285 -0.0112 -0.0922 -0.1052 156 LEU B CB  
4112  C CG  . LEU B 156 ? 0.3805 0.4778 0.4105 -0.0142 -0.0898 -0.0970 156 LEU B CG  
4113  C CD1 . LEU B 156 ? 0.3531 0.4555 0.3685 -0.0029 -0.0920 -0.0811 156 LEU B CD1 
4114  C CD2 . LEU B 156 ? 0.3704 0.4539 0.4170 -0.0224 -0.0710 -0.0903 156 LEU B CD2 
4115  N N   . PRO B 157 ? 0.4582 0.5045 0.4048 -0.0092 -0.0819 -0.1240 157 PRO B N   
4116  C CA  . PRO B 157 ? 0.5053 0.5440 0.4147 -0.0020 -0.0852 -0.1336 157 PRO B CA  
4117  C C   . PRO B 157 ? 0.5922 0.6464 0.4761 0.0070  -0.1029 -0.1342 157 PRO B C   
4118  O O   . PRO B 157 ? 0.6053 0.6735 0.4983 0.0102  -0.1094 -0.1219 157 PRO B O   
4119  C CB  . PRO B 157 ? 0.4811 0.5048 0.3732 0.0043  -0.0668 -0.1178 157 PRO B CB  
4120  C CG  . PRO B 157 ? 0.4470 0.4647 0.3706 -0.0025 -0.0549 -0.1080 157 PRO B CG  
4121  C CD  . PRO B 157 ? 0.4228 0.4565 0.3731 -0.0083 -0.0638 -0.1062 157 PRO B CD  
4122  N N   . ASN B 158 ? 0.6374 0.6880 0.4880 0.0122  -0.1107 -0.1482 158 ASN B N   
4123  C CA  . ASN B 158 ? 0.6657 0.7313 0.4922 0.0206  -0.1313 -0.1512 158 ASN B CA  
4124  C C   . ASN B 158 ? 0.6033 0.6697 0.4091 0.0317  -0.1260 -0.1256 158 ASN B C   
4125  O O   . ASN B 158 ? 0.5323 0.5846 0.3238 0.0348  -0.1071 -0.1122 158 ASN B O   
4126  C CB  . ASN B 158 ? 0.7641 0.8232 0.5512 0.0252  -0.1396 -0.1712 158 ASN B CB  
4127  C CG  . ASN B 158 ? 0.8759 0.9533 0.6458 0.0314  -0.1672 -0.1811 158 ASN B CG  
4128  O OD1 . ASN B 158 ? 0.9046 0.9954 0.7042 0.0230  -0.1837 -0.1988 158 ASN B OD1 
4129  N ND2 . ASN B 158 ? 0.9277 1.0046 0.6546 0.0451  -0.1700 -0.1663 158 ASN B ND2 
4130  N N   . ASN B 159 ? 0.6080 0.6914 0.4192 0.0367  -0.1422 -0.1190 159 ASN B N   
4131  C CA  . ASN B 159 ? 0.6275 0.7109 0.4216 0.0476  -0.1399 -0.0952 159 ASN B CA  
4132  C C   . ASN B 159 ? 0.5485 0.6265 0.3689 0.0438  -0.1222 -0.0768 159 ASN B C   
4133  O O   . ASN B 159 ? 0.5228 0.5978 0.3323 0.0513  -0.1180 -0.0575 159 ASN B O   
4134  C CB  . ASN B 159 ? 0.7271 0.7969 0.4676 0.0584  -0.1337 -0.0879 159 ASN B CB  
4135  C CG  . ASN B 159 ? 0.8451 0.9223 0.5501 0.0672  -0.1556 -0.0995 159 ASN B CG  
4136  O OD1 . ASN B 159 ? 0.9091 0.9793 0.5875 0.0671  -0.1561 -0.1157 159 ASN B OD1 
4137  N ND2 . ASN B 159 ? 0.8726 0.9632 0.5835 0.0735  -0.1724 -0.0909 159 ASN B ND2 
4138  N N   . VAL B 160 ? 0.5010 0.5762 0.3543 0.0324  -0.1119 -0.0825 160 VAL B N   
4139  C CA  . VAL B 160 ? 0.4753 0.5464 0.3515 0.0292  -0.0975 -0.0669 160 VAL B CA  
4140  C C   . VAL B 160 ? 0.5118 0.5989 0.4142 0.0298  -0.1077 -0.0625 160 VAL B C   
4141  O O   . VAL B 160 ? 0.5048 0.6070 0.4285 0.0260  -0.1207 -0.0757 160 VAL B O   
4142  C CB  . VAL B 160 ? 0.4086 0.4706 0.3080 0.0185  -0.0841 -0.0726 160 VAL B CB  
4143  C CG1 . VAL B 160 ? 0.3287 0.3909 0.2535 0.0150  -0.0748 -0.0597 160 VAL B CG1 
4144  C CG2 . VAL B 160 ? 0.4076 0.4531 0.2840 0.0207  -0.0707 -0.0715 160 VAL B CG2 
4145  N N   . GLN B 161 ? 0.5540 0.6383 0.4571 0.0348  -0.1016 -0.0448 161 GLN B N   
4146  C CA  . GLN B 161 ? 0.5536 0.6516 0.4755 0.0394  -0.1115 -0.0395 161 GLN B CA  
4147  C C   . GLN B 161 ? 0.4132 0.5113 0.3648 0.0345  -0.1006 -0.0327 161 GLN B C   
4148  O O   . GLN B 161 ? 0.4132 0.5180 0.3764 0.0401  -0.1046 -0.0257 161 GLN B O   
4149  C CB  . GLN B 161 ? 0.6682 0.7614 0.5615 0.0524  -0.1167 -0.0248 161 GLN B CB  
4150  C CG  . GLN B 161 ? 0.8107 0.9108 0.6771 0.0603  -0.1346 -0.0319 161 GLN B CG  
4151  C CD  . GLN B 161 ? 0.9064 0.9931 0.7306 0.0721  -0.1329 -0.0157 161 GLN B CD  
4152  O OE1 . GLN B 161 ? 0.8965 0.9716 0.7194 0.0748  -0.1211 0.0017  161 GLN B OE1 
4153  N NE2 . GLN B 161 ? 0.9750 1.0619 0.7633 0.0787  -0.1437 -0.0217 161 GLN B NE2 
4154  N N   . GLY B 162 ? 0.2981 0.3878 0.2600 0.0253  -0.0869 -0.0350 162 GLY B N   
4155  C CA  . GLY B 162 ? 0.2707 0.3585 0.2539 0.0210  -0.0760 -0.0290 162 GLY B CA  
4156  C C   . GLY B 162 ? 0.2906 0.3641 0.2709 0.0142  -0.0621 -0.0281 162 GLY B C   
4157  O O   . GLY B 162 ? 0.3037 0.3713 0.2748 0.0113  -0.0610 -0.0353 162 GLY B O   
4158  N N   . ALA B 163 ? 0.2883 0.3560 0.2764 0.0126  -0.0523 -0.0198 163 ALA B N   
4159  C CA  . ALA B 163 ? 0.2939 0.3489 0.2806 0.0078  -0.0408 -0.0173 163 ALA B CA  
4160  C C   . ALA B 163 ? 0.3282 0.3759 0.3093 0.0109  -0.0349 -0.0056 163 ALA B C   
4161  O O   . ALA B 163 ? 0.3028 0.3546 0.2885 0.0141  -0.0370 -0.0014 163 ALA B O   
4162  C CB  . ALA B 163 ? 0.2735 0.3300 0.2809 -0.0003 -0.0353 -0.0228 163 ALA B CB  
4163  N N   . LEU B 164 ? 0.3243 0.3616 0.2977 0.0103  -0.0280 -0.0016 164 LEU B N   
4164  C CA  . LEU B 164 ? 0.3111 0.3430 0.2840 0.0116  -0.0237 0.0071  164 LEU B CA  
4165  C C   . LEU B 164 ? 0.3035 0.3301 0.2832 0.0076  -0.0179 0.0073  164 LEU B C   
4166  O O   . LEU B 164 ? 0.3614 0.3825 0.3417 0.0052  -0.0143 0.0045  164 LEU B O   
4167  C CB  . LEU B 164 ? 0.3676 0.3945 0.3302 0.0148  -0.0212 0.0128  164 LEU B CB  
4168  C CG  . LEU B 164 ? 0.4443 0.4659 0.4025 0.0143  -0.0160 0.0099  164 LEU B CG  
4169  C CD1 . LEU B 164 ? 0.4608 0.4778 0.4247 0.0146  -0.0108 0.0156  164 LEU B CD1 
4170  C CD2 . LEU B 164 ? 0.5131 0.5351 0.4566 0.0180  -0.0157 0.0088  164 LEU B CD2 
4171  N N   . GLY B 165 ? 0.2855 0.3122 0.2685 0.0076  -0.0166 0.0106  165 GLY B N   
4172  C CA  . GLY B 165 ? 0.2792 0.3000 0.2635 0.0049  -0.0109 0.0122  165 GLY B CA  
4173  C C   . GLY B 165 ? 0.2982 0.3126 0.2754 0.0076  -0.0109 0.0186  165 GLY B C   
4174  O O   . GLY B 165 ? 0.2808 0.2971 0.2563 0.0100  -0.0147 0.0204  165 GLY B O   
4175  N N   . LEU B 166 ? 0.2548 0.2611 0.2294 0.0073  -0.0074 0.0217  166 LEU B N   
4176  C CA  . LEU B 166 ? 0.2728 0.2749 0.2423 0.0108  -0.0097 0.0274  166 LEU B CA  
4177  C C   . LEU B 166 ? 0.2721 0.2672 0.2325 0.0112  -0.0069 0.0315  166 LEU B C   
4178  O O   . LEU B 166 ? 0.2987 0.2881 0.2532 0.0148  -0.0091 0.0369  166 LEU B O   
4179  C CB  A LEU B 166 ? 0.2295 0.2279 0.2027 0.0133  -0.0091 0.0295  166 LEU B CB  
4180  C CB  B LEU B 166 ? 0.2292 0.2278 0.2026 0.0132  -0.0091 0.0293  166 LEU B CB  
4181  C CG  A LEU B 166 ? 0.2454 0.2491 0.2240 0.0147  -0.0097 0.0277  166 LEU B CG  
4182  C CG  B LEU B 166 ? 0.2587 0.2633 0.2376 0.0154  -0.0111 0.0290  166 LEU B CG  
4183  C CD1 A LEU B 166 ? 0.2390 0.2495 0.2207 0.0157  -0.0141 0.0299  166 LEU B CD1 
4184  C CD1 B LEU B 166 ? 0.2498 0.2606 0.2278 0.0137  -0.0120 0.0258  166 LEU B CD1 
4185  C CD2 A LEU B 166 ? 0.2487 0.2546 0.2258 0.0123  -0.0079 0.0216  166 LEU B CD2 
4186  C CD2 B LEU B 166 ? 0.2282 0.2291 0.2113 0.0176  -0.0067 0.0283  166 LEU B CD2 
4187  N N   . GLY B 167 ? 0.2871 0.2833 0.2465 0.0081  -0.0018 0.0292  167 GLY B N   
4188  C CA  . GLY B 167 ? 0.3232 0.3115 0.2709 0.0083  0.0044  0.0340  167 GLY B CA  
4189  C C   . GLY B 167 ? 0.3283 0.3160 0.2603 0.0127  -0.0004 0.0354  167 GLY B C   
4190  O O   . GLY B 167 ? 0.3136 0.3072 0.2478 0.0145  -0.0085 0.0315  167 GLY B O   
4191  N N   . GLN B 168 ? 0.3509 0.3299 0.2658 0.0144  0.0050  0.0408  168 GLN B N   
4192  C CA  . GLN B 168 ? 0.3726 0.3501 0.2674 0.0190  0.0001  0.0402  168 GLN B CA  
4193  C C   . GLN B 168 ? 0.3871 0.3698 0.2806 0.0177  0.0060  0.0328  168 GLN B C   
4194  O O   . GLN B 168 ? 0.4306 0.4089 0.3109 0.0177  0.0172  0.0347  168 GLN B O   
4195  C CB  . GLN B 168 ? 0.3809 0.3455 0.2515 0.0232  0.0031  0.0502  168 GLN B CB  
4196  C CG  . GLN B 168 ? 0.3813 0.3415 0.2520 0.0280  -0.0068 0.0570  168 GLN B CG  
4197  C CD  . GLN B 168 ? 0.3697 0.3388 0.2426 0.0316  -0.0229 0.0515  168 GLN B CD  
4198  O OE1 . GLN B 168 ? 0.4161 0.3849 0.2701 0.0352  -0.0299 0.0488  168 GLN B OE1 
4199  N NE2 . GLN B 168 ? 0.3435 0.3207 0.2401 0.0301  -0.0282 0.0488  168 GLN B NE2 
4200  N N   . ALA B 169 ? 0.3643 0.3556 0.2713 0.0173  -0.0006 0.0249  169 ALA B N   
4201  C CA  . ALA B 169 ? 0.3228 0.3196 0.2347 0.0172  0.0041  0.0171  169 ALA B CA  
4202  C C   . ALA B 169 ? 0.3046 0.3039 0.2232 0.0190  -0.0069 0.0109  169 ALA B C   
4203  O O   . ALA B 169 ? 0.3246 0.3251 0.2521 0.0181  -0.0150 0.0131  169 ALA B O   
4204  C CB  . ALA B 169 ? 0.2918 0.2969 0.2249 0.0132  0.0120  0.0160  169 ALA B CB  
4205  N N   . PRO B 170 ? 0.3361 0.3351 0.2517 0.0215  -0.0057 0.0030  170 PRO B N   
4206  C CA  . PRO B 170 ? 0.3396 0.3361 0.2588 0.0229  -0.0159 -0.0034 170 PRO B CA  
4207  C C   . PRO B 170 ? 0.3122 0.3123 0.2534 0.0213  -0.0210 -0.0020 170 PRO B C   
4208  O O   . PRO B 170 ? 0.3136 0.3102 0.2589 0.0205  -0.0293 -0.0037 170 PRO B O   
4209  C CB  . PRO B 170 ? 0.3426 0.3364 0.2550 0.0266  -0.0101 -0.0129 170 PRO B CB  
4210  C CG  . PRO B 170 ? 0.3721 0.3717 0.2866 0.0266  0.0041  -0.0106 170 PRO B CG  
4211  C CD  . PRO B 170 ? 0.3572 0.3562 0.2640 0.0234  0.0064  -0.0008 170 PRO B CD  
4212  N N   . ILE B 171 ? 0.3041 0.3108 0.2588 0.0208  -0.0166 0.0008  171 ILE B N   
4213  C CA  . ILE B 171 ? 0.2926 0.3008 0.2612 0.0203  -0.0218 0.0038  171 ILE B CA  
4214  C C   . ILE B 171 ? 0.2871 0.3002 0.2592 0.0177  -0.0215 0.0102  171 ILE B C   
4215  O O   . ILE B 171 ? 0.2853 0.3020 0.2655 0.0182  -0.0228 0.0125  171 ILE B O   
4216  C CB  . ILE B 171 ? 0.2909 0.3014 0.2715 0.0242  -0.0207 0.0010  171 ILE B CB  
4217  C CG1 . ILE B 171 ? 0.2739 0.2948 0.2614 0.0253  -0.0144 -0.0006 171 ILE B CG1 
4218  C CG2 . ILE B 171 ? 0.3129 0.3152 0.2916 0.0274  -0.0212 -0.0064 171 ILE B CG2 
4219  C CD1 . ILE B 171 ? 0.2563 0.2833 0.2596 0.0302  -0.0170 -0.0010 171 ILE B CD1 
4220  N N   . SER B 172 ? 0.2909 0.3024 0.2547 0.0158  -0.0202 0.0130  172 SER B N   
4221  C CA  . SER B 172 ? 0.2944 0.3077 0.2615 0.0140  -0.0200 0.0176  172 SER B CA  
4222  C C   . SER B 172 ? 0.2843 0.2974 0.2575 0.0140  -0.0249 0.0203  172 SER B C   
4223  O O   . SER B 172 ? 0.2883 0.2989 0.2639 0.0143  -0.0290 0.0192  172 SER B O   
4224  C CB  . SER B 172 ? 0.3055 0.3145 0.2638 0.0134  -0.0178 0.0210  172 SER B CB  
4225  O OG  . SER B 172 ? 0.3366 0.3422 0.2881 0.0153  -0.0238 0.0218  172 SER B OG  
4226  N N   . LEU B 173 ? 0.2820 0.2974 0.2585 0.0134  -0.0233 0.0232  173 LEU B N   
4227  C CA  . LEU B 173 ? 0.3135 0.3292 0.2955 0.0135  -0.0244 0.0268  173 LEU B CA  
4228  C C   . LEU B 173 ? 0.3407 0.3561 0.3279 0.0128  -0.0274 0.0282  173 LEU B C   
4229  O O   . LEU B 173 ? 0.3457 0.3608 0.3414 0.0115  -0.0297 0.0288  173 LEU B O   
4230  C CB  . LEU B 173 ? 0.3012 0.3189 0.2817 0.0138  -0.0206 0.0283  173 LEU B CB  
4231  C CG  . LEU B 173 ? 0.2922 0.3106 0.2773 0.0141  -0.0180 0.0327  173 LEU B CG  
4232  C CD1 . LEU B 173 ? 0.2571 0.2737 0.2439 0.0143  -0.0182 0.0363  173 LEU B CD1 
4233  C CD2 . LEU B 173 ? 0.3009 0.3201 0.2800 0.0155  -0.0132 0.0319  173 LEU B CD2 
4234  N N   . GLN B 174 ? 0.3275 0.3428 0.3116 0.0137  -0.0279 0.0287  174 GLN B N   
4235  C CA  . GLN B 174 ? 0.3117 0.3294 0.3031 0.0145  -0.0331 0.0300  174 GLN B CA  
4236  C C   . GLN B 174 ? 0.3282 0.3446 0.3176 0.0137  -0.0407 0.0256  174 GLN B C   
4237  O O   . GLN B 174 ? 0.3460 0.3660 0.3483 0.0120  -0.0460 0.0243  174 GLN B O   
4238  C CB  . GLN B 174 ? 0.2856 0.3020 0.2731 0.0177  -0.0332 0.0329  174 GLN B CB  
4239  C CG  . GLN B 174 ? 0.2883 0.2989 0.2598 0.0198  -0.0362 0.0331  174 GLN B CG  
4240  C CD  . GLN B 174 ? 0.2856 0.2907 0.2465 0.0182  -0.0285 0.0324  174 GLN B CD  
4241  O OE1 . GLN B 174 ? 0.3100 0.3170 0.2764 0.0158  -0.0235 0.0307  174 GLN B OE1 
4242  N NE2 . GLN B 174 ? 0.2841 0.2833 0.2299 0.0195  -0.0274 0.0337  174 GLN B NE2 
4243  N N   . ASN B 175 ? 0.3530 0.3646 0.3279 0.0145  -0.0405 0.0222  175 ASN B N   
4244  C CA  . ASN B 175 ? 0.3546 0.3634 0.3239 0.0146  -0.0472 0.0158  175 ASN B CA  
4245  C C   . ASN B 175 ? 0.3267 0.3344 0.3105 0.0115  -0.0490 0.0122  175 ASN B C   
4246  O O   . ASN B 175 ? 0.3102 0.3174 0.3009 0.0096  -0.0568 0.0070  175 ASN B O   
4247  C CB  A ASN B 175 ? 0.3805 0.3841 0.3307 0.0168  -0.0430 0.0127  175 ASN B CB  
4248  C CB  B ASN B 175 ? 0.3886 0.3922 0.3395 0.0166  -0.0425 0.0127  175 ASN B CB  
4249  C CG  A ASN B 175 ? 0.3560 0.3570 0.2890 0.0198  -0.0429 0.0169  175 ASN B CG  
4250  C CG  B ASN B 175 ? 0.4598 0.4591 0.3961 0.0185  -0.0489 0.0055  175 ASN B CG  
4251  O OD1 A ASN B 175 ? 0.3733 0.3759 0.3061 0.0218  -0.0510 0.0192  175 ASN B OD1 
4252  O OD1 B ASN B 175 ? 0.5416 0.5411 0.4851 0.0171  -0.0580 -0.0002 175 ASN B OD1 
4253  N ND2 A ASN B 175 ? 0.2748 0.2720 0.1953 0.0205  -0.0334 0.0186  175 ASN B ND2 
4254  N ND2 B ASN B 175 ? 0.4906 0.4857 0.4059 0.0213  -0.0435 0.0051  175 ASN B ND2 
4255  N N   . GLN B 176 ? 0.3470 0.3537 0.3364 0.0109  -0.0424 0.0154  176 GLN B N   
4256  C CA  . GLN B 176 ? 0.3288 0.3310 0.3303 0.0089  -0.0425 0.0148  176 GLN B CA  
4257  C C   . GLN B 176 ? 0.3229 0.3286 0.3423 0.0049  -0.0431 0.0191  176 GLN B C   
4258  O O   . GLN B 176 ? 0.3111 0.3127 0.3443 0.0012  -0.0453 0.0170  176 GLN B O   
4259  C CB  . GLN B 176 ? 0.2303 0.2301 0.2300 0.0114  -0.0365 0.0186  176 GLN B CB  
4260  C CG  . GLN B 176 ? 0.2820 0.2800 0.2729 0.0152  -0.0353 0.0130  176 GLN B CG  
4261  C CD  . GLN B 176 ? 0.2705 0.2674 0.2650 0.0189  -0.0327 0.0158  176 GLN B CD  
4262  O OE1 . GLN B 176 ? 0.2704 0.2593 0.2719 0.0203  -0.0336 0.0165  176 GLN B OE1 
4263  N NE2 . GLN B 176 ? 0.2556 0.2603 0.2466 0.0207  -0.0303 0.0175  176 GLN B NE2 
4264  N N   . LEU B 177 ? 0.3070 0.3199 0.3286 0.0054  -0.0396 0.0247  177 LEU B N   
4265  C CA  . LEU B 177 ? 0.2964 0.3152 0.3379 0.0021  -0.0381 0.0283  177 LEU B CA  
4266  C C   . LEU B 177 ? 0.2719 0.2966 0.3265 -0.0001 -0.0486 0.0223  177 LEU B C   
4267  O O   . LEU B 177 ? 0.2977 0.3249 0.3744 -0.0053 -0.0503 0.0210  177 LEU B O   
4268  C CB  . LEU B 177 ? 0.2776 0.3027 0.3182 0.0047  -0.0310 0.0341  177 LEU B CB  
4269  C CG  . LEU B 177 ? 0.2538 0.2751 0.2820 0.0067  -0.0221 0.0389  177 LEU B CG  
4270  C CD1 . LEU B 177 ? 0.2163 0.2426 0.2424 0.0094  -0.0161 0.0410  177 LEU B CD1 
4271  C CD2 . LEU B 177 ? 0.2362 0.2529 0.2713 0.0042  -0.0163 0.0445  177 LEU B CD2 
4272  N N   . PHE B 178 ? 0.2599 0.2866 0.3010 0.0038  -0.0559 0.0188  178 PHE B N   
4273  C CA  . PHE B 178 ? 0.2877 0.3203 0.3354 0.0036  -0.0691 0.0126  178 PHE B CA  
4274  C C   . PHE B 178 ? 0.3053 0.3324 0.3597 -0.0014 -0.0760 0.0031  178 PHE B C   
4275  O O   . PHE B 178 ? 0.3023 0.3358 0.3792 -0.0060 -0.0842 -0.0021 178 PHE B O   
4276  C CB  . PHE B 178 ? 0.2955 0.3259 0.3175 0.0100  -0.0754 0.0114  178 PHE B CB  
4277  C CG  . PHE B 178 ? 0.3055 0.3385 0.3219 0.0153  -0.0706 0.0198  178 PHE B CG  
4278  C CD1 . PHE B 178 ? 0.3328 0.3735 0.3693 0.0154  -0.0652 0.0252  178 PHE B CD1 
4279  C CD2 . PHE B 178 ? 0.2667 0.2924 0.2571 0.0202  -0.0701 0.0221  178 PHE B CD2 
4280  C CE1 . PHE B 178 ? 0.3142 0.3543 0.3456 0.0208  -0.0606 0.0313  178 PHE B CE1 
4281  C CE2 . PHE B 178 ? 0.2523 0.2766 0.2388 0.0246  -0.0651 0.0297  178 PHE B CE2 
4282  C CZ  . PHE B 178 ? 0.2420 0.2730 0.2491 0.0252  -0.0612 0.0336  178 PHE B CZ  
4283  N N   . SER B 179 ? 0.3271 0.3424 0.3638 -0.0004 -0.0728 -0.0005 179 SER B N   
4284  C CA  . SER B 179 ? 0.3044 0.3116 0.3430 -0.0034 -0.0797 -0.0118 179 SER B CA  
4285  C C   . SER B 179 ? 0.3123 0.3146 0.3775 -0.0103 -0.0752 -0.0106 179 SER B C   
4286  O O   . SER B 179 ? 0.3330 0.3322 0.4139 -0.0158 -0.0829 -0.0200 179 SER B O   
4287  C CB  . SER B 179 ? 0.3482 0.3445 0.3611 0.0012  -0.0762 -0.0166 179 SER B CB  
4288  O OG  . SER B 179 ? 0.4273 0.4171 0.4430 0.0018  -0.0652 -0.0109 179 SER B OG  
4289  N N   . HIS B 180 ? 0.3060 0.3067 0.3760 -0.0103 -0.0629 0.0008  180 HIS B N   
4290  C CA  . HIS B 180 ? 0.2975 0.2909 0.3896 -0.0163 -0.0566 0.0049  180 HIS B CA  
4291  C C   . HIS B 180 ? 0.3182 0.3223 0.4418 -0.0238 -0.0581 0.0057  180 HIS B C   
4292  O O   . HIS B 180 ? 0.3182 0.3164 0.4660 -0.0316 -0.0586 0.0023  180 HIS B O   
4293  C CB  . HIS B 180 ? 0.2570 0.2455 0.3405 -0.0128 -0.0437 0.0178  180 HIS B CB  
4294  C CG  . HIS B 180 ? 0.2884 0.2644 0.3871 -0.0170 -0.0361 0.0244  180 HIS B CG  
4295  N ND1 . HIS B 180 ? 0.3464 0.3253 0.4614 -0.0214 -0.0262 0.0351  180 HIS B ND1 
4296  C CD2 . HIS B 180 ? 0.2822 0.2410 0.3828 -0.0171 -0.0357 0.0224  180 HIS B CD2 
4297  C CE1 . HIS B 180 ? 0.2848 0.2478 0.4091 -0.0244 -0.0195 0.0411  180 HIS B CE1 
4298  N NE2 . HIS B 180 ? 0.3414 0.2914 0.4581 -0.0216 -0.0259 0.0334  180 HIS B NE2 
4299  N N   . PHE B 181 ? 0.3115 0.3313 0.4379 -0.0216 -0.0584 0.0096  181 PHE B N   
4300  C CA  . PHE B 181 ? 0.2629 0.2966 0.4230 -0.0274 -0.0575 0.0115  181 PHE B CA  
4301  C C   . PHE B 181 ? 0.2771 0.3248 0.4497 -0.0279 -0.0751 0.0004  181 PHE B C   
4302  O O   . PHE B 181 ? 0.3202 0.3832 0.5259 -0.0324 -0.0773 -0.0001 181 PHE B O   
4303  C CB  . PHE B 181 ? 0.2528 0.2951 0.4121 -0.0235 -0.0444 0.0234  181 PHE B CB  
4304  C CG  . PHE B 181 ? 0.2819 0.3124 0.4317 -0.0235 -0.0279 0.0346  181 PHE B CG  
4305  C CD1 . PHE B 181 ? 0.2933 0.3198 0.4661 -0.0308 -0.0171 0.0410  181 PHE B CD1 
4306  C CD2 . PHE B 181 ? 0.3249 0.3479 0.4428 -0.0163 -0.0237 0.0390  181 PHE B CD2 
4307  C CE1 . PHE B 181 ? 0.2907 0.3046 0.4496 -0.0293 -0.0025 0.0531  181 PHE B CE1 
4308  C CE2 . PHE B 181 ? 0.3175 0.3306 0.4244 -0.0150 -0.0114 0.0490  181 PHE B CE2 
4309  C CZ  . PHE B 181 ? 0.3089 0.3166 0.4338 -0.0208 -0.0011 0.0567  181 PHE B CZ  
4310  N N   . GLY B 182 ? 0.2743 0.3180 0.4208 -0.0228 -0.0876 -0.0081 182 GLY B N   
4311  C CA  . GLY B 182 ? 0.2909 0.3471 0.4433 -0.0216 -0.1064 -0.0180 182 GLY B CA  
4312  C C   . GLY B 182 ? 0.2818 0.3553 0.4405 -0.0152 -0.1085 -0.0110 182 GLY B C   
4313  O O   . GLY B 182 ? 0.2804 0.3706 0.4638 -0.0159 -0.1217 -0.0160 182 GLY B O   
4314  N N   . LEU B 183 ? 0.3231 0.3927 0.4611 -0.0086 -0.0965 -0.0002 183 LEU B N   
4315  C CA  . LEU B 183 ? 0.2927 0.3745 0.4359 -0.0015 -0.0956 0.0070  183 LEU B CA  
4316  C C   . LEU B 183 ? 0.3170 0.4001 0.4375 0.0074  -0.1109 0.0049  183 LEU B C   
4317  O O   . LEU B 183 ? 0.3540 0.4259 0.4451 0.0088  -0.1175 -0.0005 183 LEU B O   
4318  C CB  . LEU B 183 ? 0.2762 0.3503 0.4044 0.0018  -0.0772 0.0174  183 LEU B CB  
4319  C CG  . LEU B 183 ? 0.3179 0.3881 0.4577 -0.0043 -0.0605 0.0226  183 LEU B CG  
4320  C CD1 . LEU B 183 ? 0.3101 0.3720 0.4270 0.0002  -0.0468 0.0300  183 LEU B CD1 
4321  C CD2 . LEU B 183 ? 0.3267 0.4125 0.5061 -0.0084 -0.0557 0.0246  183 LEU B CD2 
4322  N N   . LYS B 184 ? 0.3207 0.4167 0.4540 0.0142  -0.1159 0.0095  184 LYS B N   
4323  C CA  . LYS B 184 ? 0.3245 0.4170 0.4302 0.0250  -0.1261 0.0127  184 LYS B CA  
4324  C C   . LYS B 184 ? 0.2814 0.3555 0.3526 0.0281  -0.1114 0.0201  184 LYS B C   
4325  O O   . LYS B 184 ? 0.2663 0.3366 0.3427 0.0253  -0.0951 0.0246  184 LYS B O   
4326  C CB  . LYS B 184 ? 0.5575 0.6660 0.6870 0.0334  -0.1330 0.0180  184 LYS B CB  
4327  C CG  . LYS B 184 ? 0.7306 0.8303 0.8291 0.0463  -0.1393 0.0261  184 LYS B CG  
4328  C CD  . LYS B 184 ? 0.7456 0.8618 0.8681 0.0569  -0.1527 0.0300  184 LYS B CD  
4329  C CE  . LYS B 184 ? 0.5810 0.6841 0.6719 0.0707  -0.1573 0.0409  184 LYS B CE  
4330  N NZ  . LYS B 184 ? 0.5619 0.6433 0.6283 0.0718  -0.1369 0.0498  184 LYS B NZ  
4331  N N   . ARG B 185 ? 0.2997 0.3626 0.3357 0.0335  -0.1172 0.0209  185 ARG B N   
4332  C CA  . ARG B 185 ? 0.2822 0.3289 0.2891 0.0354  -0.1036 0.0271  185 ARG B CA  
4333  C C   . ARG B 185 ? 0.2912 0.3352 0.2980 0.0428  -0.0980 0.0377  185 ARG B C   
4334  O O   . ARG B 185 ? 0.3022 0.3389 0.2877 0.0506  -0.1033 0.0437  185 ARG B O   
4335  C CB  . ARG B 185 ? 0.3274 0.3630 0.2980 0.0377  -0.1092 0.0240  185 ARG B CB  
4336  C CG  . ARG B 185 ? 0.3729 0.4094 0.3448 0.0312  -0.1153 0.0113  185 ARG B CG  
4337  C CD  . ARG B 185 ? 0.4731 0.4975 0.4069 0.0335  -0.1172 0.0059  185 ARG B CD  
4338  N NE  . ARG B 185 ? 0.4997 0.5128 0.4183 0.0319  -0.0992 0.0095  185 ARG B NE  
4339  C CZ  . ARG B 185 ? 0.4676 0.4776 0.3934 0.0261  -0.0907 0.0036  185 ARG B CZ  
4340  N NH1 . ARG B 185 ? 0.4604 0.4634 0.3753 0.0258  -0.0761 0.0071  185 ARG B NH1 
4341  N NH2 . ARG B 185 ? 0.4657 0.4794 0.4115 0.0208  -0.0967 -0.0055 185 ARG B NH2 
4342  N N   . GLN B 186 ? 0.2652 0.3130 0.2936 0.0408  -0.0862 0.0402  186 GLN B N   
4343  C CA  . GLN B 186 ? 0.3151 0.3601 0.3489 0.0475  -0.0798 0.0477  186 GLN B CA  
4344  C C   . GLN B 186 ? 0.3216 0.3652 0.3651 0.0423  -0.0633 0.0467  186 GLN B C   
4345  O O   . GLN B 186 ? 0.3353 0.3876 0.3950 0.0362  -0.0603 0.0425  186 GLN B O   
4346  C CB  . GLN B 186 ? 0.3230 0.3834 0.3842 0.0546  -0.0907 0.0492  186 GLN B CB  
4347  C CG  . GLN B 186 ? 0.3309 0.3883 0.4015 0.0635  -0.0848 0.0563  186 GLN B CG  
4348  C CD  . GLN B 186 ? 0.3303 0.4080 0.4377 0.0699  -0.0938 0.0561  186 GLN B CD  
4349  O OE1 . GLN B 186 ? 0.3582 0.4463 0.4709 0.0750  -0.1123 0.0559  186 GLN B OE1 
4350  N NE2 . GLN B 186 ? 0.3323 0.4174 0.4661 0.0697  -0.0807 0.0553  186 GLN B NE2 
4351  N N   . PHE B 187 ? 0.3197 0.3509 0.3514 0.0442  -0.0526 0.0502  187 PHE B N   
4352  C CA  . PHE B 187 ? 0.2899 0.3212 0.3308 0.0412  -0.0391 0.0480  187 PHE B CA  
4353  C C   . PHE B 187 ? 0.3111 0.3338 0.3535 0.0478  -0.0327 0.0513  187 PHE B C   
4354  O O   . PHE B 187 ? 0.3311 0.3429 0.3619 0.0528  -0.0362 0.0564  187 PHE B O   
4355  C CB  . PHE B 187 ? 0.2933 0.3179 0.3182 0.0337  -0.0320 0.0444  187 PHE B CB  
4356  C CG  . PHE B 187 ? 0.3119 0.3224 0.3155 0.0332  -0.0288 0.0455  187 PHE B CG  
4357  C CD1 . PHE B 187 ? 0.3055 0.3115 0.2927 0.0322  -0.0341 0.0464  187 PHE B CD1 
4358  C CD2 . PHE B 187 ? 0.3110 0.3128 0.3121 0.0331  -0.0193 0.0446  187 PHE B CD2 
4359  C CE1 . PHE B 187 ? 0.3125 0.3068 0.2836 0.0308  -0.0281 0.0480  187 PHE B CE1 
4360  C CE2 . PHE B 187 ? 0.2992 0.2889 0.2867 0.0309  -0.0154 0.0452  187 PHE B CE2 
4361  C CZ  . PHE B 187 ? 0.3064 0.2930 0.2799 0.0295  -0.0188 0.0478  187 PHE B CZ  
4362  N N   . SER B 188 ? 0.3073 0.3335 0.3632 0.0483  -0.0224 0.0484  188 SER B N   
4363  C CA  . SER B 188 ? 0.3258 0.3442 0.3881 0.0554  -0.0153 0.0492  188 SER B CA  
4364  C C   . SER B 188 ? 0.3626 0.3721 0.4156 0.0518  -0.0023 0.0429  188 SER B C   
4365  O O   . SER B 188 ? 0.3598 0.3762 0.4117 0.0468  0.0031  0.0387  188 SER B O   
4366  C CB  . SER B 188 ? 0.3420 0.3756 0.4340 0.0625  -0.0155 0.0500  188 SER B CB  
4367  O OG  . SER B 188 ? 0.3433 0.3870 0.4456 0.0665  -0.0307 0.0545  188 SER B OG  
4368  N N   . VAL B 189 ? 0.3578 0.3507 0.4037 0.0545  0.0024  0.0421  189 VAL B N   
4369  C CA  . VAL B 189 ? 0.3458 0.3298 0.3821 0.0504  0.0123  0.0335  189 VAL B CA  
4370  C C   . VAL B 189 ? 0.3175 0.2944 0.3645 0.0578  0.0216  0.0288  189 VAL B C   
4371  O O   . VAL B 189 ? 0.3230 0.2882 0.3769 0.0645  0.0212  0.0326  189 VAL B O   
4372  C CB  . VAL B 189 ? 0.3121 0.2811 0.3324 0.0445  0.0114  0.0328  189 VAL B CB  
4373  C CG1 . VAL B 189 ? 0.3105 0.2745 0.3226 0.0389  0.0179  0.0219  189 VAL B CG1 
4374  C CG2 . VAL B 189 ? 0.2896 0.2650 0.3004 0.0392  0.0037  0.0372  189 VAL B CG2 
4375  N N   . CYS B 190 ? 0.2841 0.2667 0.3309 0.0575  0.0306  0.0209  190 CYS B N   
4376  C CA  . CYS B 190 ? 0.3011 0.2751 0.3542 0.0644  0.0413  0.0134  190 CYS B CA  
4377  C C   . CYS B 190 ? 0.3109 0.2776 0.3442 0.0593  0.0481  0.0008  190 CYS B C   
4378  O O   . CYS B 190 ? 0.3577 0.3337 0.3841 0.0593  0.0549  -0.0037 190 CYS B O   
4379  C CB  . CYS B 190 ? 0.3940 0.3839 0.4688 0.0723  0.0479  0.0150  190 CYS B CB  
4380  S SG  . CYS B 190 ? 0.4332 0.4124 0.5279 0.0861  0.0578  0.0104  190 CYS B SG  
4381  N N   . LEU B 191 ? 0.4167 0.3664 0.4405 0.0549  0.0460  -0.0048 191 LEU B N   
4382  C CA  . LEU B 191 ? 0.3870 0.3306 0.3928 0.0496  0.0488  -0.0188 191 LEU B CA  
4383  C C   . LEU B 191 ? 0.3558 0.2891 0.3618 0.0562  0.0599  -0.0314 191 LEU B C   
4384  O O   . LEU B 191 ? 0.3829 0.3048 0.4044 0.0633  0.0646  -0.0310 191 LEU B O   
4385  C CB  . LEU B 191 ? 0.3580 0.2896 0.3592 0.0408  0.0424  -0.0218 191 LEU B CB  
4386  C CG  . LEU B 191 ? 0.3272 0.2667 0.3272 0.0343  0.0334  -0.0113 191 LEU B CG  
4387  C CD1 . LEU B 191 ? 0.3436 0.2714 0.3429 0.0255  0.0310  -0.0160 191 LEU B CD1 
4388  C CD2 . LEU B 191 ? 0.3364 0.2944 0.3260 0.0317  0.0290  -0.0094 191 LEU B CD2 
4389  N N   . SER B 192 ? 0.4491 0.3859 0.4359 0.0551  0.0640  -0.0427 192 SER B N   
4390  C CA  . SER B 192 ? 0.3951 0.3213 0.3756 0.0612  0.0750  -0.0579 192 SER B CA  
4391  C C   . SER B 192 ? 0.4590 0.3663 0.4295 0.0552  0.0712  -0.0749 192 SER B C   
4392  O O   . SER B 192 ? 0.4520 0.3622 0.4091 0.0463  0.0614  -0.0794 192 SER B O   
4393  C CB  . SER B 192 ? 0.4033 0.3427 0.3639 0.0641  0.0826  -0.0611 192 SER B CB  
4394  O OG  . SER B 192 ? 0.4386 0.3676 0.3869 0.0703  0.0941  -0.0778 192 SER B OG  
4395  N N   . ARG B 193 ? 0.4741 0.3621 0.4546 0.0604  0.0788  -0.0848 193 ARG B N   
4396  C CA  . ARG B 193 ? 0.4633 0.3305 0.4389 0.0549  0.0770  -0.1035 193 ARG B CA  
4397  C C   . ARG B 193 ? 0.5335 0.4032 0.4796 0.0532  0.0766  -0.1236 193 ARG B C   
4398  O O   . ARG B 193 ? 0.5533 0.4133 0.4920 0.0451  0.0691  -0.1397 193 ARG B O   
4399  C CB  . ARG B 193 ? 0.6059 0.4501 0.6014 0.0632  0.0871  -0.1077 193 ARG B CB  
4400  C CG  . ARG B 193 ? 0.7112 0.5299 0.7045 0.0592  0.0888  -0.1301 193 ARG B CG  
4401  C CD  . ARG B 193 ? 0.8375 0.6292 0.8546 0.0674  0.0983  -0.1311 193 ARG B CD  
4402  N NE  . ARG B 193 ? 0.9879 0.7748 1.0264 0.0667  0.0944  -0.1083 193 ARG B NE  
4403  C CZ  . ARG B 193 ? 1.1030 0.8751 1.1628 0.0777  0.1004  -0.0970 193 ARG B CZ  
4404  N NH1 . ARG B 193 ? 1.1636 0.9238 1.2319 0.0906  0.1118  -0.1072 193 ARG B NH1 
4405  N NH2 . ARG B 193 ? 1.1112 0.8799 1.1830 0.0767  0.0949  -0.0755 193 ARG B NH2 
4406  N N   . TYR B 194 ? 0.5622 0.4457 0.4911 0.0607  0.0843  -0.1223 194 TYR B N   
4407  C CA  . TYR B 194 ? 0.5989 0.4824 0.4941 0.0624  0.0864  -0.1407 194 TYR B CA  
4408  C C   . TYR B 194 ? 0.5563 0.4583 0.4263 0.0576  0.0760  -0.1347 194 TYR B C   
4409  O O   . TYR B 194 ? 0.5134 0.4313 0.3886 0.0581  0.0762  -0.1151 194 TYR B O   
4410  C CB  . TYR B 194 ? 0.6686 0.5526 0.5574 0.0753  0.1056  -0.1437 194 TYR B CB  
4411  C CG  . TYR B 194 ? 0.7312 0.6021 0.6528 0.0830  0.1164  -0.1426 194 TYR B CG  
4412  C CD1 . TYR B 194 ? 0.7958 0.6412 0.7230 0.0842  0.1189  -0.1617 194 TYR B CD1 
4413  C CD2 . TYR B 194 ? 0.7330 0.6164 0.6813 0.0895  0.1230  -0.1229 194 TYR B CD2 
4414  C CE1 . TYR B 194 ? 0.8307 0.6619 0.7882 0.0929  0.1284  -0.1593 194 TYR B CE1 
4415  C CE2 . TYR B 194 ? 0.7707 0.6433 0.7497 0.0985  0.1308  -0.1209 194 TYR B CE2 
4416  C CZ  . TYR B 194 ? 0.8397 0.6853 0.8226 0.1008  0.1339  -0.1383 194 TYR B CZ  
4417  O OH  . TYR B 194 ? 0.8926 0.7252 0.9066 0.1114  0.1415  -0.1350 194 TYR B OH  
4418  N N   . SER B 195 ? 0.5625 0.4623 0.4064 0.0534  0.0659  -0.1518 195 SER B N   
4419  C CA  . SER B 195 ? 0.5628 0.4793 0.3810 0.0512  0.0550  -0.1457 195 SER B CA  
4420  C C   . SER B 195 ? 0.5713 0.4964 0.3606 0.0609  0.0679  -0.1382 195 SER B C   
4421  O O   . SER B 195 ? 0.5747 0.5129 0.3471 0.0607  0.0627  -0.1256 195 SER B O   
4422  C CB  . SER B 195 ? 0.5797 0.4932 0.3772 0.0456  0.0387  -0.1671 195 SER B CB  
4423  O OG  . SER B 195 ? 0.6470 0.5469 0.4205 0.0514  0.0456  -0.1898 195 SER B OG  
4424  N N   . THR B 196 ? 0.6126 0.5294 0.3978 0.0696  0.0863  -0.1454 196 THR B N   
4425  C CA  . THR B 196 ? 0.6436 0.5666 0.4000 0.0790  0.1028  -0.1411 196 THR B CA  
4426  C C   . THR B 196 ? 0.6681 0.6042 0.4480 0.0825  0.1177  -0.1176 196 THR B C   
4427  O O   . THR B 196 ? 0.6912 0.6338 0.4519 0.0889  0.1338  -0.1111 196 THR B O   
4428  C CB  . THR B 196 ? 0.6609 0.5693 0.3994 0.0877  0.1178  -0.1634 196 THR B CB  
4429  O OG1 . THR B 196 ? 0.6251 0.5235 0.4035 0.0896  0.1262  -0.1664 196 THR B OG1 
4430  C CG2 . THR B 196 ? 0.6909 0.5873 0.3997 0.0845  0.1029  -0.1893 196 THR B CG2 
4431  N N   . SER B 197 ? 0.6315 0.5716 0.4528 0.0779  0.1126  -0.1052 197 SER B N   
4432  C CA  . SER B 197 ? 0.5707 0.5251 0.4185 0.0795  0.1218  -0.0842 197 SER B CA  
4433  C C   . SER B 197 ? 0.5220 0.4825 0.3969 0.0712  0.1055  -0.0703 197 SER B C   
4434  O O   . SER B 197 ? 0.5754 0.5268 0.4621 0.0666  0.0936  -0.0762 197 SER B O   
4435  C CB  . SER B 197 ? 0.5663 0.5190 0.4404 0.0884  0.1400  -0.0872 197 SER B CB  
4436  O OG  . SER B 197 ? 0.5563 0.4949 0.4528 0.0885  0.1337  -0.0963 197 SER B OG  
4437  N N   . ASN B 198 ? 0.4422 0.4171 0.3267 0.0693  0.1063  -0.0521 198 ASN B N   
4438  C CA  . ASN B 198 ? 0.4030 0.3840 0.3069 0.0619  0.0914  -0.0396 198 ASN B CA  
4439  C C   . ASN B 198 ? 0.3803 0.3632 0.3221 0.0628  0.0905  -0.0332 198 ASN B C   
4440  O O   . ASN B 198 ? 0.4737 0.4594 0.4341 0.0696  0.1027  -0.0328 198 ASN B O   
4441  C CB  . ASN B 198 ? 0.5578 0.5512 0.4569 0.0593  0.0921  -0.0241 198 ASN B CB  
4442  C CG  . ASN B 198 ? 0.5685 0.5597 0.4298 0.0581  0.0865  -0.0260 198 ASN B CG  
4443  O OD1 . ASN B 198 ? 0.5855 0.5690 0.4273 0.0572  0.0769  -0.0393 198 ASN B OD1 
4444  N ND2 . ASN B 198 ? 0.5581 0.5560 0.4102 0.0581  0.0918  -0.0124 198 ASN B ND2 
4445  N N   . GLY B 199 ? 0.3706 0.3327 0.3181 0.0479  0.1230  -0.0403 199 GLY B N   
4446  C CA  . GLY B 199 ? 0.3339 0.3051 0.3228 0.0454  0.1169  -0.0363 199 GLY B CA  
4447  C C   . GLY B 199 ? 0.3456 0.3319 0.3548 0.0398  0.1109  -0.0250 199 GLY B C   
4448  O O   . GLY B 199 ? 0.3376 0.3259 0.3329 0.0406  0.1168  -0.0189 199 GLY B O   
4449  N N   . ALA B 200 ? 0.3579 0.3527 0.3974 0.0344  0.0997  -0.0222 200 ALA B N   
4450  C CA  . ALA B 200 ? 0.3532 0.3572 0.4097 0.0279  0.0949  -0.0134 200 ALA B CA  
4451  C C   . ALA B 200 ? 0.3476 0.3541 0.4179 0.0203  0.0766  -0.0149 200 ALA B C   
4452  O O   . ALA B 200 ? 0.3446 0.3502 0.4214 0.0205  0.0685  -0.0199 200 ALA B O   
4453  C CB  . ALA B 200 ? 0.3592 0.3741 0.4464 0.0290  0.1084  -0.0040 200 ALA B CB  
4454  N N   . ILE B 201 ? 0.3261 0.3328 0.3973 0.0146  0.0716  -0.0101 201 ILE B N   
4455  C CA  . ILE B 201 ? 0.3219 0.3296 0.4071 0.0072  0.0575  -0.0103 201 ILE B CA  
4456  C C   . ILE B 201 ? 0.3313 0.3439 0.4416 0.0007  0.0609  -0.0037 201 ILE B C   
4457  O O   . ILE B 201 ? 0.3523 0.3616 0.4595 0.0005  0.0722  0.0023  201 ILE B O   
4458  C CB  . ILE B 201 ? 0.3222 0.3218 0.3842 0.0058  0.0486  -0.0120 201 ILE B CB  
4459  C CG1 . ILE B 201 ? 0.3720 0.3699 0.4125 0.0098  0.0455  -0.0182 201 ILE B CG1 
4460  C CG2 . ILE B 201 ? 0.2895 0.2867 0.3605 -0.0004 0.0353  -0.0136 201 ILE B CG2 
4461  C CD1 . ILE B 201 ? 0.3965 0.3924 0.4190 0.0088  0.0367  -0.0187 201 ILE B CD1 
4462  N N   . LEU B 202 ? 0.3195 0.3402 0.4548 -0.0054 0.0508  -0.0043 202 LEU B N   
4463  C CA  . LEU B 202 ? 0.2939 0.3219 0.4574 -0.0154 0.0503  0.0007  202 LEU B CA  
4464  C C   . LEU B 202 ? 0.2686 0.2871 0.4265 -0.0251 0.0343  -0.0034 202 LEU B C   
4465  O O   . LEU B 202 ? 0.2852 0.3023 0.4346 -0.0239 0.0212  -0.0084 202 LEU B O   
4466  C CB  . LEU B 202 ? 0.3045 0.3549 0.5050 -0.0149 0.0506  0.0043  202 LEU B CB  
4467  C CG  . LEU B 202 ? 0.3583 0.4217 0.5790 -0.0088 0.0703  0.0118  202 LEU B CG  
4468  C CD1 . LEU B 202 ? 0.3853 0.4388 0.5781 0.0048  0.0830  0.0088  202 LEU B CD1 
4469  C CD2 . LEU B 202 ? 0.3589 0.4478 0.6209 -0.0082 0.0667  0.0166  202 LEU B CD2 
4470  N N   . PHE B 203 ? 0.2801 0.2887 0.4402 -0.0344 0.0368  -0.0013 203 PHE B N   
4471  C CA  . PHE B 203 ? 0.2571 0.2504 0.4062 -0.0436 0.0238  -0.0066 203 PHE B CA  
4472  C C   . PHE B 203 ? 0.2506 0.2510 0.4289 -0.0597 0.0166  -0.0064 203 PHE B C   
4473  O O   . PHE B 203 ? 0.2820 0.2842 0.4789 -0.0666 0.0274  -0.0008 203 PHE B O   
4474  C CB  . PHE B 203 ? 0.2822 0.2505 0.4029 -0.0412 0.0325  -0.0056 203 PHE B CB  
4475  C CG  . PHE B 203 ? 0.2859 0.2523 0.3808 -0.0271 0.0378  -0.0045 203 PHE B CG  
4476  C CD1 . PHE B 203 ? 0.2826 0.2433 0.3570 -0.0226 0.0282  -0.0094 203 PHE B CD1 
4477  C CD2 . PHE B 203 ? 0.2804 0.2516 0.3714 -0.0191 0.0522  0.0017  203 PHE B CD2 
4478  C CE1 . PHE B 203 ? 0.3390 0.3018 0.3943 -0.0122 0.0316  -0.0079 203 PHE B CE1 
4479  C CE2 . PHE B 203 ? 0.2886 0.2604 0.3560 -0.0084 0.0542  0.0021  203 PHE B CE2 
4480  C CZ  . PHE B 203 ? 0.3420 0.3111 0.3938 -0.0058 0.0434  -0.0027 203 PHE B CZ  
4481  N N   . GLY B 204 ? 0.2491 0.2546 0.4316 -0.0664 -0.0022 -0.0120 204 GLY B N   
4482  C CA  . GLY B 204 ? 0.2547 0.2713 0.4654 -0.0835 -0.0133 -0.0125 204 GLY B CA  
4483  C C   . GLY B 204 ? 0.2650 0.3153 0.5065 -0.0819 -0.0254 -0.0092 204 GLY B C   
4484  O O   . GLY B 204 ? 0.2391 0.2984 0.4771 -0.0670 -0.0231 -0.0070 204 GLY B O   
4485  N N   . ASP B 205 ? 0.3134 0.3819 0.5851 -0.0977 -0.0386 -0.0083 205 ASP B N   
4486  C CA  . ASP B 205 ? 0.3375 0.4415 0.6411 -0.0963 -0.0531 -0.0033 205 ASP B CA  
4487  C C   . ASP B 205 ? 0.3086 0.4436 0.6534 -0.0875 -0.0381 0.0087  205 ASP B C   
4488  O O   . ASP B 205 ? 0.2961 0.4438 0.6722 -0.0980 -0.0294 0.0145  205 ASP B O   
4489  C CB  . ASP B 205 ? 0.3687 0.4843 0.6903 -0.1180 -0.0750 -0.0065 205 ASP B CB  
4490  C CG  . ASP B 205 ? 0.3756 0.5283 0.7246 -0.1157 -0.0944 -0.0008 205 ASP B CG  
4491  O OD1 . ASP B 205 ? 0.3941 0.5572 0.7423 -0.0961 -0.0915 0.0048  205 ASP B OD1 
4492  O OD2 . ASP B 205 ? 0.3966 0.5641 0.7597 -0.1326 -0.1119 -0.0023 205 ASP B OD2 
4493  N N   . ILE B 206 ? 0.3275 0.4757 0.6760 -0.0694 -0.0355 0.0132  206 ILE B N   
4494  C CA  . ILE B 206 ? 0.3718 0.5456 0.7559 -0.0582 -0.0181 0.0243  206 ILE B CA  
4495  C C   . ILE B 206 ? 0.4010 0.6179 0.8372 -0.0629 -0.0300 0.0344  206 ILE B C   
4496  O O   . ILE B 206 ? 0.4401 0.6833 0.9142 -0.0552 -0.0153 0.0456  206 ILE B O   
4497  C CB  . ILE B 206 ? 0.3518 0.5175 0.7168 -0.0360 -0.0079 0.0245  206 ILE B CB  
4498  C CG1 . ILE B 206 ? 0.3426 0.5099 0.6972 -0.0315 -0.0283 0.0225  206 ILE B CG1 
4499  C CG2 . ILE B 206 ? 0.3581 0.4896 0.6791 -0.0304 0.0062  0.0170  206 ILE B CG2 
4500  C CD1 . ILE B 206 ? 0.3449 0.5019 0.6831 -0.0122 -0.0194 0.0227  206 ILE B CD1 
4501  N N   . ASN B 207 ? 0.4244 0.6489 0.8622 -0.0765 -0.0565 0.0308  207 ASN B N   
4502  C CA  . ASN B 207 ? 0.4230 0.6864 0.8966 -0.0806 -0.0726 0.0392  207 ASN B CA  
4503  C C   . ASN B 207 ? 0.4214 0.6892 0.9032 -0.1051 -0.0807 0.0357  207 ASN B C   
4504  O O   . ASN B 207 ? 0.4573 0.7460 0.9485 -0.1150 -0.1005 0.0358  207 ASN B O   
4505  C CB  . ASN B 207 ? 0.4768 0.7419 0.9315 -0.0757 -0.0968 0.0368  207 ASN B CB  
4506  C CG  . ASN B 207 ? 0.5200 0.7754 0.9609 -0.0517 -0.0884 0.0398  207 ASN B CG  
4507  O OD1 . ASN B 207 ? 0.5139 0.7819 0.9770 -0.0349 -0.0697 0.0489  207 ASN B OD1 
4508  N ND2 . ASN B 207 ? 0.5508 0.7775 0.9453 -0.0491 -0.0992 0.0310  207 ASN B ND2 
4509  N N   . ASP B 208 ? 0.3998 0.6476 0.8781 -0.1145 -0.0642 0.0328  208 ASP B N   
4510  C CA  . ASP B 208 ? 0.4339 0.6775 0.9163 -0.1383 -0.0682 0.0286  208 ASP B CA  
4511  C C   . ASP B 208 ? 0.4609 0.7317 0.9844 -0.1376 -0.0497 0.0413  208 ASP B C   
4512  O O   . ASP B 208 ? 0.4544 0.7177 0.9815 -0.1257 -0.0246 0.0474  208 ASP B O   
4513  C CB  . ASP B 208 ? 0.4822 0.6793 0.9288 -0.1485 -0.0608 0.0179  208 ASP B CB  
4514  C CG  . ASP B 208 ? 0.5385 0.7251 0.9866 -0.1734 -0.0625 0.0132  208 ASP B CG  
4515  O OD1 . ASP B 208 ? 0.5700 0.7881 1.0492 -0.1849 -0.0701 0.0174  208 ASP B OD1 
4516  O OD2 . ASP B 208 ? 0.5477 0.6936 0.9663 -0.1813 -0.0548 0.0056  208 ASP B OD2 
4517  N N   . PRO B 209 ? 0.4968 0.8018 1.0513 -0.1487 -0.0619 0.0457  209 PRO B N   
4518  C CA  . PRO B 209 ? 0.4961 0.8323 1.0942 -0.1492 -0.0463 0.0586  209 PRO B CA  
4519  C C   . PRO B 209 ? 0.4921 0.8051 1.0876 -0.1555 -0.0213 0.0605  209 PRO B C   
4520  O O   . PRO B 209 ? 0.5146 0.8439 1.1356 -0.1452 0.0007  0.0728  209 PRO B O   
4521  C CB  . PRO B 209 ? 0.5395 0.9044 1.1600 -0.1705 -0.0693 0.0564  209 PRO B CB  
4522  C CG  . PRO B 209 ? 0.5488 0.8850 1.1280 -0.1849 -0.0927 0.0394  209 PRO B CG  
4523  C CD  . PRO B 209 ? 0.5161 0.8293 1.0625 -0.1641 -0.0915 0.0369  209 PRO B CD  
4524  N N   . ASN B 210 ? 0.5041 0.7772 1.0663 -0.1702 -0.0231 0.0492  210 ASN B N   
4525  C CA  . ASN B 210 ? 0.5247 0.7710 1.0791 -0.1739 0.0014  0.0520  210 ASN B CA  
4526  C C   . ASN B 210 ? 0.4934 0.7297 1.0373 -0.1485 0.0256  0.0586  210 ASN B C   
4527  O O   . ASN B 210 ? 0.4921 0.7195 1.0382 -0.1444 0.0504  0.0665  210 ASN B O   
4528  C CB  . ASN B 210 ? 0.5802 0.7801 1.0954 -0.1908 -0.0045 0.0388  210 ASN B CB  
4529  C CG  . ASN B 210 ? 0.6522 0.8538 1.1723 -0.2188 -0.0229 0.0308  210 ASN B CG  
4530  O OD1 . ASN B 210 ? 0.6848 0.8683 1.1767 -0.2290 -0.0435 0.0168  210 ASN B OD1 
4531  N ND2 . ASN B 210 ? 0.6855 0.9094 1.2408 -0.2318 -0.0150 0.0390  210 ASN B ND2 
4532  N N   . ASN B 211 ? 0.4787 0.7145 1.0076 -0.1318 0.0187  0.0550  211 ASN B N   
4533  C CA  . ASN B 211 ? 0.4523 0.6776 0.9671 -0.1088 0.0404  0.0586  211 ASN B CA  
4534  C C   . ASN B 211 ? 0.4342 0.6911 0.9741 -0.0887 0.0499  0.0689  211 ASN B C   
4535  O O   . ASN B 211 ? 0.4336 0.6817 0.9585 -0.0687 0.0664  0.0700  211 ASN B O   
4536  C CB  . ASN B 211 ? 0.4164 0.6168 0.8961 -0.1027 0.0302  0.0474  211 ASN B CB  
4537  C CG  . ASN B 211 ? 0.3933 0.5569 0.8425 -0.1187 0.0234  0.0371  211 ASN B CG  
4538  O OD1 . ASN B 211 ? 0.4144 0.5602 0.8591 -0.1270 0.0382  0.0396  211 ASN B OD1 
4539  N ND2 . ASN B 211 ? 0.3513 0.4973 0.7672 -0.1195 0.0024  0.0251  211 ASN B ND2 
4540  N N   . ASN B 212 ? 0.4068 0.6987 0.9829 -0.0937 0.0408  0.0761  212 ASN B N   
4541  C CA  . ASN B 212 ? 0.4201 0.7405 1.0200 -0.0733 0.0494  0.0865  212 ASN B CA  
4542  C C   . ASN B 212 ? 0.3820 0.6970 0.9806 -0.0555 0.0821  0.0948  212 ASN B C   
4543  O O   . ASN B 212 ? 0.3860 0.7053 0.9828 -0.0333 0.0933  0.0987  212 ASN B O   
4544  C CB  . ASN B 212 ? 0.4843 0.8457 1.1269 -0.0828 0.0367  0.0946  212 ASN B CB  
4545  C CG  . ASN B 212 ? 0.4923 0.8813 1.1588 -0.0600 0.0459  0.1063  212 ASN B CG  
4546  O OD1 . ASN B 212 ? 0.4579 0.8429 1.1109 -0.0425 0.0421  0.1048  212 ASN B OD1 
4547  N ND2 . ASN B 212 ? 0.5344 0.9482 1.2350 -0.0589 0.0610  0.1184  212 ASN B ND2 
4548  N N   . ASN B 213 ? 0.3453 0.6479 0.9414 -0.0648 0.0979  0.0975  213 ASN B N   
4549  C CA  . ASN B 213 ? 0.3432 0.6407 0.9354 -0.0491 0.1285  0.1061  213 ASN B CA  
4550  C C   . ASN B 213 ? 0.3293 0.5941 0.8760 -0.0313 0.1435  0.0995  213 ASN B C   
4551  O O   . ASN B 213 ? 0.3381 0.5991 0.8738 -0.0113 0.1646  0.1037  213 ASN B O   
4552  C CB  . ASN B 213 ? 0.4212 0.7139 1.0221 -0.0652 0.1390  0.1115  213 ASN B CB  
4553  C CG  . ASN B 213 ? 0.5206 0.8489 1.1685 -0.0815 0.1281  0.1187  213 ASN B CG  
4554  O OD1 . ASN B 213 ? 0.5852 0.9144 1.2404 -0.1051 0.1081  0.1128  213 ASN B OD1 
4555  N ND2 . ASN B 213 ? 0.5210 0.8786 1.1996 -0.0693 0.1405  0.1308  213 ASN B ND2 
4556  N N   . TYR B 214 ? 0.2909 0.5305 0.8087 -0.0393 0.1328  0.0887  214 TYR B N   
4557  C CA  . TYR B 214 ? 0.2711 0.4823 0.7457 -0.0245 0.1445  0.0815  214 TYR B CA  
4558  C C   . TYR B 214 ? 0.2543 0.4697 0.7227 -0.0085 0.1371  0.0758  214 TYR B C   
4559  O O   . TYR B 214 ? 0.2361 0.4355 0.6755 0.0097  0.1528  0.0725  214 TYR B O   
4560  C CB  . TYR B 214 ? 0.2359 0.4196 0.6833 -0.0378 0.1372  0.0732  214 TYR B CB  
4561  C CG  . TYR B 214 ? 0.2676 0.4202 0.6596 -0.0217 0.1479  0.0660  214 TYR B CG  
4562  C CD1 . TYR B 214 ? 0.3039 0.4445 0.6767 -0.0127 0.1741  0.0723  214 TYR B CD1 
4563  C CD2 . TYR B 214 ? 0.2667 0.4025 0.6231 -0.0154 0.1309  0.0532  214 TYR B CD2 
4564  C CE1 . TYR B 214 ? 0.2993 0.4137 0.6185 0.0013  0.1806  0.0653  214 TYR B CE1 
4565  C CE2 . TYR B 214 ? 0.2820 0.3921 0.5885 -0.0025 0.1384  0.0465  214 TYR B CE2 
4566  C CZ  . TYR B 214 ? 0.2872 0.3877 0.5753 0.0054  0.1622  0.0522  214 TYR B CZ  
4567  O OH  . TYR B 214 ? 0.3122 0.3902 0.5503 0.0168  0.1674  0.0455  214 TYR B OH  
4568  N N   . ILE B 215 ? 0.2547 0.4887 0.7460 -0.0156 0.1125  0.0742  215 ILE B N   
4569  C CA  . ILE B 215 ? 0.2916 0.5266 0.7761 -0.0012 0.1038  0.0697  215 ILE B CA  
4570  C C   . ILE B 215 ? 0.3257 0.5855 0.8373 0.0126  0.1077  0.0796  215 ILE B C   
4571  O O   . ILE B 215 ? 0.3493 0.6114 0.8596 0.0246  0.0998  0.0784  215 ILE B O   
4572  C CB  . ILE B 215 ? 0.3833 0.6145 0.8593 -0.0135 0.0724  0.0609  215 ILE B CB  
4573  C CG1 . ILE B 215 ? 0.3950 0.6543 0.9085 -0.0328 0.0519  0.0659  215 ILE B CG1 
4574  C CG2 . ILE B 215 ? 0.3795 0.5718 0.8041 -0.0219 0.0675  0.0484  215 ILE B CG2 
4575  C CD1 . ILE B 215 ? 0.4162 0.7025 0.9516 -0.0260 0.0353  0.0712  215 ILE B CD1 
4576  N N   . HIS B 216 ? 0.3508 0.6278 0.8867 0.0113  0.1209  0.0902  216 HIS B N   
4577  C CA  . HIS B 216 ? 0.3408 0.6447 0.9075 0.0235  0.1257  0.1014  216 HIS B CA  
4578  C C   . HIS B 216 ? 0.3391 0.6272 0.8846 0.0490  0.1417  0.1003  216 HIS B C   
4579  O O   . HIS B 216 ? 0.3270 0.6292 0.8880 0.0602  0.1354  0.1051  216 HIS B O   
4580  C CB  . HIS B 216 ? 0.3999 0.7198 0.9914 0.0196  0.1427  0.1126  216 HIS B CB  
4581  C CG  . HIS B 216 ? 0.4767 0.8266 1.1032 0.0318  0.1487  0.1253  216 HIS B CG  
4582  N ND1 . HIS B 216 ? 0.5325 0.8729 1.1487 0.0544  0.1742  0.1300  216 HIS B ND1 
4583  C CD2 . HIS B 216 ? 0.4932 0.8817 1.1630 0.0255  0.1321  0.1341  216 HIS B CD2 
4584  C CE1 . HIS B 216 ? 0.5436 0.9157 1.1979 0.0623  0.1747  0.1424  216 HIS B CE1 
4585  N NE2 . HIS B 216 ? 0.5167 0.9203 1.2051 0.0452  0.1490  0.1455  216 HIS B NE2 
4586  N N   . ASN B 217 ? 0.3831 0.6390 0.8889 0.0579  0.1619  0.0933  217 ASN B N   
4587  C CA  . ASN B 217 ? 0.4388 0.6723 0.9162 0.0799  0.1778  0.0892  217 ASN B CA  
4588  C C   . ASN B 217 ? 0.4698 0.6880 0.9287 0.0864  0.1634  0.0797  217 ASN B C   
4589  O O   . ASN B 217 ? 0.5502 0.7506 0.9905 0.1038  0.1737  0.0771  217 ASN B O   
4590  C CB  . ASN B 217 ? 0.4585 0.6600 0.8917 0.0850  0.2001  0.0824  217 ASN B CB  
4591  C CG  . ASN B 217 ? 0.4907 0.6643 0.8884 0.1054  0.2167  0.0761  217 ASN B CG  
4592  O OD1 . ASN B 217 ? 0.5214 0.7017 0.9322 0.1185  0.2304  0.0841  217 ASN B OD1 
4593  N ND2 . ASN B 217 ? 0.4784 0.6194 0.8303 0.1075  0.2153  0.0611  217 ASN B ND2 
4594  N N   . SER B 218 ? 0.3938 0.6166 0.8568 0.0724  0.1400  0.0748  218 SER B N   
4595  C CA  . SER B 218 ? 0.2697 0.4769 0.7147 0.0778  0.1264  0.0665  218 SER B CA  
4596  C C   . SER B 218 ? 0.2428 0.4763 0.7191 0.0775  0.1041  0.0747  218 SER B C   
4597  O O   . SER B 218 ? 0.2437 0.4674 0.7086 0.0799  0.0892  0.0700  218 SER B O   
4598  C CB  . SER B 218 ? 0.2523 0.4395 0.6673 0.0632  0.1131  0.0542  218 SER B CB  
4599  O OG  . SER B 218 ? 0.2361 0.4441 0.6737 0.0445  0.0892  0.0570  218 SER B OG  
4600  N N   . LEU B 219 ? 0.2302 0.4974 0.7449 0.0743  0.1015  0.0873  219 LEU B N   
4601  C CA  . LEU B 219 ? 0.2637 0.5612 0.8081 0.0696  0.0768  0.0953  219 LEU B CA  
4602  C C   . LEU B 219 ? 0.2656 0.5590 0.8062 0.0891  0.0741  0.0994  219 LEU B C   
4603  O O   . LEU B 219 ? 0.2545 0.5574 0.7986 0.0855  0.0504  0.1007  219 LEU B O   
4604  C CB  . LEU B 219 ? 0.2914 0.6269 0.8782 0.0619  0.0769  0.1077  219 LEU B CB  
4605  C CG  . LEU B 219 ? 0.2550 0.5994 0.8510 0.0361  0.0673  0.1044  219 LEU B CG  
4606  C CD1 . LEU B 219 ? 0.2521 0.6308 0.8893 0.0284  0.0711  0.1162  219 LEU B CD1 
4607  C CD2 . LEU B 219 ? 0.2358 0.5817 0.8251 0.0190  0.0358  0.0971  219 LEU B CD2 
4608  N N   . ASP B 220 ? 0.2926 0.5673 0.8206 0.1092  0.0982  0.1007  220 ASP B N   
4609  C CA  . ASP B 220 ? 0.3540 0.6191 0.8761 0.1278  0.0981  0.1047  220 ASP B CA  
4610  C C   . ASP B 220 ? 0.3578 0.5912 0.8452 0.1275  0.0874  0.0934  220 ASP B C   
4611  O O   . ASP B 220 ? 0.3795 0.6136 0.8672 0.1340  0.0736  0.0979  220 ASP B O   
4612  C CB  . ASP B 220 ? 0.4469 0.6917 0.9576 0.1481  0.1277  0.1065  220 ASP B CB  
4613  C CG  . ASP B 220 ? 0.5484 0.8264 1.0972 0.1520  0.1392  0.1208  220 ASP B CG  
4614  O OD1 . ASP B 220 ? 0.5190 0.8378 1.1080 0.1474  0.1228  0.1333  220 ASP B OD1 
4615  O OD2 . ASP B 220 ? 0.6373 0.9002 1.1747 0.1598  0.1648  0.1197  220 ASP B OD2 
4616  N N   . VAL B 221 ? 0.3286 0.5342 0.7856 0.1202  0.0943  0.0795  221 VAL B N   
4617  C CA  . VAL B 221 ? 0.2797 0.4564 0.7056 0.1177  0.0843  0.0682  221 VAL B CA  
4618  C C   . VAL B 221 ? 0.2451 0.4419 0.6834 0.1030  0.0536  0.0704  221 VAL B C   
4619  O O   . VAL B 221 ? 0.2397 0.4221 0.6591 0.1053  0.0397  0.0691  221 VAL B O   
4620  C CB  . VAL B 221 ? 0.3265 0.4726 0.7146 0.1097  0.0959  0.0525  221 VAL B CB  
4621  C CG1 . VAL B 221 ? 0.3293 0.4401 0.6698 0.1016  0.0819  0.0389  221 VAL B CG1 
4622  C CG2 . VAL B 221 ? 0.3743 0.4990 0.7453 0.1240  0.1252  0.0492  221 VAL B CG2 
4623  N N   . LEU B 222 ? 0.2559 0.4803 0.7164 0.0855  0.0427  0.0724  222 LEU B N   
4624  C CA  . LEU B 222 ? 0.2701 0.5052 0.7280 0.0673  0.0129  0.0704  222 LEU B CA  
4625  C C   . LEU B 222 ? 0.3226 0.5843 0.8040 0.0732  -0.0066 0.0828  222 LEU B C   
4626  O O   . LEU B 222 ? 0.3279 0.5862 0.7937 0.0657  -0.0296 0.0803  222 LEU B O   
4627  C CB  . LEU B 222 ? 0.2506 0.5071 0.7291 0.0466  0.0073  0.0699  222 LEU B CB  
4628  C CG  . LEU B 222 ? 0.2525 0.4825 0.7021 0.0371  0.0222  0.0585  222 LEU B CG  
4629  C CD1 . LEU B 222 ? 0.2152 0.4641 0.6871 0.0160  0.0155  0.0597  222 LEU B CD1 
4630  C CD2 . LEU B 222 ? 0.2658 0.4546 0.6593 0.0339  0.0167  0.0439  222 LEU B CD2 
4631  N N   . HIS B 223 ? 0.3629 0.6461 0.8696 0.0848  0.0024  0.0947  223 HIS B N   
4632  C CA  . HIS B 223 ? 0.3930 0.7005 0.9161 0.0920  -0.0137 0.1069  223 HIS B CA  
4633  C C   . HIS B 223 ? 0.3979 0.6799 0.8957 0.1081  -0.0157 0.1082  223 HIS B C   
4634  O O   . HIS B 223 ? 0.4203 0.7168 0.9212 0.1113  -0.0344 0.1165  223 HIS B O   
4635  C CB  . HIS B 223 ? 0.4298 0.7644 0.9872 0.1031  0.0003  0.1197  223 HIS B CB  
4636  C CG  . HIS B 223 ? 0.4460 0.8103 1.0329 0.0862  -0.0002 0.1213  223 HIS B CG  
4637  N ND1 . HIS B 223 ? 0.4484 0.8342 1.0660 0.0940  0.0174  0.1315  223 HIS B ND1 
4638  C CD2 . HIS B 223 ? 0.4206 0.7935 1.0096 0.0617  -0.0150 0.1142  223 HIS B CD2 
4639  C CE1 . HIS B 223 ? 0.4358 0.8436 1.0749 0.0747  0.0133  0.1312  223 HIS B CE1 
4640  N NE2 . HIS B 223 ? 0.4200 0.8189 1.0414 0.0546  -0.0061 0.1203  223 HIS B NE2 
4641  N N   . ASP B 224 ? 0.3948 0.6376 0.8665 0.1189  0.0052  0.1004  224 ASP B N   
4642  C CA  . ASP B 224 ? 0.3884 0.5993 0.8337 0.1339  0.0079  0.1009  224 ASP B CA  
4643  C C   . ASP B 224 ? 0.3352 0.5153 0.7467 0.1249  -0.0010 0.0891  224 ASP B C   
4644  O O   . ASP B 224 ? 0.3206 0.4647 0.7021 0.1336  0.0059  0.0857  224 ASP B O   
4645  C CB  . ASP B 224 ? 0.4049 0.5861 0.8383 0.1518  0.0379  0.0989  224 ASP B CB  
4646  C CG  . ASP B 224 ? 0.3985 0.6048 0.8615 0.1642  0.0481  0.1119  224 ASP B CG  
4647  O OD1 . ASP B 224 ? 0.3740 0.6181 0.8650 0.1630  0.0301  0.1244  224 ASP B OD1 
4648  O OD2 . ASP B 224 ? 0.4066 0.5942 0.8632 0.1750  0.0737  0.1092  224 ASP B OD2 
4649  N N   . LEU B 225 ? 0.3253 0.5101 0.7249 0.1027  -0.0146 0.0789  225 LEU B N   
4650  C CA  . LEU B 225 ? 0.3069 0.4583 0.6583 0.0895  -0.0233 0.0648  225 LEU B CA  
4651  C C   . LEU B 225 ? 0.2801 0.4267 0.6168 0.0931  -0.0413 0.0711  225 LEU B C   
4652  O O   . LEU B 225 ? 0.2920 0.4700 0.6537 0.0963  -0.0581 0.0841  225 LEU B O   
4653  C CB  . LEU B 225 ? 0.2918 0.4508 0.6364 0.0674  -0.0343 0.0551  225 LEU B CB  
4654  C CG  . LEU B 225 ? 0.2909 0.4411 0.6304 0.0597  -0.0174 0.0453  225 LEU B CG  
4655  C CD1 . LEU B 225 ? 0.3285 0.4778 0.6531 0.0391  -0.0309 0.0368  225 LEU B CD1 
4656  C CD2 . LEU B 225 ? 0.2804 0.3924 0.5847 0.0661  0.0014  0.0351  225 LEU B CD2 
4657  N N   . VAL B 226 ? 0.3092 0.4179 0.6057 0.0923  -0.0374 0.0627  226 VAL B N   
4658  C CA  . VAL B 226 ? 0.3299 0.4273 0.6054 0.0951  -0.0509 0.0682  226 VAL B CA  
4659  C C   . VAL B 226 ? 0.3151 0.3966 0.5542 0.0771  -0.0615 0.0557  226 VAL B C   
4660  O O   . VAL B 226 ? 0.3483 0.4123 0.5705 0.0680  -0.0512 0.0427  226 VAL B O   
4661  C CB  . VAL B 226 ? 0.3613 0.4251 0.6225 0.1106  -0.0341 0.0712  226 VAL B CB  
4662  C CG1 . VAL B 226 ? 0.4097 0.4551 0.6423 0.1104  -0.0448 0.0752  226 VAL B CG1 
4663  C CG2 . VAL B 226 ? 0.3934 0.4722 0.6889 0.1318  -0.0252 0.0867  226 VAL B CG2 
4664  N N   . TYR B 227 ? 0.3043 0.3921 0.5303 0.0730  -0.0813 0.0602  227 TYR B N   
4665  C CA  . TYR B 227 ? 0.3039 0.3772 0.4956 0.0578  -0.0901 0.0493  227 TYR B CA  
4666  C C   . TYR B 227 ? 0.3194 0.3674 0.4769 0.0614  -0.0919 0.0518  227 TYR B C   
4667  O O   . TYR B 227 ? 0.3681 0.4163 0.5284 0.0742  -0.0946 0.0648  227 TYR B O   
4668  C CB  . TYR B 227 ? 0.3342 0.4330 0.5328 0.0457  -0.1115 0.0487  227 TYR B CB  
4669  C CG  . TYR B 227 ? 0.3542 0.4726 0.5816 0.0365  -0.1080 0.0435  227 TYR B CG  
4670  C CD1 . TYR B 227 ? 0.3974 0.5008 0.6091 0.0237  -0.1008 0.0302  227 TYR B CD1 
4671  C CD2 . TYR B 227 ? 0.4028 0.5548 0.6743 0.0419  -0.1097 0.0538  227 TYR B CD2 
4672  C CE1 . TYR B 227 ? 0.4529 0.5709 0.6889 0.0158  -0.0953 0.0270  227 TYR B CE1 
4673  C CE2 . TYR B 227 ? 0.4524 0.6219 0.7511 0.0331  -0.1040 0.0505  227 TYR B CE2 
4674  C CZ  . TYR B 227 ? 0.5126 0.6632 0.7919 0.0198  -0.0966 0.0370  227 TYR B CZ  
4675  O OH  . TYR B 227 ? 0.6130 0.7786 0.9181 0.0111  -0.0894 0.0351  227 TYR B OH  
4676  N N   . THR B 228 ? 0.3216 0.3488 0.4486 0.0510  -0.0889 0.0411  228 THR B N   
4677  C CA  . THR B 228 ? 0.3440 0.3496 0.4386 0.0522  -0.0898 0.0437  228 THR B CA  
4678  C C   . THR B 228 ? 0.3498 0.3487 0.4173 0.0394  -0.0952 0.0335  228 THR B C   
4679  O O   . THR B 228 ? 0.3594 0.3609 0.4309 0.0303  -0.0915 0.0232  228 THR B O   
4680  C CB  . THR B 228 ? 0.3948 0.3740 0.4826 0.0569  -0.0709 0.0432  228 THR B CB  
4681  O OG1 . THR B 228 ? 0.3986 0.3597 0.4611 0.0593  -0.0710 0.0498  228 THR B OG1 
4682  C CG2 . THR B 228 ? 0.3573 0.3273 0.4395 0.0464  -0.0598 0.0293  228 THR B CG2 
4683  N N   . PRO B 229 ? 0.3460 0.3350 0.3843 0.0400  -0.1026 0.0374  229 PRO B N   
4684  C CA  . PRO B 229 ? 0.3722 0.3525 0.3825 0.0303  -0.1061 0.0282  229 PRO B CA  
4685  C C   . PRO B 229 ? 0.3578 0.3233 0.3600 0.0250  -0.0900 0.0197  229 PRO B C   
4686  O O   . PRO B 229 ? 0.3362 0.2918 0.3409 0.0282  -0.0775 0.0221  229 PRO B O   
4687  C CB  . PRO B 229 ? 0.3618 0.3318 0.3411 0.0359  -0.1132 0.0366  229 PRO B CB  
4688  C CG  . PRO B 229 ? 0.3289 0.3122 0.3243 0.0462  -0.1220 0.0498  229 PRO B CG  
4689  C CD  . PRO B 229 ? 0.3125 0.2987 0.3411 0.0511  -0.1087 0.0515  229 PRO B CD  
4690  N N   . LEU B 230 ? 0.3874 0.3518 0.3806 0.0165  -0.0910 0.0100  230 LEU B N   
4691  C CA  . LEU B 230 ? 0.3578 0.3128 0.3443 0.0126  -0.0776 0.0035  230 LEU B CA  
4692  C C   . LEU B 230 ? 0.3975 0.3380 0.3514 0.0125  -0.0759 0.0028  230 LEU B C   
4693  O O   . LEU B 230 ? 0.4376 0.3737 0.3728 0.0104  -0.0856 0.0001  230 LEU B O   
4694  C CB  . LEU B 230 ? 0.3350 0.2976 0.3358 0.0058  -0.0765 -0.0048 230 LEU B CB  
4695  C CG  . LEU B 230 ? 0.3212 0.2778 0.3169 0.0027  -0.0643 -0.0104 230 LEU B CG  
4696  C CD1 . LEU B 230 ? 0.2802 0.2378 0.2861 0.0053  -0.0537 -0.0087 230 LEU B CD1 
4697  C CD2 . LEU B 230 ? 0.3239 0.2874 0.3333 -0.0033 -0.0656 -0.0160 230 LEU B CD2 
4698  N N   . THR B 231 ? 0.4137 0.3466 0.3604 0.0144  -0.0634 0.0054  231 THR B N   
4699  C CA  . THR B 231 ? 0.4189 0.3400 0.3378 0.0160  -0.0576 0.0061  231 THR B CA  
4700  C C   . THR B 231 ? 0.3965 0.3197 0.3210 0.0136  -0.0457 0.0024  231 THR B C   
4701  O O   . THR B 231 ? 0.3771 0.3095 0.3231 0.0108  -0.0412 0.0014  231 THR B O   
4702  C CB  . THR B 231 ? 0.4626 0.3760 0.3680 0.0218  -0.0526 0.0169  231 THR B CB  
4703  O OG1 . THR B 231 ? 0.4324 0.3498 0.3599 0.0212  -0.0462 0.0215  231 THR B OG1 
4704  C CG2 . THR B 231 ? 0.4608 0.3700 0.3498 0.0265  -0.0650 0.0221  231 THR B CG2 
4705  N N   . ILE B 232 ? 0.4110 0.3251 0.3140 0.0155  -0.0405 0.0007  232 ILE B N   
4706  C CA  . ILE B 232 ? 0.3885 0.3058 0.2957 0.0154  -0.0299 -0.0013 232 ILE B CA  
4707  C C   . ILE B 232 ? 0.3775 0.2915 0.2705 0.0214  -0.0179 0.0060  232 ILE B C   
4708  O O   . ILE B 232 ? 0.4122 0.3122 0.2787 0.0263  -0.0167 0.0079  232 ILE B O   
4709  C CB  . ILE B 232 ? 0.3834 0.2914 0.2808 0.0137  -0.0320 -0.0096 232 ILE B CB  
4710  C CG1 . ILE B 232 ? 0.3565 0.2699 0.2699 0.0069  -0.0443 -0.0152 232 ILE B CG1 
4711  C CG2 . ILE B 232 ? 0.3538 0.2661 0.2580 0.0157  -0.0207 -0.0094 232 ILE B CG2 
4712  C CD1 . ILE B 232 ? 0.3244 0.2544 0.2677 0.0045  -0.0420 -0.0146 232 ILE B CD1 
4713  N N   . SER B 233 ? 0.3677 0.2960 0.2780 0.0207  -0.0091 0.0106  233 SER B N   
4714  C CA  . SER B 233 ? 0.4047 0.3364 0.3090 0.0262  0.0037  0.0195  233 SER B CA  
4715  C C   . SER B 233 ? 0.4332 0.3584 0.3221 0.0341  0.0130  0.0189  233 SER B C   
4716  O O   . SER B 233 ? 0.4487 0.3672 0.3347 0.0336  0.0097  0.0112  233 SER B O   
4717  C CB  . SER B 233 ? 0.4129 0.3661 0.3444 0.0207  0.0079  0.0248  233 SER B CB  
4718  O OG  . SER B 233 ? 0.4008 0.3668 0.3450 0.0197  0.0084  0.0214  233 SER B OG  
4719  N N   . LYS B 234 ? 0.4354 0.3625 0.3165 0.0420  0.0265  0.0281  234 LYS B N   
4720  C CA  . LYS B 234 ? 0.4509 0.3700 0.3170 0.0527  0.0389  0.0293  234 LYS B CA  
4721  C C   . LYS B 234 ? 0.4352 0.3715 0.3236 0.0527  0.0405  0.0297  234 LYS B C   
4722  O O   . LYS B 234 ? 0.4711 0.3979 0.3489 0.0616  0.0492  0.0296  234 LYS B O   
4723  C CB  . LYS B 234 ? 0.5071 0.4315 0.3679 0.0625  0.0556  0.0420  234 LYS B CB  
4724  C CG  . LYS B 234 ? 0.6158 0.5214 0.4489 0.0653  0.0574  0.0439  234 LYS B CG  
4725  C CD  . LYS B 234 ? 0.7396 0.6549 0.5733 0.0746  0.0766  0.0588  234 LYS B CD  
4726  C CE  . LYS B 234 ? 0.8588 0.7583 0.6671 0.0765  0.0788  0.0635  234 LYS B CE  
4727  N NZ  . LYS B 234 ? 0.9130 0.8307 0.7362 0.0809  0.0966  0.0809  234 LYS B NZ  
4728  N N   . GLN B 235 ? 0.4185 0.3777 0.3352 0.0433  0.0328  0.0303  235 GLN B N   
4729  C CA  . GLN B 235 ? 0.4262 0.4033 0.3611 0.0435  0.0332  0.0315  235 GLN B CA  
4730  C C   . GLN B 235 ? 0.4008 0.3695 0.3365 0.0375  0.0231  0.0208  235 GLN B C   
4731  O O   . GLN B 235 ? 0.3991 0.3802 0.3465 0.0378  0.0232  0.0217  235 GLN B O   
4732  C CB  . GLN B 235 ? 0.5071 0.5160 0.4702 0.0364  0.0313  0.0385  235 GLN B CB  
4733  C CG  . GLN B 235 ? 0.5938 0.6204 0.5654 0.0425  0.0432  0.0522  235 GLN B CG  
4734  C CD  . GLN B 235 ? 0.7268 0.7581 0.6946 0.0580  0.0559  0.0602  235 GLN B CD  
4735  O OE1 . GLN B 235 ? 0.7533 0.7893 0.7248 0.0613  0.0541  0.0589  235 GLN B OE1 
4736  N NE2 . GLN B 235 ? 0.7945 0.8225 0.7535 0.0692  0.0708  0.0696  235 GLN B NE2 
4737  N N   . GLY B 236 ? 0.4074 0.3564 0.3308 0.0328  0.0151  0.0122  236 GLY B N   
4738  C CA  . GLY B 236 ? 0.4369 0.3792 0.3638 0.0269  0.0068  0.0034  236 GLY B CA  
4739  C C   . GLY B 236 ? 0.4138 0.3702 0.3613 0.0181  -0.0019 0.0004  236 GLY B C   
4740  O O   . GLY B 236 ? 0.3898 0.3467 0.3452 0.0144  -0.0056 -0.0047 236 GLY B O   
4741  N N   . GLU B 237 ? 0.3838 0.3489 0.3390 0.0148  -0.0035 0.0038  237 GLU B N   
4742  C CA  . GLU B 237 ? 0.3104 0.2834 0.2818 0.0073  -0.0095 0.0006  237 GLU B CA  
4743  C C   . GLU B 237 ? 0.3212 0.2823 0.2911 0.0054  -0.0170 -0.0033 237 GLU B C   
4744  O O   . GLU B 237 ? 0.3404 0.2904 0.2966 0.0084  -0.0190 -0.0013 237 GLU B O   
4745  C CB  . GLU B 237 ? 0.2965 0.2816 0.2777 0.0030  -0.0070 0.0059  237 GLU B CB  
4746  C CG  . GLU B 237 ? 0.3134 0.3182 0.3017 0.0041  -0.0015 0.0119  237 GLU B CG  
4747  C CD  . GLU B 237 ? 0.3668 0.3827 0.3636 0.0004  0.0025  0.0201  237 GLU B CD  
4748  O OE1 . GLU B 237 ? 0.4002 0.4078 0.3877 0.0055  0.0082  0.0262  237 GLU B OE1 
4749  O OE2 . GLU B 237 ? 0.3537 0.3862 0.3655 -0.0084 0.0000  0.0204  237 GLU B OE2 
4750  N N   . TYR B 238 ? 0.3416 0.3058 0.3249 0.0014  -0.0207 -0.0078 238 TYR B N   
4751  C CA  . TYR B 238 ? 0.2964 0.2541 0.2843 0.0013  -0.0273 -0.0095 238 TYR B CA  
4752  C C   . TYR B 238 ? 0.2995 0.2530 0.2910 0.0007  -0.0271 -0.0057 238 TYR B C   
4753  O O   . TYR B 238 ? 0.3151 0.2711 0.3144 -0.0036 -0.0231 -0.0069 238 TYR B O   
4754  C CB  . TYR B 238 ? 0.2836 0.2462 0.2854 -0.0003 -0.0282 -0.0150 238 TYR B CB  
4755  C CG  . TYR B 238 ? 0.2670 0.2307 0.2661 -0.0004 -0.0274 -0.0175 238 TYR B CG  
4756  C CD1 . TYR B 238 ? 0.2979 0.2553 0.2922 -0.0008 -0.0332 -0.0186 238 TYR B CD1 
4757  C CD2 . TYR B 238 ? 0.2710 0.2408 0.2716 -0.0007 -0.0211 -0.0186 238 TYR B CD2 
4758  C CE1 . TYR B 238 ? 0.3166 0.2701 0.3081 -0.0027 -0.0313 -0.0214 238 TYR B CE1 
4759  C CE2 . TYR B 238 ? 0.2851 0.2523 0.2828 -0.0001 -0.0184 -0.0193 238 TYR B CE2 
4760  C CZ  . TYR B 238 ? 0.2932 0.2505 0.2870 -0.0017 -0.0228 -0.0211 238 TYR B CZ  
4761  O OH  . TYR B 238 ? 0.3133 0.2629 0.3035 -0.0028 -0.0192 -0.0223 238 TYR B OH  
4762  N N   . PHE B 239 ? 0.3063 0.2518 0.2904 0.0044  -0.0315 -0.0009 239 PHE B N   
4763  C CA  . PHE B 239 ? 0.3330 0.2709 0.3190 0.0054  -0.0302 0.0050  239 PHE B CA  
4764  C C   . PHE B 239 ? 0.3475 0.2816 0.3380 0.0108  -0.0374 0.0077  239 PHE B C   
4765  O O   . PHE B 239 ? 0.3577 0.2951 0.3428 0.0133  -0.0459 0.0075  239 PHE B O   
4766  C CB  . PHE B 239 ? 0.3712 0.3036 0.3414 0.0071  -0.0262 0.0131  239 PHE B CB  
4767  C CG  . PHE B 239 ? 0.3774 0.3168 0.3515 0.0018  -0.0174 0.0145  239 PHE B CG  
4768  C CD1 . PHE B 239 ? 0.3856 0.3347 0.3557 0.0023  -0.0144 0.0128  239 PHE B CD1 
4769  C CD2 . PHE B 239 ? 0.3930 0.3294 0.3759 -0.0040 -0.0121 0.0184  239 PHE B CD2 
4770  C CE1 . PHE B 239 ? 0.3764 0.3380 0.3543 -0.0018 -0.0075 0.0161  239 PHE B CE1 
4771  C CE2 . PHE B 239 ? 0.4053 0.3532 0.3959 -0.0110 -0.0060 0.0202  239 PHE B CE2 
4772  C CZ  . PHE B 239 ? 0.3961 0.3593 0.3853 -0.0093 -0.0043 0.0198  239 PHE B CZ  
4773  N N   . ILE B 240 ? 0.3617 0.2886 0.3621 0.0125  -0.0343 0.0109  240 ILE B N   
4774  C CA  . ILE B 240 ? 0.3919 0.3153 0.3963 0.0208  -0.0399 0.0182  240 ILE B CA  
4775  C C   . ILE B 240 ? 0.3970 0.3045 0.3947 0.0236  -0.0341 0.0278  240 ILE B C   
4776  O O   . ILE B 240 ? 0.4357 0.3358 0.4305 0.0170  -0.0255 0.0272  240 ILE B O   
4777  C CB  . ILE B 240 ? 0.3315 0.2590 0.3573 0.0244  -0.0393 0.0152  240 ILE B CB  
4778  C CG1 . ILE B 240 ? 0.3362 0.2522 0.3676 0.0203  -0.0277 0.0093  240 ILE B CG1 
4779  C CG2 . ILE B 240 ? 0.3387 0.2827 0.3732 0.0219  -0.0447 0.0084  240 ILE B CG2 
4780  C CD1 . ILE B 240 ? 0.3582 0.2724 0.4064 0.0265  -0.0232 0.0072  240 ILE B CD1 
4781  N N   . GLN B 241 ? 0.4038 0.3074 0.4004 0.0331  -0.0389 0.0379  241 GLN B N   
4782  C CA  . GLN B 241 ? 0.4121 0.2980 0.4007 0.0371  -0.0323 0.0494  241 GLN B CA  
4783  C C   . GLN B 241 ? 0.4079 0.2796 0.4126 0.0421  -0.0249 0.0521  241 GLN B C   
4784  O O   . GLN B 241 ? 0.4143 0.2919 0.4318 0.0517  -0.0294 0.0551  241 GLN B O   
4785  C CB  . GLN B 241 ? 0.4670 0.3544 0.4367 0.0459  -0.0413 0.0613  241 GLN B CB  
4786  C CG  . GLN B 241 ? 0.5778 0.4464 0.5379 0.0530  -0.0343 0.0768  241 GLN B CG  
4787  C CD  . GLN B 241 ? 0.6461 0.4998 0.6009 0.0440  -0.0193 0.0782  241 GLN B CD  
4788  O OE1 . GLN B 241 ? 0.6339 0.4954 0.5860 0.0344  -0.0163 0.0701  241 GLN B OE1 
4789  N NE2 . GLN B 241 ? 0.6783 0.5112 0.6335 0.0473  -0.0094 0.0898  241 GLN B NE2 
4790  N N   . VAL B 242 ? 0.3993 0.2519 0.4042 0.0348  -0.0127 0.0505  242 VAL B N   
4791  C CA  . VAL B 242 ? 0.3957 0.2254 0.4099 0.0387  -0.0028 0.0525  242 VAL B CA  
4792  C C   . VAL B 242 ? 0.4697 0.2779 0.4737 0.0425  0.0040  0.0679  242 VAL B C   
4793  O O   . VAL B 242 ? 0.5064 0.3071 0.5028 0.0315  0.0102  0.0689  242 VAL B O   
4794  C CB  . VAL B 242 ? 0.3739 0.1933 0.3931 0.0253  0.0057  0.0377  242 VAL B CB  
4795  C CG1 . VAL B 242 ? 0.3816 0.1698 0.4051 0.0286  0.0175  0.0378  242 VAL B CG1 
4796  C CG2 . VAL B 242 ? 0.3926 0.2330 0.4190 0.0232  0.0000  0.0248  242 VAL B CG2 
4797  N N   . ASN B 243 ? 0.4522 0.2528 0.4572 0.0586  0.0031  0.0817  243 ASN B N   
4798  C CA  . ASN B 243 ? 0.4921 0.2708 0.4860 0.0647  0.0104  0.0990  243 ASN B CA  
4799  C C   . ASN B 243 ? 0.5241 0.2667 0.5229 0.0587  0.0276  0.0980  243 ASN B C   
4800  O O   . ASN B 243 ? 0.5619 0.2839 0.5519 0.0545  0.0372  0.1081  243 ASN B O   
4801  C CB  . ASN B 243 ? 0.5328 0.3170 0.5263 0.0855  0.0028  0.1157  243 ASN B CB  
4802  C CG  . ASN B 243 ? 0.5487 0.3590 0.5268 0.0893  -0.0135 0.1212  243 ASN B CG  
4803  O OD1 . ASN B 243 ? 0.5634 0.3848 0.5303 0.0779  -0.0171 0.1124  243 ASN B OD1 
4804  N ND2 . ASN B 243 ? 0.5749 0.3949 0.5512 0.1059  -0.0238 0.1359  243 ASN B ND2 
4805  N N   . ALA B 244 ? 0.4936 0.2263 0.5050 0.0580  0.0327  0.0858  244 ALA B N   
4806  C CA  . ALA B 244 ? 0.5075 0.2001 0.5200 0.0519  0.0491  0.0819  244 ALA B CA  
4807  C C   . ALA B 244 ? 0.5009 0.1891 0.5211 0.0473  0.0523  0.0625  244 ALA B C   
4808  O O   . ALA B 244 ? 0.4980 0.2121 0.5265 0.0551  0.0441  0.0575  244 ALA B O   
4809  C CB  . ALA B 244 ? 0.5338 0.1984 0.5458 0.0706  0.0586  0.1006  244 ALA B CB  
4810  N N   . ILE B 245 ? 0.5757 0.2307 0.5918 0.0334  0.0642  0.0513  245 ILE B N   
4811  C CA  . ILE B 245 ? 0.5803 0.2175 0.5970 0.0323  0.0716  0.0342  245 ILE B CA  
4812  C C   . ILE B 245 ? 0.5927 0.1968 0.6066 0.0437  0.0842  0.0391  245 ILE B C   
4813  O O   . ILE B 245 ? 0.6086 0.1892 0.6157 0.0357  0.0905  0.0435  245 ILE B O   
4814  C CB  . ILE B 245 ? 0.5653 0.1960 0.5742 0.0062  0.0717  0.0136  245 ILE B CB  
4815  C CG1 . ILE B 245 ? 0.5486 0.2240 0.5603 -0.0048 0.0566  0.0108  245 ILE B CG1 
4816  C CG2 . ILE B 245 ? 0.5528 0.1685 0.5562 0.0068  0.0777  -0.0048 245 ILE B CG2 
4817  C CD1 . ILE B 245 ? 0.5946 0.2691 0.6017 -0.0303 0.0550  -0.0036 245 ILE B CD1 
4818  N N   . ARG B 246 ? 0.5732 0.1818 0.5943 0.0627  0.0871  0.0394  246 ARG B N   
4819  C CA  . ARG B 246 ? 0.6151 0.1995 0.6349 0.0761  0.0987  0.0446  246 ARG B CA  
4820  C C   . ARG B 246 ? 0.6418 0.2015 0.6514 0.0688  0.1091  0.0242  246 ARG B C   
4821  O O   . ARG B 246 ? 0.6247 0.1975 0.6359 0.0702  0.1083  0.0121  246 ARG B O   
4822  C CB  . ARG B 246 ? 0.6076 0.2153 0.6437 0.1030  0.0965  0.0602  246 ARG B CB  
4823  C CG  . ARG B 246 ? 0.7895 0.3738 0.8259 0.1185  0.1100  0.0666  246 ARG B CG  
4824  C CD  . ARG B 246 ? 0.7914 0.4034 0.8471 0.1409  0.1093  0.0737  246 ARG B CD  
4825  N NE  . ARG B 246 ? 0.7534 0.4004 0.8249 0.1567  0.0962  0.0953  246 ARG B NE  
4826  C CZ  . ARG B 246 ? 0.6971 0.3847 0.7893 0.1682  0.0865  0.1003  246 ARG B CZ  
4827  N NH1 . ARG B 246 ? 0.6587 0.3561 0.7584 0.1659  0.0902  0.0859  246 ARG B NH1 
4828  N NH2 . ARG B 246 ? 0.6879 0.4079 0.7923 0.1803  0.0719  0.1195  246 ARG B NH2 
4829  N N   . VAL B 247 ? 0.6879 0.2109 0.6858 0.0618  0.1194  0.0210  247 VAL B N   
4830  C CA  . VAL B 247 ? 0.7472 0.2420 0.7320 0.0577  0.1302  0.0031  247 VAL B CA  
4831  C C   . VAL B 247 ? 0.7932 0.2597 0.7773 0.0756  0.1451  0.0133  247 VAL B C   
4832  O O   . VAL B 247 ? 0.8081 0.2472 0.7863 0.0702  0.1508  0.0194  247 VAL B O   
4833  C CB  . VAL B 247 ? 0.7780 0.2514 0.7464 0.0280  0.1283  -0.0151 247 VAL B CB  
4834  C CG1 . VAL B 247 ? 0.8510 0.2952 0.8019 0.0243  0.1380  -0.0344 247 VAL B CG1 
4835  C CG2 . VAL B 247 ? 0.6974 0.2011 0.6679 0.0105  0.1138  -0.0230 247 VAL B CG2 
4836  N N   . ASN B 248 ? 0.4816 0.3019 0.7701 0.1287  0.1354  0.0369  248 ASN B N   
4837  C CA  . ASN B 248 ? 0.5253 0.3307 0.8347 0.1487  0.1306  0.0469  248 ASN B CA  
4838  C C   . ASN B 248 ? 0.4927 0.2987 0.8096 0.1507  0.1024  0.0732  248 ASN B C   
4839  O O   . ASN B 248 ? 0.5171 0.3654 0.8563 0.1513  0.0860  0.0855  248 ASN B O   
4840  C CB  . ASN B 248 ? 0.6644 0.4108 0.9447 0.1512  0.1447  0.0323  248 ASN B CB  
4841  C CG  . ASN B 248 ? 0.7215 0.4638 0.9892 0.1542  0.1708  0.0071  248 ASN B CG  
4842  O OD1 . ASN B 248 ? 0.6846 0.4693 0.9745 0.1597  0.1808  0.0043  248 ASN B OD1 
4843  N ND2 . ASN B 248 ? 0.8010 0.4883 1.0289 0.1489  0.1807  -0.0105 248 ASN B ND2 
4844  N N   . LYS B 249 ? 0.5383 0.2952 0.8314 0.1502  0.0946  0.0828  249 LYS B N   
4845  C CA  . LYS B 249 ? 0.6322 0.3871 0.9198 0.1502  0.0674  0.1095  249 LYS B CA  
4846  C C   . LYS B 249 ? 0.5950 0.3229 0.8391 0.1264  0.0643  0.1184  249 LYS B C   
4847  O O   . LYS B 249 ? 0.5751 0.2832 0.7966 0.1238  0.0463  0.1409  249 LYS B O   
4848  C CB  . LYS B 249 ? 0.7521 0.4748 1.0458 0.1699  0.0550  0.1226  249 LYS B CB  
4849  C CG  . LYS B 249 ? 0.8351 0.5597 1.1612 0.1916  0.0705  0.1078  249 LYS B CG  
4850  C CD  . LYS B 249 ? 0.9316 0.6500 1.2818 0.2159  0.0503  0.1255  249 LYS B CD  
4851  C CE  . LYS B 249 ? 0.9363 0.7080 1.3134 0.2176  0.0242  0.1427  249 LYS B CE  
4852  N NZ  . LYS B 249 ? 1.0038 0.7754 1.4064 0.2407  -0.0008 0.1611  249 LYS B NZ  
4853  N N   . HIS B 250 ? 0.5673 0.2974 0.7983 0.1081  0.0820  0.1011  250 HIS B N   
4854  C CA  . HIS B 250 ? 0.5885 0.3047 0.7869 0.0826  0.0836  0.1073  250 HIS B CA  
4855  C C   . HIS B 250 ? 0.5332 0.3055 0.7305 0.0747  0.0753  0.1063  250 HIS B C   
4856  O O   . HIS B 250 ? 0.4174 0.2276 0.6394 0.0824  0.0777  0.0934  250 HIS B O   
4857  C CB  . HIS B 250 ? 0.5255 0.2137 0.7062 0.0623  0.1023  0.0856  250 HIS B CB  
4858  C CG  . HIS B 250 ? 0.6314 0.2648 0.7957 0.0609  0.1046  0.0838  250 HIS B CG  
4859  N ND1 . HIS B 250 ? 0.6952 0.2930 0.8334 0.0432  0.0999  0.1001  250 HIS B ND1 
4860  C CD2 . HIS B 250 ? 0.6388 0.2443 0.8054 0.0736  0.1120  0.0670  250 HIS B CD2 
4861  C CE1 . HIS B 250 ? 0.7391 0.2878 0.8672 0.0451  0.1012  0.0941  250 HIS B CE1 
4862  N NE2 . HIS B 250 ? 0.7214 0.2722 0.8651 0.0645  0.1084  0.0734  250 HIS B NE2 
4863  N N   . LEU B 251 ? 0.5196 0.2942 0.6855 0.0606  0.0657  0.1214  251 LEU B N   
4864  C CA  . LEU B 251 ? 0.4568 0.2750 0.6095 0.0516  0.0581  0.1193  251 LEU B CA  
4865  C C   . LEU B 251 ? 0.4551 0.2786 0.5819 0.0263  0.0717  0.1105  251 LEU B C   
4866  O O   . LEU B 251 ? 0.4883 0.2824 0.5926 0.0134  0.0785  0.1221  251 LEU B O   
4867  C CB  . LEU B 251 ? 0.4828 0.2987 0.6147 0.0588  0.0358  0.1433  251 LEU B CB  
4868  C CG  . LEU B 251 ? 0.4645 0.2909 0.6296 0.0824  0.0132  0.1543  251 LEU B CG  
4869  C CD1 . LEU B 251 ? 0.4826 0.3003 0.6129 0.0844  -0.0137 0.1769  251 LEU B CD1 
4870  C CD2 . LEU B 251 ? 0.4030 0.2782 0.6049 0.0861  0.0137  0.1367  251 LEU B CD2 
4871  N N   . VAL B 252 ? 0.4107 0.2713 0.5449 0.0192  0.0762  0.0913  252 VAL B N   
4872  C CA  . VAL B 252 ? 0.4028 0.2794 0.5219 -0.0011 0.0852  0.0847  252 VAL B CA  
4873  C C   . VAL B 252 ? 0.3996 0.3028 0.4997 0.0029  0.0758  0.0915  252 VAL B C   
4874  O O   . VAL B 252 ? 0.3915 0.3216 0.5014 0.0115  0.0660  0.0829  252 VAL B O   
4875  C CB  . VAL B 252 ? 0.3743 0.2705 0.5094 -0.0097 0.0916  0.0603  252 VAL B CB  
4876  C CG1 . VAL B 252 ? 0.3580 0.2747 0.4892 -0.0298 0.0984  0.0552  252 VAL B CG1 
4877  C CG2 . VAL B 252 ? 0.3802 0.2415 0.5243 -0.0104 0.0983  0.0506  252 VAL B CG2 
4878  N N   . ILE B 253 ? 0.4218 0.3122 0.4906 -0.0036 0.0794  0.1072  253 ILE B N   
4879  C CA  . ILE B 253 ? 0.4003 0.3022 0.4377 0.0022  0.0699  0.1136  253 ILE B CA  
4880  C C   . ILE B 253 ? 0.3889 0.3118 0.4082 -0.0088 0.0861  0.1072  253 ILE B C   
4881  O O   . ILE B 253 ? 0.4546 0.3648 0.4539 -0.0198 0.1038  0.1180  253 ILE B O   
4882  C CB  . ILE B 253 ? 0.4523 0.3166 0.4534 0.0088  0.0587  0.1385  253 ILE B CB  
4883  C CG1 . ILE B 253 ? 0.4376 0.2848 0.4669 0.0236  0.0417  0.1459  253 ILE B CG1 
4884  C CG2 . ILE B 253 ? 0.4465 0.3142 0.4057 0.0151  0.0438  0.1430  253 ILE B CG2 
4885  C CD1 . ILE B 253 ? 0.5037 0.3037 0.5039 0.0284  0.0331  0.1727  253 ILE B CD1 
4886  N N   . PRO B 254 ? 0.4101 0.3650 0.4383 -0.0049 0.0816  0.0907  254 PRO B N   
4887  C CA  . PRO B 254 ? 0.4403 0.4185 0.4600 -0.0101 0.0966  0.0825  254 PRO B CA  
4888  C C   . PRO B 254 ? 0.5163 0.4783 0.4817 -0.0060 0.1023  0.0934  254 PRO B C   
4889  O O   . PRO B 254 ? 0.5630 0.5019 0.4950 0.0034  0.0826  0.1019  254 PRO B O   
4890  C CB  . PRO B 254 ? 0.4027 0.4082 0.4422 -0.0030 0.0840  0.0640  254 PRO B CB  
4891  C CG  . PRO B 254 ? 0.3818 0.3826 0.4472 0.0006  0.0707  0.0617  254 PRO B CG  
4892  C CD  . PRO B 254 ? 0.3871 0.3579 0.4384 0.0052  0.0639  0.0795  254 PRO B CD  
4893  N N   . THR B 255 ? 0.5303 0.5023 0.4869 -0.0133 0.1290  0.0942  255 THR B N   
4894  C CA  . THR B 255 ? 0.5895 0.5459 0.4876 -0.0072 0.1405  0.1001  255 THR B CA  
4895  C C   . THR B 255 ? 0.6089 0.5947 0.5112 0.0012  0.1495  0.0810  255 THR B C   
4896  O O   . THR B 255 ? 0.6565 0.6293 0.5093 0.0088  0.1631  0.0808  255 THR B O   
4897  C CB  . THR B 255 ? 0.6071 0.5474 0.4820 -0.0192 0.1720  0.1182  255 THR B CB  
4898  O OG1 . THR B 255 ? 0.6017 0.5813 0.5303 -0.0313 0.1985  0.1116  255 THR B OG1 
4899  C CG2 . THR B 255 ? 0.6066 0.5090 0.4710 -0.0267 0.1635  0.1392  255 THR B CG2 
4900  N N   . GLY B 271 ? 1.2796 0.9311 0.6476 0.0580  -0.1024 -0.0010 271 GLY B N   
4901  C CA  . GLY B 271 ? 1.2583 0.9088 0.6420 0.0616  -0.1055 -0.0226 271 GLY B CA  
4902  C C   . GLY B 271 ? 1.2010 0.8822 0.6143 0.0744  -0.0640 -0.0323 271 GLY B C   
4903  O O   . GLY B 271 ? 1.2084 0.8777 0.5981 0.0873  -0.0338 -0.0481 271 GLY B O   
4904  N N   . GLU B 272 ? 1.1259 0.8641 0.6301 0.0680  -0.0594 -0.0211 272 GLU B N   
4905  C CA  . GLU B 272 ? 1.0751 0.8590 0.6406 0.0753  -0.0218 -0.0267 272 GLU B CA  
4906  C C   . GLU B 272 ? 0.9029 0.7279 0.5541 0.0672  -0.0376 -0.0259 272 GLU B C   
4907  O O   . GLU B 272 ? 0.8479 0.6762 0.5233 0.0551  -0.0700 -0.0170 272 GLU B O   
4908  C CB  . GLU B 272 ? 1.1486 0.9584 0.7286 0.0750  0.0138  -0.0118 272 GLU B CB  
4909  C CG  . GLU B 272 ? 1.1700 1.0251 0.8063 0.0817  0.0538  -0.0170 272 GLU B CG  
4910  C CD  . GLU B 272 ? 1.2607 1.1095 0.8579 0.0899  0.0978  -0.0152 272 GLU B CD  
4911  O OE1 . GLU B 272 ? 1.3354 1.1444 0.8606 0.0880  0.0991  -0.0060 272 GLU B OE1 
4912  O OE2 . GLU B 272 ? 1.2539 1.1373 0.8925 0.0981  0.1311  -0.0219 272 GLU B OE2 
4913  N N   . ILE B 273 ? 0.8350 0.6903 0.5306 0.0744  -0.0146 -0.0345 273 ILE B N   
4914  C CA  . ILE B 273 ? 0.7828 0.6710 0.5473 0.0673  -0.0258 -0.0335 273 ILE B CA  
4915  C C   . ILE B 273 ? 0.7294 0.6537 0.5436 0.0568  -0.0211 -0.0168 273 ILE B C   
4916  O O   . ILE B 273 ? 0.7743 0.7079 0.5847 0.0578  0.0010  -0.0092 273 ILE B O   
4917  C CB  . ILE B 273 ? 0.7032 0.6116 0.4979 0.0791  -0.0053 -0.0455 273 ILE B CB  
4918  C CG1 . ILE B 273 ? 0.7935 0.6646 0.5365 0.0962  0.0012  -0.0629 273 ILE B CG1 
4919  C CG2 . ILE B 273 ? 0.5994 0.5268 0.4453 0.0714  -0.0217 -0.0444 273 ILE B CG2 
4920  C CD1 . ILE B 273 ? 0.7972 0.6879 0.5766 0.1101  0.0155  -0.0726 273 ILE B CD1 
4921  N N   . GLY B 274 ? 0.6459 0.5871 0.5051 0.0466  -0.0398 -0.0110 274 GLY B N   
4922  C CA  . GLY B 274 ? 0.5757 0.5463 0.4819 0.0394  -0.0339 0.0019  274 GLY B CA  
4923  C C   . GLY B 274 ? 0.5384 0.5371 0.4745 0.0415  -0.0050 -0.0001 274 GLY B C   
4924  O O   . GLY B 274 ? 0.5454 0.5503 0.4801 0.0487  0.0086  -0.0105 274 GLY B O   
4925  N N   . GLY B 275 ? 0.4719 0.4863 0.4368 0.0355  0.0029  0.0100  275 GLY B N   
4926  C CA  . GLY B 275 ? 0.4403 0.4770 0.4313 0.0339  0.0260  0.0082  275 GLY B CA  
4927  C C   . GLY B 275 ? 0.3870 0.4439 0.4192 0.0293  0.0242  0.0034  275 GLY B C   
4928  O O   . GLY B 275 ? 0.4030 0.4775 0.4567 0.0268  0.0373  -0.0004 275 GLY B O   
4929  N N   . ALA B 276 ? 0.3364 0.3903 0.3790 0.0268  0.0082  0.0043  276 ALA B N   
4930  C CA  . ALA B 276 ? 0.2870 0.3541 0.3582 0.0222  0.0099  0.0007  276 ALA B CA  
4931  C C   . ALA B 276 ? 0.2776 0.3415 0.3439 0.0238  -0.0003 -0.0064 276 ALA B C   
4932  O O   . ALA B 276 ? 0.2844 0.3363 0.3425 0.0227  -0.0145 -0.0044 276 ALA B O   
4933  C CB  . ALA B 276 ? 0.2724 0.3403 0.3650 0.0180  0.0076  0.0087  276 ALA B CB  
4934  N N   . LEU B 277 ? 0.2683 0.3409 0.3403 0.0255  0.0044  -0.0136 277 LEU B N   
4935  C CA  . LEU B 277 ? 0.2831 0.3480 0.3488 0.0278  -0.0060 -0.0183 277 LEU B CA  
4936  C C   . LEU B 277 ? 0.2882 0.3502 0.3622 0.0188  -0.0083 -0.0141 277 LEU B C   
4937  O O   . LEU B 277 ? 0.3005 0.3704 0.3866 0.0136  0.0016  -0.0128 277 LEU B O   
4938  C CB  . LEU B 277 ? 0.2882 0.3644 0.3600 0.0344  -0.0036 -0.0255 277 LEU B CB  
4939  C CG  . LEU B 277 ? 0.3000 0.3652 0.3645 0.0387  -0.0166 -0.0285 277 LEU B CG  
4940  C CD1 . LEU B 277 ? 0.2988 0.3419 0.3426 0.0490  -0.0254 -0.0320 277 LEU B CD1 
4941  C CD2 . LEU B 277 ? 0.3362 0.4198 0.4179 0.0436  -0.0173 -0.0330 277 LEU B CD2 
4942  N N   . ILE B 278 ? 0.2872 0.3344 0.3521 0.0167  -0.0192 -0.0123 278 ILE B N   
4943  C CA  . ILE B 278 ? 0.2859 0.3288 0.3543 0.0078  -0.0166 -0.0073 278 ILE B CA  
4944  C C   . ILE B 278 ? 0.3074 0.3362 0.3568 0.0105  -0.0243 -0.0102 278 ILE B C   
4945  O O   . ILE B 278 ? 0.3360 0.3502 0.3730 0.0170  -0.0365 -0.0127 278 ILE B O   
4946  C CB  . ILE B 278 ? 0.2562 0.2938 0.3354 -0.0010 -0.0217 0.0014  278 ILE B CB  
4947  C CG1 . ILE B 278 ? 0.2486 0.2995 0.3480 -0.0008 -0.0215 0.0055  278 ILE B CG1 
4948  C CG2 . ILE B 278 ? 0.2201 0.2569 0.3054 -0.0105 -0.0099 0.0080  278 ILE B CG2 
4949  C CD1 . ILE B 278 ? 0.2582 0.3082 0.3752 -0.0093 -0.0343 0.0140  278 ILE B CD1 
4950  N N   . THR B 279 ? 0.2892 0.3171 0.3314 0.0067  -0.0187 -0.0102 279 THR B N   
4951  C CA  . THR B 279 ? 0.3040 0.3166 0.3248 0.0103  -0.0305 -0.0113 279 THR B CA  
4952  C C   . THR B 279 ? 0.3485 0.3456 0.3466 0.0006  -0.0243 -0.0063 279 THR B C   
4953  O O   . THR B 279 ? 0.3381 0.3410 0.3398 -0.0061 -0.0074 -0.0063 279 THR B O   
4954  C CB  . THR B 279 ? 0.2717 0.3004 0.3011 0.0201  -0.0372 -0.0198 279 THR B CB  
4955  O OG1 . THR B 279 ? 0.3558 0.3702 0.3684 0.0254  -0.0538 -0.0190 279 THR B OG1 
4956  C CG2 . THR B 279 ? 0.2707 0.3140 0.3086 0.0133  -0.0275 -0.0238 279 THR B CG2 
4957  N N   . THR B 280 ? 0.3672 0.3402 0.3375 0.0013  -0.0369 -0.0021 280 THR B N   
4958  C CA  . THR B 280 ? 0.3768 0.3281 0.3119 -0.0076 -0.0307 0.0031  280 THR B CA  
4959  C C   . THR B 280 ? 0.3953 0.3382 0.3064 -0.0026 -0.0485 -0.0017 280 THR B C   
4960  O O   . THR B 280 ? 0.4372 0.3540 0.3053 -0.0092 -0.0481 0.0019  280 THR B O   
4961  C CB  . THR B 280 ? 0.4095 0.3306 0.3209 -0.0152 -0.0311 0.0165  280 THR B CB  
4962  O OG1 . THR B 280 ? 0.4085 0.3137 0.3147 -0.0056 -0.0549 0.0180  280 THR B OG1 
4963  C CG2 . THR B 280 ? 0.4042 0.3361 0.3443 -0.0248 -0.0146 0.0229  280 THR B CG2 
4964  N N   . THR B 281 ? 0.3725 0.3374 0.3103 0.0086  -0.0638 -0.0095 281 THR B N   
4965  C CA  . THR B 281 ? 0.4099 0.3702 0.3353 0.0147  -0.0887 -0.0116 281 THR B CA  
4966  C C   . THR B 281 ? 0.3722 0.3502 0.3062 0.0095  -0.0921 -0.0214 281 THR B C   
4967  O O   . THR B 281 ? 0.3830 0.3633 0.3158 0.0127  -0.1168 -0.0236 281 THR B O   
4968  C CB  . THR B 281 ? 0.4111 0.3827 0.3644 0.0327  -0.1072 -0.0120 281 THR B CB  
4969  O OG1 . THR B 281 ? 0.3638 0.3685 0.3607 0.0391  -0.0947 -0.0194 281 THR B OG1 
4970  C CG2 . THR B 281 ? 0.4525 0.3893 0.3818 0.0365  -0.1123 -0.0022 281 THR B CG2 
4971  N N   . HIS B 282 ? 0.3763 0.3625 0.3174 0.0004  -0.0696 -0.0266 282 HIS B N   
4972  C CA  . HIS B 282 ? 0.4283 0.4120 0.3585 -0.0090 -0.0710 -0.0358 282 HIS B CA  
4973  C C   . HIS B 282 ? 0.4335 0.3984 0.3399 -0.0174 -0.0424 -0.0373 282 HIS B C   
4974  O O   . HIS B 282 ? 0.4096 0.3835 0.3359 -0.0154 -0.0219 -0.0322 282 HIS B O   
4975  C CB  . HIS B 282 ? 0.4042 0.4251 0.3862 -0.0082 -0.0754 -0.0433 282 HIS B CB  
4976  C CG  . HIS B 282 ? 0.3260 0.3708 0.3463 -0.0040 -0.0538 -0.0418 282 HIS B CG  
4977  N ND1 . HIS B 282 ? 0.3420 0.3804 0.3601 -0.0092 -0.0303 -0.0419 282 HIS B ND1 
4978  C CD2 . HIS B 282 ? 0.2710 0.3434 0.3292 0.0058  -0.0531 -0.0403 282 HIS B CD2 
4979  C CE1 . HIS B 282 ? 0.3140 0.3735 0.3641 -0.0040 -0.0202 -0.0391 282 HIS B CE1 
4980  N NE2 . HIS B 282 ? 0.2775 0.3559 0.3479 0.0046  -0.0320 -0.0387 282 HIS B NE2 
4981  N N   . PRO B 283 ? 0.4446 0.3811 0.3072 -0.0260 -0.0418 -0.0446 283 PRO B N   
4982  C CA  . PRO B 283 ? 0.4491 0.3645 0.2870 -0.0301 -0.0097 -0.0466 283 PRO B CA  
4983  C C   . PRO B 283 ? 0.4466 0.3823 0.3273 -0.0290 0.0102  -0.0519 283 PRO B C   
4984  O O   . PRO B 283 ? 0.4620 0.4041 0.3599 -0.0255 0.0349  -0.0461 283 PRO B O   
4985  C CB  . PRO B 283 ? 0.5072 0.3803 0.2787 -0.0381 -0.0169 -0.0562 283 PRO B CB  
4986  C CG  . PRO B 283 ? 0.5191 0.4019 0.3003 -0.0408 -0.0556 -0.0619 283 PRO B CG  
4987  C CD  . PRO B 283 ? 0.4761 0.3938 0.3044 -0.0312 -0.0712 -0.0509 283 PRO B CD  
4988  N N   . TYR B 284 ? 0.4369 0.3828 0.3378 -0.0325 -0.0015 -0.0611 284 TYR B N   
4989  C CA  . TYR B 284 ? 0.4211 0.3748 0.3523 -0.0323 0.0174  -0.0652 284 TYR B CA  
4990  C C   . TYR B 284 ? 0.3909 0.3824 0.3773 -0.0269 0.0168  -0.0573 284 TYR B C   
4991  O O   . TYR B 284 ? 0.4109 0.4238 0.4145 -0.0239 0.0001  -0.0529 284 TYR B O   
4992  C CB  . TYR B 284 ? 0.4582 0.3910 0.3731 -0.0426 0.0085  -0.0795 284 TYR B CB  
4993  C CG  . TYR B 284 ? 0.4881 0.3749 0.3340 -0.0475 0.0078  -0.0888 284 TYR B CG  
4994  C CD1 . TYR B 284 ? 0.5393 0.4011 0.3536 -0.0417 0.0387  -0.0888 284 TYR B CD1 
4995  C CD2 . TYR B 284 ? 0.5280 0.3972 0.3400 -0.0572 -0.0235 -0.0964 284 TYR B CD2 
4996  C CE1 . TYR B 284 ? 0.6114 0.4270 0.3533 -0.0452 0.0437  -0.0967 284 TYR B CE1 
4997  C CE2 . TYR B 284 ? 0.6195 0.4387 0.3544 -0.0617 -0.0253 -0.1046 284 TYR B CE2 
4998  C CZ  . TYR B 284 ? 0.6734 0.4638 0.3691 -0.0554 0.0111  -0.1049 284 TYR B CZ  
4999  O OH  . TYR B 284 ? 0.7903 0.5260 0.3998 -0.0590 0.0161  -0.1129 284 TYR B OH  
5000  N N   . THR B 285 ? 0.3947 0.3903 0.4047 -0.0241 0.0354  -0.0554 285 THR B N   
5001  C CA  . THR B 285 ? 0.3300 0.3532 0.3806 -0.0196 0.0360  -0.0473 285 THR B CA  
5002  C C   . THR B 285 ? 0.3185 0.3525 0.3868 -0.0268 0.0256  -0.0515 285 THR B C   
5003  O O   . THR B 285 ? 0.3688 0.3856 0.4296 -0.0360 0.0253  -0.0599 285 THR B O   
5004  C CB  . THR B 285 ? 0.2759 0.2961 0.3432 -0.0138 0.0554  -0.0417 285 THR B CB  
5005  O OG1 . THR B 285 ? 0.3088 0.3287 0.3724 -0.0087 0.0641  -0.0358 285 THR B OG1 
5006  C CG2 . THR B 285 ? 0.2342 0.2745 0.3310 -0.0099 0.0533  -0.0324 285 THR B CG2 
5007  N N   . VAL B 286 ? 0.2831 0.3446 0.3749 -0.0232 0.0177  -0.0462 286 VAL B N   
5008  C CA  . VAL B 286 ? 0.2706 0.3520 0.3887 -0.0299 0.0103  -0.0481 286 VAL B CA  
5009  C C   . VAL B 286 ? 0.2648 0.3583 0.4059 -0.0286 0.0250  -0.0400 286 VAL B C   
5010  O O   . VAL B 286 ? 0.2670 0.3659 0.4064 -0.0183 0.0307  -0.0328 286 VAL B O   
5011  C CB  . VAL B 286 ? 0.2687 0.3731 0.3979 -0.0241 -0.0065 -0.0483 286 VAL B CB  
5012  C CG1 . VAL B 286 ? 0.2387 0.3747 0.4097 -0.0285 -0.0087 -0.0478 286 VAL B CG1 
5013  C CG2 . VAL B 286 ? 0.2798 0.3669 0.3803 -0.0267 -0.0255 -0.0542 286 VAL B CG2 
5014  N N   . LEU B 287 ? 0.2571 0.3494 0.4143 -0.0404 0.0299  -0.0404 287 LEU B N   
5015  C CA  . LEU B 287 ? 0.2609 0.3589 0.4335 -0.0412 0.0451  -0.0301 287 LEU B CA  
5016  C C   . LEU B 287 ? 0.2592 0.3872 0.4658 -0.0501 0.0466  -0.0280 287 LEU B C   
5017  O O   . LEU B 287 ? 0.2524 0.3894 0.4784 -0.0628 0.0348  -0.0350 287 LEU B O   
5018  C CB  . LEU B 287 ? 0.2628 0.3291 0.4275 -0.0480 0.0542  -0.0285 287 LEU B CB  
5019  C CG  . LEU B 287 ? 0.2858 0.3252 0.4277 -0.0389 0.0572  -0.0312 287 LEU B CG  
5020  C CD1 . LEU B 287 ? 0.3437 0.3492 0.4816 -0.0444 0.0657  -0.0328 287 LEU B CD1 
5021  C CD2 . LEU B 287 ? 0.2597 0.3065 0.4004 -0.0249 0.0616  -0.0200 287 LEU B CD2 
5022  N N   . SER B 288 ? 0.2791 0.4227 0.4936 -0.0441 0.0613  -0.0182 288 SER B N   
5023  C CA  . SER B 288 ? 0.3058 0.4807 0.5580 -0.0528 0.0706  -0.0144 288 SER B CA  
5024  C C   . SER B 288 ? 0.3599 0.5203 0.6260 -0.0745 0.0750  -0.0113 288 SER B C   
5025  O O   . SER B 288 ? 0.4051 0.5284 0.6454 -0.0768 0.0768  -0.0094 288 SER B O   
5026  C CB  . SER B 288 ? 0.3224 0.5088 0.5688 -0.0417 0.0914  -0.0048 288 SER B CB  
5027  O OG  . SER B 288 ? 0.3553 0.5107 0.5710 -0.0427 0.1027  0.0059  288 SER B OG  
5028  N N   . HIS B 289 ? 0.3343 0.5239 0.6455 -0.0902 0.0763  -0.0105 289 HIS B N   
5029  C CA  . HIS B 289 ? 0.3039 0.4774 0.6303 -0.1148 0.0723  -0.0102 289 HIS B CA  
5030  C C   . HIS B 289 ? 0.3119 0.4463 0.6181 -0.1236 0.0901  0.0011  289 HIS B C   
5031  O O   . HIS B 289 ? 0.2773 0.3726 0.5702 -0.1349 0.0823  -0.0043 289 HIS B O   
5032  C CB  . HIS B 289 ? 0.3259 0.5390 0.6931 -0.1250 0.0692  -0.0052 289 HIS B CB  
5033  C CG  . HIS B 289 ? 0.4001 0.5994 0.7842 -0.1525 0.0624  -0.0038 289 HIS B CG  
5034  N ND1 . HIS B 289 ? 0.4333 0.6082 0.8143 -0.1677 0.0364  -0.0177 289 HIS B ND1 
5035  C CD2 . HIS B 289 ? 0.4341 0.6367 0.8341 -0.1690 0.0771  0.0093  289 HIS B CD2 
5036  C CE1 . HIS B 289 ? 0.4741 0.6359 0.8679 -0.1922 0.0340  -0.0136 289 HIS B CE1 
5037  N NE2 . HIS B 289 ? 0.4750 0.6551 0.8835 -0.1941 0.0589  0.0036  289 HIS B NE2 
5038  N N   . SER B 290 ? 0.3752 0.5126 0.6691 -0.1160 0.1117  0.0166  290 SER B N   
5039  C CA  . SER B 290 ? 0.4403 0.5377 0.7121 -0.1235 0.1263  0.0308  290 SER B CA  
5040  C C   . SER B 290 ? 0.3993 0.4537 0.6340 -0.1105 0.1192  0.0282  290 SER B C   
5041  O O   . SER B 290 ? 0.4294 0.4415 0.6517 -0.1176 0.1197  0.0322  290 SER B O   
5042  C CB  . SER B 290 ? 0.5427 0.6488 0.7979 -0.1166 0.1488  0.0477  290 SER B CB  
5043  O OG  . SER B 290 ? 0.6466 0.7200 0.8892 -0.1309 0.1602  0.0633  290 SER B OG  
5044  N N   . ILE B 291 ? 0.3538 0.4179 0.5693 -0.0891 0.1109  0.0218  291 ILE B N   
5045  C CA  . ILE B 291 ? 0.3196 0.3518 0.5064 -0.0745 0.1024  0.0192  291 ILE B CA  
5046  C C   . ILE B 291 ? 0.3010 0.3124 0.4895 -0.0809 0.0909  0.0035  291 ILE B C   
5047  O O   . ILE B 291 ? 0.3409 0.3135 0.5159 -0.0786 0.0924  0.0037  291 ILE B O   
5048  C CB  . ILE B 291 ? 0.3381 0.3881 0.5103 -0.0547 0.0955  0.0160  291 ILE B CB  
5049  C CG1 . ILE B 291 ? 0.3906 0.4485 0.5469 -0.0470 0.1057  0.0294  291 ILE B CG1 
5050  C CG2 . ILE B 291 ? 0.3489 0.3752 0.5048 -0.0416 0.0876  0.0135  291 ILE B CG2 
5051  C CD1 . ILE B 291 ? 0.3983 0.4670 0.5370 -0.0295 0.0961  0.0254  291 ILE B CD1 
5052  N N   . PHE B 292 ? 0.2875 0.3215 0.4902 -0.0881 0.0790  -0.0101 292 PHE B N   
5053  C CA  . PHE B 292 ? 0.3026 0.3132 0.4957 -0.0957 0.0658  -0.0268 292 PHE B CA  
5054  C C   . PHE B 292 ? 0.3864 0.3596 0.5817 -0.1139 0.0683  -0.0276 292 PHE B C   
5055  O O   . PHE B 292 ? 0.4279 0.3582 0.5986 -0.1119 0.0668  -0.0376 292 PHE B O   
5056  C CB  . PHE B 292 ? 0.3091 0.3505 0.5182 -0.1034 0.0480  -0.0378 292 PHE B CB  
5057  C CG  . PHE B 292 ? 0.3600 0.3717 0.5500 -0.1146 0.0306  -0.0551 292 PHE B CG  
5058  C CD1 . PHE B 292 ? 0.3836 0.3719 0.5335 -0.1018 0.0267  -0.0656 292 PHE B CD1 
5059  C CD2 . PHE B 292 ? 0.4140 0.4196 0.6235 -0.1395 0.0182  -0.0609 292 PHE B CD2 
5060  C CE1 . PHE B 292 ? 0.4512 0.4052 0.5703 -0.1113 0.0124  -0.0826 292 PHE B CE1 
5061  C CE2 . PHE B 292 ? 0.4838 0.4550 0.6655 -0.1506 -0.0018 -0.0789 292 PHE B CE2 
5062  C CZ  . PHE B 292 ? 0.4863 0.4291 0.6173 -0.1354 -0.0040 -0.0903 292 PHE B CZ  
5063  N N   . GLU B 293 ? 0.4053 0.3930 0.6304 -0.1321 0.0741  -0.0172 293 GLU B N   
5064  C CA  . GLU B 293 ? 0.4985 0.4483 0.7292 -0.1543 0.0758  -0.0158 293 GLU B CA  
5065  C C   . GLU B 293 ? 0.4933 0.3929 0.6967 -0.1433 0.0887  -0.0064 293 GLU B C   
5066  O O   . GLU B 293 ? 0.4963 0.3447 0.6825 -0.1481 0.0853  -0.0156 293 GLU B O   
5067  C CB  . GLU B 293 ? 0.5409 0.5219 0.8115 -0.1750 0.0844  -0.0010 293 GLU B CB  
5068  C CG  . GLU B 293 ? 0.5491 0.5719 0.8534 -0.1900 0.0662  -0.0083 293 GLU B CG  
5069  C CD  . GLU B 293 ? 0.5949 0.5839 0.8980 -0.2144 0.0463  -0.0187 293 GLU B CD  
5070  O OE1 . GLU B 293 ? 0.6221 0.6302 0.9535 -0.2351 0.0434  -0.0094 293 GLU B OE1 
5071  O OE2 . GLU B 293 ? 0.6052 0.5468 0.8759 -0.2134 0.0347  -0.0364 293 GLU B OE2 
5072  N N   . VAL B 294 ? 0.4647 0.3754 0.6615 -0.1270 0.1016  0.0114  294 VAL B N   
5073  C CA  . VAL B 294 ? 0.4857 0.3514 0.6613 -0.1156 0.1097  0.0240  294 VAL B CA  
5074  C C   . VAL B 294 ? 0.4937 0.3379 0.6504 -0.0922 0.1046  0.0119  294 VAL B C   
5075  O O   . VAL B 294 ? 0.5381 0.3336 0.6838 -0.0877 0.1069  0.0091  294 VAL B O   
5076  C CB  . VAL B 294 ? 0.4394 0.3192 0.6075 -0.1066 0.1207  0.0476  294 VAL B CB  
5077  C CG1 . VAL B 294 ? 0.4653 0.2985 0.6115 -0.0914 0.1222  0.0616  294 VAL B CG1 
5078  C CG2 . VAL B 294 ? 0.4058 0.2988 0.5907 -0.1307 0.1337  0.0609  294 VAL B CG2 
5079  N N   . PHE B 295 ? 0.4316 0.3107 0.5866 -0.0776 0.0995  0.0043  295 PHE B N   
5080  C CA  . PHE B 295 ? 0.3846 0.2507 0.5276 -0.0568 0.0993  -0.0051 295 PHE B CA  
5081  C C   . PHE B 295 ? 0.4297 0.2572 0.5576 -0.0616 0.0990  -0.0261 295 PHE B C   
5082  O O   . PHE B 295 ? 0.4743 0.2657 0.5928 -0.0468 0.1073  -0.0299 295 PHE B O   
5083  C CB  . PHE B 295 ? 0.3442 0.2537 0.4880 -0.0465 0.0937  -0.0093 295 PHE B CB  
5084  C CG  . PHE B 295 ? 0.3655 0.2666 0.5001 -0.0305 0.0966  -0.0199 295 PHE B CG  
5085  C CD1 . PHE B 295 ? 0.3634 0.2595 0.5066 -0.0103 0.1027  -0.0100 295 PHE B CD1 
5086  C CD2 . PHE B 295 ? 0.3642 0.2622 0.4823 -0.0357 0.0934  -0.0385 295 PHE B CD2 
5087  C CE1 . PHE B 295 ? 0.3747 0.2685 0.5181 0.0040  0.1104  -0.0183 295 PHE B CE1 
5088  C CE2 . PHE B 295 ? 0.3837 0.2718 0.4891 -0.0219 0.1019  -0.0470 295 PHE B CE2 
5089  C CZ  . PHE B 295 ? 0.3973 0.2861 0.5193 -0.0019 0.1131  -0.0368 295 PHE B CZ  
5090  N N   . THR B 296 ? 0.4500 0.2826 0.5747 -0.0816 0.0886  -0.0402 296 THR B N   
5091  C CA  . THR B 296 ? 0.4962 0.2871 0.5938 -0.0876 0.0845  -0.0627 296 THR B CA  
5092  C C   . THR B 296 ? 0.5650 0.2949 0.6536 -0.0937 0.0904  -0.0651 296 THR B C   
5093  O O   . THR B 296 ? 0.6099 0.2921 0.6701 -0.0838 0.0971  -0.0808 296 THR B O   
5094  C CB  . THR B 296 ? 0.5132 0.3209 0.6100 -0.1106 0.0644  -0.0757 296 THR B CB  
5095  O OG1 . THR B 296 ? 0.5214 0.3747 0.6189 -0.1010 0.0582  -0.0759 296 THR B OG1 
5096  C CG2 . THR B 296 ? 0.5941 0.3479 0.6511 -0.1189 0.0566  -0.0996 296 THR B CG2 
5097  N N   . GLN B 297 ? 0.5794 0.3068 0.6896 -0.1085 0.0908  -0.0486 297 GLN B N   
5098  C CA  . GLN B 297 ? 0.6440 0.3078 0.7458 -0.1165 0.0952  -0.0479 297 GLN B CA  
5099  C C   . GLN B 297 ? 0.6529 0.2871 0.7479 -0.0860 0.1098  -0.0390 297 GLN B C   
5100  O O   . GLN B 297 ? 0.7363 0.3198 0.8095 -0.0758 0.1127  -0.0499 297 GLN B O   
5101  C CB  . GLN B 297 ? 0.6783 0.3507 0.8043 -0.1416 0.0930  -0.0282 297 GLN B CB  
5102  C CG  . GLN B 297 ? 0.7938 0.4086 0.9044 -0.1510 0.0885  -0.0258 297 GLN B CG  
5103  C CD  . GLN B 297 ? 0.8868 0.4645 0.9736 -0.1634 0.0721  -0.0524 297 GLN B CD  
5104  O OE1 . GLN B 297 ? 0.9299 0.5327 1.0262 -0.1862 0.0555  -0.0626 297 GLN B OE1 
5105  N NE2 . GLN B 297 ? 0.9073 0.4253 0.9627 -0.1467 0.0747  -0.0635 297 GLN B NE2 
5106  N N   . VAL B 298 ? 0.5969 0.2715 0.7089 -0.0689 0.1140  -0.0185 298 VAL B N   
5107  C CA  . VAL B 298 ? 0.5757 0.2343 0.6913 -0.0382 0.1226  -0.0077 298 VAL B CA  
5108  C C   . VAL B 298 ? 0.5795 0.2258 0.6845 -0.0181 0.1312  -0.0295 298 VAL B C   
5109  O O   . VAL B 298 ? 0.6025 0.2147 0.7053 0.0027  0.1396  -0.0313 298 VAL B O   
5110  C CB  . VAL B 298 ? 0.4892 0.1989 0.6216 -0.0247 0.1193  0.0148  298 VAL B CB  
5111  C CG1 . VAL B 298 ? 0.5123 0.2197 0.6576 0.0075  0.1227  0.0214  298 VAL B CG1 
5112  C CG2 . VAL B 298 ? 0.5019 0.2059 0.6336 -0.0381 0.1171  0.0391  298 VAL B CG2 
5113  N N   . PHE B 299 ? 0.5772 0.2563 0.6727 -0.0234 0.1284  -0.0450 299 PHE B N   
5114  C CA  . PHE B 299 ? 0.5823 0.2462 0.6596 -0.0065 0.1409  -0.0648 299 PHE B CA  
5115  C C   . PHE B 299 ? 0.6671 0.2677 0.7095 -0.0120 0.1432  -0.0847 299 PHE B C   
5116  O O   . PHE B 299 ? 0.7305 0.3090 0.7627 0.0104  0.1555  -0.0907 299 PHE B O   
5117  C CB  . PHE B 299 ? 0.5364 0.2404 0.6000 -0.0133 0.1355  -0.0758 299 PHE B CB  
5118  C CG  . PHE B 299 ? 0.5849 0.2780 0.6290 0.0059  0.1539  -0.0908 299 PHE B CG  
5119  C CD1 . PHE B 299 ? 0.6370 0.2804 0.6330 0.0016  0.1593  -0.1152 299 PHE B CD1 
5120  C CD2 . PHE B 299 ? 0.5405 0.2740 0.6126 0.0272  0.1655  -0.0791 299 PHE B CD2 
5121  C CE1 . PHE B 299 ? 0.6606 0.3036 0.6334 0.0192  0.1768  -0.1238 299 PHE B CE1 
5122  C CE2 . PHE B 299 ? 0.5671 0.2979 0.6258 0.0431  0.1860  -0.0894 299 PHE B CE2 
5123  C CZ  . PHE B 299 ? 0.6204 0.3087 0.6271 0.0390  0.1920  -0.1100 299 PHE B CZ  
5124  N N   . ALA B 300 ? 0.6840 0.2657 0.7099 -0.0419 0.1271  -0.0932 300 ALA B N   
5125  C CA  . ALA B 300 ? 0.7117 0.2384 0.6999 -0.0498 0.1201  -0.1117 300 ALA B CA  
5126  C C   . ALA B 300 ? 0.8061 0.2918 0.7988 -0.0344 0.1266  -0.1031 300 ALA B C   
5127  O O   . ALA B 300 ? 0.8707 0.3111 0.8340 -0.0237 0.1306  -0.1193 300 ALA B O   
5128  C CB  . ALA B 300 ? 0.7499 0.2725 0.7335 -0.0866 0.0960  -0.1173 300 ALA B CB  
5129  N N   . ASN B 301 ? 0.7763 0.2761 0.8028 -0.0320 0.1272  -0.0773 301 ASN B N   
5130  C CA  . ASN B 301 ? 0.8120 0.2740 0.8439 -0.0163 0.1300  -0.0648 301 ASN B CA  
5131  C C   . ASN B 301 ? 0.8383 0.3030 0.8797 0.0225  0.1457  -0.0649 301 ASN B C   
5132  O O   . ASN B 301 ? 0.8996 0.3257 0.9401 0.0388  0.1475  -0.0622 301 ASN B O   
5133  C CB  . ASN B 301 ? 0.7948 0.2729 0.8531 -0.0249 0.1243  -0.0344 301 ASN B CB  
5134  C CG  . ASN B 301 ? 0.8248 0.2965 0.8800 -0.0632 0.1116  -0.0305 301 ASN B CG  
5135  O OD1 . ASN B 301 ? 0.8201 0.2646 0.8561 -0.0831 0.1018  -0.0495 301 ASN B OD1 
5136  N ND2 . ASN B 301 ? 0.8323 0.3327 0.9072 -0.0743 0.1108  -0.0049 301 ASN B ND2 
5137  N N   . ASN B 302 ? 0.8204 0.3328 0.8750 0.0367  0.1563  -0.0671 302 ASN B N   
5138  C CA  . ASN B 302 ? 0.8645 0.3924 0.9381 0.0704  0.1716  -0.0656 302 ASN B CA  
5139  C C   . ASN B 302 ? 0.9292 0.4436 0.9702 0.0772  0.1868  -0.0920 302 ASN B C   
5140  O O   . ASN B 302 ? 0.9295 0.4742 0.9861 0.0983  0.2033  -0.0926 302 ASN B O   
5141  C CB  . ASN B 302 ? 0.7953 0.3886 0.9106 0.0814  0.1725  -0.0468 302 ASN B CB  
5142  C CG  . ASN B 302 ? 0.7795 0.3818 0.9240 0.0849  0.1584  -0.0182 302 ASN B CG  
5143  O OD1 . ASN B 302 ? 0.8227 0.4270 0.9920 0.1081  0.1571  -0.0053 302 ASN B OD1 
5144  N ND2 . ASN B 302 ? 0.7410 0.3500 0.8815 0.0619  0.1472  -0.0074 302 ASN B ND2 
5145  N N   . MET B 303 ? 0.8217 0.5303 0.9842 0.0551  0.0916  -0.1523 303 MET B N   
5146  C CA  . MET B 303 ? 0.7951 0.5449 0.9626 0.0553  0.1064  -0.1713 303 MET B CA  
5147  C C   . MET B 303 ? 0.8587 0.5462 0.9840 0.0554  0.1060  -0.1921 303 MET B C   
5148  O O   . MET B 303 ? 0.9145 0.5351 1.0083 0.0432  0.0973  -0.1885 303 MET B O   
5149  C CB  . MET B 303 ? 0.7230 0.5223 0.8972 0.0244  0.1148  -0.1594 303 MET B CB  
5150  C CG  . MET B 303 ? 0.6406 0.5000 0.8487 0.0240  0.1179  -0.1412 303 MET B CG  
5151  S SD  . MET B 303 ? 0.8047 0.7282 1.0450 0.0471  0.1345  -0.1577 303 MET B SD  
5152  C CE  . MET B 303 ? 0.5338 0.4780 0.7433 0.0238  0.1505  -0.1660 303 MET B CE  
5153  N N   . PRO B 304 ? 0.8513 0.5538 0.9697 0.0669  0.1178  -0.2144 304 PRO B N   
5154  C CA  . PRO B 304 ? 0.9036 0.5471 0.9751 0.0637  0.1181  -0.2350 304 PRO B CA  
5155  C C   . PRO B 304 ? 0.9265 0.5592 0.9761 0.0234  0.1141  -0.2308 304 PRO B C   
5156  O O   . PRO B 304 ? 0.9181 0.5970 0.9730 0.0086  0.1194  -0.2306 304 PRO B O   
5157  C CB  . PRO B 304 ? 0.9120 0.5861 0.9846 0.0843  0.1357  -0.2569 304 PRO B CB  
5158  C CG  . PRO B 304 ? 0.8466 0.6024 0.9623 0.0815  0.1473  -0.2455 304 PRO B CG  
5159  C CD  . PRO B 304 ? 0.7974 0.5680 0.9489 0.0842  0.1341  -0.2229 304 PRO B CD  
5160  N N   . LYS B 305 ? 0.9634 0.5320 0.9866 0.0062  0.1045  -0.2297 305 LYS B N   
5161  C CA  . LYS B 305 ? 0.9304 0.4938 0.9483 -0.0343 0.0993  -0.2263 305 LYS B CA  
5162  C C   . LYS B 305 ? 0.9526 0.5151 0.9444 -0.0444 0.0975  -0.2468 305 LYS B C   
5163  O O   . LYS B 305 ? 0.9329 0.5208 0.9331 -0.0725 0.0899  -0.2456 305 LYS B O   
5164  C CB  . LYS B 305 ? 0.9622 0.4498 0.9555 -0.0505 0.0950  -0.2243 305 LYS B CB  
5165  C CG  . LYS B 305 ? 0.9408 0.4251 0.9417 -0.0945 0.0928  -0.2222 305 LYS B CG  
5166  C CD  . LYS B 305 ? 0.9579 0.3969 0.9377 -0.1022 0.0878  -0.2041 305 LYS B CD  
5167  C CE  . LYS B 305 ? 0.9137 0.3867 0.9236 -0.1362 0.0892  -0.1871 305 LYS B CE  
5168  N NZ  . LYS B 305 ? 0.9241 0.3681 0.9168 -0.1340 0.0893  -0.1646 305 LYS B NZ  
5169  N N   . GLN B 306 ? 0.9835 0.5192 0.9446 -0.0179 0.1039  -0.2661 306 GLN B N   
5170  C CA  . GLN B 306 ? 1.0038 0.5204 0.9243 -0.0228 0.1037  -0.2876 306 GLN B CA  
5171  C C   . GLN B 306 ? 0.9511 0.5291 0.8801 -0.0179 0.1131  -0.2878 306 GLN B C   
5172  O O   . GLN B 306 ? 0.9694 0.5307 0.8572 -0.0209 0.1145  -0.3046 306 GLN B O   
5173  C CB  . GLN B 306 ? 1.0869 0.5389 0.9642 0.0068  0.1108  -0.3091 306 GLN B CB  
5174  C CG  . GLN B 306 ? 1.0288 0.4969 0.9325 0.0509  0.1228  -0.3083 306 GLN B CG  
5175  C CD  . GLN B 306 ? 1.0093 0.4592 0.9349 0.0554  0.1122  -0.2904 306 GLN B CD  
5176  O OE1 . GLN B 306 ? 1.0171 0.4292 0.9290 0.0258  0.1019  -0.2810 306 GLN B OE1 
5177  N NE2 . GLN B 306 ? 0.9907 0.4656 0.9496 0.0909  0.1150  -0.2868 306 GLN B NE2 
5178  N N   . ALA B 307 ? 0.8764 0.5177 0.8507 -0.0148 0.1186  -0.2682 307 ALA B N   
5179  C CA  . ALA B 307 ? 0.8535 0.5465 0.8291 -0.0138 0.1294  -0.2669 307 ALA B CA  
5180  C C   . ALA B 307 ? 0.8223 0.5488 0.8085 -0.0424 0.1145  -0.2515 307 ALA B C   
5181  O O   . ALA B 307 ? 0.7727 0.5297 0.7464 -0.0453 0.1195  -0.2498 307 ALA B O   
5182  C CB  . ALA B 307 ? 0.7860 0.5264 0.8008 0.0110  0.1480  -0.2593 307 ALA B CB  
5183  N N   . GLN B 308 ? 0.8293 0.5467 0.8362 -0.0632 0.0975  -0.2415 308 GLN B N   
5184  C CA  . GLN B 308 ? 0.8180 0.5727 0.8458 -0.0865 0.0829  -0.2280 308 GLN B CA  
5185  C C   . GLN B 308 ? 0.8860 0.6265 0.8770 -0.1021 0.0646  -0.2438 308 GLN B C   
5186  O O   . GLN B 308 ? 0.9615 0.6534 0.9124 -0.1035 0.0597  -0.2646 308 GLN B O   
5187  C CB  . GLN B 308 ? 0.8142 0.5661 0.8805 -0.1048 0.0752  -0.2151 308 GLN B CB  
5188  C CG  . GLN B 308 ? 0.8359 0.5813 0.9224 -0.0895 0.0889  -0.2007 308 GLN B CG  
5189  C CD  . GLN B 308 ? 0.8600 0.5969 0.9751 -0.1101 0.0865  -0.1861 308 GLN B CD  
5190  O OE1 . GLN B 308 ? 0.8673 0.6201 1.0020 -0.1354 0.0772  -0.1859 308 GLN B OE1 
5191  N NE2 . GLN B 308 ? 0.8627 0.5697 0.9787 -0.0991 0.0948  -0.1759 308 GLN B NE2 
5192  N N   . VAL B 309 ? 0.8689 0.6472 0.8670 -0.1114 0.0528  -0.2341 309 VAL B N   
5193  C CA  . VAL B 309 ? 0.9074 0.6742 0.8714 -0.1250 0.0273  -0.2465 309 VAL B CA  
5194  C C   . VAL B 309 ? 0.8689 0.6742 0.8791 -0.1427 0.0032  -0.2350 309 VAL B C   
5195  O O   . VAL B 309 ? 0.7867 0.6251 0.8478 -0.1437 0.0127  -0.2165 309 VAL B O   
5196  C CB  . VAL B 309 ? 0.9210 0.6828 0.8266 -0.1128 0.0360  -0.2506 309 VAL B CB  
5197  C CG1 . VAL B 309 ? 0.9736 0.6971 0.8367 -0.0957 0.0621  -0.2672 309 VAL B CG1 
5198  C CG2 . VAL B 309 ? 0.8440 0.6545 0.7705 -0.1059 0.0494  -0.2284 309 VAL B CG2 
5199  N N   . LYS B 310 ? 0.9276 0.7250 0.9203 -0.1556 -0.0292 -0.2475 310 LYS B N   
5200  C CA  . LYS B 310 ? 0.8993 0.7379 0.9398 -0.1683 -0.0564 -0.2407 310 LYS B CA  
5201  C C   . LYS B 310 ? 0.8528 0.7330 0.9083 -0.1560 -0.0446 -0.2165 310 LYS B C   
5202  O O   . LYS B 310 ? 0.8883 0.7606 0.8915 -0.1425 -0.0362 -0.2120 310 LYS B O   
5203  C CB  . LYS B 310 ? 0.9680 0.7880 0.9705 -0.1750 -0.0972 -0.2581 310 LYS B CB  
5204  C CG  . LYS B 310 ? 1.0400 0.8275 1.0419 -0.1940 -0.1201 -0.2819 310 LYS B CG  
5205  C CD  . LYS B 310 ? 1.1392 0.8656 1.0463 -0.1886 -0.1351 -0.2998 310 LYS B CD  
5206  C CE  . LYS B 310 ? 1.2160 0.8999 1.1106 -0.2081 -0.1587 -0.3243 310 LYS B CE  
5207  N NZ  . LYS B 310 ? 1.1876 0.9164 1.1642 -0.2306 -0.1928 -0.3294 310 LYS B NZ  
5208  N N   . ALA B 311 ? 0.7588 0.6777 0.8812 -0.1624 -0.0404 -0.2017 311 ALA B N   
5209  C CA  . ALA B 311 ? 0.6875 0.6413 0.8241 -0.1521 -0.0294 -0.1779 311 ALA B CA  
5210  C C   . ALA B 311 ? 0.7045 0.6649 0.8058 -0.1457 -0.0554 -0.1774 311 ALA B C   
5211  O O   . ALA B 311 ? 0.7631 0.7191 0.8628 -0.1521 -0.0904 -0.1928 311 ALA B O   
5212  C CB  . ALA B 311 ? 0.6293 0.6149 0.8385 -0.1621 -0.0231 -0.1654 311 ALA B CB  
5213  N N   . VAL B 312 ? 0.6823 0.6484 0.7510 -0.1334 -0.0404 -0.1604 312 VAL B N   
5214  C CA  . VAL B 312 ? 0.7206 0.6759 0.7345 -0.1267 -0.0630 -0.1600 312 VAL B CA  
5215  C C   . VAL B 312 ? 0.7024 0.6848 0.7276 -0.1197 -0.0570 -0.1361 312 VAL B C   
5216  O O   . VAL B 312 ? 0.6651 0.6638 0.7103 -0.1179 -0.0258 -0.1188 312 VAL B O   
5217  C CB  . VAL B 312 ? 0.9207 0.8314 0.8460 -0.1212 -0.0483 -0.1685 312 VAL B CB  
5218  C CG1 . VAL B 312 ? 0.9365 0.8267 0.7903 -0.1150 -0.0583 -0.1613 312 VAL B CG1 
5219  C CG2 . VAL B 312 ? 1.0108 0.8814 0.9051 -0.1268 -0.0643 -0.1944 312 VAL B CG2 
5220  N N   . GLY B 313 ? 0.7233 0.7065 0.7337 -0.1146 -0.0904 -0.1360 313 GLY B N   
5221  C CA  . GLY B 313 ? 0.7000 0.6973 0.7045 -0.1057 -0.0885 -0.1146 313 GLY B CA  
5222  C C   . GLY B 313 ? 0.6100 0.6516 0.7017 -0.1084 -0.0760 -0.1013 313 GLY B C   
5223  O O   . GLY B 313 ? 0.5958 0.6590 0.7544 -0.1172 -0.0834 -0.1125 313 GLY B O   
5224  N N   . PRO B 314 ? 0.5613 0.6106 0.6473 -0.1039 -0.0524 -0.0778 314 PRO B N   
5225  C CA  . PRO B 314 ? 0.5224 0.6005 0.6717 -0.1058 -0.0344 -0.0612 314 PRO B CA  
5226  C C   . PRO B 314 ? 0.5252 0.6036 0.7060 -0.1153 -0.0030 -0.0585 314 PRO B C   
5227  O O   . PRO B 314 ? 0.4941 0.5841 0.7182 -0.1190 0.0140  -0.0453 314 PRO B O   
5228  C CB  . PRO B 314 ? 0.4986 0.5681 0.6022 -0.0971 -0.0248 -0.0381 314 PRO B CB  
5229  C CG  . PRO B 314 ? 0.5398 0.5798 0.5675 -0.0976 -0.0169 -0.0409 314 PRO B CG  
5230  C CD  . PRO B 314 ? 0.5868 0.6092 0.5924 -0.0984 -0.0415 -0.0663 314 PRO B CD  
5231  N N   . PHE B 315 ? 0.5577 0.6170 0.7115 -0.1179 0.0040  -0.0715 315 PHE B N   
5232  C CA  . PHE B 315 ? 0.5408 0.5928 0.7126 -0.1214 0.0305  -0.0695 315 PHE B CA  
5233  C C   . PHE B 315 ? 0.6072 0.6540 0.8244 -0.1321 0.0289  -0.0839 315 PHE B C   
5234  O O   . PHE B 315 ? 0.6673 0.7142 0.8942 -0.1387 0.0071  -0.1029 315 PHE B O   
5235  C CB  . PHE B 315 ? 0.5291 0.5635 0.6518 -0.1157 0.0427  -0.0772 315 PHE B CB  
5236  C CG  . PHE B 315 ? 0.5192 0.5553 0.5957 -0.1105 0.0518  -0.0641 315 PHE B CG  
5237  C CD1 . PHE B 315 ? 0.4607 0.5095 0.5492 -0.1094 0.0683  -0.0418 315 PHE B CD1 
5238  C CD2 . PHE B 315 ? 0.5813 0.5985 0.5952 -0.1090 0.0455  -0.0746 315 PHE B CD2 
5239  C CE1 . PHE B 315 ? 0.4823 0.5306 0.5277 -0.1087 0.0781  -0.0306 315 PHE B CE1 
5240  C CE2 . PHE B 315 ? 0.6035 0.6156 0.5690 -0.1085 0.0586  -0.0633 315 PHE B CE2 
5241  C CZ  . PHE B 315 ? 0.5641 0.5947 0.5484 -0.1093 0.0751  -0.0416 315 PHE B CZ  
5242  N N   . GLY B 316 ? 0.6025 0.6379 0.8405 -0.1348 0.0510  -0.0758 316 GLY B N   
5243  C CA  . GLY B 316 ? 0.5978 0.6169 0.8698 -0.1480 0.0543  -0.0875 316 GLY B CA  
5244  C C   . GLY B 316 ? 0.6332 0.6185 0.8813 -0.1449 0.0615  -0.1009 316 GLY B C   
5245  O O   . GLY B 316 ? 0.6935 0.6568 0.9542 -0.1569 0.0593  -0.1162 316 GLY B O   
5246  N N   . LEU B 317 ? 0.6068 0.5877 0.8217 -0.1291 0.0711  -0.0968 317 LEU B N   
5247  C CA  . LEU B 317 ? 0.5612 0.5121 0.7574 -0.1205 0.0796  -0.1100 317 LEU B CA  
5248  C C   . LEU B 317 ? 0.5535 0.5118 0.7113 -0.1070 0.0825  -0.1193 317 LEU B C   
5249  O O   . LEU B 317 ? 0.5066 0.4854 0.6567 -0.0975 0.0942  -0.1076 317 LEU B O   
5250  C CB  . LEU B 317 ? 0.5081 0.4411 0.7149 -0.1126 0.0947  -0.0960 317 LEU B CB  
5251  C CG  . LEU B 317 ? 0.5160 0.4128 0.7091 -0.0988 0.1010  -0.1077 317 LEU B CG  
5252  C CD1 . LEU B 317 ? 0.4936 0.3490 0.6802 -0.1106 0.0955  -0.1261 317 LEU B CD1 
5253  C CD2 . LEU B 317 ? 0.5239 0.4051 0.7250 -0.0891 0.1083  -0.0903 317 LEU B CD2 
5254  N N   . CYS B 318 ? 0.5797 0.5178 0.7108 -0.1090 0.0735  -0.1414 318 CYS B N   
5255  C CA  . CYS B 318 ? 0.5871 0.5207 0.6722 -0.0991 0.0798  -0.1536 318 CYS B CA  
5256  C C   . CYS B 318 ? 0.6168 0.5161 0.6812 -0.0888 0.0899  -0.1749 318 CYS B C   
5257  O O   . CYS B 318 ? 0.6182 0.4875 0.6906 -0.0933 0.0828  -0.1846 318 CYS B O   
5258  C CB  . CYS B 318 ? 0.6092 0.5390 0.6597 -0.1086 0.0579  -0.1615 318 CYS B CB  
5259  S SG  . CYS B 318 ? 0.6364 0.6000 0.6934 -0.1131 0.0459  -0.1397 318 CYS B SG  
5260  N N   . TYR B 319 ? 0.6434 0.5450 0.6796 -0.0754 0.1091  -0.1829 319 TYR B N   
5261  C CA  . TYR B 319 ? 0.6663 0.5375 0.6832 -0.0610 0.1227  -0.2042 319 TYR B CA  
5262  C C   . TYR B 319 ? 0.7204 0.5716 0.6770 -0.0599 0.1319  -0.2223 319 TYR B C   
5263  O O   . TYR B 319 ? 0.7323 0.5961 0.6605 -0.0673 0.1336  -0.2166 319 TYR B O   
5264  C CB  . TYR B 319 ? 0.6723 0.5654 0.7250 -0.0403 0.1441  -0.1999 319 TYR B CB  
5265  C CG  . TYR B 319 ? 0.6632 0.5559 0.7591 -0.0393 0.1341  -0.1841 319 TYR B CG  
5266  C CD1 . TYR B 319 ? 0.6206 0.5453 0.7452 -0.0475 0.1303  -0.1595 319 TYR B CD1 
5267  C CD2 . TYR B 319 ? 0.7045 0.5541 0.8017 -0.0311 0.1291  -0.1936 319 TYR B CD2 
5268  C CE1 . TYR B 319 ? 0.6106 0.5231 0.7629 -0.0478 0.1233  -0.1452 319 TYR B CE1 
5269  C CE2 . TYR B 319 ? 0.6933 0.5280 0.8154 -0.0319 0.1214  -0.1794 319 TYR B CE2 
5270  C CZ  . TYR B 319 ? 0.6653 0.5307 0.8142 -0.0406 0.1192  -0.1554 319 TYR B CZ  
5271  O OH  . TYR B 319 ? 0.6853 0.5241 0.8477 -0.0422 0.1137  -0.1417 319 TYR B OH  
5272  N N   . ASP B 320 ? 0.8026 0.6131 0.7306 -0.0503 0.1392  -0.2445 320 ASP B N   
5273  C CA  . ASP B 320 ? 0.9066 0.6903 0.7722 -0.0460 0.1570  -0.2636 320 ASP B CA  
5274  C C   . ASP B 320 ? 0.8825 0.7063 0.7737 -0.0297 0.1942  -0.2628 320 ASP B C   
5275  O O   . ASP B 320 ? 0.8688 0.7090 0.8074 -0.0104 0.2063  -0.2656 320 ASP B O   
5276  C CB  . ASP B 320 ? 1.0174 0.7412 0.8446 -0.0401 0.1541  -0.2876 320 ASP B CB  
5277  C CG  . ASP B 320 ? 1.1574 0.8449 0.9173 -0.0315 0.1805  -0.3097 320 ASP B CG  
5278  O OD1 . ASP B 320 ? 1.1864 0.8922 0.9247 -0.0329 0.2031  -0.3079 320 ASP B OD1 
5279  O OD2 . ASP B 320 ? 1.2454 0.8779 0.9665 -0.0253 0.1801  -0.3299 320 ASP B OD2 
5280  N N   . SER B 321 ? 0.8891 0.7221 0.7437 -0.0370 0.2125  -0.2625 321 SER B N   
5281  C CA  . SER B 321 ? 0.8639 0.7441 0.7501 -0.0290 0.2483  -0.2606 321 SER B CA  
5282  C C   . SER B 321 ? 0.9301 0.8106 0.8325 -0.0059 0.2817  -0.2848 321 SER B C   
5283  O O   . SER B 321 ? 0.9022 0.8347 0.8668 0.0071  0.3033  -0.2843 321 SER B O   
5284  C CB  . SER B 321 ? 0.9108 0.7857 0.7378 -0.0464 0.2643  -0.2580 321 SER B CB  
5285  O OG  . SER B 321 ? 0.9310 0.7964 0.7331 -0.0637 0.2301  -0.2391 321 SER B OG  
5286  N N   . ARG B 322 ? 1.0141 0.8365 0.8621 0.0000  0.2845  -0.3068 322 ARG B N   
5287  C CA  . ARG B 322 ? 1.0675 0.8820 0.9218 0.0247  0.3190  -0.3331 322 ARG B CA  
5288  C C   . ARG B 322 ? 1.0420 0.8770 0.9704 0.0514  0.3089  -0.3339 322 ARG B C   
5289  O O   . ARG B 322 ? 1.0501 0.9182 1.0270 0.0762  0.3365  -0.3481 322 ARG B O   
5290  C CB  . ARG B 322 ? 1.1562 0.8909 0.9201 0.0234  0.3227  -0.3556 322 ARG B CB  
5291  C CG  . ARG B 322 ? 1.2020 0.8997 0.8767 -0.0006 0.3301  -0.3569 322 ARG B CG  
5292  C CD  . ARG B 322 ? 1.2995 0.9134 0.8792 0.0006  0.3377  -0.3803 322 ARG B CD  
5293  N NE  . ARG B 322 ? 1.3460 0.9521 0.8746 -0.0060 0.3666  -0.3793 322 ARG B NE  
5294  C CZ  . ARG B 322 ? 1.4245 0.9941 0.9096 0.0041  0.3892  -0.3931 322 ARG B CZ  
5295  N NH1 . ARG B 322 ? 1.4587 0.9969 0.9429 0.0239  0.3848  -0.4088 322 ARG B NH1 
5296  N NH2 . ARG B 322 ? 1.4779 1.0381 0.9177 -0.0064 0.4169  -0.3910 322 ARG B NH2 
5297  N N   . LYS B 323 ? 1.0081 0.8237 0.9477 0.0469  0.2702  -0.3198 323 LYS B N   
5298  C CA  . LYS B 323 ? 0.9997 0.8256 0.9990 0.0711  0.2599  -0.3181 323 LYS B CA  
5299  C C   . LYS B 323 ? 1.0075 0.9042 1.0721 0.0671  0.2595  -0.2957 323 LYS B C   
5300  O O   . LYS B 323 ? 1.0191 0.9531 1.0817 0.0537  0.2793  -0.2917 323 LYS B O   
5301  C CB  . LYS B 323 ? 0.9837 0.7544 0.9631 0.0639  0.2248  -0.3123 323 LYS B CB  
5302  C CG  . LYS B 323 ? 0.9482 0.7130 0.9733 0.0861  0.2110  -0.3076 323 LYS B CG  
5303  C CD  . LYS B 323 ? 1.0159 0.7170 1.0101 0.1100  0.2120  -0.3309 323 LYS B CD  
5304  C CE  . LYS B 323 ? 1.0028 0.7002 1.0408 0.1407  0.2016  -0.3291 323 LYS B CE  
5305  N NZ  . LYS B 323 ? 0.9513 0.7258 1.0603 0.1613  0.2162  -0.3266 323 LYS B NZ  
5306  N N   . ILE B 324 ? 1.0200 0.9291 1.1352 0.0782  0.2390  -0.2820 324 ILE B N   
5307  C CA  . ILE B 324 ? 0.9856 0.9506 1.1521 0.0710  0.2334  -0.2586 324 ILE B CA  
5308  C C   . ILE B 324 ? 0.9926 1.0235 1.2062 0.0807  0.2629  -0.2662 324 ILE B C   
5309  O O   . ILE B 324 ? 0.9703 1.0440 1.2426 0.0885  0.2556  -0.2547 324 ILE B O   
5310  C CB  . ILE B 324 ? 0.8785 0.8461 1.0149 0.0364  0.2209  -0.2360 324 ILE B CB  
5311  C CG1 . ILE B 324 ? 0.9040 0.8181 1.0082 0.0231  0.1929  -0.2303 324 ILE B CG1 
5312  C CG2 . ILE B 324 ? 0.8143 0.8323 0.9933 0.0278  0.2170  -0.2113 324 ILE B CG2 
5313  C CD1 . ILE B 324 ? 0.9091 0.7954 1.0379 0.0370  0.1758  -0.2265 324 ILE B CD1 
5314  N N   . SER B 325 ? 1.0255 1.0613 1.2124 0.0789  0.2968  -0.2866 325 SER B N   
5315  C CA  . SER B 325 ? 1.0267 1.1256 1.2587 0.0825  0.3315  -0.2967 325 SER B CA  
5316  C C   . SER B 325 ? 1.0242 1.1521 1.3280 0.1191  0.3268  -0.3076 325 SER B C   
5317  O O   . SER B 325 ? 1.0468 1.1536 1.3425 0.1430  0.3353  -0.3269 325 SER B O   
5318  C CB  . SER B 325 ? 1.1194 1.2008 1.2904 0.0702  0.3658  -0.3118 325 SER B CB  
5319  O OG  . SER B 325 ? 1.1594 1.2878 1.3721 0.0820  0.3879  -0.3183 325 SER B OG  
5320  N N   . GLY B 326 ? 1.0013 1.1718 1.3682 0.1234  0.3068  -0.2916 326 GLY B N   
5321  C CA  . GLY B 326 ? 1.0172 1.2218 1.4530 0.1549  0.2930  -0.2960 326 GLY B CA  
5322  C C   . GLY B 326 ? 0.9916 1.1735 1.4505 0.1662  0.2546  -0.2827 326 GLY B C   
5323  O O   . GLY B 326 ? 1.0330 1.2221 1.5366 0.1958  0.2317  -0.2851 326 GLY B O   
5324  N N   . GLY B 327 ? 0.9389 1.0826 1.3483 0.1391  0.2390  -0.2599 327 GLY B N   
5325  C CA  . GLY B 327 ? 0.9296 1.0102 1.3133 0.1443  0.2020  -0.2445 327 GLY B CA  
5326  C C   . GLY B 327 ? 0.8704 0.9335 1.2307 0.1156  0.1800  -0.2114 327 GLY B C   
5327  O O   . GLY B 327 ? 0.9199 0.9211 1.2446 0.1124  0.1584  -0.2015 327 GLY B O   
5328  N N   . ALA B 328 ? 0.7588 0.8713 1.1364 0.0941  0.1873  -0.1950 328 ALA B N   
5329  C CA  . ALA B 328 ? 0.6494 0.7450 1.0092 0.0718  0.1669  -0.1640 328 ALA B CA  
5330  C C   . ALA B 328 ? 0.5424 0.6474 0.9447 0.0866  0.1443  -0.1520 328 ALA B C   
5331  O O   . ALA B 328 ? 0.5416 0.6959 0.9987 0.1040  0.1483  -0.1642 328 ALA B O   
5332  C CB  . ALA B 328 ? 0.6366 0.7651 0.9780 0.0411  0.1828  -0.1509 328 ALA B CB  
5333  N N   . PRO B 329 ? 0.4798 0.5353 0.8565 0.0790  0.1203  -0.1293 329 PRO B N   
5334  C CA  . PRO B 329 ? 0.4712 0.5141 0.8713 0.0945  0.0934  -0.1178 329 PRO B CA  
5335  C C   . PRO B 329 ? 0.4481 0.5384 0.8738 0.0788  0.0913  -0.0986 329 PRO B C   
5336  O O   . PRO B 329 ? 0.4365 0.5602 0.8516 0.0525  0.1110  -0.0899 329 PRO B O   
5337  C CB  . PRO B 329 ? 0.4926 0.4498 0.8387 0.0874  0.0757  -0.1018 329 PRO B CB  
5338  C CG  . PRO B 329 ? 0.4768 0.4287 0.7878 0.0576  0.0936  -0.0963 329 PRO B CG  
5339  C CD  . PRO B 329 ? 0.4744 0.4737 0.7977 0.0589  0.1166  -0.1182 329 PRO B CD  
5340  N N   . SER B 330 ? 0.4614 0.5491 0.9161 0.0959  0.0649  -0.0934 330 SER B N   
5341  C CA  . SER B 330 ? 0.4579 0.5700 0.9248 0.0797  0.0550  -0.0719 330 SER B CA  
5342  C C   . SER B 330 ? 0.4560 0.5157 0.8606 0.0523  0.0539  -0.0424 330 SER B C   
5343  O O   . SER B 330 ? 0.5096 0.4947 0.8726 0.0563  0.0393  -0.0335 330 SER B O   
5344  C CB  . SER B 330 ? 0.4844 0.5848 0.9837 0.1056  0.0180  -0.0722 330 SER B CB  
5345  O OG  . SER B 330 ? 0.5334 0.5447 0.9736 0.1036  -0.0076 -0.0494 330 SER B OG  
5346  N N   . VAL B 331 ? 0.4726 0.3599 0.7207 0.0548  0.1163  -0.0140 331 VAL B N   
5347  C CA  . VAL B 331 ? 0.4911 0.3538 0.7034 0.0391  0.1115  0.0072  331 VAL B CA  
5348  C C   . VAL B 331 ? 0.4549 0.3411 0.6675 0.0324  0.1028  0.0212  331 VAL B C   
5349  O O   . VAL B 331 ? 0.4579 0.3815 0.6792 0.0213  0.1110  0.0172  331 VAL B O   
5350  C CB  . VAL B 331 ? 0.5224 0.3839 0.7135 0.0212  0.1209  0.0005  331 VAL B CB  
5351  C CG1 . VAL B 331 ? 0.4821 0.3254 0.6553 0.0052  0.1143  0.0152  331 VAL B CG1 
5352  C CG2 . VAL B 331 ? 0.5528 0.3899 0.7492 0.0286  0.1262  -0.0179 331 VAL B CG2 
5353  N N   . ASP B 332 ? 0.4149 0.2740 0.6134 0.0382  0.0875  0.0371  332 ASP B N   
5354  C CA  . ASP B 332 ? 0.3989 0.2787 0.6019 0.0363  0.0739  0.0462  332 ASP B CA  
5355  C C   . ASP B 332 ? 0.3842 0.2353 0.5503 0.0226  0.0709  0.0616  332 ASP B C   
5356  O O   . ASP B 332 ? 0.4329 0.2349 0.5661 0.0226  0.0747  0.0687  332 ASP B O   
5357  C CB  . ASP B 332 ? 0.4732 0.3491 0.6948 0.0616  0.0501  0.0441  332 ASP B CB  
5358  C CG  . ASP B 332 ? 0.5065 0.4118 0.7806 0.0769  0.0528  0.0216  332 ASP B CG  
5359  O OD1 . ASP B 332 ? 0.5123 0.4568 0.8087 0.0642  0.0768  0.0074  332 ASP B OD1 
5360  O OD2 . ASP B 332 ? 0.5374 0.4209 0.8267 0.1016  0.0306  0.0169  332 ASP B OD2 
5361  N N   . LEU B 333 ? 0.3452 0.2250 0.5200 0.0095  0.0672  0.0646  333 LEU B N   
5362  C CA  . LEU B 333 ? 0.3584 0.2182 0.5080 -0.0015 0.0629  0.0730  333 LEU B CA  
5363  C C   . LEU B 333 ? 0.3999 0.2522 0.5362 0.0138  0.0408  0.0781  333 LEU B C   
5364  O O   . LEU B 333 ? 0.4022 0.2936 0.5744 0.0214  0.0259  0.0725  333 LEU B O   
5365  C CB  . LEU B 333 ? 0.3137 0.2055 0.4848 -0.0218 0.0646  0.0711  333 LEU B CB  
5366  C CG  . LEU B 333 ? 0.2883 0.1848 0.4671 -0.0349 0.0753  0.0658  333 LEU B CG  
5367  C CD1 . LEU B 333 ? 0.2509 0.1687 0.4441 -0.0521 0.0677  0.0665  333 LEU B CD1 
5368  C CD2 . LEU B 333 ? 0.3501 0.2093 0.5091 -0.0371 0.0838  0.0590  333 LEU B CD2 
5369  N N   . ILE B 334 ? 0.4110 0.2088 0.4935 0.0174  0.0388  0.0872  334 ILE B N   
5370  C CA  . ILE B 334 ? 0.4557 0.2336 0.5061 0.0326  0.0120  0.0925  334 ILE B CA  
5371  C C   . ILE B 334 ? 0.4741 0.2648 0.5158 0.0153  0.0139  0.0897  334 ILE B C   
5372  O O   . ILE B 334 ? 0.4955 0.2583 0.5061 -0.0044 0.0370  0.0907  334 ILE B O   
5373  C CB  . ILE B 334 ? 0.5417 0.2405 0.5172 0.0431  0.0085  0.1070  334 ILE B CB  
5374  C CG1 . ILE B 334 ? 0.6431 0.3245 0.6345 0.0559  0.0127  0.1080  334 ILE B CG1 
5375  C CG2 . ILE B 334 ? 0.6046 0.2762 0.5392 0.0660  -0.0318 0.1121  334 ILE B CG2 
5376  C CD1 . ILE B 334 ? 0.6140 0.3405 0.6687 0.0799  -0.0128 0.0950  334 ILE B CD1 
5377  N N   . LEU B 335 ? 0.4445 0.2771 0.5209 0.0227  -0.0100 0.0820  335 LEU B N   
5378  C CA  . LEU B 335 ? 0.4369 0.2952 0.5272 0.0050  -0.0086 0.0747  335 LEU B CA  
5379  C C   . LEU B 335 ? 0.5143 0.3386 0.5456 0.0110  -0.0263 0.0736  335 LEU B C   
5380  O O   . LEU B 335 ? 0.6052 0.3775 0.5730 0.0289  -0.0420 0.0824  335 LEU B O   
5381  C CB  . LEU B 335 ? 0.3302 0.2554 0.5003 0.0032  -0.0182 0.0651  335 LEU B CB  
5382  C CG  . LEU B 335 ? 0.2876 0.2403 0.4993 -0.0064 0.0024  0.0666  335 LEU B CG  
5383  C CD1 . LEU B 335 ? 0.2467 0.2543 0.5252 -0.0132 -0.0006 0.0598  335 LEU B CD1 
5384  C CD2 . LEU B 335 ? 0.2751 0.2081 0.4687 -0.0271 0.0255  0.0705  335 LEU B CD2 
5385  N N   . ASP B 336 ? 0.5738 0.4237 0.6233 -0.0043 -0.0253 0.0622  336 ASP B N   
5386  C CA  . ASP B 336 ? 0.6779 0.4969 0.6666 -0.0056 -0.0336 0.0557  336 ASP B CA  
5387  C C   . ASP B 336 ? 0.7522 0.5351 0.6852 0.0245  -0.0725 0.0605  336 ASP B C   
5388  O O   . ASP B 336 ? 0.7321 0.5504 0.7191 0.0462  -0.1057 0.0543  336 ASP B O   
5389  C CB  . ASP B 336 ? 0.6776 0.5508 0.7275 -0.0181 -0.0409 0.0364  336 ASP B CB  
5390  C CG  . ASP B 336 ? 0.7822 0.6280 0.7722 -0.0246 -0.0424 0.0226  336 ASP B CG  
5391  O OD1 . ASP B 336 ? 0.8160 0.6340 0.7723 -0.0477 -0.0071 0.0173  336 ASP B OD1 
5392  O OD2 . ASP B 336 ? 0.8156 0.6700 0.7983 -0.0074 -0.0781 0.0122  336 ASP B OD2 
5393  N N   . LYS B 337 ? 0.8721 0.5777 0.6960 0.0249  -0.0665 0.0712  337 LYS B N   
5394  C CA  . LYS B 337 ? 1.0168 0.6661 0.7591 0.0532  -0.1094 0.0778  337 LYS B CA  
5395  C C   . LYS B 337 ? 1.0770 0.7178 0.8434 0.0842  -0.1421 0.0877  337 LYS B C   
5396  O O   . LYS B 337 ? 1.1667 0.7769 0.8994 0.1151  -0.1941 0.0865  337 LYS B O   
5397  C CB  . LYS B 337 ? 1.0031 0.6872 0.7642 0.0637  -0.1472 0.0557  337 LYS B CB  
5398  C CG  . LYS B 337 ? 1.0610 0.7128 0.7426 0.0428  -0.1273 0.0465  337 LYS B CG  
5399  C CD  . LYS B 337 ? 1.0507 0.7343 0.7490 0.0565  -0.1703 0.0212  337 LYS B CD  
5400  C CE  . LYS B 337 ? 1.0949 0.7617 0.7344 0.0307  -0.1417 0.0048  337 LYS B CE  
5401  N NZ  . LYS B 337 ? 1.1885 0.7709 0.7081 0.0091  -0.0932 0.0224  337 LYS B NZ  
5402  N N   . ASN B 338 ? 1.0393 0.7048 0.8647 0.0771  -0.1147 0.0935  338 ASN B N   
5403  C CA  . ASN B 338 ? 1.0491 0.7207 0.9202 0.1028  -0.1375 0.0954  338 ASN B CA  
5404  C C   . ASN B 338 ? 1.0212 0.7513 0.9795 0.1283  -0.1824 0.0734  338 ASN B C   
5405  O O   . ASN B 338 ? 1.0405 0.7599 1.0230 0.1576  -0.2169 0.0689  338 ASN B O   
5406  C CB  . ASN B 338 ? 1.1951 0.7689 0.9665 0.1223  -0.1576 0.1163  338 ASN B CB  
5407  C CG  . ASN B 338 ? 1.2885 0.7948 0.9732 0.0956  -0.1091 0.1370  338 ASN B CG  
5408  O OD1 . ASN B 338 ? 1.2565 0.7962 0.9742 0.0653  -0.0615 0.1318  338 ASN B OD1 
5409  N ND2 . ASN B 338 ? 1.4181 0.8240 0.9935 0.1064  -0.1221 0.1593  338 ASN B ND2 
5410  N N   . ASP B 339 ? 0.9605 0.7521 0.9756 0.1171  -0.1822 0.0562  339 ASP B N   
5411  C CA  . ASP B 339 ? 0.9265 0.7789 1.0391 0.1363  -0.2180 0.0307  339 ASP B CA  
5412  C C   . ASP B 339 ? 0.8430 0.7620 1.0643 0.1282  -0.1909 0.0209  339 ASP B C   
5413  O O   . ASP B 339 ? 0.8720 0.8382 1.1858 0.1444  -0.2122 -0.0028 339 ASP B O   
5414  C CB  . ASP B 339 ? 0.9142 0.8034 1.0493 0.1256  -0.2262 0.0151  339 ASP B CB  
5415  C CG  . ASP B 339 ? 1.0401 0.8665 1.0688 0.1379  -0.2597 0.0166  339 ASP B CG  
5416  O OD1 . ASP B 339 ? 1.1187 0.9047 1.1134 0.1715  -0.3125 0.0121  339 ASP B OD1 
5417  O OD2 . ASP B 339 ? 1.0822 0.8951 1.0575 0.1140  -0.2340 0.0204  339 ASP B OD2 
5418  N N   . ALA B 340 ? 0.7207 0.6432 0.9320 0.1015  -0.1424 0.0356  340 ALA B N   
5419  C CA  . ALA B 340 ? 0.5776 0.5568 0.8708 0.0881  -0.1116 0.0280  340 ALA B CA  
5420  C C   . ALA B 340 ? 0.5013 0.4537 0.7581 0.0769  -0.0774 0.0433  340 ALA B C   
5421  O O   . ALA B 340 ? 0.5518 0.4479 0.7312 0.0736  -0.0714 0.0596  340 ALA B O   
5422  C CB  . ALA B 340 ? 0.4988 0.5283 0.8395 0.0617  -0.0925 0.0234  340 ALA B CB  
5423  N N   . VAL B 341 ? 0.4246 0.4160 0.7386 0.0704  -0.0533 0.0348  341 VAL B N   
5424  C CA  . VAL B 341 ? 0.4039 0.3774 0.6946 0.0618  -0.0236 0.0426  341 VAL B CA  
5425  C C   . VAL B 341 ? 0.3418 0.3590 0.6688 0.0369  0.0100  0.0389  341 VAL B C   
5426  O O   . VAL B 341 ? 0.3325 0.3961 0.7218 0.0343  0.0154  0.0245  341 VAL B O   
5427  C CB  . VAL B 341 ? 0.4140 0.3768 0.7256 0.0870  -0.0341 0.0316  341 VAL B CB  
5428  C CG1 . VAL B 341 ? 0.3537 0.3188 0.6659 0.0763  -0.0001 0.0301  341 VAL B CG1 
5429  C CG2 . VAL B 341 ? 0.5014 0.3966 0.7504 0.1093  -0.0664 0.0440  341 VAL B CG2 
5430  N N   . TRP B 342 ? 0.3117 0.3103 0.6000 0.0179  0.0319  0.0505  342 TRP B N   
5431  C CA  . TRP B 342 ? 0.2592 0.2845 0.5643 -0.0021 0.0582  0.0485  342 TRP B CA  
5432  C C   . TRP B 342 ? 0.3237 0.3353 0.6138 0.0032  0.0751  0.0423  342 TRP B C   
5433  O O   . TRP B 342 ? 0.3556 0.3330 0.6051 -0.0009 0.0790  0.0491  342 TRP B O   
5434  C CB  . TRP B 342 ? 0.3014 0.3160 0.5807 -0.0257 0.0621  0.0614  342 TRP B CB  
5435  C CG  . TRP B 342 ? 0.2873 0.3239 0.5796 -0.0465 0.0789  0.0638  342 TRP B CG  
5436  C CD1 . TRP B 342 ? 0.3070 0.3650 0.6145 -0.0507 0.1021  0.0559  342 TRP B CD1 
5437  C CD2 . TRP B 342 ? 0.3040 0.3377 0.5921 -0.0673 0.0750  0.0748  342 TRP B CD2 
5438  N NE1 . TRP B 342 ? 0.3059 0.3669 0.6045 -0.0750 0.1154  0.0655  342 TRP B NE1 
5439  C CE2 . TRP B 342 ? 0.3289 0.3730 0.6132 -0.0826 0.0934  0.0773  342 TRP B CE2 
5440  C CE3 . TRP B 342 ? 0.3094 0.3285 0.5825 -0.0706 0.0549  0.0765  342 TRP B CE3 
5441  C CZ2 . TRP B 342 ? 0.3423 0.3737 0.5955 -0.0978 0.0840  0.0843  342 TRP B CZ2 
5442  C CZ3 . TRP B 342 ? 0.2998 0.3159 0.5528 -0.0816 0.0456  0.0767  342 TRP B CZ3 
5443  C CH2 . TRP B 342 ? 0.3246 0.3432 0.5679 -0.0952 0.0579  0.0832  342 TRP B CH2 
5444  N N   . ARG B 343 ? 0.3439 0.3839 0.6756 0.0123  0.0854  0.0243  343 ARG B N   
5445  C CA  . ARG B 343 ? 0.3777 0.4089 0.7024 0.0187  0.1014  0.0124  343 ARG B CA  
5446  C C   . ARG B 343 ? 0.4201 0.4512 0.7097 -0.0052 0.1271  0.0157  343 ARG B C   
5447  O O   . ARG B 343 ? 0.4661 0.5200 0.7621 -0.0237 0.1416  0.0180  343 ARG B O   
5448  C CB  . ARG B 343 ? 0.4072 0.4733 0.7977 0.0344  0.1069  -0.0150 343 ARG B CB  
5449  C CG  . ARG B 343 ? 0.4607 0.5156 0.8839 0.0650  0.0696  -0.0210 343 ARG B CG  
5450  C CD  . ARG B 343 ? 0.7618 0.8559 1.2737 0.0837  0.0675  -0.0564 343 ARG B CD  
5451  N NE  . ARG B 343 ? 0.7562 0.9078 1.3388 0.0717  0.0841  -0.0765 343 ARG B NE  
5452  C CZ  . ARG B 343 ? 0.7658 0.9575 1.3845 0.0523  0.1297  -0.0986 343 ARG B CZ  
5453  N NH1 . ARG B 343 ? 0.8409 1.0230 1.4263 0.0453  0.1586  -0.1047 343 ARG B NH1 
5454  N NH2 . ARG B 343 ? 0.7091 0.9457 1.3906 0.0379  0.1482  -0.1161 343 ARG B NH2 
5455  N N   . ILE B 344 ? 0.4159 0.4161 0.6661 -0.0049 0.1303  0.0158  344 ILE B N   
5456  C CA  . ILE B 344 ? 0.3940 0.3849 0.6012 -0.0238 0.1450  0.0168  344 ILE B CA  
5457  C C   . ILE B 344 ? 0.4463 0.4427 0.6473 -0.0198 0.1665  -0.0054 344 ILE B C   
5458  O O   . ILE B 344 ? 0.5035 0.4859 0.7134 -0.0030 0.1618  -0.0175 344 ILE B O   
5459  C CB  . ILE B 344 ? 0.3912 0.3431 0.5630 -0.0279 0.1282  0.0271  344 ILE B CB  
5460  C CG1 . ILE B 344 ? 0.3642 0.3121 0.5458 -0.0326 0.1107  0.0435  344 ILE B CG1 
5461  C CG2 . ILE B 344 ? 0.3973 0.3336 0.5228 -0.0440 0.1312  0.0271  344 ILE B CG2 
5462  C CD1 . ILE B 344 ? 0.3452 0.2590 0.5103 -0.0374 0.0986  0.0466  344 ILE B CD1 
5463  N N   . SER B 345 ? 0.4449 0.4573 0.6267 -0.0373 0.1923  -0.0112 345 SER B N   
5464  C CA  . SER B 345 ? 0.4917 0.5120 0.6615 -0.0373 0.2200  -0.0372 345 SER B CA  
5465  C C   . SER B 345 ? 0.5029 0.4861 0.6160 -0.0349 0.2111  -0.0428 345 SER B C   
5466  O O   . SER B 345 ? 0.5033 0.4538 0.5681 -0.0440 0.1911  -0.0255 345 SER B O   
5467  C CB  . SER B 345 ? 0.5708 0.6076 0.7172 -0.0629 0.2566  -0.0397 345 SER B CB  
5468  O OG  . SER B 345 ? 0.6796 0.7055 0.7739 -0.0699 0.2827  -0.0600 345 SER B OG  
5469  N N   . SER B 346 ? 0.5410 0.5306 0.6686 -0.0217 0.2234  -0.0716 346 SER B N   
5470  C CA  . SER B 346 ? 0.5986 0.5566 0.6821 -0.0172 0.2142  -0.0845 346 SER B CA  
5471  C C   . SER B 346 ? 0.6935 0.6324 0.6891 -0.0378 0.2270  -0.0855 346 SER B C   
5472  O O   . SER B 346 ? 0.7417 0.6482 0.6877 -0.0352 0.2113  -0.0951 346 SER B O   
5473  C CB  . SER B 346 ? 0.5174 0.4882 0.6446 0.0024  0.2242  -0.1184 346 SER B CB  
5474  O OG  . SER B 346 ? 0.5589 0.5582 0.6803 -0.0060 0.2614  -0.1453 346 SER B OG  
5475  N N   . GLU B 347 ? 0.7114 0.6645 0.6845 -0.0587 0.2543  -0.0759 347 GLU B N   
5476  C CA  . GLU B 347 ? 0.7760 0.6960 0.6466 -0.0813 0.2669  -0.0697 347 GLU B CA  
5477  C C   . GLU B 347 ? 0.7445 0.6265 0.5735 -0.0911 0.2312  -0.0340 347 GLU B C   
5478  O O   . GLU B 347 ? 0.8284 0.6646 0.5632 -0.1059 0.2227  -0.0221 347 GLU B O   
5479  C CB  . GLU B 347 ? 0.8512 0.7965 0.7147 -0.1042 0.3201  -0.0756 347 GLU B CB  
5480  C CG  . GLU B 347 ? 0.9223 0.9147 0.8519 -0.0955 0.3576  -0.1165 347 GLU B CG  
5481  C CD  . GLU B 347 ? 1.0773 1.0926 1.0014 -0.1234 0.4169  -0.1277 347 GLU B CD  
5482  O OE1 . GLU B 347 ? 1.1940 1.1724 1.0296 -0.1513 0.4299  -0.1009 347 GLU B OE1 
5483  O OE2 . GLU B 347 ? 1.0819 1.1463 1.0924 -0.1164 0.4417  -0.1614 347 GLU B OE2 
5484  N N   . ASN B 348 ? 0.6569 0.5559 0.5556 -0.0831 0.2100  -0.0179 348 ASN B N   
5485  C CA  . ASN B 348 ? 0.6574 0.5277 0.5425 -0.0886 0.1730  0.0089  348 ASN B CA  
5486  C C   . ASN B 348 ? 0.6648 0.5125 0.5670 -0.0712 0.1348  0.0005  348 ASN B C   
5487  O O   . ASN B 348 ? 0.7141 0.5227 0.5765 -0.0748 0.1023  0.0065  348 ASN B O   
5488  C CB  . ASN B 348 ? 0.6453 0.5466 0.5929 -0.0935 0.1760  0.0273  348 ASN B CB  
5489  C CG  . ASN B 348 ? 0.6830 0.5591 0.6248 -0.1009 0.1409  0.0510  348 ASN B CG  
5490  O OD1 . ASN B 348 ? 0.6909 0.5478 0.6441 -0.0904 0.1097  0.0476  348 ASN B OD1 
5491  N ND2 . ASN B 348 ? 0.7168 0.5916 0.6468 -0.1205 0.1476  0.0720  348 ASN B ND2 
5492  N N   . PHE B 349 ? 0.6191 0.4865 0.5829 -0.0529 0.1375  -0.0149 349 PHE B N   
5493  C CA  . PHE B 349 ? 0.6185 0.4629 0.6075 -0.0418 0.1089  -0.0220 349 PHE B CA  
5494  C C   . PHE B 349 ? 0.7213 0.5424 0.6857 -0.0319 0.0997  -0.0498 349 PHE B C   
5495  O O   . PHE B 349 ? 0.7460 0.5447 0.7336 -0.0252 0.0752  -0.0607 349 PHE B O   
5496  C CB  . PHE B 349 ? 0.4866 0.3470 0.5443 -0.0299 0.1135  -0.0197 349 PHE B CB  
5497  C CG  . PHE B 349 ? 0.4735 0.3537 0.5623 -0.0144 0.1344  -0.0349 349 PHE B CG  
5498  C CD1 . PHE B 349 ? 0.4811 0.3490 0.5766 -0.0018 0.1360  -0.0596 349 PHE B CD1 
5499  C CD2 . PHE B 349 ? 0.4555 0.3644 0.5792 -0.0098 0.1463  -0.0268 349 PHE B CD2 
5500  C CE1 . PHE B 349 ? 0.4836 0.3675 0.6178 0.0140  0.1509  -0.0747 349 PHE B CE1 
5501  C CE2 . PHE B 349 ? 0.4617 0.3852 0.6247 0.0077  0.1569  -0.0432 349 PHE B CE2 
5502  C CZ  . PHE B 349 ? 0.4609 0.3709 0.6292 0.0193  0.1595  -0.0661 349 PHE B CZ  
5503  N N   . MET B 350 ? 0.6480 0.4393 0.6174 0.0125  0.0581  -0.1038 350 MET B N   
5504  C CA  . MET B 350 ? 0.6856 0.4602 0.6275 -0.0048 0.0643  -0.1285 350 MET B CA  
5505  C C   . MET B 350 ? 0.6827 0.4879 0.5941 -0.0148 0.0604  -0.1346 350 MET B C   
5506  O O   . MET B 350 ? 0.7045 0.5261 0.6134 -0.0049 0.0679  -0.1315 350 MET B O   
5507  C CB  . MET B 350 ? 0.7490 0.4860 0.6960 0.0029  0.0853  -0.1488 350 MET B CB  
5508  C CG  . MET B 350 ? 0.7716 0.4700 0.7454 0.0113  0.0872  -0.1427 350 MET B CG  
5509  S SD  . MET B 350 ? 0.7634 0.4394 0.7271 -0.0119 0.0752  -0.1409 350 MET B SD  
5510  C CE  . MET B 350 ? 0.6312 0.2909 0.5606 -0.0364 0.0839  -0.1773 350 MET B CE  
5511  N N   . VAL B 351 ? 0.6741 0.4878 0.5638 -0.0351 0.0473  -0.1412 351 VAL B N   
5512  C CA  . VAL B 351 ? 0.6566 0.4990 0.5150 -0.0455 0.0375  -0.1436 351 VAL B CA  
5513  C C   . VAL B 351 ? 0.7234 0.5476 0.5436 -0.0632 0.0430  -0.1723 351 VAL B C   
5514  O O   . VAL B 351 ? 0.7755 0.5728 0.5970 -0.0746 0.0456  -0.1886 351 VAL B O   
5515  C CB  . VAL B 351 ? 0.6662 0.5402 0.5324 -0.0547 0.0137  -0.1281 351 VAL B CB  
5516  C CG1 . VAL B 351 ? 0.6881 0.5908 0.5236 -0.0631 -0.0003 -0.1273 351 VAL B CG1 
5517  C CG2 . VAL B 351 ? 0.5787 0.4663 0.4785 -0.0394 0.0102  -0.1030 351 VAL B CG2 
5518  N N   . GLN B 352 ? 0.7537 0.5892 0.5364 -0.0670 0.0457  -0.1790 352 GLN B N   
5519  C CA  . GLN B 352 ? 0.8239 0.6412 0.5606 -0.0857 0.0510  -0.2080 352 GLN B CA  
5520  C C   . GLN B 352 ? 0.8978 0.7402 0.6068 -0.1067 0.0227  -0.2079 352 GLN B C   
5521  O O   . GLN B 352 ? 0.9625 0.8193 0.6286 -0.1136 0.0160  -0.2084 352 GLN B O   
5522  C CB  . GLN B 352 ? 0.8249 0.6347 0.5283 -0.0805 0.0738  -0.2188 352 GLN B CB  
5523  C CG  . GLN B 352 ? 0.9045 0.6760 0.5760 -0.0925 0.0948  -0.2554 352 GLN B CG  
5524  C CD  . GLN B 352 ? 0.9724 0.7089 0.6879 -0.0791 0.1149  -0.2650 352 GLN B CD  
5525  O OE1 . GLN B 352 ? 1.0093 0.7211 0.7233 -0.0864 0.1191  -0.2820 352 GLN B OE1 
5526  N NE2 . GLN B 352 ? 0.9927 0.7357 0.7571 -0.0555 0.1206  -0.2437 352 GLN B NE2 
5527  N N   . ALA B 353 ? 0.9185 0.7676 0.6546 -0.1164 0.0057  -0.2050 353 ALA B N   
5528  C CA  . ALA B 353 ? 0.9669 0.8430 0.6901 -0.1372 -0.0230 -0.2070 353 ALA B CA  
5529  C C   . ALA B 353 ? 1.0629 0.9353 0.7254 -0.1569 -0.0295 -0.2295 353 ALA B C   
5530  O O   . ALA B 353 ? 1.1060 1.0093 0.7441 -0.1626 -0.0526 -0.2191 353 ALA B O   
5531  C CB  . ALA B 353 ? 0.9561 0.8243 0.7123 -0.1512 -0.0289 -0.2148 353 ALA B CB  
5532  N N   . GLN B 354 ? 1.0830 0.9179 0.7240 -0.1636 -0.0096 -0.2562 354 GLN B N   
5533  C CA  . GLN B 354 ? 1.1110 0.9457 0.7061 -0.1757 -0.0163 -0.2697 354 GLN B CA  
5534  C C   . GLN B 354 ? 1.0963 0.8961 0.6675 -0.1679 0.0164  -0.2871 354 GLN B C   
5535  O O   . GLN B 354 ? 1.0946 0.8713 0.6924 -0.1518 0.0428  -0.2886 354 GLN B O   
5536  C CB  . GLN B 354 ? 1.1777 1.0122 0.7798 -0.1965 -0.0346 -0.2846 354 GLN B CB  
5537  C CG  . GLN B 354 ? 1.2007 1.0785 0.8254 -0.2069 -0.0704 -0.2697 354 GLN B CG  
5538  C CD  . GLN B 354 ? 1.2899 1.1651 0.9315 -0.2273 -0.0836 -0.2861 354 GLN B CD  
5539  O OE1 . GLN B 354 ? 1.3424 1.1795 0.9893 -0.2323 -0.0640 -0.3051 354 GLN B OE1 
5540  N NE2 . GLN B 354 ? 1.3052 1.2212 0.9592 -0.2380 -0.1168 -0.2779 354 GLN B NE2 
5541  N N   . ASP B 355 ? 1.0821 0.8810 0.6047 -0.1780 0.0138  -0.2983 355 ASP B N   
5542  C CA  . ASP B 355 ? 1.1052 0.8707 0.6047 -0.1761 0.0437  -0.3206 355 ASP B CA  
5543  C C   . ASP B 355 ? 1.1009 0.8308 0.6378 -0.1740 0.0615  -0.3382 355 ASP B C   
5544  O O   . ASP B 355 ? 1.1510 0.8715 0.6914 -0.1901 0.0489  -0.3514 355 ASP B O   
5545  C CB  . ASP B 355 ? 1.1932 0.9605 0.6361 -0.1943 0.0316  -0.3344 355 ASP B CB  
5546  C CG  . ASP B 355 ? 1.2891 1.0287 0.6976 -0.1914 0.0644  -0.3534 355 ASP B CG  
5547  O OD1 . ASP B 355 ? 1.2893 1.0015 0.7274 -0.1789 0.0952  -0.3646 355 ASP B OD1 
5548  O OD2 . ASP B 355 ? 1.3592 1.1048 0.7125 -0.2013 0.0591  -0.3566 355 ASP B OD2 
5549  N N   . GLY B 356 ? 1.0615 0.7727 0.6301 -0.1533 0.0895  -0.3360 356 GLY B N   
5550  C CA  . GLY B 356 ? 1.0568 0.7325 0.6649 -0.1459 0.1068  -0.3470 356 GLY B CA  
5551  C C   . GLY B 356 ? 1.0182 0.6916 0.6684 -0.1486 0.0911  -0.3364 356 GLY B C   
5552  O O   . GLY B 356 ? 1.0503 0.6923 0.7240 -0.1494 0.0991  -0.3459 356 GLY B O   
5553  N N   . VAL B 357 ? 0.9662 0.6712 0.6272 -0.1496 0.0706  -0.3158 357 VAL B N   
5554  C CA  . VAL B 357 ? 0.9258 0.6294 0.6290 -0.1517 0.0594  -0.3039 357 VAL B CA  
5555  C C   . VAL B 357 ? 0.8742 0.5890 0.6062 -0.1323 0.0632  -0.2812 357 VAL B C   
5556  O O   . VAL B 357 ? 0.8537 0.6007 0.5716 -0.1305 0.0529  -0.2687 357 VAL B O   
5557  C CB  . VAL B 357 ? 0.9169 0.6500 0.6152 -0.1755 0.0282  -0.3019 357 VAL B CB  
5558  C CG1 . VAL B 357 ? 0.8556 0.5896 0.6004 -0.1782 0.0206  -0.2882 357 VAL B CG1 
5559  C CG2 . VAL B 357 ? 0.9280 0.6478 0.6011 -0.1949 0.0237  -0.3253 357 VAL B CG2 
5560  N N   . SER B 358 ? 0.8447 0.5321 0.6167 -0.1181 0.0760  -0.2741 358 SER B N   
5561  C CA  . SER B 358 ? 0.7723 0.4695 0.5761 -0.0962 0.0790  -0.2497 358 SER B CA  
5562  C C   . SER B 358 ? 0.7412 0.4427 0.5810 -0.0973 0.0647  -0.2277 358 SER B C   
5563  O O   . SER B 358 ? 0.7769 0.4403 0.6334 -0.1006 0.0721  -0.2328 358 SER B O   
5564  C CB  . SER B 358 ? 0.7856 0.4530 0.6095 -0.0722 0.1052  -0.2532 358 SER B CB  
5565  O OG  . SER B 358 ? 0.7711 0.4541 0.6312 -0.0492 0.1036  -0.2253 358 SER B OG  
5566  N N   . CYS B 359 ? 0.7023 0.4468 0.5536 -0.0935 0.0468  -0.2026 359 CYS B N   
5567  C CA  . CYS B 359 ? 0.6312 0.3866 0.5098 -0.0994 0.0337  -0.1844 359 CYS B CA  
5568  C C   . CYS B 359 ? 0.5729 0.3344 0.4805 -0.0774 0.0349  -0.1561 359 CYS B C   
5569  O O   . CYS B 359 ? 0.5498 0.3303 0.4590 -0.0596 0.0363  -0.1447 359 CYS B O   
5570  C CB  . CYS B 359 ? 0.5849 0.3867 0.4569 -0.1146 0.0113  -0.1802 359 CYS B CB  
5571  S SG  . CYS B 359 ? 0.8051 0.6059 0.6441 -0.1454 0.0015  -0.2117 359 CYS B SG  
5572  N N   . LEU B 360 ? 0.6000 0.3460 0.5281 -0.0810 0.0337  -0.1445 360 LEU B N   
5573  C CA  . LEU B 360 ? 0.5608 0.3142 0.5099 -0.0642 0.0316  -0.1172 360 LEU B CA  
5574  C C   . LEU B 360 ? 0.5436 0.3462 0.4973 -0.0651 0.0174  -0.1024 360 LEU B C   
5575  O O   . LEU B 360 ? 0.5896 0.4097 0.5495 -0.0817 0.0092  -0.1018 360 LEU B O   
5576  C CB  . LEU B 360 ? 0.5674 0.2860 0.5286 -0.0707 0.0355  -0.1086 360 LEU B CB  
5577  C CG  . LEU B 360 ? 0.5135 0.2345 0.4877 -0.0580 0.0323  -0.0808 360 LEU B CG  
5578  C CD1 . LEU B 360 ? 0.4995 0.2145 0.4806 -0.0317 0.0348  -0.0716 360 LEU B CD1 
5579  C CD2 . LEU B 360 ? 0.5376 0.2174 0.5141 -0.0688 0.0378  -0.0742 360 LEU B CD2 
5580  N N   . GLY B 361 ? 0.4812 0.3048 0.4370 -0.0468 0.0159  -0.0903 361 GLY B N   
5581  C CA  . GLY B 361 ? 0.4531 0.3196 0.4111 -0.0455 0.0041  -0.0789 361 GLY B CA  
5582  C C   . GLY B 361 ? 0.4240 0.3046 0.4008 -0.0437 -0.0009 -0.0598 361 GLY B C   
5583  O O   . GLY B 361 ? 0.4250 0.3245 0.4079 -0.0313 -0.0039 -0.0459 361 GLY B O   
5584  N N   . PHE B 362 ? 0.4746 0.3433 0.4590 -0.0579 0.0004  -0.0603 362 PHE B N   
5585  C CA  . PHE B 362 ? 0.4606 0.3438 0.4595 -0.0606 -0.0010 -0.0455 362 PHE B CA  
5586  C C   . PHE B 362 ? 0.4519 0.3569 0.4633 -0.0815 -0.0054 -0.0538 362 PHE B C   
5587  O O   . PHE B 362 ? 0.5129 0.4028 0.5214 -0.0977 -0.0040 -0.0685 362 PHE B O   
5588  C CB  . PHE B 362 ? 0.4651 0.3118 0.4623 -0.0584 0.0076  -0.0345 362 PHE B CB  
5589  C CG  . PHE B 362 ? 0.4867 0.3172 0.4792 -0.0374 0.0083  -0.0247 362 PHE B CG  
5590  C CD1 . PHE B 362 ? 0.4946 0.3033 0.4837 -0.0285 0.0122  -0.0341 362 PHE B CD1 
5591  C CD2 . PHE B 362 ? 0.4734 0.3111 0.4673 -0.0270 0.0055  -0.0075 362 PHE B CD2 
5592  C CE1 . PHE B 362 ? 0.4863 0.2850 0.4804 -0.0087 0.0127  -0.0255 362 PHE B CE1 
5593  C CE2 . PHE B 362 ? 0.4813 0.3081 0.4758 -0.0089 0.0033  0.0011  362 PHE B CE2 
5594  C CZ  . PHE B 362 ? 0.4923 0.3017 0.4904 0.0008  0.0066  -0.0073 362 PHE B CZ  
5595  N N   . VAL B 363 ? 0.3862 0.3271 0.4153 -0.0814 -0.0102 -0.0457 363 VAL B N   
5596  C CA  . VAL B 363 ? 0.3901 0.3606 0.4410 -0.0995 -0.0157 -0.0537 363 VAL B CA  
5597  C C   . VAL B 363 ? 0.3657 0.3442 0.4379 -0.1063 -0.0054 -0.0449 363 VAL B C   
5598  O O   . VAL B 363 ? 0.3484 0.3222 0.4167 -0.0939 0.0013  -0.0315 363 VAL B O   
5599  C CB  . VAL B 363 ? 0.3889 0.4016 0.4477 -0.0939 -0.0324 -0.0549 363 VAL B CB  
5600  C CG1 . VAL B 363 ? 0.3880 0.3880 0.4162 -0.0881 -0.0387 -0.0629 363 VAL B CG1 
5601  C CG2 . VAL B 363 ? 0.3900 0.4212 0.4584 -0.0762 -0.0323 -0.0393 363 VAL B CG2 
5602  N N   . ASP B 364 ? 0.4025 0.3934 0.4966 -0.1280 -0.0032 -0.0540 364 ASP B N   
5603  C CA  . ASP B 364 ? 0.4475 0.4461 0.5637 -0.1398 0.0115  -0.0488 364 ASP B CA  
5604  C C   . ASP B 364 ? 0.4236 0.4703 0.5710 -0.1312 0.0084  -0.0440 364 ASP B C   
5605  O O   . ASP B 364 ? 0.4159 0.5033 0.5906 -0.1329 -0.0065 -0.0509 364 ASP B O   
5606  C CB  . ASP B 364 ? 0.4976 0.4969 0.6330 -0.1682 0.0157  -0.0623 364 ASP B CB  
5607  C CG  . ASP B 364 ? 0.5092 0.5037 0.6603 -0.1844 0.0377  -0.0569 364 ASP B CG  
5608  O OD1 . ASP B 364 ? 0.4993 0.4983 0.6493 -0.1745 0.0488  -0.0447 364 ASP B OD1 
5609  O OD2 . ASP B 364 ? 0.5512 0.5381 0.7156 -0.2096 0.0451  -0.0664 364 ASP B OD2 
5610  N N   . GLY B 365 ? 0.3911 0.4318 0.5342 -0.1217 0.0216  -0.0324 365 GLY B N   
5611  C CA  . GLY B 365 ? 0.3352 0.4161 0.5095 -0.1129 0.0229  -0.0295 365 GLY B CA  
5612  C C   . GLY B 365 ? 0.3563 0.4640 0.5709 -0.1305 0.0377  -0.0354 365 GLY B C   
5613  O O   . GLY B 365 ? 0.3658 0.5102 0.6160 -0.1236 0.0410  -0.0354 365 GLY B O   
5614  N N   . GLY B 366 ? 0.3891 0.4789 0.6022 -0.1535 0.0477  -0.0412 366 GLY B N   
5615  C CA  . GLY B 366 ? 0.4330 0.5475 0.6860 -0.1740 0.0653  -0.0476 366 GLY B CA  
5616  C C   . GLY B 366 ? 0.4903 0.5795 0.7228 -0.1768 0.0934  -0.0386 366 GLY B C   
5617  O O   . GLY B 366 ? 0.5077 0.5566 0.6922 -0.1652 0.0954  -0.0274 366 GLY B O   
5618  N N   . VAL B 367 ? 0.5338 0.6485 0.8033 -0.1929 0.1151  -0.0441 367 VAL B N   
5619  C CA  . VAL B 367 ? 0.5902 0.6788 0.8359 -0.2027 0.1465  -0.0376 367 VAL B CA  
5620  C C   . VAL B 367 ? 0.6214 0.7286 0.8735 -0.1857 0.1583  -0.0360 367 VAL B C   
5621  O O   . VAL B 367 ? 0.6919 0.7724 0.9099 -0.1897 0.1812  -0.0304 367 VAL B O   
5622  C CB  . VAL B 367 ? 0.6167 0.7150 0.8839 -0.2223 0.1619  -0.0426 367 VAL B CB  
5623  C CG1 . VAL B 367 ? 0.6169 0.6859 0.8697 -0.2398 0.1529  -0.0438 367 VAL B CG1 
5624  C CG2 . VAL B 367 ? 0.5999 0.7634 0.9360 -0.2180 0.1560  -0.0538 367 VAL B CG2 
5625  N N   . HIS B 368 ? 0.5886 0.7394 0.8815 -0.1662 0.1417  -0.0408 368 HIS B N   
5626  C CA  . HIS B 368 ? 0.6193 0.7860 0.9226 -0.1475 0.1513  -0.0408 368 HIS B CA  
5627  C C   . HIS B 368 ? 0.6156 0.7734 0.8959 -0.1208 0.1260  -0.0334 368 HIS B C   
5628  O O   . HIS B 368 ? 0.6009 0.7869 0.9120 -0.1022 0.1210  -0.0351 368 HIS B O   
5629  C CB  . HIS B 368 ? 0.6435 0.8671 1.0184 -0.1442 0.1548  -0.0508 368 HIS B CB  
5630  C CG  . HIS B 368 ? 0.6947 0.9197 1.0770 -0.1611 0.1791  -0.0555 368 HIS B CG  
5631  N ND1 . HIS B 368 ? 0.6924 0.9557 1.1257 -0.1700 0.1738  -0.0622 368 HIS B ND1 
5632  C CD2 . HIS B 368 ? 0.7509 0.9464 1.0978 -0.1699 0.2087  -0.0547 368 HIS B CD2 
5633  C CE1 . HIS B 368 ? 0.7473 1.0036 1.1783 -0.1848 0.2010  -0.0655 368 HIS B CE1 
5634  N NE2 . HIS B 368 ? 0.7838 0.9987 1.1613 -0.1846 0.2226  -0.0611 368 HIS B NE2 
5635  N N   . ALA B 369 ? 0.5916 0.7081 0.8192 -0.1192 0.1123  -0.0249 369 ALA B N   
5636  C CA  . ALA B 369 ? 0.4921 0.5971 0.6953 -0.0972 0.0907  -0.0179 369 ALA B CA  
5637  C C   . ALA B 369 ? 0.5081 0.6014 0.6920 -0.0840 0.1012  -0.0143 369 ALA B C   
5638  O O   . ALA B 369 ? 0.5437 0.6213 0.7099 -0.0936 0.1248  -0.0153 369 ALA B O   
5639  C CB  . ALA B 369 ? 0.4375 0.5019 0.5951 -0.0997 0.0785  -0.0113 369 ALA B CB  
5640  N N   . ARG B 370 ? 0.5146 0.6145 0.7001 -0.0636 0.0844  -0.0109 370 ARG B N   
5641  C CA  . ARG B 370 ? 0.5403 0.6298 0.7114 -0.0511 0.0922  -0.0096 370 ARG B CA  
5642  C C   . ARG B 370 ? 0.5138 0.5580 0.6247 -0.0571 0.0969  -0.0031 370 ARG B C   
5643  O O   . ARG B 370 ? 0.5398 0.5688 0.6287 -0.0615 0.1149  -0.0053 370 ARG B O   
5644  C CB  . ARG B 370 ? 0.5784 0.6797 0.7617 -0.0302 0.0715  -0.0054 370 ARG B CB  
5645  C CG  . ARG B 370 ? 0.6340 0.7149 0.7933 -0.0187 0.0749  -0.0032 370 ARG B CG  
5646  C CD  . ARG B 370 ? 0.7131 0.8037 0.8941 -0.0184 0.0984  -0.0126 370 ARG B CD  
5647  N NE  . ARG B 370 ? 0.7661 0.8326 0.9193 -0.0125 0.1060  -0.0145 370 ARG B NE  
5648  C CZ  . ARG B 370 ? 0.8136 0.8511 0.9220 -0.0243 0.1204  -0.0174 370 ARG B CZ  
5649  N NH1 . ARG B 370 ? 0.8586 0.8851 0.9441 -0.0415 0.1296  -0.0160 370 ARG B NH1 
5650  N NH2 . ARG B 370 ? 0.8035 0.8208 0.8870 -0.0203 0.1249  -0.0213 370 ARG B NH2 
5651  N N   . ALA B 371 ? 0.4590 0.4818 0.5435 -0.0580 0.0809  0.0044  371 ALA B N   
5652  C CA  . ALA B 371 ? 0.4456 0.4273 0.4788 -0.0618 0.0802  0.0131  371 ALA B CA  
5653  C C   . ALA B 371 ? 0.4132 0.3734 0.4322 -0.0724 0.0752  0.0182  371 ALA B C   
5654  O O   . ALA B 371 ? 0.3998 0.3762 0.4455 -0.0753 0.0689  0.0133  371 ALA B O   
5655  C CB  . ALA B 371 ? 0.4070 0.3801 0.4243 -0.0452 0.0632  0.0183  371 ALA B CB  
5656  N N   . GLY B 372 ? 0.4176 0.3393 0.3939 -0.0784 0.0769  0.0280  372 GLY B N   
5657  C CA  . GLY B 372 ? 0.4282 0.3232 0.3920 -0.0862 0.0723  0.0339  372 GLY B CA  
5658  C C   . GLY B 372 ? 0.3974 0.2948 0.3724 -0.0718 0.0519  0.0332  372 GLY B C   
5659  O O   . GLY B 372 ? 0.4494 0.3426 0.4357 -0.0773 0.0488  0.0290  372 GLY B O   
5660  N N   . ILE B 373 ? 0.3926 0.2956 0.3635 -0.0551 0.0398  0.0359  373 ILE B N   
5661  C CA  . ILE B 373 ? 0.3812 0.2894 0.3623 -0.0408 0.0240  0.0347  373 ILE B CA  
5662  C C   . ILE B 373 ? 0.3255 0.2640 0.3253 -0.0287 0.0186  0.0305  373 ILE B C   
5663  O O   . ILE B 373 ? 0.3726 0.3122 0.3642 -0.0242 0.0199  0.0334  373 ILE B O   
5664  C CB  . ILE B 373 ? 0.4134 0.2925 0.3713 -0.0314 0.0135  0.0453  373 ILE B CB  
5665  C CG1 . ILE B 373 ? 0.4721 0.3136 0.4085 -0.0414 0.0174  0.0534  373 ILE B CG1 
5666  C CG2 . ILE B 373 ? 0.3948 0.2819 0.3677 -0.0173 0.0022  0.0418  373 ILE B CG2 
5667  C CD1 . ILE B 373 ? 0.4864 0.2973 0.4000 -0.0316 0.0052  0.0677  373 ILE B CD1 
5668  N N   . ALA B 374 ? 0.3187 0.2781 0.3395 -0.0243 0.0119  0.0241  374 ALA B N   
5669  C CA  . ALA B 374 ? 0.2996 0.2819 0.3340 -0.0121 0.0053  0.0236  374 ALA B CA  
5670  C C   . ALA B 374 ? 0.3085 0.2884 0.3397 -0.0034 -0.0047 0.0233  374 ALA B C   
5671  O O   . ALA B 374 ? 0.3525 0.3388 0.3885 -0.0070 -0.0082 0.0171  374 ALA B O   
5672  C CB  . ALA B 374 ? 0.2756 0.2896 0.3385 -0.0144 0.0069  0.0181  374 ALA B CB  
5673  N N   . LEU B 375 ? 0.3062 0.2772 0.3289 0.0065  -0.0082 0.0286  375 LEU B N   
5674  C CA  . LEU B 375 ? 0.3166 0.2864 0.3389 0.0149  -0.0134 0.0279  375 LEU B CA  
5675  C C   . LEU B 375 ? 0.3120 0.3042 0.3434 0.0195  -0.0161 0.0270  375 LEU B C   
5676  O O   . LEU B 375 ? 0.3395 0.3412 0.3776 0.0233  -0.0159 0.0311  375 LEU B O   
5677  C CB  . LEU B 375 ? 0.3189 0.2764 0.3367 0.0228  -0.0164 0.0341  375 LEU B CB  
5678  C CG  . LEU B 375 ? 0.3470 0.2801 0.3519 0.0196  -0.0175 0.0395  375 LEU B CG  
5679  C CD1 . LEU B 375 ? 0.3334 0.2611 0.3357 0.0268  -0.0252 0.0469  375 LEU B CD1 
5680  C CD2 . LEU B 375 ? 0.3767 0.2911 0.3805 0.0193  -0.0167 0.0366  375 LEU B CD2 
5681  N N   . GLY B 376 ? 0.2953 0.2925 0.3237 0.0184  -0.0185 0.0217  376 GLY B N   
5682  C CA  . GLY B 376 ? 0.2800 0.2969 0.3111 0.0207  -0.0235 0.0231  376 GLY B CA  
5683  C C   . GLY B 376 ? 0.3014 0.3164 0.3222 0.0270  -0.0223 0.0247  376 GLY B C   
5684  O O   . GLY B 376 ? 0.3226 0.3259 0.3431 0.0314  -0.0171 0.0248  376 GLY B O   
5685  N N   . ALA B 377 ? 0.2999 0.3267 0.3125 0.0267  -0.0273 0.0262  377 ALA B N   
5686  C CA  . ALA B 377 ? 0.3073 0.3318 0.3066 0.0308  -0.0230 0.0293  377 ALA B CA  
5687  C C   . ALA B 377 ? 0.3636 0.3743 0.3511 0.0292  -0.0138 0.0186  377 ALA B C   
5688  O O   . ALA B 377 ? 0.3857 0.3921 0.3745 0.0341  -0.0043 0.0194  377 ALA B O   
5689  C CB  . ALA B 377 ? 0.2856 0.3219 0.2707 0.0293  -0.0316 0.0352  377 ALA B CB  
5690  N N   . HIS B 378 ? 0.3582 0.3620 0.3381 0.0221  -0.0151 0.0073  378 HIS B N   
5691  C CA  . HIS B 378 ? 0.3579 0.3452 0.3278 0.0213  -0.0046 -0.0052 378 HIS B CA  
5692  C C   . HIS B 378 ? 0.3359 0.3108 0.3263 0.0302  0.0027  -0.0038 378 HIS B C   
5693  O O   . HIS B 378 ? 0.3658 0.3338 0.3599 0.0360  0.0135  -0.0089 378 HIS B O   
5694  C CB  . HIS B 378 ? 0.3903 0.3693 0.3492 0.0101  -0.0082 -0.0184 378 HIS B CB  
5695  C CG  . HIS B 378 ? 0.5012 0.4635 0.4411 0.0070  0.0027  -0.0345 378 HIS B CG  
5696  N ND1 . HIS B 378 ? 0.5901 0.5570 0.4996 0.0007  0.0036  -0.0413 378 HIS B ND1 
5697  C CD2 . HIS B 378 ? 0.5639 0.5025 0.5094 0.0095  0.0141  -0.0459 378 HIS B CD2 
5698  C CE1 . HIS B 378 ? 0.6369 0.5839 0.5327 -0.0016 0.0178  -0.0587 378 HIS B CE1 
5699  N NE2 . HIS B 378 ? 0.6143 0.5439 0.5351 0.0047  0.0245  -0.0619 378 HIS B NE2 
5700  N N   . HIS B 379 ? 0.3190 0.2921 0.3236 0.0313  -0.0035 0.0036  379 HIS B N   
5701  C CA  . HIS B 379 ? 0.3008 0.2633 0.3217 0.0394  -0.0020 0.0082  379 HIS B CA  
5702  C C   . HIS B 379 ? 0.3341 0.3082 0.3682 0.0475  0.0007  0.0144  379 HIS B C   
5703  O O   . HIS B 379 ? 0.3718 0.3415 0.4218 0.0552  0.0049  0.0132  379 HIS B O   
5704  C CB  . HIS B 379 ? 0.2939 0.2523 0.3176 0.0361  -0.0094 0.0160  379 HIS B CB  
5705  C CG  . HIS B 379 ? 0.3345 0.2820 0.3681 0.0430  -0.0125 0.0234  379 HIS B CG  
5706  N ND1 . HIS B 379 ? 0.3564 0.2810 0.3910 0.0453  -0.0131 0.0235  379 HIS B ND1 
5707  C CD2 . HIS B 379 ? 0.3552 0.3107 0.3975 0.0478  -0.0173 0.0313  379 HIS B CD2 
5708  C CE1 . HIS B 379 ? 0.3579 0.2787 0.4009 0.0522  -0.0204 0.0330  379 HIS B CE1 
5709  N NE2 . HIS B 379 ? 0.3550 0.2955 0.4024 0.0528  -0.0233 0.0367  379 HIS B NE2 
5710  N N   . LEU B 380 ? 0.3376 0.3266 0.3688 0.0457  -0.0016 0.0210  380 LEU B N   
5711  C CA  . LEU B 380 ? 0.2744 0.2735 0.3178 0.0498  0.0012  0.0273  380 LEU B CA  
5712  C C   . LEU B 380 ? 0.2876 0.2912 0.3295 0.0511  0.0137  0.0232  380 LEU B C   
5713  O O   . LEU B 380 ? 0.3120 0.3228 0.3717 0.0542  0.0193  0.0257  380 LEU B O   
5714  C CB  . LEU B 380 ? 0.2546 0.2620 0.2938 0.0471  -0.0036 0.0355  380 LEU B CB  
5715  C CG  . LEU B 380 ? 0.2704 0.2755 0.3125 0.0452  -0.0114 0.0385  380 LEU B CG  
5716  C CD1 . LEU B 380 ? 0.2493 0.2623 0.2907 0.0444  -0.0135 0.0442  380 LEU B CD1 
5717  C CD2 . LEU B 380 ? 0.2754 0.2763 0.3292 0.0474  -0.0140 0.0408  380 LEU B CD2 
5718  N N   . GLU B 381 ? 0.2924 0.2924 0.3114 0.0467  0.0185  0.0162  381 GLU B N   
5719  C CA  . GLU B 381 ? 0.2986 0.3004 0.3056 0.0452  0.0331  0.0113  381 GLU B CA  
5720  C C   . GLU B 381 ? 0.3715 0.3715 0.4023 0.0519  0.0470  0.0026  381 GLU B C   
5721  O O   . GLU B 381 ? 0.4105 0.4001 0.4532 0.0567  0.0458  -0.0049 381 GLU B O   
5722  C CB  . GLU B 381 ? 0.3206 0.3161 0.2927 0.0374  0.0333  0.0028  381 GLU B CB  
5723  C CG  . GLU B 381 ? 0.3479 0.3509 0.2982 0.0318  0.0206  0.0130  381 GLU B CG  
5724  C CD  . GLU B 381 ? 0.3830 0.3828 0.3036 0.0229  0.0136  0.0040  381 GLU B CD  
5725  O OE1 . GLU B 381 ? 0.4077 0.3959 0.3220 0.0199  0.0207  -0.0119 381 GLU B OE1 
5726  O OE2 . GLU B 381 ? 0.4095 0.4179 0.3135 0.0189  0.0004  0.0125  381 GLU B OE2 
5727  N N   . GLU B 382 ? 0.3781 0.3880 0.4177 0.0521  0.0610  0.0041  382 GLU B N   
5728  C CA  . GLU B 382 ? 0.3285 0.3448 0.4010 0.0588  0.0769  -0.0037 382 GLU B CA  
5729  C C   . GLU B 382 ? 0.2971 0.3205 0.4128 0.0680  0.0652  0.0011  382 GLU B C   
5730  O O   . GLU B 382 ? 0.3014 0.3283 0.4504 0.0772  0.0719  -0.0057 382 GLU B O   
5731  C CB  . GLU B 382 ? 0.3789 0.3823 0.4423 0.0610  0.0916  -0.0212 382 GLU B CB  
5732  C CG  . GLU B 382 ? 0.4365 0.4330 0.4527 0.0501  0.1050  -0.0285 382 GLU B CG  
5733  C CD  . GLU B 382 ? 0.4661 0.4747 0.4761 0.0443  0.1200  -0.0214 382 GLU B CD  
5734  O OE1 . GLU B 382 ? 0.4977 0.5201 0.5474 0.0491  0.1327  -0.0213 382 GLU B OE1 
5735  O OE2 . GLU B 382 ? 0.4905 0.4947 0.4567 0.0343  0.1188  -0.0152 382 GLU B OE2 
5736  N N   . ASN B 383 ? 0.2774 0.3028 0.3922 0.0658  0.0473  0.0127  383 ASN B N   
5737  C CA  . ASN B 383 ? 0.2898 0.3228 0.4369 0.0710  0.0337  0.0187  383 ASN B CA  
5738  C C   . ASN B 383 ? 0.2689 0.3134 0.4211 0.0643  0.0301  0.0272  383 ASN B C   
5739  O O   . ASN B 383 ? 0.3028 0.3427 0.4289 0.0575  0.0307  0.0320  383 ASN B O   
5740  C CB  . ASN B 383 ? 0.3012 0.3190 0.4368 0.0728  0.0160  0.0225  383 ASN B CB  
5741  C CG  . ASN B 383 ? 0.3525 0.3540 0.4875 0.0792  0.0187  0.0150  383 ASN B CG  
5742  O OD1 . ASN B 383 ? 0.3612 0.3636 0.5266 0.0894  0.0204  0.0123  383 ASN B OD1 
5743  N ND2 . ASN B 383 ? 0.3700 0.3565 0.4740 0.0732  0.0190  0.0111  383 ASN B ND2 
5744  N N   . LEU B 384 ? 0.2623 0.3213 0.4502 0.0663  0.0249  0.0291  384 LEU B N   
5745  C CA  . LEU B 384 ? 0.2643 0.3303 0.4570 0.0581  0.0192  0.0354  384 LEU B CA  
5746  C C   . LEU B 384 ? 0.2743 0.3322 0.4585 0.0574  -0.0021 0.0398  384 LEU B C   
5747  O O   . LEU B 384 ? 0.2824 0.3439 0.4846 0.0627  -0.0153 0.0401  384 LEU B O   
5748  C CB  . LEU B 384 ? 0.2538 0.3424 0.4907 0.0567  0.0248  0.0335  384 LEU B CB  
5749  C CG  . LEU B 384 ? 0.2508 0.3437 0.4936 0.0459  0.0181  0.0381  384 LEU B CG  
5750  C CD1 . LEU B 384 ? 0.2896 0.3726 0.5081 0.0369  0.0334  0.0425  384 LEU B CD1 
5751  C CD2 . LEU B 384 ? 0.2694 0.3883 0.5634 0.0441  0.0159  0.0350  384 LEU B CD2 
5752  N N   . VAL B 385 ? 0.3022 0.3485 0.4588 0.0513  -0.0048 0.0434  385 VAL B N   
5753  C CA  . VAL B 385 ? 0.3021 0.3381 0.4441 0.0491  -0.0200 0.0454  385 VAL B CA  
5754  C C   . VAL B 385 ? 0.2734 0.3089 0.4163 0.0404  -0.0226 0.0463  385 VAL B C   
5755  O O   . VAL B 385 ? 0.2495 0.2789 0.3819 0.0371  -0.0139 0.0483  385 VAL B O   
5756  C CB  . VAL B 385 ? 0.3020 0.3235 0.4138 0.0499  -0.0190 0.0459  385 VAL B CB  
5757  C CG1 . VAL B 385 ? 0.2751 0.2855 0.3712 0.0467  -0.0303 0.0469  385 VAL B CG1 
5758  C CG2 . VAL B 385 ? 0.2753 0.2937 0.3849 0.0559  -0.0149 0.0427  385 VAL B CG2 
5759  N N   . VAL B 386 ? 0.2614 0.3013 0.4159 0.0367  -0.0362 0.0448  386 VAL B N   
5760  C CA  . VAL B 386 ? 0.2867 0.3255 0.4448 0.0263  -0.0392 0.0422  386 VAL B CA  
5761  C C   . VAL B 386 ? 0.2944 0.3157 0.4229 0.0216  -0.0470 0.0397  386 VAL B C   
5762  O O   . VAL B 386 ? 0.2974 0.3149 0.4132 0.0218  -0.0606 0.0399  386 VAL B O   
5763  C CB  . VAL B 386 ? 0.3232 0.3810 0.5144 0.0217  -0.0510 0.0397  386 VAL B CB  
5764  C CG1 . VAL B 386 ? 0.3111 0.3651 0.5037 0.0078  -0.0544 0.0344  386 VAL B CG1 
5765  C CG2 . VAL B 386 ? 0.2984 0.3767 0.5255 0.0257  -0.0393 0.0403  386 VAL B CG2 
5766  N N   . PHE B 387 ? 0.3128 0.3217 0.4303 0.0175  -0.0371 0.0378  387 PHE B N   
5767  C CA  . PHE B 387 ? 0.3124 0.3042 0.4052 0.0125  -0.0387 0.0323  387 PHE B CA  
5768  C C   . PHE B 387 ? 0.3066 0.2936 0.4029 0.0004  -0.0441 0.0242  387 PHE B C   
5769  O O   . PHE B 387 ? 0.3513 0.3307 0.4567 -0.0041 -0.0344 0.0216  387 PHE B O   
5770  C CB  . PHE B 387 ? 0.3003 0.2817 0.3850 0.0172  -0.0246 0.0338  387 PHE B CB  
5771  C CG  . PHE B 387 ? 0.2929 0.2788 0.3705 0.0259  -0.0222 0.0391  387 PHE B CG  
5772  C CD1 . PHE B 387 ? 0.2883 0.2848 0.3764 0.0316  -0.0187 0.0451  387 PHE B CD1 
5773  C CD2 . PHE B 387 ? 0.3467 0.3258 0.4060 0.0263  -0.0222 0.0366  387 PHE B CD2 
5774  C CE1 . PHE B 387 ? 0.3281 0.3273 0.4077 0.0372  -0.0174 0.0474  387 PHE B CE1 
5775  C CE2 . PHE B 387 ? 0.3615 0.3451 0.4169 0.0316  -0.0203 0.0402  387 PHE B CE2 
5776  C CZ  . PHE B 387 ? 0.3311 0.3244 0.3965 0.0369  -0.0191 0.0450  387 PHE B CZ  
5777  N N   . ASP B 388 ? 0.2997 0.2892 0.3867 -0.0056 -0.0609 0.0208  388 ASP B N   
5778  C CA  . ASP B 388 ? 0.3380 0.3258 0.4259 -0.0196 -0.0714 0.0115  388 ASP B CA  
5779  C C   . ASP B 388 ? 0.3777 0.3404 0.4273 -0.0278 -0.0679 0.0010  388 ASP B C   
5780  O O   . ASP B 388 ? 0.4379 0.3937 0.4562 -0.0316 -0.0790 -0.0006 388 ASP B O   
5781  C CB  . ASP B 388 ? 0.3265 0.3334 0.4255 -0.0212 -0.0955 0.0147  388 ASP B CB  
5782  C CG  . ASP B 388 ? 0.4467 0.4593 0.5539 -0.0374 -0.1110 0.0050  388 ASP B CG  
5783  O OD1 . ASP B 388 ? 0.4752 0.4712 0.5716 -0.0493 -0.1025 -0.0064 388 ASP B OD1 
5784  O OD2 . ASP B 388 ? 0.4986 0.5326 0.6250 -0.0382 -0.1332 0.0085  388 ASP B OD2 
5785  N N   . LEU B 389 ? 0.3494 0.2961 0.4005 -0.0305 -0.0510 -0.0060 389 LEU B N   
5786  C CA  . LEU B 389 ? 0.3777 0.2998 0.3969 -0.0360 -0.0418 -0.0182 389 LEU B CA  
5787  C C   . LEU B 389 ? 0.4024 0.3130 0.3994 -0.0544 -0.0530 -0.0335 389 LEU B C   
5788  O O   . LEU B 389 ? 0.4568 0.3488 0.4158 -0.0611 -0.0494 -0.0441 389 LEU B O   
5789  C CB  . LEU B 389 ? 0.4073 0.3153 0.4410 -0.0295 -0.0200 -0.0198 389 LEU B CB  
5790  C CG  . LEU B 389 ? 0.4073 0.3296 0.4602 -0.0133 -0.0139 -0.0039 389 LEU B CG  
5791  C CD1 . LEU B 389 ? 0.4169 0.3283 0.4888 -0.0065 0.0013  -0.0003 389 LEU B CD1 
5792  C CD2 . LEU B 389 ? 0.4102 0.3356 0.4446 -0.0058 -0.0119 -0.0009 389 LEU B CD2 
5793  N N   . GLU B 390 ? 0.4029 0.3254 0.4224 -0.0642 -0.0666 -0.0357 390 GLU B N   
5794  C CA  . GLU B 390 ? 0.4098 0.3235 0.4090 -0.0841 -0.0808 -0.0516 390 GLU B CA  
5795  C C   . GLU B 390 ? 0.4382 0.3575 0.4016 -0.0888 -0.1045 -0.0493 390 GLU B C   
5796  O O   . GLU B 390 ? 0.5084 0.4109 0.4316 -0.1046 -0.1126 -0.0632 390 GLU B O   
5797  C CB  . GLU B 390 ? 0.4220 0.3519 0.4619 -0.0947 -0.0904 -0.0541 390 GLU B CB  
5798  C CG  . GLU B 390 ? 0.4892 0.4044 0.5549 -0.0934 -0.0662 -0.0560 390 GLU B CG  
5799  C CD  . GLU B 390 ? 0.5829 0.5028 0.6809 -0.1103 -0.0700 -0.0636 390 GLU B CD  
5800  O OE1 . GLU B 390 ? 0.6470 0.5947 0.7628 -0.1199 -0.0930 -0.0640 390 GLU B OE1 
5801  O OE2 . GLU B 390 ? 0.5650 0.4604 0.6731 -0.1139 -0.0500 -0.0686 390 GLU B OE2 
5802  N N   . ARG B 391 ? 0.4276 0.3674 0.4027 -0.0753 -0.1154 -0.0315 391 ARG B N   
5803  C CA  . ARG B 391 ? 0.4763 0.4189 0.4194 -0.0768 -0.1395 -0.0241 391 ARG B CA  
5804  C C   . ARG B 391 ? 0.4977 0.4265 0.4104 -0.0655 -0.1270 -0.0144 391 ARG B C   
5805  O O   . ARG B 391 ? 0.5799 0.5047 0.4618 -0.0656 -0.1429 -0.0051 391 ARG B O   
5806  C CB  A ARG B 391 ? 0.4597 0.4353 0.4446 -0.0706 -0.1647 -0.0111 391 ARG B CB  
5807  C CB  B ARG B 391 ? 0.4594 0.4350 0.4445 -0.0707 -0.1646 -0.0113 391 ARG B CB  
5808  C CG  A ARG B 391 ? 0.5003 0.4893 0.4898 -0.0872 -0.1941 -0.0186 391 ARG B CG  
5809  C CG  B ARG B 391 ? 0.4677 0.4625 0.4912 -0.0835 -0.1759 -0.0209 391 ARG B CG  
5810  C CD  A ARG B 391 ? 0.4978 0.5264 0.5506 -0.0800 -0.2121 -0.0089 391 ARG B CD  
5811  C CD  B ARG B 391 ? 0.4815 0.5131 0.5509 -0.0777 -0.2019 -0.0097 391 ARG B CD  
5812  N NE  A ARG B 391 ? 0.4771 0.5182 0.5808 -0.0752 -0.1878 -0.0109 391 ARG B NE  
5813  N NE  B ARG B 391 ? 0.5108 0.5427 0.5504 -0.0743 -0.2304 0.0013  391 ARG B NE  
5814  C CZ  A ARG B 391 ? 0.4706 0.5446 0.6340 -0.0764 -0.1940 -0.0101 391 ARG B CZ  
5815  C CZ  B ARG B 391 ? 0.5137 0.5742 0.5826 -0.0733 -0.2632 0.0091  391 ARG B CZ  
5816  N NH1 A ARG B 391 ? 0.4585 0.5603 0.6457 -0.0808 -0.2261 -0.0081 391 ARG B NH1 
5817  N NH1 B ARG B 391 ? 0.4107 0.5045 0.5416 -0.0765 -0.2672 0.0042  391 ARG B NH1 
5818  N NH2 A ARG B 391 ? 0.4595 0.5390 0.6591 -0.0737 -0.1681 -0.0108 391 ARG B NH2 
5819  N NH2 B ARG B 391 ? 0.5298 0.5836 0.5654 -0.0665 -0.2807 0.0215  391 ARG B NH2 
5820  N N   . SER B 392 ? 0.4300 0.3512 0.3526 -0.0568 -0.0993 -0.0161 392 SER B N   
5821  C CA  . SER B 392 ? 0.4012 0.3127 0.3037 -0.0479 -0.0847 -0.0094 392 SER B CA  
5822  C C   . SER B 392 ? 0.3849 0.3088 0.2951 -0.0369 -0.0982 0.0087  392 SER B C   
5823  O O   . SER B 392 ? 0.4006 0.3123 0.2747 -0.0389 -0.1047 0.0155  392 SER B O   
5824  C CB  . SER B 392 ? 0.4411 0.3266 0.2871 -0.0608 -0.0778 -0.0199 392 SER B CB  
5825  O OG  . SER B 392 ? 0.4383 0.3155 0.2753 -0.0543 -0.0549 -0.0183 392 SER B OG  
5826  N N   . ARG B 393 ? 0.3424 0.2877 0.2985 -0.0256 -0.1007 0.0163  393 ARG B N   
5827  C CA  . ARG B 393 ? 0.3297 0.2854 0.2993 -0.0139 -0.1113 0.0308  393 ARG B CA  
5828  C C   . ARG B 393 ? 0.3540 0.3253 0.3647 -0.0014 -0.0975 0.0341  393 ARG B C   
5829  O O   . ARG B 393 ? 0.3461 0.3241 0.3786 -0.0027 -0.0864 0.0281  393 ARG B O   
5830  C CB  . ARG B 393 ? 0.3306 0.2995 0.3108 -0.0156 -0.1406 0.0366  393 ARG B CB  
5831  C CG  . ARG B 393 ? 0.3129 0.3059 0.3392 -0.0176 -0.1449 0.0308  393 ARG B CG  
5832  C CD  . ARG B 393 ? 0.3844 0.3950 0.4258 -0.0216 -0.1758 0.0341  393 ARG B CD  
5833  N NE  . ARG B 393 ? 0.3812 0.4189 0.4770 -0.0233 -0.1741 0.0284  393 ARG B NE  
5834  C CZ  . ARG B 393 ? 0.4040 0.4708 0.5423 -0.0222 -0.1955 0.0316  393 ARG B CZ  
5835  N NH1 . ARG B 393 ? 0.3898 0.4621 0.5232 -0.0169 -0.2239 0.0423  393 ARG B NH1 
5836  N NH2 . ARG B 393 ? 0.4270 0.5178 0.6155 -0.0262 -0.1878 0.0251  393 ARG B NH2 
5837  N N   . VAL B 394 ? 0.3624 0.3357 0.3794 0.0094  -0.0975 0.0436  394 VAL B N   
5838  C CA  . VAL B 394 ? 0.3518 0.3387 0.4018 0.0203  -0.0860 0.0460  394 VAL B CA  
5839  C C   . VAL B 394 ? 0.3694 0.3712 0.4495 0.0294  -0.0992 0.0526  394 VAL B C   
5840  O O   . VAL B 394 ? 0.3791 0.3729 0.4478 0.0328  -0.1139 0.0602  394 VAL B O   
5841  C CB  . VAL B 394 ? 0.3844 0.3604 0.4194 0.0250  -0.0719 0.0480  394 VAL B CB  
5842  C CG1 . VAL B 394 ? 0.3836 0.3713 0.4446 0.0346  -0.0627 0.0495  394 VAL B CG1 
5843  C CG2 . VAL B 394 ? 0.3859 0.3534 0.4042 0.0190  -0.0579 0.0414  394 VAL B CG2 
5844  N N   . GLY B 395 ? 0.3306 0.3526 0.4496 0.0337  -0.0925 0.0505  395 GLY B N   
5845  C CA  . GLY B 395 ? 0.2785 0.3181 0.4355 0.0441  -0.0990 0.0542  395 GLY B CA  
5846  C C   . GLY B 395 ? 0.2810 0.3230 0.4517 0.0535  -0.0794 0.0529  395 GLY B C   
5847  O O   . GLY B 395 ? 0.2936 0.3321 0.4532 0.0501  -0.0625 0.0493  395 GLY B O   
5848  N N   . PHE B 396 ? 0.2956 0.3415 0.4885 0.0656  -0.0820 0.0556  396 PHE B N   
5849  C CA  . PHE B 396 ? 0.2859 0.3314 0.4880 0.0733  -0.0620 0.0512  396 PHE B CA  
5850  C C   . PHE B 396 ? 0.2755 0.3350 0.5143 0.0830  -0.0597 0.0480  396 PHE B C   
5851  O O   . PHE B 396 ? 0.3181 0.3836 0.5688 0.0853  -0.0756 0.0514  396 PHE B O   
5852  C CB  . PHE B 396 ? 0.3032 0.3227 0.4697 0.0746  -0.0584 0.0524  396 PHE B CB  
5853  C CG  . PHE B 396 ? 0.3488 0.3511 0.5012 0.0777  -0.0747 0.0599  396 PHE B CG  
5854  C CD1 . PHE B 396 ? 0.3821 0.3798 0.5484 0.0878  -0.0752 0.0602  396 PHE B CD1 
5855  C CD2 . PHE B 396 ? 0.3736 0.3625 0.4946 0.0695  -0.0876 0.0662  396 PHE B CD2 
5856  C CE1 . PHE B 396 ? 0.4167 0.3961 0.5657 0.0899  -0.0890 0.0690  396 PHE B CE1 
5857  C CE2 . PHE B 396 ? 0.3937 0.3646 0.4937 0.0700  -0.1003 0.0742  396 PHE B CE2 
5858  C CZ  . PHE B 396 ? 0.4108 0.3769 0.5251 0.0804  -0.1013 0.0767  396 PHE B CZ  
5859  N N   . ASN B 397 ? 0.2692 0.3344 0.5249 0.0884  -0.0389 0.0410  397 ASN B N   
5860  C CA  . ASN B 397 ? 0.2768 0.3544 0.5673 0.0976  -0.0327 0.0357  397 ASN B CA  
5861  C C   . ASN B 397 ? 0.3098 0.3670 0.5904 0.1074  -0.0425 0.0389  397 ASN B C   
5862  O O   . ASN B 397 ? 0.3332 0.3652 0.5839 0.1082  -0.0402 0.0398  397 ASN B O   
5863  C CB  . ASN B 397 ? 0.2407 0.3262 0.5466 0.0999  -0.0042 0.0255  397 ASN B CB  
5864  C CG  . ASN B 397 ? 0.2170 0.2803 0.4878 0.0994  0.0083  0.0225  397 ASN B CG  
5865  O OD1 . ASN B 397 ? 0.2614 0.3161 0.4952 0.0887  0.0053  0.0263  397 ASN B OD1 
5866  N ND2 . ASN B 397 ? 0.2500 0.3023 0.5228 0.1072  0.0231  0.0133  397 ASN B ND2 
5867  N N   . SER B 398 ? 0.3297 0.3975 0.6369 0.1143  -0.0543 0.0418  398 SER B N   
5868  C CA  . SER B 398 ? 0.3611 0.4090 0.6619 0.1247  -0.0645 0.0477  398 SER B CA  
5869  C C   . SER B 398 ? 0.3715 0.4140 0.6946 0.1368  -0.0462 0.0386  398 SER B C   
5870  O O   . SER B 398 ? 0.4193 0.4388 0.7361 0.1461  -0.0497 0.0419  398 SER B O   
5871  C CB  . SER B 398 ? 0.3842 0.4456 0.7034 0.1278  -0.0879 0.0569  398 SER B CB  
5872  O OG  . SER B 398 ? 0.3989 0.4930 0.7677 0.1309  -0.0832 0.0507  398 SER B OG  
5873  N N   . ASN B 399 ? 0.3378 0.3996 0.6866 0.1364  -0.0251 0.0268  399 ASN B N   
5874  C CA  . ASN B 399 ? 0.3546 0.4073 0.7160 0.1454  -0.0028 0.0147  399 ASN B CA  
5875  C C   . ASN B 399 ? 0.3081 0.3598 0.6513 0.1366  0.0205  0.0041  399 ASN B C   
5876  O O   . ASN B 399 ? 0.3105 0.3769 0.6473 0.1261  0.0205  0.0069  399 ASN B O   
5877  C CB  . ASN B 399 ? 0.4045 0.4819 0.8174 0.1547  0.0043  0.0090  399 ASN B CB  
5878  C CG  . ASN B 399 ? 0.4544 0.5362 0.8884 0.1644  -0.0210 0.0211  399 ASN B CG  
5879  O OD1 . ASN B 399 ? 0.5044 0.5615 0.9302 0.1748  -0.0285 0.0260  399 ASN B OD1 
5880  N ND2 . ASN B 399 ? 0.4551 0.5679 0.9177 0.1608  -0.0340 0.0258  399 ASN B ND2 
5881  N N   . SER B 400 ? 0.3152 0.3483 0.6490 0.1404  0.0410  -0.0084 400 SER B N   
5882  C CA  . SER B 400 ? 0.3375 0.3672 0.6477 0.1319  0.0637  -0.0189 400 SER B CA  
5883  C C   . SER B 400 ? 0.3910 0.4514 0.7228 0.1261  0.0813  -0.0234 400 SER B C   
5884  O O   . SER B 400 ? 0.4187 0.4988 0.7886 0.1308  0.0841  -0.0256 400 SER B O   
5885  C CB  . SER B 400 ? 0.3422 0.3460 0.6372 0.1356  0.0843  -0.0353 400 SER B CB  
5886  O OG  . SER B 400 ? 0.3857 0.4010 0.7109 0.1418  0.1026  -0.0468 400 SER B OG  
5887  N N   . LEU B 401 ? 0.4092 0.4732 0.7173 0.1155  0.0937  -0.0238 401 LEU B N   
5888  C CA  . LEU B 401 ? 0.4194 0.5075 0.7408 0.1073  0.1144  -0.0272 401 LEU B CA  
5889  C C   . LEU B 401 ? 0.4548 0.5433 0.7852 0.1098  0.1420  -0.0439 401 LEU B C   
5890  O O   . LEU B 401 ? 0.4730 0.5843 0.8353 0.1078  0.1534  -0.0466 401 LEU B O   
5891  C CB  . LEU B 401 ? 0.4094 0.4906 0.6788 0.0913  0.1201  -0.0223 401 LEU B CB  
5892  C CG  . LEU B 401 ? 0.3794 0.4591 0.6311 0.0844  0.0931  -0.0062 401 LEU B CG  
5893  C CD1 . LEU B 401 ? 0.3273 0.4033 0.5375 0.0698  0.1007  -0.0005 401 LEU B CD1 
5894  C CD2 . LEU B 401 ? 0.3846 0.4873 0.6867 0.0882  0.0776  0.0011  401 LEU B CD2 
5895  N N   . LYS B 402 ? 0.4592 0.5212 0.7622 0.1135  0.1527  -0.0562 402 LYS B N   
5896  C CA  . LYS B 402 ? 0.4656 0.5242 0.7695 0.1139  0.1811  -0.0743 402 LYS B CA  
5897  C C   . LYS B 402 ? 0.4615 0.5353 0.8207 0.1261  0.1779  -0.0758 402 LYS B C   
5898  O O   . LYS B 402 ? 0.4817 0.5680 0.8594 0.1251  0.2017  -0.0868 402 LYS B O   
5899  C CB  . LYS B 402 ? 0.5127 0.5366 0.7740 0.1137  0.1904  -0.0890 402 LYS B CB  
5900  C CG  . LYS B 402 ? 0.6324 0.6484 0.8953 0.1153  0.2163  -0.1087 402 LYS B CG  
5901  C CD  . LYS B 402 ? 0.7400 0.7200 0.9520 0.1102  0.2257  -0.1256 402 LYS B CD  
5902  C CE  . LYS B 402 ? 0.7960 0.7510 1.0224 0.1222  0.2084  -0.1262 402 LYS B CE  
5903  N NZ  . LYS B 402 ? 0.8500 0.7694 1.0291 0.1143  0.2208  -0.1465 402 LYS B NZ  
5904  N N   . SER B 403 ? 0.4561 0.5302 0.8406 0.1368  0.1484  -0.0636 403 SER B N   
5905  C CA  . SER B 403 ? 0.4811 0.5711 0.9185 0.1494  0.1419  -0.0624 403 SER B CA  
5906  C C   . SER B 403 ? 0.4322 0.5608 0.9096 0.1442  0.1441  -0.0582 403 SER B C   
5907  O O   . SER B 403 ? 0.4489 0.5964 0.9743 0.1530  0.1457  -0.0607 403 SER B O   
5908  C CB  . SER B 403 ? 0.5015 0.5793 0.9461 0.1605  0.1084  -0.0481 403 SER B CB  
5909  O OG  . SER B 403 ? 0.4806 0.5772 0.9331 0.1559  0.0823  -0.0316 403 SER B OG  
5910  N N   . TYR B 404 ? 0.3725 0.5120 0.8318 0.1298  0.1447  -0.0521 404 TYR B N   
5911  C CA  . TYR B 404 ? 0.3357 0.5081 0.8280 0.1210  0.1511  -0.0498 404 TYR B CA  
5912  C C   . TYR B 404 ? 0.3639 0.5388 0.8418 0.1102  0.1894  -0.0623 404 TYR B C   
5913  O O   . TYR B 404 ? 0.3706 0.5695 0.8725 0.1007  0.2019  -0.0623 404 TYR B O   
5914  C CB  . TYR B 404 ? 0.2931 0.4736 0.7749 0.1100  0.1304  -0.0354 404 TYR B CB  
5915  C CG  . TYR B 404 ? 0.2928 0.4715 0.7824 0.1171  0.0926  -0.0227 404 TYR B CG  
5916  C CD1 . TYR B 404 ? 0.3183 0.5216 0.8525 0.1204  0.0745  -0.0177 404 TYR B CD1 
5917  C CD2 . TYR B 404 ? 0.3129 0.4646 0.7621 0.1194  0.0755  -0.0158 404 TYR B CD2 
5918  C CE1 . TYR B 404 ? 0.3401 0.5396 0.8729 0.1253  0.0405  -0.0060 404 TYR B CE1 
5919  C CE2 . TYR B 404 ? 0.3234 0.4704 0.7714 0.1237  0.0432  -0.0039 404 TYR B CE2 
5920  C CZ  . TYR B 404 ? 0.3535 0.5236 0.8407 0.1265  0.0258  0.0011  404 TYR B CZ  
5921  O OH  . TYR B 404 ? 0.3906 0.5546 0.8698 0.1296  -0.0059 0.0131  404 TYR B OH  
5922  N N   . GLY B 405 ? 0.3980 0.5461 0.8328 0.1100  0.2080  -0.0733 405 GLY B N   
5923  C CA  . GLY B 405 ? 0.4405 0.5841 0.8426 0.0971  0.2432  -0.0845 405 GLY B CA  
5924  C C   . GLY B 405 ? 0.4326 0.5723 0.7893 0.0804  0.2466  -0.0747 405 GLY B C   
5925  O O   . GLY B 405 ? 0.4542 0.5953 0.7862 0.0664  0.2725  -0.0776 405 GLY B O   
5926  N N   . LYS B 406 ? 0.4029 0.5361 0.7473 0.0817  0.2204  -0.0617 406 LYS B N   
5927  C CA  . LYS B 406 ? 0.3572 0.4880 0.6673 0.0683  0.2196  -0.0489 406 LYS B CA  
5928  C C   . LYS B 406 ? 0.3767 0.4799 0.6301 0.0679  0.2156  -0.0478 406 LYS B C   
5929  O O   . LYS B 406 ? 0.3864 0.4725 0.6319 0.0779  0.2055  -0.0551 406 LYS B O   
5930  C CB  . LYS B 406 ? 0.3225 0.4719 0.6695 0.0682  0.1927  -0.0337 406 LYS B CB  
5931  C CG  . LYS B 406 ? 0.3604 0.5386 0.7659 0.0685  0.1901  -0.0349 406 LYS B CG  
5932  C CD  . LYS B 406 ? 0.4365 0.6269 0.8435 0.0526  0.2180  -0.0363 406 LYS B CD  
5933  C CE  . LYS B 406 ? 0.4872 0.7072 0.9566 0.0549  0.2192  -0.0415 406 LYS B CE  
5934  N NZ  . LYS B 406 ? 0.4923 0.7261 0.9999 0.0631  0.1826  -0.0338 406 LYS B NZ  
5935  N N   . THR B 407 ? 0.3854 0.4789 0.5878 0.0529  0.2127  -0.0355 407 THR B N   
5936  C CA  . THR B 407 ? 0.3695 0.4379 0.5105 0.0485  0.1923  -0.0285 407 THR B CA  
5937  C C   . THR B 407 ? 0.3634 0.4334 0.4945 0.0412  0.1713  -0.0079 407 THR B C   
5938  O O   . THR B 407 ? 0.3607 0.4465 0.5215 0.0361  0.1777  -0.0009 407 THR B O   
5939  C CB  . THR B 407 ? 0.3992 0.4489 0.4760 0.0375  0.2126  -0.0360 407 THR B CB  
5940  O OG1 . THR B 407 ? 0.4017 0.4549 0.4576 0.0238  0.2280  -0.0250 407 THR B OG1 
5941  C CG2 . THR B 407 ? 0.4139 0.4612 0.5008 0.0423  0.2418  -0.0598 407 THR B CG2 
5942  N N   . CYS B 408 ? 0.3459 0.3997 0.4379 0.0399  0.1483  0.0005  408 CYS B N   
5943  C CA  . CYS B 408 ? 0.3243 0.3768 0.4078 0.0343  0.1318  0.0183  408 CYS B CA  
5944  C C   . CYS B 408 ? 0.3626 0.4091 0.4137 0.0217  0.1479  0.0285  408 CYS B C   
5945  O O   . CYS B 408 ? 0.3821 0.4283 0.4391 0.0165  0.1426  0.0425  408 CYS B O   
5946  C CB  . CYS B 408 ? 0.2987 0.3379 0.3543 0.0370  0.1059  0.0238  408 CYS B CB  
5947  S SG  . CYS B 408 ? 0.4165 0.4607 0.5102 0.0468  0.0811  0.0243  408 CYS B SG  
5948  N N   . SER B 409 ? 0.3735 0.4124 0.3888 0.0159  0.1691  0.0214  409 SER B N   
5949  C CA  . SER B 409 ? 0.4310 0.4606 0.4083 0.0026  0.1859  0.0329  409 SER B CA  
5950  C C   . SER B 409 ? 0.4385 0.4829 0.4535 -0.0043 0.2144  0.0316  409 SER B C   
5951  O O   . SER B 409 ? 0.4771 0.5141 0.4760 -0.0157 0.2234  0.0467  409 SER B O   
5952  C CB  . SER B 409 ? 0.5385 0.5521 0.4525 -0.0038 0.1970  0.0260  409 SER B CB  
5953  O OG  . SER B 409 ? 0.5863 0.5897 0.4697 0.0001  0.1688  0.0281  409 SER B OG  
5954  N N   . ASN B 410 ? 0.4091 0.4743 0.4772 0.0024  0.2286  0.0144  410 ASN B N   
5955  C CA  . ASN B 410 ? 0.4324 0.5181 0.5457 -0.0048 0.2570  0.0114  410 ASN B CA  
5956  C C   . ASN B 410 ? 0.3938 0.5070 0.5854 0.0016  0.2435  0.0107  410 ASN B C   
5957  O O   . ASN B 410 ? 0.4099 0.5446 0.6474 -0.0038 0.2599  0.0061  410 ASN B O   
5958  C CB  . ASN B 410 ? 0.5040 0.5956 0.6183 -0.0052 0.2899  -0.0089 410 ASN B CB  
5959  C CG  . ASN B 410 ? 0.4854 0.5866 0.6383 0.0127  0.2834  -0.0284 410 ASN B CG  
5960  O OD1 . ASN B 410 ? 0.4307 0.5472 0.6371 0.0251  0.2625  -0.0279 410 ASN B OD1 
5961  N ND2 . ASN B 410 ? 0.4556 0.5448 0.5783 0.0134  0.2999  -0.0450 410 ASN B ND2 
5962  N N   . LEU B 411 ? 0.3755 0.4865 0.5767 0.0114  0.2090  0.0152  411 LEU B N   
5963  C CA  . LEU B 411 ? 0.3253 0.4588 0.5888 0.0152  0.1915  0.0160  411 LEU B CA  
5964  C C   . LEU B 411 ? 0.3507 0.4878 0.6260 -0.0007 0.1970  0.0271  411 LEU B C   
5965  O O   . LEU B 411 ? 0.3235 0.4874 0.6585 -0.0049 0.2009  0.0232  411 LEU B O   
5966  C CB  A LEU B 411 ? 0.2640 0.3874 0.5191 0.0252  0.1553  0.0204  411 LEU B CB  
5967  C CB  B LEU B 411 ? 0.2640 0.3876 0.5193 0.0255  0.1555  0.0201  411 LEU B CB  
5968  C CG  A LEU B 411 ? 0.2450 0.3798 0.5362 0.0411  0.1398  0.0111  411 LEU B CG  
5969  C CG  B LEU B 411 ? 0.2253 0.3709 0.5387 0.0327  0.1345  0.0175  411 LEU B CG  
5970  C CD1 A LEU B 411 ? 0.2179 0.3402 0.4940 0.0457  0.1060  0.0188  411 LEU B CD1 
5971  C CD1 B LEU B 411 ? 0.2245 0.3951 0.5917 0.0427  0.1482  0.0044  411 LEU B CD1 
5972  C CD2 A LEU B 411 ? 0.2232 0.3919 0.5876 0.0437  0.1455  0.0047  411 LEU B CD2 
5973  C CD2 B LEU B 411 ? 0.2152 0.3448 0.5062 0.0418  0.1038  0.0212  411 LEU B CD2 
5974  N N   . PHE B 412 ? 0.3805 0.4899 0.6002 -0.0097 0.1971  0.0412  412 PHE B N   
5975  C CA  . PHE B 412 ? 0.3452 0.4470 0.5651 -0.0256 0.2044  0.0541  412 PHE B CA  
5976  C C   . PHE B 412 ? 0.3906 0.4721 0.5588 -0.0370 0.2316  0.0632  412 PHE B C   
5977  O O   . PHE B 412 ? 0.4234 0.4912 0.5423 -0.0324 0.2352  0.0619  412 PHE B O   
5978  C CB  . PHE B 412 ? 0.3168 0.3990 0.5203 -0.0241 0.1752  0.0656  412 PHE B CB  
5979  C CG  . PHE B 412 ? 0.2916 0.3882 0.5295 -0.0135 0.1477  0.0571  412 PHE B CG  
5980  C CD1 . PHE B 412 ? 0.2881 0.4087 0.5835 -0.0186 0.1425  0.0508  412 PHE B CD1 
5981  C CD2 . PHE B 412 ? 0.3067 0.3942 0.5196 -0.0001 0.1274  0.0553  412 PHE B CD2 
5982  C CE1 . PHE B 412 ? 0.2532 0.3861 0.5742 -0.0097 0.1155  0.0443  412 PHE B CE1 
5983  C CE2 . PHE B 412 ? 0.3099 0.4078 0.5489 0.0083  0.1037  0.0490  412 PHE B CE2 
5984  C CZ  . PHE B 412 ? 0.2062 0.3258 0.4965 0.0039  0.0969  0.0442  412 PHE B CZ  
5985  N N   . ASP B 413 ? 0.4182 0.4972 0.5965 -0.0539 0.2512  0.0720  413 ASP B N   
5986  C CA  . ASP B 413 ? 0.5244 0.5784 0.6446 -0.0660 0.2707  0.0832  413 ASP B CA  
5987  C C   . ASP B 413 ? 0.5851 0.6026 0.6504 -0.0654 0.2548  0.1060  413 ASP B C   
5988  O O   . ASP B 413 ? 0.5619 0.5675 0.6415 -0.0686 0.2409  0.1170  413 ASP B O   
5989  C CB  . ASP B 413 ? 0.5292 0.5897 0.6739 -0.0828 0.2874  0.0834  413 ASP B CB  
5990  C CG  . ASP B 413 ? 0.6008 0.6408 0.6879 -0.0952 0.3092  0.0924  413 ASP B CG  
5991  O OD1 . ASP B 413 ? 0.5903 0.6008 0.6110 -0.0945 0.3036  0.1071  413 ASP B OD1 
5992  O OD2 . ASP B 413 ? 0.7010 0.7558 0.8099 -0.1059 0.3309  0.0851  413 ASP B OD2 
5993  N N   . LEU B 414 ? 0.5940 0.5945 0.5973 -0.0599 0.2506  0.1103  414 LEU B N   
5994  C CA  . LEU B 414 ? 0.6051 0.5749 0.5571 -0.0562 0.2278  0.1308  414 LEU B CA  
5995  C C   . LEU B 414 ? 0.7371 0.6798 0.6235 -0.0687 0.2408  0.1484  414 LEU B C   
5996  O O   . LEU B 414 ? 0.7636 0.6831 0.6009 -0.0644 0.2214  0.1656  414 LEU B O   
5997  C CB  . LEU B 414 ? 0.5238 0.4975 0.4581 -0.0397 0.2001  0.1227  414 LEU B CB  
5998  C CG  . LEU B 414 ? 0.4178 0.4139 0.4065 -0.0268 0.1800  0.1066  414 LEU B CG  
5999  C CD1 . LEU B 414 ? 0.4017 0.3993 0.3687 -0.0140 0.1588  0.0984  414 LEU B CD1 
6000  C CD2 . LEU B 414 ? 0.4153 0.4055 0.4340 -0.0253 0.1626  0.1152  414 LEU B CD2 
6001  N N   . ASN B 415 ? 0.8279 0.7774 0.7167 -0.0832 0.2661  0.1429  415 ASN B N   
6002  C CA  . ASN B 415 ? 0.9286 0.8548 0.7580 -0.0957 0.2724  0.1602  415 ASN B CA  
6003  C C   . ASN B 415 ? 0.9316 0.8358 0.7694 -0.1029 0.2651  0.1810  415 ASN B C   
6004  O O   . ASN B 415 ? 0.8704 0.7846 0.7618 -0.1096 0.2749  0.1751  415 ASN B O   
6005  C CB  . ASN B 415 ? 1.0096 0.9503 0.8354 -0.1081 0.3045  0.1474  415 ASN B CB  
6006  C CG  . ASN B 415 ? 1.0142 0.9726 0.8311 -0.1009 0.3137  0.1239  415 ASN B CG  
6007  O OD1 . ASN B 415 ? 0.9959 0.9802 0.8586 -0.1007 0.3343  0.1021  415 ASN B OD1 
6008  N ND2 . ASN B 415 ? 1.0306 0.9748 0.7900 -0.0948 0.2973  0.1277  415 ASN B ND2 
6009  N N   . ASN B 416 ? 1.0247 0.8997 0.8108 -0.1015 0.2460  0.2046  416 ASN B N   
6010  C CA  . ASN B 416 ? 1.1033 0.9501 0.8904 -0.1058 0.2351  0.2264  416 ASN B CA  
6011  C C   . ASN B 416 ? 1.1308 0.9729 0.9303 -0.1252 0.2601  0.2310  416 ASN B C   
6012  O O   . ASN B 416 ? 1.1212 0.9445 0.9428 -0.1302 0.2561  0.2409  416 ASN B O   
6013  C CB  . ASN B 416 ? 1.1903 1.0112 0.9180 -0.1001 0.2095  0.2509  416 ASN B CB  
6014  C CG  . ASN B 416 ? 1.1841 1.0092 0.9089 -0.0803 0.1804  0.2472  416 ASN B CG  
6015  O OD1 . ASN B 416 ? 1.1778 0.9952 0.9347 -0.0681 0.1621  0.2489  416 ASN B OD1 
6016  N ND2 . ASN B 416 ? 1.1752 1.0141 0.8639 -0.0771 0.1776  0.2399  416 ASN B ND2 
6017  N N   . LYS C 11  ? 0.7353 1.0550 1.2172 0.0434  0.1077  -0.0960 11  LYS C N   
6018  C CA  . LYS C 11  ? 0.7470 1.0470 1.1725 0.0386  0.0889  -0.0896 11  LYS C CA  
6019  C C   . LYS C 11  ? 0.7024 0.9983 1.1108 0.0372  0.1007  -0.0561 11  LYS C C   
6020  O O   . LYS C 11  ? 0.7207 1.0493 1.1164 0.0477  0.1319  -0.0380 11  LYS C O   
6021  C CB  . LYS C 11  ? 0.7898 1.1157 1.1609 0.0475  0.0915  -0.1087 11  LYS C CB  
6022  C CG  . LYS C 11  ? 0.7830 1.0901 1.1580 0.0426  0.0643  -0.1394 11  LYS C CG  
6023  C CD  . LYS C 11  ? 0.7627 1.1015 1.0976 0.0519  0.0692  -0.1645 11  LYS C CD  
6024  C CE  . LYS C 11  ? 0.7194 1.0408 1.0759 0.0474  0.0469  -0.1962 11  LYS C CE  
6025  N NZ  . LYS C 11  ? 0.6739 0.9446 1.0516 0.0344  0.0193  -0.1847 11  LYS C NZ  
6026  N N   . PRO C 12  ? 0.6339 0.8904 1.0475 0.0250  0.0772  -0.0474 12  PRO C N   
6027  C CA  . PRO C 12  ? 0.6089 0.8553 1.0167 0.0217  0.0856  -0.0194 12  PRO C CA  
6028  C C   . PRO C 12  ? 0.5695 0.8284 0.9114 0.0279  0.0921  -0.0094 12  PRO C C   
6029  O O   . PRO C 12  ? 0.5759 0.8348 0.8792 0.0289  0.0766  -0.0284 12  PRO C O   
6030  C CB  . PRO C 12  ? 0.6015 0.8035 1.0282 0.0076  0.0528  -0.0244 12  PRO C CB  
6031  C CG  . PRO C 12  ? 0.5829 0.7715 0.9916 0.0056  0.0261  -0.0489 12  PRO C CG  
6032  C CD  . PRO C 12  ? 0.5981 0.8182 1.0230 0.0147  0.0412  -0.0646 12  PRO C CD  
6033  N N   . ASN C 13  ? 0.5009 0.7696 0.8362 0.0320  0.1139  0.0201  13  ASN C N   
6034  C CA  . ASN C 13  ? 0.4249 0.7088 0.7017 0.0395  0.1200  0.0325  13  ASN C CA  
6035  C C   . ASN C 13  ? 0.3836 0.6313 0.6502 0.0291  0.1038  0.0425  13  ASN C C   
6036  O O   . ASN C 13  ? 0.3887 0.6418 0.6115 0.0331  0.1044  0.0523  13  ASN C O   
6037  C CB  . ASN C 13  ? 0.4887 0.8123 0.7601 0.0543  0.1573  0.0633  13  ASN C CB  
6038  C CG  . ASN C 13  ? 0.6394 1.0082 0.9017 0.0687  0.1768  0.0529  13  ASN C CG  
6039  O OD1 . ASN C 13  ? 0.7151 1.0969 1.0213 0.0722  0.1985  0.0598  13  ASN C OD1 
6040  N ND2 . ASN C 13  ? 0.6942 1.0856 0.9051 0.0761  0.1669  0.0305  13  ASN C ND2 
6041  N N   . LEU C 14  ? 0.3230 0.5351 0.6302 0.0163  0.0876  0.0375  14  LEU C N   
6042  C CA  . LEU C 14  ? 0.3060 0.4842 0.6053 0.0068  0.0736  0.0442  14  LEU C CA  
6043  C C   . LEU C 14  ? 0.2841 0.4263 0.6068 -0.0057 0.0435  0.0239  14  LEU C C   
6044  O O   . LEU C 14  ? 0.2618 0.4022 0.6348 -0.0088 0.0408  0.0170  14  LEU C O   
6045  C CB  . LEU C 14  ? 0.2940 0.4749 0.6256 0.0080  0.0984  0.0740  14  LEU C CB  
6046  C CG  . LEU C 14  ? 0.2883 0.4417 0.6115 0.0013  0.0928  0.0846  14  LEU C CG  
6047  C CD1 . LEU C 14  ? 0.2816 0.4475 0.5456 0.0089  0.0968  0.0948  14  LEU C CD1 
6048  C CD2 . LEU C 14  ? 0.2761 0.4299 0.6572 0.0010  0.1178  0.1099  14  LEU C CD2 
6049  N N   . LEU C 15  ? 0.2881 0.4040 0.5726 -0.0115 0.0213  0.0153  15  LEU C N   
6050  C CA  . LEU C 15  ? 0.2845 0.3668 0.5751 -0.0210 -0.0095 -0.0019 15  LEU C CA  
6051  C C   . LEU C 15  ? 0.2875 0.3424 0.5661 -0.0280 -0.0168 0.0036  15  LEU C C   
6052  O O   . LEU C 15  ? 0.3070 0.3641 0.5575 -0.0257 -0.0035 0.0173  15  LEU C O   
6053  C CB  . LEU C 15  ? 0.2693 0.3454 0.5236 -0.0200 -0.0284 -0.0181 15  LEU C CB  
6054  C CG  . LEU C 15  ? 0.2777 0.3834 0.5387 -0.0121 -0.0188 -0.0273 15  LEU C CG  
6055  C CD1 . LEU C 15  ? 0.2771 0.3744 0.5057 -0.0116 -0.0351 -0.0423 15  LEU C CD1 
6056  C CD2 . LEU C 15  ? 0.2527 0.3655 0.5700 -0.0122 -0.0197 -0.0349 15  LEU C CD2 
6057  N N   . VAL C 16  ? 0.3006 0.3314 0.6017 -0.0357 -0.0387 -0.0086 16  VAL C N   
6058  C CA  . VAL C 16  ? 0.3472 0.3541 0.6450 -0.0422 -0.0448 -0.0084 16  VAL C CA  
6059  C C   . VAL C 16  ? 0.3778 0.3577 0.6497 -0.0468 -0.0778 -0.0267 16  VAL C C   
6060  O O   . VAL C 16  ? 0.3511 0.3294 0.6419 -0.0472 -0.0983 -0.0393 16  VAL C O   
6061  C CB  . VAL C 16  ? 0.3357 0.3442 0.7003 -0.0464 -0.0344 -0.0053 16  VAL C CB  
6062  C CG1 . VAL C 16  ? 0.3587 0.3429 0.7214 -0.0529 -0.0397 -0.0094 16  VAL C CG1 
6063  C CG2 . VAL C 16  ? 0.2780 0.3149 0.6722 -0.0399 0.0020  0.0186  16  VAL C CG2 
6064  N N   . LEU C 17  ? 0.3888 0.3495 0.6161 -0.0486 -0.0817 -0.0262 17  LEU C N   
6065  C CA  . LEU C 17  ? 0.3619 0.2977 0.5564 -0.0513 -0.1092 -0.0401 17  LEU C CA  
6066  C C   . LEU C 17  ? 0.3835 0.3010 0.5778 -0.0565 -0.1117 -0.0470 17  LEU C C   
6067  O O   . LEU C 17  ? 0.3890 0.3012 0.5623 -0.0569 -0.0949 -0.0380 17  LEU C O   
6068  C CB  . LEU C 17  ? 0.3368 0.2656 0.4739 -0.0476 -0.1109 -0.0352 17  LEU C CB  
6069  C CG  . LEU C 17  ? 0.3605 0.2643 0.4583 -0.0481 -0.1350 -0.0439 17  LEU C CG  
6070  C CD1 . LEU C 17  ? 0.4021 0.3061 0.5166 -0.0460 -0.1601 -0.0527 17  LEU C CD1 
6071  C CD2 . LEU C 17  ? 0.3642 0.2598 0.4132 -0.0453 -0.1291 -0.0354 17  LEU C CD2 
6072  N N   . PRO C 18  ? 0.3868 0.2969 0.6101 -0.0603 -0.1326 -0.0651 18  PRO C N   
6073  C CA  . PRO C 18  ? 0.4011 0.2942 0.6235 -0.0651 -0.1376 -0.0786 18  PRO C CA  
6074  C C   . PRO C 18  ? 0.4317 0.3047 0.5826 -0.0630 -0.1506 -0.0838 18  PRO C C   
6075  O O   . PRO C 18  ? 0.3872 0.2568 0.5017 -0.0585 -0.1689 -0.0841 18  PRO C O   
6076  C CB  . PRO C 18  ? 0.4282 0.3278 0.6947 -0.0653 -0.1563 -0.0972 18  PRO C CB  
6077  C CG  . PRO C 18  ? 0.3989 0.3183 0.7109 -0.0636 -0.1518 -0.0887 18  PRO C CG  
6078  C CD  . PRO C 18  ? 0.3833 0.3042 0.6539 -0.0605 -0.1500 -0.0756 18  PRO C CD  
6079  N N   . VAL C 19  ? 0.4560 0.3159 0.5900 -0.0654 -0.1384 -0.0856 19  VAL C N   
6080  C CA  . VAL C 19  ? 0.4600 0.3014 0.5277 -0.0629 -0.1453 -0.0895 19  VAL C CA  
6081  C C   . VAL C 19  ? 0.5046 0.3330 0.5790 -0.0668 -0.1525 -0.1136 19  VAL C C   
6082  O O   . VAL C 19  ? 0.5099 0.3431 0.6440 -0.0720 -0.1434 -0.1214 19  VAL C O   
6083  C CB  . VAL C 19  ? 0.4309 0.2696 0.4651 -0.0609 -0.1198 -0.0683 19  VAL C CB  
6084  C CG1 . VAL C 19  ? 0.4226 0.2785 0.4600 -0.0574 -0.1119 -0.0502 19  VAL C CG1 
6085  C CG2 . VAL C 19  ? 0.4734 0.3130 0.5395 -0.0644 -0.0946 -0.0626 19  VAL C CG2 
6086  N N   . GLN C 20  ? 0.5257 0.3397 0.5428 -0.0635 -0.1679 -0.1261 20  GLN C N   
6087  C CA  . GLN C 20  ? 0.5331 0.3433 0.5495 -0.0643 -0.1704 -0.1501 20  GLN C CA  
6088  C C   . GLN C 20  ? 0.5477 0.3362 0.5039 -0.0627 -0.1628 -0.1539 20  GLN C C   
6089  O O   . GLN C 20  ? 0.5667 0.3471 0.4649 -0.0573 -0.1635 -0.1390 20  GLN C O   
6090  C CB  . GLN C 20  ? 0.5697 0.3943 0.5803 -0.0587 -0.1964 -0.1661 20  GLN C CB  
6091  C CG  . GLN C 20  ? 0.6388 0.4649 0.6593 -0.0604 -0.2007 -0.1941 20  GLN C CG  
6092  C CD  . GLN C 20  ? 0.6772 0.5201 0.6999 -0.0549 -0.2278 -0.2095 20  GLN C CD  
6093  O OE1 . GLN C 20  ? 0.7163 0.5599 0.6944 -0.0500 -0.2417 -0.2257 20  GLN C OE1 
6094  N NE2 . GLN C 20  ? 0.6767 0.5342 0.7508 -0.0547 -0.2353 -0.2043 20  GLN C NE2 
6095  N N   . GLU C 21  ? 0.5674 0.3490 0.5420 -0.0667 -0.1507 -0.1712 21  GLU C N   
6096  C CA  . GLU C 21  ? 0.6235 0.3856 0.5450 -0.0644 -0.1421 -0.1795 21  GLU C CA  
6097  C C   . GLU C 21  ? 0.6717 0.4401 0.5413 -0.0575 -0.1608 -0.1995 21  GLU C C   
6098  O O   . GLU C 21  ? 0.6680 0.4531 0.5625 -0.0579 -0.1764 -0.2189 21  GLU C O   
6099  C CB  . GLU C 21  ? 0.6416 0.3954 0.6112 -0.0709 -0.1189 -0.1909 21  GLU C CB  
6100  C CG  . GLU C 21  ? 0.7006 0.4383 0.6272 -0.0685 -0.0965 -0.1869 21  GLU C CG  
6101  C CD  . GLU C 21  ? 0.7981 0.5262 0.7003 -0.0673 -0.1036 -0.2244 21  GLU C CD  
6102  O OE1 . GLU C 21  ? 0.8508 0.5955 0.7675 -0.0681 -0.1209 -0.2439 21  GLU C OE1 
6103  O OE2 . GLU C 21  ? 0.8080 0.5215 0.6773 -0.0650 -0.0851 -0.2264 21  GLU C OE2 
6104  N N   . ASP C 22  ? 0.6852 0.4408 0.4824 -0.0504 -0.1579 -0.1919 22  ASP C N   
6105  C CA  . ASP C 22  ? 0.7368 0.5000 0.4803 -0.0421 -0.1701 -0.2073 22  ASP C CA  
6106  C C   . ASP C 22  ? 0.7649 0.5175 0.4969 -0.0442 -0.1531 -0.2306 22  ASP C C   
6107  O O   . ASP C 22  ? 0.7871 0.5186 0.4962 -0.0438 -0.1307 -0.2203 22  ASP C O   
6108  C CB  . ASP C 22  ? 0.7730 0.5317 0.4478 -0.0313 -0.1733 -0.1804 22  ASP C CB  
6109  C CG  . ASP C 22  ? 0.8483 0.6155 0.4626 -0.0208 -0.1805 -0.1902 22  ASP C CG  
6110  O OD1 . ASP C 22  ? 0.9179 0.7058 0.5371 -0.0184 -0.2022 -0.2087 22  ASP C OD1 
6111  O OD2 . ASP C 22  ? 0.8302 0.5841 0.3911 -0.0147 -0.1636 -0.1767 22  ASP C OD2 
6112  N N   . ALA C 23  ? 0.7990 0.5640 0.5483 -0.0469 -0.1627 -0.2617 23  ALA C N   
6113  C CA  . ALA C 23  ? 0.8278 0.5816 0.5802 -0.0511 -0.1458 -0.2876 23  ALA C CA  
6114  C C   . ALA C 23  ? 0.8712 0.6180 0.5467 -0.0419 -0.1340 -0.2853 23  ALA C C   
6115  O O   . ALA C 23  ? 0.8695 0.5984 0.5407 -0.0430 -0.1089 -0.2893 23  ALA C O   
6116  C CB  . ALA C 23  ? 0.8326 0.5992 0.6103 -0.0541 -0.1627 -0.3198 23  ALA C CB  
6117  N N   . SER C 24  ? 0.8950 0.6567 0.5135 -0.0314 -0.1511 -0.2750 24  SER C N   
6118  C CA  . SER C 24  ? 0.9403 0.7005 0.4848 -0.0202 -0.1405 -0.2670 24  SER C CA  
6119  C C   . SER C 24  ? 0.8713 0.6067 0.3964 -0.0172 -0.1139 -0.2361 24  SER C C   
6120  O O   . SER C 24  ? 0.8925 0.6167 0.3909 -0.0143 -0.0905 -0.2398 24  SER C O   
6121  C CB  . SER C 24  ? 0.9987 0.7785 0.4959 -0.0091 -0.1636 -0.2521 24  SER C CB  
6122  O OG  . SER C 24  ? 1.0543 0.8323 0.4831 0.0025  -0.1496 -0.2355 24  SER C OG  
6123  N N   . THR C 25  ? 0.8384 0.5649 0.3779 -0.0191 -0.1163 -0.2054 25  THR C N   
6124  C CA  . THR C 25  ? 0.8237 0.5267 0.3408 -0.0187 -0.0921 -0.1721 25  THR C CA  
6125  C C   . THR C 25  ? 0.7965 0.4831 0.3667 -0.0308 -0.0717 -0.1683 25  THR C C   
6126  O O   . THR C 25  ? 0.7687 0.4476 0.3385 -0.0316 -0.0450 -0.1442 25  THR C O   
6127  C CB  . THR C 25  ? 0.7877 0.4939 0.2880 -0.0141 -0.1031 -0.1379 25  THR C CB  
6128  O OG1 . THR C 25  ? 0.7853 0.4997 0.3370 -0.0211 -0.1223 -0.1392 25  THR C OG1 
6129  C CG2 . THR C 25  ? 0.8347 0.5589 0.2897 -0.0010 -0.1184 -0.1329 25  THR C CG2 
6130  N N   . GLY C 26  ? 0.7648 0.4594 0.3994 -0.0391 -0.0815 -0.1857 26  GLY C N   
6131  C CA  . GLY C 26  ? 0.6795 0.3744 0.3812 -0.0479 -0.0592 -0.1727 26  GLY C CA  
6132  C C   . GLY C 26  ? 0.6628 0.3680 0.3836 -0.0492 -0.0587 -0.1382 26  GLY C C   
6133  O O   . GLY C 26  ? 0.6424 0.3523 0.4093 -0.0539 -0.0406 -0.1210 26  GLY C O   
6134  N N   . LEU C 27  ? 0.6544 0.3646 0.3395 -0.0439 -0.0791 -0.1288 27  LEU C N   
6135  C CA  . LEU C 27  ? 0.5986 0.3192 0.3000 -0.0443 -0.0814 -0.1012 27  LEU C CA  
6136  C C   . LEU C 27  ? 0.6287 0.3642 0.3733 -0.0476 -0.1034 -0.1087 27  LEU C C   
6137  O O   . LEU C 27  ? 0.6802 0.4180 0.4352 -0.0484 -0.1225 -0.1348 27  LEU C O   
6138  C CB  . LEU C 27  ? 0.7046 0.4206 0.3504 -0.0362 -0.0870 -0.0833 27  LEU C CB  
6139  C CG  . LEU C 27  ? 0.6997 0.4009 0.3021 -0.0319 -0.0636 -0.0721 27  LEU C CG  
6140  C CD1 . LEU C 27  ? 0.6918 0.3889 0.2476 -0.0231 -0.0697 -0.0523 27  LEU C CD1 
6141  C CD2 . LEU C 27  ? 0.6472 0.3498 0.2861 -0.0374 -0.0371 -0.0562 27  LEU C CD2 
6142  N N   . HIS C 28  ? 0.5740 0.3212 0.3444 -0.0488 -0.1010 -0.0872 28  HIS C N   
6143  C CA  . HIS C 28  ? 0.5631 0.3261 0.3795 -0.0516 -0.1165 -0.0900 28  HIS C CA  
6144  C C   . HIS C 28  ? 0.5803 0.3495 0.3792 -0.0465 -0.1339 -0.0778 28  HIS C C   
6145  O O   . HIS C 28  ? 0.5767 0.3419 0.3467 -0.0427 -0.1258 -0.0589 28  HIS C O   
6146  C CB  . HIS C 28  ? 0.4997 0.2752 0.3705 -0.0566 -0.0958 -0.0764 28  HIS C CB  
6147  C CG  . HIS C 28  ? 0.4747 0.2457 0.3798 -0.0613 -0.0801 -0.0867 28  HIS C CG  
6148  N ND1 . HIS C 28  ? 0.4961 0.2757 0.4633 -0.0661 -0.0808 -0.0960 28  HIS C ND1 
6149  C CD2 . HIS C 28  ? 0.4881 0.2459 0.3800 -0.0617 -0.0622 -0.0897 28  HIS C CD2 
6150  C CE1 . HIS C 28  ? 0.4841 0.2554 0.4772 -0.0693 -0.0637 -0.1034 28  HIS C CE1 
6151  N NE2 . HIS C 28  ? 0.4968 0.2549 0.4440 -0.0666 -0.0527 -0.1006 28  HIS C NE2 
6152  N N   . TRP C 29  ? 0.6078 0.3872 0.4332 -0.0467 -0.1571 -0.0891 29  TRP C N   
6153  C CA  . TRP C 29  ? 0.6129 0.3986 0.4300 -0.0412 -0.1763 -0.0795 29  TRP C CA  
6154  C C   . TRP C 29  ? 0.5687 0.3723 0.4467 -0.0447 -0.1873 -0.0848 29  TRP C C   
6155  O O   . TRP C 29  ? 0.5692 0.3790 0.4922 -0.0507 -0.1846 -0.0987 29  TRP C O   
6156  C CB  . TRP C 29  ? 0.6577 0.4360 0.4246 -0.0330 -0.2011 -0.0883 29  TRP C CB  
6157  C CG  . TRP C 29  ? 0.6494 0.4420 0.4409 -0.0326 -0.2146 -0.1139 29  TRP C CG  
6158  C CD1 . TRP C 29  ? 0.6672 0.4567 0.4546 -0.0354 -0.2087 -0.1354 29  TRP C CD1 
6159  C CD2 . TRP C 29  ? 0.6454 0.4580 0.4741 -0.0301 -0.2355 -0.1220 29  TRP C CD2 
6160  N NE1 . TRP C 29  ? 0.6722 0.4797 0.4921 -0.0354 -0.2253 -0.1575 29  TRP C NE1 
6161  C CE2 . TRP C 29  ? 0.6778 0.4992 0.5224 -0.0320 -0.2419 -0.1488 29  TRP C CE2 
6162  C CE3 . TRP C 29  ? 0.6496 0.4729 0.5022 -0.0264 -0.2488 -0.1102 29  TRP C CE3 
6163  C CZ2 . TRP C 29  ? 0.6963 0.5366 0.5783 -0.0304 -0.2618 -0.1630 29  TRP C CZ2 
6164  C CZ3 . TRP C 29  ? 0.6636 0.5048 0.5531 -0.0242 -0.2678 -0.1236 29  TRP C CZ3 
6165  C CH2 . TRP C 29  ? 0.6770 0.5265 0.5800 -0.0262 -0.2745 -0.1493 29  TRP C CH2 
6166  N N   . ALA C 30  ? 0.5626 0.3741 0.4470 -0.0407 -0.1977 -0.0732 30  ALA C N   
6167  C CA  . ALA C 30  ? 0.5825 0.4115 0.5237 -0.0426 -0.2082 -0.0776 30  ALA C CA  
6168  C C   . ALA C 30  ? 0.6003 0.4348 0.5362 -0.0340 -0.2307 -0.0734 30  ALA C C   
6169  O O   . ALA C 30  ? 0.6044 0.4279 0.4985 -0.0282 -0.2356 -0.0603 30  ALA C O   
6170  C CB  . ALA C 30  ? 0.5494 0.3915 0.5231 -0.0453 -0.1843 -0.0634 30  ALA C CB  
6171  N N   . ASN C 31  ? 0.6019 0.4526 0.5833 -0.0326 -0.2425 -0.0829 31  ASN C N   
6172  C CA  . ASN C 31  ? 0.6337 0.4917 0.6265 -0.0250 -0.2610 -0.0769 31  ASN C CA  
6173  C C   . ASN C 31  ? 0.6096 0.4759 0.6394 -0.0269 -0.2514 -0.0664 31  ASN C C   
6174  O O   . ASN C 31  ? 0.6039 0.4839 0.6817 -0.0323 -0.2386 -0.0711 31  ASN C O   
6175  C CB  . ASN C 31  ? 0.6227 0.4946 0.6516 -0.0226 -0.2776 -0.0928 31  ASN C CB  
6176  C CG  . ASN C 31  ? 0.6757 0.5444 0.6612 -0.0160 -0.2965 -0.1022 31  ASN C CG  
6177  O OD1 . ASN C 31  ? 0.6996 0.5601 0.6356 -0.0078 -0.3063 -0.0902 31  ASN C OD1 
6178  N ND2 . ASN C 31  ? 0.7039 0.5801 0.7079 -0.0192 -0.2998 -0.1236 31  ASN C ND2 
6179  N N   . ILE C 32  ? 0.6022 0.4612 0.6114 -0.0223 -0.2560 -0.0522 32  ILE C N   
6180  C CA  . ILE C 32  ? 0.5772 0.4462 0.6233 -0.0234 -0.2480 -0.0463 32  ILE C CA  
6181  C C   . ILE C 32  ? 0.5858 0.4618 0.6635 -0.0161 -0.2664 -0.0444 32  ILE C C   
6182  O O   . ILE C 32  ? 0.6205 0.4871 0.6716 -0.0083 -0.2858 -0.0374 32  ILE C O   
6183  C CB  . ILE C 32  ? 0.5540 0.4130 0.5695 -0.0218 -0.2314 -0.0318 32  ILE C CB  
6184  C CG1 . ILE C 32  ? 0.5446 0.3950 0.5232 -0.0266 -0.2111 -0.0306 32  ILE C CG1 
6185  C CG2 . ILE C 32  ? 0.4827 0.3571 0.5397 -0.0225 -0.2169 -0.0314 32  ILE C CG2 
6186  C CD1 . ILE C 32  ? 0.5119 0.3776 0.5190 -0.0330 -0.1906 -0.0367 32  ILE C CD1 
6187  N N   . HIS C 33  ? 0.5625 0.4559 0.6961 -0.0175 -0.2590 -0.0497 33  HIS C N   
6188  C CA  . HIS C 33  ? 0.5239 0.4239 0.6955 -0.0107 -0.2743 -0.0485 33  HIS C CA  
6189  C C   . HIS C 33  ? 0.4661 0.3647 0.6490 -0.0079 -0.2729 -0.0392 33  HIS C C   
6190  O O   . HIS C 33  ? 0.4132 0.3213 0.6139 -0.0124 -0.2529 -0.0429 33  HIS C O   
6191  C CB  . HIS C 33  ? 0.4769 0.3959 0.7072 -0.0126 -0.2662 -0.0595 33  HIS C CB  
6192  C CG  . HIS C 33  ? 0.4588 0.3803 0.6936 -0.0149 -0.2702 -0.0700 33  HIS C CG  
6193  N ND1 . HIS C 33  ? 0.4854 0.4057 0.7043 -0.0220 -0.2556 -0.0743 33  HIS C ND1 
6194  C CD2 . HIS C 33  ? 0.4607 0.3858 0.7180 -0.0112 -0.2879 -0.0785 33  HIS C CD2 
6195  C CE1 . HIS C 33  ? 0.4820 0.4053 0.7174 -0.0228 -0.2631 -0.0858 33  HIS C CE1 
6196  N NE2 . HIS C 33  ? 0.4697 0.3966 0.7271 -0.0162 -0.2832 -0.0894 33  HIS C NE2 
6197  N N   . LYS C 34  ? 0.4904 0.3790 0.6653 0.0005  -0.2938 -0.0272 34  LYS C N   
6198  C CA  . LYS C 34  ? 0.5141 0.3981 0.7035 0.0053  -0.2910 -0.0150 34  LYS C CA  
6199  C C   . LYS C 34  ? 0.5417 0.4268 0.7670 0.0150  -0.3130 -0.0063 34  LYS C C   
6200  O O   . LYS C 34  ? 0.5998 0.4856 0.8188 0.0180  -0.3281 -0.0079 34  LYS C O   
6201  C CB  . LYS C 34  ? 0.5347 0.3976 0.6654 0.0077  -0.2830 0.0016  34  LYS C CB  
6202  C CG  . LYS C 34  ? 0.5436 0.4038 0.6355 -0.0009 -0.2622 -0.0055 34  LYS C CG  
6203  C CD  . LYS C 34  ? 0.5151 0.3593 0.5723 0.0001  -0.2455 0.0082  34  LYS C CD  
6204  C CE  . LYS C 34  ? 0.4593 0.3090 0.5602 0.0003  -0.2311 0.0074  34  LYS C CE  
6205  N NZ  . LYS C 34  ? 0.4584 0.2885 0.5352 0.0045  -0.2238 0.0262  34  LYS C NZ  
6206  N N   . ARG C 35  ? 0.5262 0.4104 0.7885 0.0192  -0.3063 0.0010  35  ARG C N   
6207  C CA  . ARG C 35  ? 0.5184 0.3990 0.8134 0.0294  -0.3221 0.0154  35  ARG C CA  
6208  C C   . ARG C 35  ? 0.4519 0.3474 0.8036 0.0285  -0.3270 0.0018  35  ARG C C   
6209  O O   . ARG C 35  ? 0.4385 0.3465 0.8048 0.0220  -0.3194 -0.0170 35  ARG C O   
6210  C CB  . ARG C 35  ? 0.5070 0.3741 0.7457 0.0372  -0.3388 0.0363  35  ARG C CB  
6211  C CG  . ARG C 35  ? 0.5181 0.3673 0.7005 0.0388  -0.3289 0.0521  35  ARG C CG  
6212  C CD  . ARG C 35  ? 0.6677 0.5090 0.7821 0.0457  -0.3399 0.0674  35  ARG C CD  
6213  N NE  . ARG C 35  ? 0.6759 0.5022 0.7340 0.0428  -0.3254 0.0727  35  ARG C NE  
6214  C CZ  . ARG C 35  ? 0.7093 0.5273 0.7009 0.0487  -0.3261 0.0857  35  ARG C CZ  
6215  N NH1 . ARG C 35  ? 0.8000 0.6266 0.7715 0.0593  -0.3427 0.0949  35  ARG C NH1 
6216  N NH2 . ARG C 35  ? 0.6392 0.4429 0.5853 0.0451  -0.3094 0.0892  35  ARG C NH2 
6217  N N   . THR C 36  ? 0.4707 0.3639 0.8569 0.0356  -0.3355 0.0135  36  THR C N   
6218  C CA  . THR C 36  ? 0.4747 0.3788 0.9123 0.0362  -0.3434 0.0043  36  THR C CA  
6219  C C   . THR C 36  ? 0.5217 0.4221 0.9453 0.0455  -0.3676 0.0236  36  THR C C   
6220  O O   . THR C 36  ? 0.5424 0.4353 0.9665 0.0529  -0.3691 0.0456  36  THR C O   
6221  C CB  . THR C 36  ? 0.4534 0.3645 0.9618 0.0352  -0.3270 -0.0050 36  THR C CB  
6222  O OG1 . THR C 36  ? 0.4246 0.3450 0.9405 0.0291  -0.3032 -0.0238 36  THR C OG1 
6223  C CG2 . THR C 36  ? 0.4866 0.4072 1.0445 0.0352  -0.3325 -0.0155 36  THR C CG2 
6224  N N   . PRO C 37  ? 0.5422 0.4497 0.9529 0.0463  -0.3852 0.0160  37  PRO C N   
6225  C CA  . PRO C 37  ? 0.5240 0.4394 0.9384 0.0386  -0.3812 -0.0078 37  PRO C CA  
6226  C C   . PRO C 37  ? 0.5695 0.4797 0.9263 0.0331  -0.3718 -0.0127 37  PRO C C   
6227  O O   . PRO C 37  ? 0.5573 0.4572 0.8577 0.0367  -0.3762 0.0018  37  PRO C O   
6228  C CB  . PRO C 37  ? 0.5623 0.4854 0.9770 0.0442  -0.4070 -0.0099 37  PRO C CB  
6229  C CG  . PRO C 37  ? 0.6055 0.5250 0.9789 0.0554  -0.4248 0.0146  37  PRO C CG  
6230  C CD  . PRO C 37  ? 0.5920 0.5026 0.9860 0.0574  -0.4105 0.0325  37  PRO C CD  
6231  N N   . LEU C 38  ? 0.5393 0.4571 0.9122 0.0253  -0.3562 -0.0314 38  LEU C N   
6232  C CA  . LEU C 38  ? 0.5274 0.4426 0.8576 0.0187  -0.3425 -0.0370 38  LEU C CA  
6233  C C   . LEU C 38  ? 0.5354 0.4450 0.8115 0.0211  -0.3603 -0.0363 38  LEU C C   
6234  O O   . LEU C 38  ? 0.5332 0.4490 0.8200 0.0252  -0.3789 -0.0420 38  LEU C O   
6235  C CB  . LEU C 38  ? 0.5202 0.4490 0.8862 0.0119  -0.3217 -0.0536 38  LEU C CB  
6236  C CG  . LEU C 38  ? 0.4925 0.4248 0.8383 0.0043  -0.2963 -0.0573 38  LEU C CG  
6237  C CD1 . LEU C 38  ? 0.4585 0.3916 0.8077 0.0038  -0.2817 -0.0522 38  LEU C CD1 
6238  C CD2 . LEU C 38  ? 0.5031 0.4522 0.8904 -0.0001 -0.2788 -0.0697 38  LEU C CD2 
6239  N N   . MET C 39  ? 0.5100 0.4091 0.7285 0.0192  -0.3546 -0.0307 39  MET C N   
6240  C CA  . MET C 39  ? 0.5580 0.4539 0.7229 0.0216  -0.3672 -0.0340 39  MET C CA  
6241  C C   . MET C 39  ? 0.5554 0.4429 0.6787 0.0142  -0.3489 -0.0379 39  MET C C   
6242  O O   . MET C 39  ? 0.5411 0.4265 0.6753 0.0080  -0.3290 -0.0359 39  MET C O   
6243  C CB  . MET C 39  ? 0.5969 0.4875 0.7196 0.0334  -0.3861 -0.0146 39  MET C CB  
6244  C CG  . MET C 39  ? 0.6118 0.4883 0.7119 0.0369  -0.3758 0.0092  39  MET C CG  
6245  S SD  . MET C 39  ? 1.0219 0.8824 1.0490 0.0331  -0.3591 0.0129  39  MET C SD  
6246  C CE  . MET C 39  ? 0.8541 0.7185 0.8154 0.0445  -0.3770 0.0173  39  MET C CE  
6247  N N   . GLN C 40  ? 0.6085 0.4938 0.6869 0.0150  -0.3552 -0.0453 40  GLN C N   
6248  C CA  . GLN C 40  ? 0.6183 0.4953 0.6614 0.0077  -0.3372 -0.0505 40  GLN C CA  
6249  C C   . GLN C 40  ? 0.6210 0.4822 0.5941 0.0128  -0.3363 -0.0355 40  GLN C C   
6250  O O   . GLN C 40  ? 0.6479 0.5094 0.5830 0.0227  -0.3519 -0.0289 40  GLN C O   
6251  C CB  . GLN C 40  ? 0.6506 0.5364 0.7028 0.0033  -0.3386 -0.0730 40  GLN C CB  
6252  C CG  . GLN C 40  ? 0.6567 0.5560 0.7791 -0.0025 -0.3304 -0.0839 40  GLN C CG  
6253  C CD  . GLN C 40  ? 0.6953 0.6029 0.8387 -0.0070 -0.3305 -0.1046 40  GLN C CD  
6254  O OE1 . GLN C 40  ? 0.7027 0.6061 0.8319 -0.0135 -0.3158 -0.1107 40  GLN C OE1 
6255  N NE2 . GLN C 40  ? 0.7718 0.6912 0.9538 -0.0034 -0.3476 -0.1161 40  GLN C NE2 
6256  N N   . VAL C 41  ? 0.5896 0.4394 0.5465 0.0068  -0.3161 -0.0290 41  VAL C N   
6257  C CA  . VAL C 41  ? 0.6324 0.4652 0.5269 0.0106  -0.3089 -0.0142 41  VAL C CA  
6258  C C   . VAL C 41  ? 0.6084 0.4351 0.4780 0.0023  -0.2921 -0.0267 41  VAL C C   
6259  O O   . VAL C 41  ? 0.5497 0.3772 0.4439 -0.0072 -0.2759 -0.0313 41  VAL C O   
6260  C CB  . VAL C 41  ? 0.6486 0.4704 0.5470 0.0116  -0.2990 0.0069  41  VAL C CB  
6261  C CG1 . VAL C 41  ? 0.6889 0.4921 0.5256 0.0185  -0.2903 0.0274  41  VAL C CG1 
6262  C CG2 . VAL C 41  ? 0.6507 0.4803 0.5957 0.0177  -0.3120 0.0162  41  VAL C CG2 
6263  N N   . PRO C 42  ? 0.6706 0.4935 0.4924 0.0063  -0.2947 -0.0324 42  PRO C N   
6264  C CA  . PRO C 42  ? 0.6870 0.5023 0.4866 -0.0011 -0.2773 -0.0442 42  PRO C CA  
6265  C C   . PRO C 42  ? 0.6513 0.4468 0.4118 -0.0022 -0.2569 -0.0262 42  PRO C C   
6266  O O   . PRO C 42  ? 0.6718 0.4576 0.3878 0.0069  -0.2557 -0.0087 42  PRO C O   
6267  C CB  . PRO C 42  ? 0.7267 0.5479 0.4911 0.0052  -0.2888 -0.0581 42  PRO C CB  
6268  C CG  . PRO C 42  ? 0.7585 0.5855 0.5007 0.0185  -0.3070 -0.0422 42  PRO C CG  
6269  C CD  . PRO C 42  ? 0.7270 0.5580 0.5203 0.0179  -0.3145 -0.0318 42  PRO C CD  
6270  N N   . LEU C 43  ? 0.5574 0.3497 0.3372 -0.0125 -0.2380 -0.0294 43  LEU C N   
6271  C CA  . LEU C 43  ? 0.6103 0.3921 0.3731 -0.0138 -0.2100 -0.0123 43  LEU C CA  
6272  C C   . LEU C 43  ? 0.6150 0.3930 0.3718 -0.0215 -0.1874 -0.0211 43  LEU C C   
6273  O O   . LEU C 43  ? 0.6154 0.4031 0.4055 -0.0283 -0.1859 -0.0361 43  LEU C O   
6274  C CB  . LEU C 43  ? 0.5240 0.3153 0.3327 -0.0163 -0.2001 -0.0028 43  LEU C CB  
6275  C CG  . LEU C 43  ? 0.5098 0.3044 0.3382 -0.0092 -0.2169 0.0078  43  LEU C CG  
6276  C CD1 . LEU C 43  ? 0.4686 0.2757 0.3484 -0.0129 -0.2055 0.0083  43  LEU C CD1 
6277  C CD2 . LEU C 43  ? 0.5790 0.3565 0.3661 -0.0001 -0.2154 0.0297  43  LEU C CD2 
6278  N N   . LEU C 44  ? 0.6065 0.3707 0.3272 -0.0200 -0.1681 -0.0096 44  LEU C N   
6279  C CA  . LEU C 44  ? 0.5905 0.3508 0.3085 -0.0263 -0.1452 -0.0151 44  LEU C CA  
6280  C C   . LEU C 44  ? 0.5392 0.3135 0.3026 -0.0330 -0.1284 -0.0123 44  LEU C C   
6281  O O   . LEU C 44  ? 0.5078 0.2894 0.2897 -0.0322 -0.1251 -0.0021 44  LEU C O   
6282  C CB  . LEU C 44  ? 0.6376 0.3808 0.3099 -0.0221 -0.1279 -0.0021 44  LEU C CB  
6283  C CG  . LEU C 44  ? 0.6376 0.3765 0.3101 -0.0278 -0.1032 -0.0064 44  LEU C CG  
6284  C CD1 . LEU C 44  ? 0.6590 0.3923 0.3136 -0.0287 -0.1075 -0.0273 44  LEU C CD1 
6285  C CD2 . LEU C 44  ? 0.6398 0.3658 0.2863 -0.0247 -0.0820 0.0112  44  LEU C CD2 
6286  N N   . LEU C 45  ? 0.5748 0.3545 0.3579 -0.0387 -0.1180 -0.0220 45  LEU C N   
6287  C CA  . LEU C 45  ? 0.5200 0.3154 0.3381 -0.0427 -0.1000 -0.0160 45  LEU C CA  
6288  C C   . LEU C 45  ? 0.5331 0.3226 0.3329 -0.0423 -0.0789 -0.0047 45  LEU C C   
6289  O O   . LEU C 45  ? 0.5241 0.3010 0.3045 -0.0432 -0.0680 -0.0067 45  LEU C O   
6290  C CB  . LEU C 45  ? 0.4733 0.2771 0.3244 -0.0474 -0.0946 -0.0252 45  LEU C CB  
6291  C CG  . LEU C 45  ? 0.4690 0.2913 0.3496 -0.0487 -0.0740 -0.0143 45  LEU C CG  
6292  C CD1 . LEU C 45  ? 0.4353 0.2802 0.3406 -0.0468 -0.0771 -0.0092 45  LEU C CD1 
6293  C CD2 . LEU C 45  ? 0.4781 0.3037 0.3905 -0.0522 -0.0646 -0.0185 45  LEU C CD2 
6294  N N   . ASP C 46  ? 0.5633 0.3625 0.3733 -0.0409 -0.0737 0.0047  46  ASP C N   
6295  C CA  . ASP C 46  ? 0.5539 0.3508 0.3561 -0.0406 -0.0560 0.0140  46  ASP C CA  
6296  C C   . ASP C 46  ? 0.5130 0.3369 0.3486 -0.0414 -0.0475 0.0153  46  ASP C C   
6297  O O   . ASP C 46  ? 0.5321 0.3696 0.3849 -0.0399 -0.0520 0.0145  46  ASP C O   
6298  C CB  . ASP C 46  ? 0.5761 0.3599 0.3619 -0.0370 -0.0586 0.0225  46  ASP C CB  
6299  C CG  . ASP C 46  ? 0.5720 0.3518 0.3565 -0.0371 -0.0398 0.0313  46  ASP C CG  
6300  O OD1 . ASP C 46  ? 0.5842 0.3705 0.3747 -0.0393 -0.0259 0.0308  46  ASP C OD1 
6301  O OD2 . ASP C 46  ? 0.5891 0.3593 0.3713 -0.0344 -0.0384 0.0400  46  ASP C OD2 
6302  N N   . LEU C 47  ? 0.4766 0.3100 0.3222 -0.0426 -0.0351 0.0171  47  LEU C N   
6303  C CA  . LEU C 47  ? 0.4365 0.3005 0.3089 -0.0408 -0.0278 0.0206  47  LEU C CA  
6304  C C   . LEU C 47  ? 0.4205 0.2978 0.2977 -0.0386 -0.0252 0.0212  47  LEU C C   
6305  O O   . LEU C 47  ? 0.4167 0.3207 0.3127 -0.0359 -0.0284 0.0168  47  LEU C O   
6306  C CB  . LEU C 47  ? 0.4232 0.2925 0.3040 -0.0407 -0.0128 0.0280  47  LEU C CB  
6307  C CG  . LEU C 47  ? 0.4003 0.3044 0.3027 -0.0359 -0.0039 0.0366  47  LEU C CG  
6308  C CD1 . LEU C 47  ? 0.3980 0.3248 0.3197 -0.0336 -0.0088 0.0355  47  LEU C CD1 
6309  C CD2 . LEU C 47  ? 0.3801 0.2848 0.2917 -0.0347 0.0119  0.0483  47  LEU C CD2 
6310  N N   . ASN C 48  ? 0.4623 0.3221 0.3256 -0.0394 -0.0186 0.0247  48  ASN C N   
6311  C CA  . ASN C 48  ? 0.4085 0.2806 0.2864 -0.0381 -0.0151 0.0234  48  ASN C CA  
6312  C C   . ASN C 48  ? 0.4311 0.2919 0.3137 -0.0384 -0.0231 0.0198  48  ASN C C   
6313  O O   . ASN C 48  ? 0.4802 0.3490 0.3832 -0.0381 -0.0201 0.0163  48  ASN C O   
6314  C CB  . ASN C 48  ? 0.3745 0.2365 0.2469 -0.0387 -0.0001 0.0307  48  ASN C CB  
6315  C CG  . ASN C 48  ? 0.3899 0.2681 0.2687 -0.0370 0.0090  0.0362  48  ASN C CG  
6316  O OD1 . ASN C 48  ? 0.4082 0.3185 0.3041 -0.0334 0.0067  0.0356  48  ASN C OD1 
6317  N ND2 . ASN C 48  ? 0.3960 0.2530 0.2614 -0.0385 0.0204  0.0422  48  ASN C ND2 
6318  N N   . GLY C 49  ? 0.4359 0.2796 0.3054 -0.0384 -0.0337 0.0204  49  GLY C N   
6319  C CA  . GLY C 49  ? 0.4255 0.2569 0.3020 -0.0372 -0.0407 0.0217  49  GLY C CA  
6320  C C   . GLY C 49  ? 0.3890 0.2442 0.3042 -0.0363 -0.0469 0.0097  49  GLY C C   
6321  O O   . GLY C 49  ? 0.4200 0.2996 0.3475 -0.0356 -0.0522 -0.0001 49  GLY C O   
6322  N N   . LYS C 50  ? 0.3861 0.2347 0.3235 -0.0360 -0.0448 0.0099  50  LYS C N   
6323  C CA  . LYS C 50  ? 0.3850 0.2572 0.3653 -0.0354 -0.0496 -0.0070 50  LYS C CA  
6324  C C   . LYS C 50  ? 0.4147 0.2884 0.4105 -0.0334 -0.0628 -0.0126 50  LYS C C   
6325  O O   . LYS C 50  ? 0.4182 0.3173 0.4457 -0.0324 -0.0668 -0.0308 50  LYS C O   
6326  C CB  . LYS C 50  ? 0.3831 0.2478 0.3954 -0.0363 -0.0416 -0.0074 50  LYS C CB  
6327  C CG  . LYS C 50  ? 0.3484 0.2224 0.3641 -0.0381 -0.0299 -0.0091 50  LYS C CG  
6328  C CD  . LYS C 50  ? 0.4042 0.2736 0.4646 -0.0396 -0.0227 -0.0130 50  LYS C CD  
6329  C CE  . LYS C 50  ? 0.4345 0.3096 0.4993 -0.0414 -0.0108 -0.0119 50  LYS C CE  
6330  N NZ  . LYS C 50  ? 0.4911 0.3589 0.6072 -0.0435 -0.0020 -0.0146 50  LYS C NZ  
6331  N N   . HIS C 51  ? 0.4192 0.2679 0.3930 -0.0320 -0.0698 0.0019  51  HIS C N   
6332  C CA  . HIS C 51  ? 0.4105 0.2590 0.4001 -0.0294 -0.0839 -0.0006 51  HIS C CA  
6333  C C   . HIS C 51  ? 0.4137 0.2425 0.3677 -0.0274 -0.0946 0.0129  51  HIS C C   
6334  O O   . HIS C 51  ? 0.4287 0.2414 0.3440 -0.0277 -0.0900 0.0235  51  HIS C O   
6335  C CB  . HIS C 51  ? 0.4324 0.2723 0.4623 -0.0272 -0.0843 0.0006  51  HIS C CB  
6336  C CG  . HIS C 51  ? 0.4106 0.2200 0.4272 -0.0251 -0.0769 0.0239  51  HIS C CG  
6337  N ND1 . HIS C 51  ? 0.4048 0.2097 0.4408 -0.0270 -0.0615 0.0259  51  HIS C ND1 
6338  C CD2 . HIS C 51  ? 0.4323 0.2165 0.4189 -0.0200 -0.0820 0.0468  51  HIS C CD2 
6339  C CE1 . HIS C 51  ? 0.4520 0.2284 0.4715 -0.0234 -0.0543 0.0515  51  HIS C CE1 
6340  N NE2 . HIS C 51  ? 0.4298 0.1942 0.4150 -0.0183 -0.0669 0.0650  51  HIS C NE2 
6341  N N   . LEU C 52  ? 0.4110 0.2435 0.3810 -0.0249 -0.1094 0.0096  52  LEU C N   
6342  C CA  . LEU C 52  ? 0.4162 0.2331 0.3598 -0.0216 -0.1246 0.0198  52  LEU C CA  
6343  C C   . LEU C 52  ? 0.4525 0.2474 0.3919 -0.0154 -0.1282 0.0388  52  LEU C C   
6344  O O   . LEU C 52  ? 0.4565 0.2524 0.4364 -0.0133 -0.1272 0.0401  52  LEU C O   
6345  C CB  . LEU C 52  ? 0.3978 0.2305 0.3674 -0.0212 -0.1396 0.0086  52  LEU C CB  
6346  C CG  . LEU C 52  ? 0.4289 0.2534 0.3821 -0.0180 -0.1600 0.0126  52  LEU C CG  
6347  C CD1 . LEU C 52  ? 0.4343 0.2796 0.4153 -0.0212 -0.1657 -0.0028 52  LEU C CD1 
6348  C CD2 . LEU C 52  ? 0.4474 0.2615 0.4134 -0.0105 -0.1750 0.0246  52  LEU C CD2 
6349  N N   . TRP C 53  ? 0.4760 0.2518 0.3683 -0.0115 -0.1314 0.0540  53  TRP C N   
6350  C CA  . TRP C 53  ? 0.5115 0.2686 0.3955 -0.0027 -0.1353 0.0773  53  TRP C CA  
6351  C C   . TRP C 53  ? 0.5752 0.3258 0.4171 0.0046  -0.1559 0.0850  53  TRP C C   
6352  O O   . TRP C 53  ? 0.6156 0.3690 0.4237 0.0020  -0.1615 0.0734  53  TRP C O   
6353  C CB  . TRP C 53  ? 0.5059 0.2459 0.3738 -0.0017 -0.1132 0.0942  53  TRP C CB  
6354  C CG  . TRP C 53  ? 0.5208 0.2524 0.3356 -0.0032 -0.1028 0.0955  53  TRP C CG  
6355  C CD1 . TRP C 53  ? 0.5307 0.2696 0.3452 -0.0112 -0.0886 0.0819  53  TRP C CD1 
6356  C CD2 . TRP C 53  ? 0.5906 0.3056 0.3460 0.0047  -0.1043 0.1118  53  TRP C CD2 
6357  N NE1 . TRP C 53  ? 0.5553 0.2815 0.3193 -0.0098 -0.0801 0.0874  53  TRP C NE1 
6358  C CE2 . TRP C 53  ? 0.5975 0.3095 0.3225 -0.0002 -0.0892 0.1040  53  TRP C CE2 
6359  C CE3 . TRP C 53  ? 0.6461 0.3510 0.3700 0.0168  -0.1175 0.1320  53  TRP C CE3 
6360  C CZ2 . TRP C 53  ? 0.6400 0.3385 0.3045 0.0059  -0.0854 0.1120  53  TRP C CZ2 
6361  C CZ3 . TRP C 53  ? 0.6638 0.3579 0.3217 0.0240  -0.1151 0.1412  53  TRP C CZ3 
6362  C CH2 . TRP C 53  ? 0.6610 0.3516 0.2902 0.0181  -0.0986 0.1294  53  TRP C CH2 
6363  N N   . VAL C 54  ? 0.5831 0.3271 0.4328 0.0144  -0.1685 0.1034  54  VAL C N   
6364  C CA  . VAL C 54  ? 0.6249 0.3666 0.4357 0.0239  -0.1920 0.1117  54  VAL C CA  
6365  C C   . VAL C 54  ? 0.6916 0.4176 0.4876 0.0379  -0.1912 0.1470  54  VAL C C   
6366  O O   . VAL C 54  ? 0.6797 0.3992 0.5198 0.0392  -0.1786 0.1616  54  VAL C O   
6367  C CB  . VAL C 54  ? 0.6071 0.3668 0.4538 0.0229  -0.2167 0.0946  54  VAL C CB  
6368  C CG1 . VAL C 54  ? 0.5909 0.3535 0.4983 0.0265  -0.2195 0.1034  54  VAL C CG1 
6369  C CG2 . VAL C 54  ? 0.7073 0.4697 0.5126 0.0315  -0.2447 0.0951  54  VAL C CG2 
6370  N N   . THR C 55  ? 0.7781 0.5056 0.5188 0.0483  -0.1994 0.1575  55  THR C N   
6371  C CA  . THR C 55  ? 0.8523 0.5806 0.5821 0.0636  -0.1930 0.1897  55  THR C CA  
6372  C C   . THR C 55  ? 0.8573 0.5966 0.6274 0.0720  -0.2147 0.1978  55  THR C C   
6373  O O   . THR C 55  ? 0.8351 0.5893 0.6106 0.0707  -0.2409 0.1783  55  THR C O   
6374  C CB  . THR C 55  ? 0.9327 0.6702 0.5923 0.0727  -0.1919 0.1943  55  THR C CB  
6375  O OG1 . THR C 55  ? 0.9341 0.6865 0.5749 0.0696  -0.2180 0.1648  55  THR C OG1 
6376  C CG2 . THR C 55  ? 0.9240 0.6497 0.5528 0.0662  -0.1639 0.1921  55  THR C CG2 
6377  N N   . CYS C 56  ? 0.8716 0.6035 0.6795 0.0798  -0.2015 0.2250  56  CYS C N   
6378  C CA  . CYS C 56  ? 0.8798 0.6204 0.7345 0.0881  -0.2175 0.2343  56  CYS C CA  
6379  C C   . CYS C 56  ? 0.9993 0.7441 0.8274 0.1103  -0.2152 0.2712  56  CYS C C   
6380  O O   . CYS C 56  ? 1.0594 0.7881 0.8823 0.1194  -0.1884 0.2989  56  CYS C O   
6381  C CB  . CYS C 56  ? 0.8128 0.5443 0.7486 0.0795  -0.2049 0.2306  56  CYS C CB  
6382  S SG  . CYS C 56  ? 0.8030 0.5391 0.7803 0.0590  -0.2128 0.1877  56  CYS C SG  
6383  N N   . SER C 57  ? 1.0382 0.8039 0.8461 0.1207  -0.2420 0.2714  57  SER C N   
6384  C CA  . SER C 57  ? 1.1422 0.9154 0.9203 0.1450  -0.2406 0.3080  57  SER C CA  
6385  C C   . SER C 57  ? 1.1903 0.9652 1.0271 0.1525  -0.2543 0.3170  57  SER C C   
6386  O O   . SER C 57  ? 1.1488 0.9216 1.0510 0.1372  -0.2609 0.2952  57  SER C O   
6387  C CB  . SER C 57  ? 1.1818 0.9850 0.8931 0.1533  -0.2606 0.3051  57  SER C CB  
6388  O OG  . SER C 57  ? 1.1733 0.9964 0.9015 0.1504  -0.2952 0.2803  57  SER C OG  
6389  N N   . GLN C 58  ? 1.2641 1.0441 1.0775 0.1770  -0.2584 0.3485  58  GLN C N   
6390  C CA  . GLN C 58  ? 1.2450 1.0297 1.1090 0.1861  -0.2748 0.3586  58  GLN C CA  
6391  C C   . GLN C 58  ? 1.2207 1.0340 1.1115 0.1765  -0.3091 0.3283  58  GLN C C   
6392  O O   . GLN C 58  ? 1.1810 0.9970 1.1376 0.1738  -0.3198 0.3241  58  GLN C O   
6393  C CB  . GLN C 58  ? 1.2973 1.0794 1.1101 0.2172  -0.2769 0.3962  58  GLN C CB  
6394  C CG  . GLN C 58  ? 1.3051 1.1245 1.0411 0.2299  -0.2927 0.3952  58  GLN C CG  
6395  C CD  . GLN C 58  ? 1.3861 1.1954 1.0494 0.2609  -0.2896 0.4261  58  GLN C CD  
6396  O OE1 . GLN C 58  ? 1.4371 1.1847 1.0934 0.2674  -0.2854 0.4484  58  GLN C OE1 
6397  N NE2 . GLN C 58  ? 1.3992 1.2738 1.0253 0.2616  -0.2988 0.4290  58  GLN C NE2 
6398  N N   . HIS C 59  ? 1.2340 1.0662 1.0778 0.1695  -0.3248 0.3039  59  HIS C N   
6399  C CA  . HIS C 59  ? 1.2179 1.0722 1.0817 0.1611  -0.3571 0.2720  59  HIS C CA  
6400  C C   . HIS C 59  ? 1.1365 0.9811 1.0422 0.1359  -0.3574 0.2324  59  HIS C C   
6401  O O   . HIS C 59  ? 1.1459 1.0041 1.0529 0.1267  -0.3775 0.2007  59  HIS C O   
6402  C CB  . HIS C 59  ? 1.2659 1.1478 1.0612 0.1683  -0.3763 0.2641  59  HIS C CB  
6403  C CG  . HIS C 59  ? 1.3422 1.2446 1.0956 0.1953  -0.3791 0.3042  59  HIS C CG  
6404  N ND1 . HIS C 59  ? 1.4008 1.3310 1.0848 0.2020  -0.3875 0.3079  59  HIS C ND1 
6405  C CD2 . HIS C 59  ? 1.3783 1.2792 1.1509 0.2177  -0.3759 0.3416  59  HIS C CD2 
6406  C CE1 . HIS C 59  ? 1.4637 1.4151 1.1260 0.2269  -0.3887 0.3509  59  HIS C CE1 
6407  N NE2 . HIS C 59  ? 1.4524 1.3824 1.1636 0.2409  -0.3805 0.3714  59  HIS C NE2 
6408  N N   . TYR C 60  ? 1.0413 0.8633 0.9841 0.1260  -0.3333 0.2349  60  TYR C N   
6409  C CA  . TYR C 60  ? 0.9037 0.7204 0.9004 0.1062  -0.3317 0.2035  60  TYR C CA  
6410  C C   . TYR C 60  ? 0.8344 0.6625 0.9029 0.1074  -0.3463 0.1995  60  TYR C C   
6411  O O   . TYR C 60  ? 0.8237 0.6481 0.9267 0.1174  -0.3395 0.2245  60  TYR C O   
6412  C CB  . TYR C 60  ? 0.8538 0.6487 0.8709 0.0972  -0.3018 0.2075  60  TYR C CB  
6413  C CG  . TYR C 60  ? 0.7518 0.5453 0.8170 0.0791  -0.2975 0.1753  60  TYR C CG  
6414  C CD1 . TYR C 60  ? 0.7171 0.5208 0.8565 0.0747  -0.3046 0.1600  60  TYR C CD1 
6415  C CD2 . TYR C 60  ? 0.7158 0.4989 0.7538 0.0685  -0.2836 0.1620  60  TYR C CD2 
6416  C CE1 . TYR C 60  ? 0.6508 0.4576 0.8320 0.0619  -0.2979 0.1315  60  TYR C CE1 
6417  C CE2 . TYR C 60  ? 0.6671 0.4522 0.7463 0.0558  -0.2790 0.1353  60  TYR C CE2 
6418  C CZ  . TYR C 60  ? 0.6351 0.4333 0.7849 0.0535  -0.2857 0.1202  60  TYR C CZ  
6419  O OH  . TYR C 60  ? 0.5896 0.3974 0.7754 0.0421  -0.2740 0.0911  60  TYR C OH  
6420  N N   . SER C 61  ? 0.7731 0.7982 0.6832 0.0673  -0.3716 -0.1405 61  SER C N   
6421  C CA  . SER C 61  ? 0.7924 0.8348 0.7443 0.0715  -0.3821 -0.1266 61  SER C CA  
6422  C C   . SER C 61  ? 0.7796 0.8104 0.7945 0.0588  -0.3705 -0.1238 61  SER C C   
6423  O O   . SER C 61  ? 0.8046 0.8338 0.8601 0.0426  -0.3672 -0.1435 61  SER C O   
6424  C CB  . SER C 61  ? 0.8244 0.9057 0.7973 0.0716  -0.4049 -0.1461 61  SER C CB  
6425  O OG  . SER C 61  ? 0.8105 0.9118 0.8291 0.0755  -0.4128 -0.1338 61  SER C OG  
6426  N N   . SER C 62  ? 0.7345 0.7568 0.7577 0.0661  -0.3626 -0.0980 62  SER C N   
6427  C CA  . SER C 62  ? 0.6709 0.6913 0.7527 0.0549  -0.3502 -0.0932 62  SER C CA  
6428  C C   . SER C 62  ? 0.6505 0.6725 0.7426 0.0679  -0.3451 -0.0685 62  SER C C   
6429  O O   . SER C 62  ? 0.6596 0.6582 0.7080 0.0806  -0.3394 -0.0494 62  SER C O   
6430  C CB  . SER C 62  ? 0.5302 0.5208 0.6093 0.0416  -0.3318 -0.0949 62  SER C CB  
6431  O OG  . SER C 62  ? 0.5252 0.5210 0.6601 0.0309  -0.3192 -0.0864 62  SER C OG  
6432  N N   . SER C 63  ? 0.6161 0.6650 0.7686 0.0639  -0.3443 -0.0691 63  SER C N   
6433  C CA  . SER C 63  ? 0.6000 0.6549 0.7707 0.0772  -0.3371 -0.0508 63  SER C CA  
6434  C C   . SER C 63  ? 0.6037 0.6416 0.7896 0.0699  -0.3143 -0.0414 63  SER C C   
6435  O O   . SER C 63  ? 0.6056 0.6475 0.8088 0.0805  -0.3046 -0.0298 63  SER C O   
6436  C CB  . SER C 63  ? 0.5639 0.6637 0.7922 0.0779  -0.3447 -0.0568 63  SER C CB  
6437  O OG  . SER C 63  ? 0.5036 0.6219 0.7857 0.0562  -0.3344 -0.0663 63  SER C OG  
6438  N N   . THR C 64  ? 0.5745 0.5955 0.7556 0.0527  -0.3054 -0.0476 64  THR C N   
6439  C CA  . THR C 64  ? 0.5172 0.5250 0.7069 0.0441  -0.2764 -0.0370 64  THR C CA  
6440  C C   . THR C 64  ? 0.5253 0.4915 0.6559 0.0427  -0.2595 -0.0310 64  THR C C   
6441  O O   . THR C 64  ? 0.5063 0.4606 0.6365 0.0343  -0.2343 -0.0241 64  THR C O   
6442  C CB  . THR C 64  ? 0.4456 0.4733 0.6889 0.0222  -0.2673 -0.0430 64  THR C CB  
6443  O OG1 . THR C 64  ? 0.4574 0.4809 0.7032 0.0108  -0.2847 -0.0606 64  THR C OG1 
6444  C CG2 . THR C 64  ? 0.3929 0.4665 0.6986 0.0222  -0.2709 -0.0420 64  THR C CG2 
6445  N N   . TYR C 65  ? 0.5062 0.4557 0.5864 0.0515  -0.2732 -0.0329 65  TYR C N   
6446  C CA  . TYR C 65  ? 0.5084 0.4257 0.5357 0.0492  -0.2568 -0.0277 65  TYR C CA  
6447  C C   . TYR C 65  ? 0.5403 0.4359 0.5447 0.0578  -0.2394 -0.0071 65  TYR C C   
6448  O O   . TYR C 65  ? 0.5599 0.4559 0.5633 0.0730  -0.2501 0.0034  65  TYR C O   
6449  C CB  . TYR C 65  ? 0.5573 0.4710 0.5368 0.0553  -0.2757 -0.0366 65  TYR C CB  
6450  C CG  . TYR C 65  ? 0.5705 0.4572 0.4906 0.0561  -0.2588 -0.0273 65  TYR C CG  
6451  C CD1 . TYR C 65  ? 0.5411 0.4178 0.4511 0.0443  -0.2429 -0.0386 65  TYR C CD1 
6452  C CD2 . TYR C 65  ? 0.6009 0.4729 0.4787 0.0685  -0.2584 -0.0055 65  TYR C CD2 
6453  C CE1 . TYR C 65  ? 0.5612 0.4204 0.4209 0.0446  -0.2262 -0.0308 65  TYR C CE1 
6454  C CE2 . TYR C 65  ? 0.6180 0.4691 0.4455 0.0662  -0.2411 0.0052  65  TYR C CE2 
6455  C CZ  . TYR C 65  ? 0.5884 0.4362 0.4073 0.0540  -0.2246 -0.0086 65  TYR C CZ  
6456  O OH  . TYR C 65  ? 0.6249 0.4588 0.3972 0.0515  -0.2066 0.0015  65  TYR C OH  
6457  N N   . GLN C 66  ? 0.5332 0.4095 0.5217 0.0486  -0.2142 -0.0027 66  GLN C N   
6458  C CA  . GLN C 66  ? 0.5779 0.4293 0.5422 0.0523  -0.1965 0.0130  66  GLN C CA  
6459  C C   . GLN C 66  ? 0.5789 0.4114 0.5038 0.0425  -0.1789 0.0143  66  GLN C C   
6460  O O   . GLN C 66  ? 0.6050 0.4452 0.5360 0.0324  -0.1732 0.0025  66  GLN C O   
6461  C CB  . GLN C 66  ? 0.6487 0.5073 0.6512 0.0496  -0.1791 0.0141  66  GLN C CB  
6462  C CG  . GLN C 66  ? 0.7600 0.6360 0.8014 0.0618  -0.1878 0.0146  66  GLN C CG  
6463  C CD  . GLN C 66  ? 0.8145 0.7038 0.8878 0.0573  -0.1665 0.0110  66  GLN C CD  
6464  O OE1 . GLN C 66  ? 0.8425 0.7136 0.8978 0.0519  -0.1477 0.0131  66  GLN C OE1 
6465  N NE2 . GLN C 66  ? 0.8267 0.7527 0.9477 0.0592  -0.1692 0.0047  66  GLN C NE2 
6466  N N   . ALA C 67  ? 0.5558 0.3639 0.4447 0.0454  -0.1699 0.0295  67  ALA C N   
6467  C CA  . ALA C 67  ? 0.5314 0.3264 0.3905 0.0344  -0.1486 0.0318  67  ALA C CA  
6468  C C   . ALA C 67  ? 0.5087 0.2915 0.3833 0.0282  -0.1275 0.0377  67  ALA C C   
6469  O O   . ALA C 67  ? 0.5319 0.2937 0.4020 0.0338  -0.1270 0.0509  67  ALA C O   
6470  C CB  . ALA C 67  ? 0.5518 0.3333 0.3574 0.0380  -0.1518 0.0447  67  ALA C CB  
6471  N N   . PRO C 68  ? 0.4830 0.2794 0.3788 0.0176  -0.1119 0.0273  68  PRO C N   
6472  C CA  . PRO C 68  ? 0.4922 0.2832 0.4024 0.0123  -0.0943 0.0287  68  PRO C CA  
6473  C C   . PRO C 68  ? 0.5345 0.2977 0.4145 0.0070  -0.0826 0.0404  68  PRO C C   
6474  O O   . PRO C 68  ? 0.5611 0.3186 0.4065 0.0022  -0.0791 0.0465  68  PRO C O   
6475  C CB  . PRO C 68  ? 0.3738 0.1886 0.3008 0.0024  -0.0815 0.0182  68  PRO C CB  
6476  C CG  . PRO C 68  ? 0.3920 0.2237 0.3354 0.0051  -0.0953 0.0123  68  PRO C CG  
6477  C CD  . PRO C 68  ? 0.4361 0.2546 0.3510 0.0120  -0.1122 0.0144  68  PRO C CD  
6478  N N   . PHE C 69  ? 0.5372 0.2846 0.4329 0.0071  -0.0759 0.0424  69  PHE C N   
6479  C CA  . PHE C 69  ? 0.5475 0.2645 0.4227 -0.0007 -0.0651 0.0550  69  PHE C CA  
6480  C C   . PHE C 69  ? 0.5252 0.2557 0.3996 -0.0179 -0.0448 0.0460  69  PHE C C   
6481  O O   . PHE C 69  ? 0.4904 0.2499 0.3857 -0.0207 -0.0396 0.0303  69  PHE C O   
6482  C CB  . PHE C 69  ? 0.6059 0.2940 0.5030 0.0062  -0.0672 0.0586  69  PHE C CB  
6483  C CG  . PHE C 69  ? 0.5845 0.2900 0.5222 0.0066  -0.0604 0.0363  69  PHE C CG  
6484  C CD1 . PHE C 69  ? 0.5915 0.3008 0.5382 -0.0081 -0.0429 0.0238  69  PHE C CD1 
6485  C CD2 . PHE C 69  ? 0.5264 0.2492 0.4933 0.0218  -0.0716 0.0269  69  PHE C CD2 
6486  C CE1 . PHE C 69  ? 0.5231 0.2546 0.5023 -0.0067 -0.0372 0.0013  69  PHE C CE1 
6487  C CE2 . PHE C 69  ? 0.5037 0.2494 0.5039 0.0229  -0.0636 0.0061  69  PHE C CE2 
6488  C CZ  . PHE C 69  ? 0.4990 0.2492 0.5030 0.0091  -0.0467 -0.0071 69  PHE C CZ  
6489  N N   . CYS C 70  ? 0.5616 0.2742 0.4128 -0.0294 -0.0334 0.0579  70  CYS C N   
6490  C CA  . CYS C 70  ? 0.5528 0.2823 0.4049 -0.0459 -0.0149 0.0496  70  CYS C CA  
6491  C C   . CYS C 70  ? 0.5482 0.2852 0.4363 -0.0510 -0.0078 0.0320  70  CYS C C   
6492  O O   . CYS C 70  ? 0.4701 0.1837 0.3763 -0.0467 -0.0118 0.0308  70  CYS C O   
6493  C CB  . CYS C 70  ? 0.5962 0.3065 0.4226 -0.0593 -0.0028 0.0675  70  CYS C CB  
6494  S SG  . CYS C 70  ? 0.6735 0.4199 0.4936 -0.0758 0.0172  0.0577  70  CYS C SG  
6495  N N   . HIS C 71  ? 0.5019 0.2747 0.4005 -0.0578 0.0012  0.0172  71  HIS C N   
6496  C CA  . HIS C 71  ? 0.4529 0.2467 0.3809 -0.0627 0.0081  -0.0023 71  HIS C CA  
6497  C C   . HIS C 71  ? 0.4400 0.2492 0.3904 -0.0492 -0.0010 -0.0123 71  HIS C C   
6498  O O   . HIS C 71  ? 0.4579 0.2847 0.4304 -0.0509 0.0038  -0.0294 71  HIS C O   
6499  C CB  . HIS C 71  ? 0.4746 0.2423 0.4146 -0.0748 0.0160  -0.0067 71  HIS C CB  
6500  C CG  . HIS C 71  ? 0.4995 0.2498 0.4206 -0.0908 0.0265  0.0079  71  HIS C CG  
6501  N ND1 . HIS C 71  ? 0.4953 0.2774 0.4092 -0.1026 0.0381  0.0048  71  HIS C ND1 
6502  C CD2 . HIS C 71  ? 0.5554 0.2634 0.4637 -0.0964 0.0277  0.0283  71  HIS C CD2 
6503  C CE1 . HIS C 71  ? 0.5235 0.2871 0.4213 -0.1162 0.0476  0.0210  71  HIS C CE1 
6504  N NE2 . HIS C 71  ? 0.5713 0.2889 0.4642 -0.1136 0.0419  0.0374  71  HIS C NE2 
6505  N N   . SER C 72  ? 0.4148 0.2223 0.3606 -0.0365 -0.0137 -0.0034 72  SER C N   
6506  C CA  . SER C 72  ? 0.4027 0.2321 0.3728 -0.0251 -0.0211 -0.0106 72  SER C CA  
6507  C C   . SER C 72  ? 0.4008 0.2739 0.3813 -0.0279 -0.0156 -0.0163 72  SER C C   
6508  O O   . SER C 72  ? 0.4001 0.2836 0.3687 -0.0356 -0.0093 -0.0142 72  SER C O   
6509  C CB  . SER C 72  ? 0.4001 0.2173 0.3666 -0.0129 -0.0375 0.0004  72  SER C CB  
6510  O OG  . SER C 72  ? 0.4308 0.2524 0.3781 -0.0152 -0.0412 0.0077  72  SER C OG  
6511  N N   . THR C 73  ? 0.4027 0.3037 0.4069 -0.0209 -0.0177 -0.0218 73  THR C N   
6512  C CA  . THR C 73  ? 0.3612 0.3038 0.3766 -0.0225 -0.0135 -0.0203 73  THR C CA  
6513  C C   . THR C 73  ? 0.3744 0.3122 0.3840 -0.0223 -0.0210 -0.0069 73  THR C C   
6514  O O   . THR C 73  ? 0.3531 0.3120 0.3651 -0.0256 -0.0168 -0.0023 73  THR C O   
6515  C CB  . THR C 73  ? 0.3391 0.3159 0.3809 -0.0155 -0.0130 -0.0254 73  THR C CB  
6516  O OG1 . THR C 73  ? 0.3634 0.3253 0.4165 -0.0065 -0.0247 -0.0211 73  THR C OG1 
6517  C CG2 . THR C 73  ? 0.3251 0.3157 0.3743 -0.0148 -0.0043 -0.0457 73  THR C CG2 
6518  N N   . GLN C 74  ? 0.4036 0.3149 0.4074 -0.0172 -0.0334 -0.0018 74  GLN C N   
6519  C CA  . GLN C 74  ? 0.3818 0.2861 0.3796 -0.0172 -0.0421 0.0046  74  GLN C CA  
6520  C C   . GLN C 74  ? 0.3645 0.2579 0.3365 -0.0222 -0.0359 0.0039  74  GLN C C   
6521  O O   . GLN C 74  ? 0.3466 0.2478 0.3215 -0.0226 -0.0364 0.0050  74  GLN C O   
6522  C CB  . GLN C 74  ? 0.3688 0.2527 0.3635 -0.0103 -0.0587 0.0065  74  GLN C CB  
6523  C CG  . GLN C 74  ? 0.3472 0.2492 0.3741 -0.0050 -0.0662 0.0068  74  GLN C CG  
6524  C CD  . GLN C 74  ? 0.4029 0.2969 0.4328 0.0028  -0.0670 0.0034  74  GLN C CD  
6525  O OE1 . GLN C 74  ? 0.4504 0.3310 0.4667 0.0011  -0.0574 0.0000  74  GLN C OE1 
6526  N NE2 . GLN C 74  ? 0.4296 0.3315 0.4815 0.0115  -0.0791 0.0032  74  GLN C NE2 
6527  N N   . CYS C 75  ? 0.3931 0.2686 0.3430 -0.0258 -0.0296 0.0026  75  CYS C N   
6528  C CA  . CYS C 75  ? 0.3824 0.2549 0.3100 -0.0318 -0.0208 0.0019  75  CYS C CA  
6529  C C   . CYS C 75  ? 0.3833 0.2862 0.3237 -0.0369 -0.0091 -0.0027 75  CYS C C   
6530  O O   . CYS C 75  ? 0.3829 0.2956 0.3178 -0.0370 -0.0053 -0.0039 75  CYS C O   
6531  C CB  . CYS C 75  ? 0.3808 0.2289 0.2862 -0.0374 -0.0153 0.0056  75  CYS C CB  
6532  S SG  . CYS C 75  ? 0.5625 0.3793 0.4462 -0.0287 -0.0309 0.0160  75  CYS C SG  
6533  N N   . SER C 76  ? 0.3864 0.3076 0.3444 -0.0391 -0.0043 -0.0067 76  SER C N   
6534  C CA  . SER C 76  ? 0.3472 0.3049 0.3170 -0.0422 0.0043  -0.0105 76  SER C CA  
6535  C C   . SER C 76  ? 0.3321 0.3074 0.3145 -0.0356 -0.0004 -0.0016 76  SER C C   
6536  O O   . SER C 76  ? 0.3712 0.3616 0.3537 -0.0349 0.0033  -0.0005 76  SER C O   
6537  C CB  . SER C 76  ? 0.3570 0.3359 0.3418 -0.0437 0.0082  -0.0191 76  SER C CB  
6538  O OG  . SER C 76  ? 0.3703 0.3904 0.3627 -0.0462 0.0150  -0.0234 76  SER C OG  
6539  N N   . ARG C 77  ? 0.3244 0.2965 0.3209 -0.0306 -0.0092 0.0053  77  ARG C N   
6540  C CA  . ARG C 77  ? 0.3195 0.3028 0.3344 -0.0266 -0.0140 0.0165  77  ARG C CA  
6541  C C   . ARG C 77  ? 0.3547 0.3167 0.3627 -0.0233 -0.0192 0.0153  77  ARG C C   
6542  O O   . ARG C 77  ? 0.3167 0.2890 0.3377 -0.0196 -0.0191 0.0215  77  ARG C O   
6543  C CB  . ARG C 77  ? 0.3389 0.3222 0.3744 -0.0252 -0.0221 0.0233  77  ARG C CB  
6544  C CG  . ARG C 77  ? 0.3625 0.3593 0.4237 -0.0246 -0.0251 0.0389  77  ARG C CG  
6545  C CD  . ARG C 77  ? 0.4141 0.4164 0.5017 -0.0264 -0.0316 0.0471  77  ARG C CD  
6546  N NE  . ARG C 77  ? 0.4813 0.4924 0.5959 -0.0286 -0.0331 0.0659  77  ARG C NE  
6547  C CZ  . ARG C 77  ? 0.4977 0.5086 0.6436 -0.0333 -0.0399 0.0766  77  ARG C CZ  
6548  N NH1 . ARG C 77  ? 0.4927 0.5007 0.6469 -0.0350 -0.0468 0.0684  77  ARG C NH1 
6549  N NH2 . ARG C 77  ? 0.5013 0.5157 0.6736 -0.0366 -0.0401 0.0969  77  ARG C NH2 
6550  N N   . ALA C 78  ? 0.3909 0.3251 0.3782 -0.0230 -0.0239 0.0070  78  ALA C N   
6551  C CA  . ALA C 78  ? 0.3790 0.2970 0.3545 -0.0187 -0.0281 0.0001  78  ALA C CA  
6552  C C   . ALA C 78  ? 0.3892 0.3194 0.3507 -0.0191 -0.0161 -0.0055 78  ALA C C   
6553  O O   . ALA C 78  ? 0.4411 0.3662 0.3961 -0.0134 -0.0170 -0.0135 78  ALA C O   
6554  C CB  . ALA C 78  ? 0.3717 0.2644 0.3243 -0.0178 -0.0369 -0.0060 78  ALA C CB  
6555  N N   . ASN C 79  ? 0.3958 0.3455 0.3557 -0.0257 -0.0050 -0.0041 79  ASN C N   
6556  C CA  . ASN C 79  ? 0.4400 0.4093 0.3922 -0.0290 0.0073  -0.0099 79  ASN C CA  
6557  C C   . ASN C 79  ? 0.4732 0.4275 0.3972 -0.0334 0.0132  -0.0161 79  ASN C C   
6558  O O   . ASN C 79  ? 0.4890 0.4562 0.4071 -0.0311 0.0201  -0.0225 79  ASN C O   
6559  C CB  . ASN C 79  ? 0.5178 0.5067 0.4878 -0.0193 0.0067  -0.0092 79  ASN C CB  
6560  C CG  . ASN C 79  ? 0.6037 0.6261 0.5757 -0.0214 0.0182  -0.0142 79  ASN C CG  
6561  O OD1 . ASN C 79  ? 0.6566 0.6948 0.6250 -0.0323 0.0260  -0.0170 79  ASN C OD1 
6562  N ND2 . ASN C 79  ? 0.6425 0.6766 0.6238 -0.0105 0.0186  -0.0177 79  ASN C ND2 
6563  N N   . THR C 80  ? 0.5257 0.4549 0.4328 -0.0385 0.0104  -0.0127 80  THR C N   
6564  C CA  . THR C 80  ? 0.5838 0.5002 0.4619 -0.0448 0.0175  -0.0117 80  THR C CA  
6565  C C   . THR C 80  ? 0.5821 0.4840 0.4566 -0.0564 0.0228  -0.0053 80  THR C C   
6566  O O   . THR C 80  ? 0.5591 0.4419 0.4389 -0.0539 0.0136  -0.0011 80  THR C O   
6567  C CB  . THR C 80  ? 0.6553 0.5497 0.5094 -0.0369 0.0066  -0.0110 80  THR C CB  
6568  O OG1 . THR C 80  ? 0.7505 0.6331 0.5739 -0.0443 0.0140  -0.0029 80  THR C OG1 
6569  C CG2 . THR C 80  ? 0.6197 0.4954 0.4840 -0.0309 -0.0103 -0.0072 80  THR C CG2 
6570  N N   . HIS C 81  ? 0.6156 0.5264 0.4845 -0.0692 0.0375  -0.0052 81  HIS C N   
6571  C CA  . HIS C 81  ? 0.6472 0.5384 0.5167 -0.0828 0.0435  0.0005  81  HIS C CA  
6572  C C   . HIS C 81  ? 0.6338 0.5091 0.4756 -0.0919 0.0525  0.0134  81  HIS C C   
6573  O O   . HIS C 81  ? 0.6661 0.5277 0.5110 -0.1074 0.0620  0.0202  81  HIS C O   
6574  C CB  . HIS C 81  ? 0.6712 0.5877 0.5674 -0.0948 0.0529  -0.0109 81  HIS C CB  
6575  C CG  . HIS C 81  ? 0.7148 0.6478 0.6342 -0.0868 0.0446  -0.0204 81  HIS C CG  
6576  N ND1 . HIS C 81  ? 0.7197 0.6851 0.6496 -0.0767 0.0412  -0.0242 81  HIS C ND1 
6577  C CD2 . HIS C 81  ? 0.7319 0.6545 0.6652 -0.0857 0.0390  -0.0252 81  HIS C CD2 
6578  C CE1 . HIS C 81  ? 0.7098 0.6874 0.6567 -0.0719 0.0353  -0.0280 81  HIS C CE1 
6579  N NE2 . HIS C 81  ? 0.7236 0.6781 0.6726 -0.0768 0.0343  -0.0311 81  HIS C NE2 
6580  N N   . GLN C 82  ? 0.6343 0.5127 0.4499 -0.0824 0.0497  0.0165  82  GLN C N   
6581  C CA  . GLN C 82  ? 0.6634 0.5322 0.4447 -0.0881 0.0575  0.0315  82  GLN C CA  
6582  C C   . GLN C 82  ? 0.6138 0.4476 0.3742 -0.0790 0.0418  0.0456  82  GLN C C   
6583  O O   . GLN C 82  ? 0.5798 0.4113 0.3397 -0.0637 0.0253  0.0383  82  GLN C O   
6584  C CB  . GLN C 82  ? 0.7583 0.6578 0.5197 -0.0814 0.0637  0.0230  82  GLN C CB  
6585  C CG  . GLN C 82  ? 0.9008 0.7919 0.6176 -0.0788 0.0640  0.0371  82  GLN C CG  
6586  C CD  . GLN C 82  ? 0.9982 0.9249 0.6935 -0.0705 0.0714  0.0235  82  GLN C CD  
6587  O OE1 . GLN C 82  ? 1.0220 0.9756 0.7395 -0.0642 0.0745  0.0028  82  GLN C OE1 
6588  N NE2 . GLN C 82  ? 1.0435 0.9727 0.6950 -0.0693 0.0745  0.0355  82  GLN C NE2 
6589  N N   . CYS C 83  ? 0.6050 0.4110 0.3536 -0.0886 0.0460  0.0666  83  CYS C N   
6590  C CA  . CYS C 83  ? 0.6370 0.4101 0.3682 -0.0780 0.0297  0.0830  83  CYS C CA  
6591  C C   . CYS C 83  ? 0.6879 0.4715 0.3735 -0.0691 0.0254  0.0918  83  CYS C C   
6592  O O   . CYS C 83  ? 0.7424 0.5514 0.4063 -0.0759 0.0408  0.0924  83  CYS C O   
6593  C CB  . CYS C 83  ? 0.6638 0.3991 0.4009 -0.0896 0.0345  0.1048  83  CYS C CB  
6594  S SG  . CYS C 83  ? 0.8502 0.5729 0.6415 -0.0960 0.0350  0.0865  83  CYS C SG  
6595  N N   . PHE C 84  ? 0.6671 0.4368 0.3395 -0.0531 0.0042  0.0959  84  PHE C N   
6596  C CA  . PHE C 84  ? 0.6807 0.4645 0.3099 -0.0419 -0.0050 0.0989  84  PHE C CA  
6597  C C   . PHE C 84  ? 0.7412 0.5004 0.3381 -0.0408 -0.0098 0.1330  84  PHE C C   
6598  O O   . PHE C 84  ? 0.7474 0.4726 0.3638 -0.0401 -0.0169 0.1480  84  PHE C O   
6599  C CB  . PHE C 84  ? 0.6727 0.4647 0.3125 -0.0248 -0.0282 0.0766  84  PHE C CB  
6600  C CG  . PHE C 84  ? 0.7322 0.5430 0.3301 -0.0127 -0.0406 0.0714  84  PHE C CG  
6601  C CD1 . PHE C 84  ? 0.7165 0.5584 0.3017 -0.0104 -0.0342 0.0477  84  PHE C CD1 
6602  C CD2 . PHE C 84  ? 0.7892 0.5893 0.3624 -0.0016 -0.0607 0.0872  84  PHE C CD2 
6603  C CE1 . PHE C 84  ? 0.7664 0.6285 0.3132 0.0016  -0.0466 0.0367  84  PHE C CE1 
6604  C CE2 . PHE C 84  ? 0.8263 0.6497 0.3591 0.0101  -0.0743 0.0790  84  PHE C CE2 
6605  C CZ  . PHE C 84  ? 0.8232 0.6778 0.3421 0.0112  -0.0670 0.0519  84  PHE C CZ  
6606  N N   . THR C 85  ? 0.7945 0.5725 0.3428 -0.0409 -0.0035 0.1465  85  THR C N   
6607  C CA  . THR C 85  ? 0.9144 0.6757 0.4230 -0.0371 -0.0098 0.1832  85  THR C CA  
6608  C C   . THR C 85  ? 0.9716 0.7645 0.4308 -0.0204 -0.0250 0.1775  85  THR C C   
6609  O O   . THR C 85  ? 0.9748 0.8059 0.4083 -0.0221 -0.0130 0.1621  85  THR C O   
6610  C CB  . THR C 85  ? 1.0810 0.8382 0.5754 -0.0576 0.0172  0.2149  85  THR C CB  
6611  O OG1 . THR C 85  ? 1.0843 0.8089 0.6255 -0.0744 0.0286  0.2173  85  THR C OG1 
6612  C CG2 . THR C 85  ? 1.0936 0.8487 0.5684 -0.0484 0.0114  0.2526  85  THR C CG2 
6613  N N   . CYS C 86  ? 1.0111 0.7926 0.4565 -0.0036 -0.0515 0.1884  86  CYS C N   
6614  C CA  . CYS C 86  ? 1.0727 0.8960 0.4817 0.0121  -0.0670 0.1748  86  CYS C CA  
6615  C C   . CYS C 86  ? 1.1496 1.0045 0.5232 0.0107  -0.0537 0.2054  86  CYS C C   
6616  O O   . CYS C 86  ? 1.1581 0.9979 0.5319 0.0132  -0.0557 0.2441  86  CYS C O   
6617  C CB  . CYS C 86  ? 1.0966 0.9155 0.5151 0.0311  -0.1008 0.1687  86  CYS C CB  
6618  S SG  . CYS C 86  ? 1.0681 0.9444 0.4555 0.0456  -0.1205 0.1344  86  CYS C SG  
6619  N N   . THR C 87  ? 1.1942 1.0976 0.5389 0.0094  -0.0417 0.1868  87  THR C N   
6620  C CA  . THR C 87  ? 1.2570 1.2011 0.5679 0.0086  -0.0240 0.2120  87  THR C CA  
6621  C C   . THR C 87  ? 1.2833 1.2354 0.5419 0.0026  -0.0504 0.1936  87  THR C C   
6622  O O   . THR C 87  ? 1.3710 1.3135 0.5673 0.0062  -0.0392 0.1983  87  THR C O   
6623  C CB  . THR C 87  ? 1.2875 1.2375 0.5867 0.0051  0.0087  0.1917  87  THR C CB  
6624  O OG1 . THR C 87  ? 1.2968 1.2508 0.5819 -0.0029 -0.0039 0.1391  87  THR C OG1 
6625  C CG2 . THR C 87  ? 1.2343 1.1594 0.5809 -0.0193 0.0265  0.2014  87  THR C CG2 
6626  N N   . ASP C 88  ? 1.2270 1.1930 0.5037 0.0204  -0.0784 0.1720  88  ASP C N   
6627  C CA  . ASP C 88  ? 1.2699 1.2535 0.5092 0.0296  -0.1017 0.1543  88  ASP C CA  
6628  C C   . ASP C 88  ? 1.3216 1.2969 0.5589 0.0384  -0.1273 0.1859  88  ASP C C   
6629  O O   . ASP C 88  ? 1.4234 1.3788 0.6243 0.0322  -0.1239 0.2258  88  ASP C O   
6630  C CB  . ASP C 88  ? 1.2269 1.2298 0.4919 0.0412  -0.1151 0.0992  88  ASP C CB  
6631  C CG  . ASP C 88  ? 1.2351 1.2500 0.5007 0.0349  -0.0908 0.0674  88  ASP C CG  
6632  O OD1 . ASP C 88  ? 1.2592 1.2915 0.4842 0.0315  -0.0742 0.0656  88  ASP C OD1 
6633  O OD2 . ASP C 88  ? 1.2166 1.2206 0.5243 0.0363  -0.0872 0.0452  88  ASP C OD2 
6634  N N   . SER C 89  ? 1.2585 1.2349 0.5350 0.0548  -0.1519 0.1671  89  SER C N   
6635  C CA  . SER C 89  ? 1.2619 1.2366 0.5416 0.0668  -0.1790 0.1902  89  SER C CA  
6636  C C   . SER C 89  ? 1.2802 1.2248 0.5705 0.0640  -0.1686 0.2458  89  SER C C   
6637  O O   . SER C 89  ? 1.2207 1.1338 0.5423 0.0608  -0.1465 0.2558  89  SER C O   
6638  C CB  . SER C 89  ? 1.1868 1.1560 0.5149 0.0821  -0.2026 0.1588  89  SER C CB  
6639  O OG  . SER C 89  ? 1.1896 1.1490 0.5355 0.0944  -0.2230 0.1866  89  SER C OG  
6640  N N   . THR C 90  ? 1.3653 1.3099 0.6248 0.0641  -0.1842 0.2800  90  THR C N   
6641  C CA  . THR C 90  ? 1.4008 1.3134 0.6799 0.0632  -0.1768 0.3309  90  THR C CA  
6642  C C   . THR C 90  ? 1.3491 1.2417 0.6907 0.0871  -0.1855 0.3361  90  THR C C   
6643  O O   . THR C 90  ? 1.3459 1.1974 0.7187 0.0920  -0.1705 0.3656  90  THR C O   
6644  C CB  . THR C 90  ? 1.6418 1.5267 0.8530 0.0623  -0.1971 0.3577  90  THR C CB  
6645  O OG1 . THR C 90  ? 1.6968 1.5121 0.9021 0.0591  -0.1883 0.3990  90  THR C OG1 
6646  C CG2 . THR C 90  ? 1.6438 1.5597 0.8686 0.0824  -0.2342 0.3537  90  THR C CG2 
6647  N N   . THR C 91  ? 1.3026 1.2069 0.6611 0.0992  -0.2089 0.2969  91  THR C N   
6648  C CA  . THR C 91  ? 1.2474 1.1191 0.6609 0.1135  -0.2209 0.2862  91  THR C CA  
6649  C C   . THR C 91  ? 1.1830 1.0447 0.6223 0.1084  -0.2199 0.2370  91  THR C C   
6650  O O   . THR C 91  ? 1.1855 1.0735 0.6022 0.1005  -0.2164 0.2059  91  THR C O   
6651  C CB  . THR C 91  ? 1.2475 1.1449 0.6705 0.1315  -0.2540 0.2883  91  THR C CB  
6652  O OG1 . THR C 91  ? 1.2589 1.2055 0.6463 0.1282  -0.2706 0.2610  91  THR C OG1 
6653  C CG2 . THR C 91  ? 1.3188 1.2134 0.7310 0.1385  -0.2576 0.3436  91  THR C CG2 
6654  N N   . THR C 92  ? 1.1135 0.9402 0.6035 0.1129  -0.2244 0.2294  92  THR C N   
6655  C CA  . THR C 92  ? 1.0785 0.8942 0.5976 0.1056  -0.2234 0.1903  92  THR C CA  
6656  C C   . THR C 92  ? 1.0431 0.8959 0.5745 0.1132  -0.2491 0.1540  92  THR C C   
6657  O O   . THR C 92  ? 1.0482 0.9287 0.5807 0.1261  -0.2709 0.1579  92  THR C O   
6658  C CB  . THR C 92  ? 1.0812 0.8556 0.6542 0.1059  -0.2201 0.1924  92  THR C CB  
6659  O OG1 . THR C 92  ? 1.1100 0.8953 0.7179 0.1233  -0.2438 0.1911  92  THR C OG1 
6660  C CG2 . THR C 92  ? 1.1027 0.8377 0.6753 0.0981  -0.1965 0.2267  92  THR C CG2 
6661  N N   . ARG C 93  ? 0.9991 0.8532 0.5429 0.1038  -0.2457 0.1187  93  ARG C N   
6662  C CA  . ARG C 93  ? 0.9852 0.8695 0.5519 0.1061  -0.2663 0.0795  93  ARG C CA  
6663  C C   . ARG C 93  ? 0.8975 0.7643 0.4911 0.0939  -0.2561 0.0532  93  ARG C C   
6664  O O   . ARG C 93  ? 0.8603 0.7001 0.4448 0.0842  -0.2326 0.0652  93  ARG C O   
6665  C CB  . ARG C 93  ? 1.0654 0.9926 0.5908 0.1074  -0.2733 0.0648  93  ARG C CB  
6666  C CG  . ARG C 93  ? 1.1223 1.0522 0.6058 0.0971  -0.2496 0.0598  93  ARG C CG  
6667  C CD  . ARG C 93  ? 1.2421 1.2181 0.6909 0.0982  -0.2579 0.0397  93  ARG C CD  
6668  N NE  . ARG C 93  ? 1.3427 1.3288 0.7542 0.0889  -0.2341 0.0312  93  ARG C NE  
6669  C CZ  . ARG C 93  ? 1.3983 1.3878 0.8242 0.0834  -0.2264 -0.0085 93  ARG C CZ  
6670  N NH1 . ARG C 93  ? 1.3980 1.3784 0.8749 0.0839  -0.2408 -0.0399 93  ARG C NH1 
6671  N NH2 . ARG C 93  ? 1.4310 1.4334 0.8251 0.0766  -0.2036 -0.0154 93  ARG C NH2 
6672  N N   . PRO C 94  ? 0.8489 0.7327 0.4829 0.0921  -0.2717 0.0192  94  PRO C N   
6673  C CA  . PRO C 94  ? 0.7757 0.6488 0.4426 0.0780  -0.2565 -0.0031 94  PRO C CA  
6674  C C   . PRO C 94  ? 0.7634 0.6375 0.3908 0.0707  -0.2351 -0.0119 94  PRO C C   
6675  O O   . PRO C 94  ? 0.8117 0.7088 0.3982 0.0759  -0.2433 -0.0269 94  PRO C O   
6676  C CB  . PRO C 94  ? 0.7631 0.6586 0.4725 0.0774  -0.2801 -0.0367 94  PRO C CB  
6677  C CG  . PRO C 94  ? 0.7775 0.6916 0.5001 0.0890  -0.3012 -0.0261 94  PRO C CG  
6678  C CD  . PRO C 94  ? 0.8333 0.7495 0.4968 0.0989  -0.2973 0.0016  94  PRO C CD  
6679  N N   . GLY C 95  ? 0.7156 0.5701 0.3569 0.0593  -0.2069 -0.0038 95  GLY C N   
6680  C CA  . GLY C 95  ? 0.7419 0.6009 0.3522 0.0528  -0.1846 -0.0106 95  GLY C CA  
6681  C C   . GLY C 95  ? 0.8133 0.6652 0.3746 0.0515  -0.1674 0.0224  95  GLY C C   
6682  O O   . GLY C 95  ? 0.8384 0.6945 0.3806 0.0436  -0.1439 0.0224  95  GLY C O   
6683  N N   . CYS C 96  ? 0.8578 0.6984 0.4038 0.0591  -0.1789 0.0523  96  CYS C N   
6684  C CA  . CYS C 96  ? 0.9056 0.7342 0.4072 0.0574  -0.1647 0.0906  96  CYS C CA  
6685  C C   . CYS C 96  ? 0.8880 0.6802 0.4143 0.0581  -0.1644 0.1226  96  CYS C C   
6686  O O   . CYS C 96  ? 0.9112 0.6998 0.4375 0.0720  -0.1861 0.1376  96  CYS C O   
6687  C CB  . CYS C 96  ? 0.9782 0.8399 0.4295 0.0680  -0.1769 0.0990  96  CYS C CB  
6688  S SG  . CYS C 96  ? 1.5773 1.4364 0.9902 0.0631  -0.1560 0.1525  96  CYS C SG  
6689  N N   . HIS C 97  ? 0.8610 0.6301 0.4136 0.0435  -0.1395 0.1286  97  HIS C N   
6690  C CA  . HIS C 97  ? 0.8465 0.5776 0.4219 0.0414  -0.1337 0.1557  97  HIS C CA  
6691  C C   . HIS C 97  ? 0.8516 0.5651 0.4199 0.0226  -0.1034 0.1721  97  HIS C C   
6692  O O   . HIS C 97  ? 0.7719 0.5070 0.3222 0.0114  -0.0858 0.1612  97  HIS C O   
6693  C CB  . HIS C 97  ? 0.7749 0.4968 0.4125 0.0436  -0.1395 0.1370  97  HIS C CB  
6694  C CG  . HIS C 97  ? 0.7569 0.4997 0.4135 0.0584  -0.1670 0.1191  97  HIS C CG  
6695  N ND1 . HIS C 97  ? 0.7409 0.5129 0.4086 0.0563  -0.1733 0.0875  97  HIS C ND1 
6696  C CD2 . HIS C 97  ? 0.7189 0.4582 0.3924 0.0749  -0.1902 0.1276  97  HIS C CD2 
6697  C CE1 . HIS C 97  ? 0.7339 0.5204 0.4239 0.0683  -0.1989 0.0776  97  HIS C CE1 
6698  N NE2 . HIS C 97  ? 0.7671 0.5374 0.4607 0.0804  -0.2096 0.1011  97  HIS C NE2 
6699  N N   . ASN C 98  ? 0.9027 0.5775 0.4888 0.0195  -0.0982 0.1972  98  ASN C N   
6700  C CA  . ASN C 98  ? 0.9937 0.6483 0.5901 -0.0014 -0.0708 0.2077  98  ASN C CA  
6701  C C   . ASN C 98  ? 0.8759 0.5146 0.5317 -0.0058 -0.0665 0.1863  98  ASN C C   
6702  O O   . ASN C 98  ? 0.8036 0.4385 0.4885 0.0087  -0.0841 0.1750  98  ASN C O   
6703  C CB  . ASN C 98  ? 1.2381 0.8728 0.8239 -0.0030 -0.0640 0.2475  98  ASN C CB  
6704  C CG  . ASN C 98  ? 1.4395 1.1090 0.9731 -0.0026 -0.0584 0.2661  98  ASN C CG  
6705  O OD1 . ASN C 98  ? 1.4022 1.1043 0.9061 -0.0082 -0.0511 0.2479  98  ASN C OD1 
6706  N ND2 . ASN C 98  ? 1.6590 1.3252 1.1827 0.0062  -0.0612 0.3018  98  ASN C ND2 
6707  N N   . ASN C 99  ? 0.8809 0.5176 0.5545 -0.0256 -0.0433 0.1787  99  ASN C N   
6708  C CA  . ASN C 99  ? 0.8854 0.5190 0.6100 -0.0300 -0.0386 0.1535  99  ASN C CA  
6709  C C   . ASN C 99  ? 0.7496 0.4167 0.4946 -0.0209 -0.0480 0.1225  99  ASN C C   
6710  O O   . ASN C 99  ? 0.7085 0.3748 0.4922 -0.0160 -0.0528 0.1069  99  ASN C O   
6711  C CB  . ASN C 99  ? 1.0363 0.6293 0.7921 -0.0223 -0.0472 0.1622  99  ASN C CB  
6712  C CG  . ASN C 99  ? 1.1157 0.7076 0.9194 -0.0306 -0.0372 0.1358  99  ASN C CG  
6713  O OD1 . ASN C 99  ? 1.1333 0.7451 0.9432 -0.0477 -0.0199 0.1213  99  ASN C OD1 
6714  N ND2 . ASN C 99  ? 1.1376 0.7130 0.9754 -0.0166 -0.0489 0.1271  99  ASN C ND2 
6715  N N   . THR C 100 ? 0.6924 0.3899 0.4136 -0.0192 -0.0498 0.1130  100 THR C N   
6716  C CA  . THR C 100 ? 0.6352 0.3605 0.3799 -0.0144 -0.0560 0.0858  100 THR C CA  
6717  C C   . THR C 100 ? 0.5948 0.3428 0.3432 -0.0276 -0.0365 0.0717  100 THR C C   
6718  O O   . THR C 100 ? 0.6171 0.3601 0.3580 -0.0412 -0.0186 0.0805  100 THR C O   
6719  C CB  . THR C 100 ? 0.6486 0.3896 0.3737 -0.0005 -0.0766 0.0803  100 THR C CB  
6720  O OG1 . THR C 100 ? 0.6687 0.4142 0.3443 -0.0008 -0.0743 0.0929  100 THR C OG1 
6721  C CG2 . THR C 100 ? 0.6686 0.3969 0.4060 0.0143  -0.0986 0.0883  100 THR C CG2 
6722  N N   . CYS C 101 ? 0.5866 0.3596 0.3501 -0.0241 -0.0398 0.0510  101 CYS C N   
6723  C CA  . CYS C 101 ? 0.5912 0.3870 0.3563 -0.0331 -0.0228 0.0395  101 CYS C CA  
6724  C C   . CYS C 101 ? 0.5457 0.3611 0.2911 -0.0261 -0.0271 0.0268  101 CYS C C   
6725  O O   . CYS C 101 ? 0.5532 0.3696 0.2994 -0.0152 -0.0452 0.0180  101 CYS C O   
6726  C CB  A CYS C 101 ? 0.5780 0.3876 0.3842 -0.0369 -0.0173 0.0267  101 CYS C CB  
6727  C CB  B CYS C 101 ? 0.5777 0.3873 0.3839 -0.0357 -0.0189 0.0263  101 CYS C CB  
6728  S SG  A CYS C 101 ? 0.5378 0.3521 0.3799 -0.0265 -0.0342 0.0182  101 CYS C SG  
6729  S SG  B CYS C 101 ? 0.5618 0.3546 0.3977 -0.0345 -0.0246 0.0301  101 CYS C SG  
6730  N N   . GLY C 102 ? 0.5214 0.3544 0.2525 -0.0328 -0.0098 0.0235  102 GLY C N   
6731  C CA  . GLY C 102 ? 0.5027 0.3568 0.2121 -0.0259 -0.0094 0.0091  102 GLY C CA  
6732  C C   . GLY C 102 ? 0.6093 0.4803 0.3522 -0.0222 -0.0078 -0.0114 102 GLY C C   
6733  O O   . GLY C 102 ? 0.5542 0.4325 0.3257 -0.0291 0.0023  -0.0108 102 GLY C O   
6734  N N   . LEU C 103 ? 0.6117 0.4893 0.3516 -0.0104 -0.0194 -0.0301 103 LEU C N   
6735  C CA  . LEU C 103 ? 0.5905 0.4766 0.3647 -0.0039 -0.0223 -0.0482 103 LEU C CA  
6736  C C   . LEU C 103 ? 0.5988 0.5014 0.3540 0.0065  -0.0212 -0.0710 103 LEU C C   
6737  O O   . LEU C 103 ? 0.6318 0.5325 0.3583 0.0128  -0.0326 -0.0796 103 LEU C O   
6738  C CB  . LEU C 103 ? 0.6026 0.4715 0.4059 0.0000  -0.0426 -0.0499 103 LEU C CB  
6739  C CG  . LEU C 103 ? 0.6425 0.5133 0.4906 0.0029  -0.0457 -0.0567 103 LEU C CG  
6740  C CD1 . LEU C 103 ? 0.6610 0.5463 0.5249 -0.0036 -0.0285 -0.0458 103 LEU C CD1 
6741  C CD2 . LEU C 103 ? 0.6245 0.4814 0.4987 0.0020  -0.0627 -0.0515 103 LEU C CD2 
6742  N N   . LEU C 104 ? 0.5464 0.4689 0.3169 0.0099  -0.0081 -0.0824 104 LEU C N   
6743  C CA  . LEU C 104 ? 0.5899 0.5307 0.3467 0.0225  -0.0061 -0.1086 104 LEU C CA  
6744  C C   . LEU C 104 ? 0.5677 0.4927 0.3559 0.0356  -0.0256 -0.1322 104 LEU C C   
6745  O O   . LEU C 104 ? 0.5279 0.4431 0.3593 0.0367  -0.0288 -0.1287 104 LEU C O   
6746  C CB  . LEU C 104 ? 0.5842 0.5566 0.3474 0.0223  0.0164  -0.1120 104 LEU C CB  
6747  C CG  . LEU C 104 ? 0.6528 0.6553 0.3882 0.0328  0.0263  -0.1352 104 LEU C CG  
6748  C CD1 . LEU C 104 ? 0.6797 0.6922 0.3600 0.0251  0.0330  -0.1235 104 LEU C CD1 
6749  C CD2 . LEU C 104 ? 0.6769 0.7138 0.4323 0.0333  0.0473  -0.1384 104 LEU C CD2 
6750  N N   . SER C 105 ? 0.5293 0.4518 0.2961 0.0442  -0.0395 -0.1543 105 SER C N   
6751  C CA  . SER C 105 ? 0.5397 0.4448 0.3377 0.0548  -0.0596 -0.1814 105 SER C CA  
6752  C C   . SER C 105 ? 0.5741 0.4963 0.3657 0.0711  -0.0567 -0.2187 105 SER C C   
6753  O O   . SER C 105 ? 0.6269 0.5781 0.3738 0.0746  -0.0451 -0.2272 105 SER C O   
6754  C CB  . SER C 105 ? 0.5573 0.4472 0.3436 0.0523  -0.0828 -0.1851 105 SER C CB  
6755  O OG  . SER C 105 ? 0.5687 0.4437 0.3661 0.0401  -0.0873 -0.1544 105 SER C OG  
6756  N N   . SER C 106 ? 0.7073 0.6122 0.5449 0.0815  -0.0668 -0.2408 106 SER C N   
6757  C CA  . SER C 106 ? 0.7318 0.6506 0.5730 0.0996  -0.0644 -0.2796 106 SER C CA  
6758  C C   . SER C 106 ? 0.6436 0.5442 0.5120 0.1037  -0.0840 -0.3024 106 SER C C   
6759  O O   . SER C 106 ? 0.6322 0.4999 0.5441 0.0988  -0.1001 -0.2973 106 SER C O   
6760  C CB  . SER C 106 ? 0.7315 0.6524 0.6142 0.1102  -0.0527 -0.2805 106 SER C CB  
6761  O OG  . SER C 106 ? 0.7500 0.7080 0.6084 0.1069  -0.0280 -0.2638 106 SER C OG  
6762  N N   . ASN C 107 ? 0.6100 0.4251 0.2748 0.0041  -0.0218 -0.0320 107 ASN C N   
6763  C CA  . ASN C 107 ? 0.6715 0.4699 0.3153 0.0088  -0.0289 -0.0442 107 ASN C CA  
6764  C C   . ASN C 107 ? 0.6575 0.4697 0.3247 0.0147  -0.0114 -0.0532 107 ASN C C   
6765  O O   . ASN C 107 ? 0.6843 0.4983 0.3411 0.0166  0.0113  -0.0551 107 ASN C O   
6766  C CB  . ASN C 107 ? 0.7280 0.4955 0.3110 0.0081  -0.0274 -0.0463 107 ASN C CB  
6767  C CG  . ASN C 107 ? 0.7582 0.5040 0.3134 0.0119  -0.0355 -0.0610 107 ASN C CG  
6768  O OD1 . ASN C 107 ? 0.7202 0.4727 0.2968 0.0166  -0.0292 -0.0709 107 ASN C OD1 
6769  N ND2 . ASN C 107 ? 0.7287 0.4461 0.2336 0.0100  -0.0496 -0.0624 107 ASN C ND2 
6770  N N   . PRO C 108 ? 0.6358 0.4577 0.3355 0.0181  -0.0211 -0.0581 108 PRO C N   
6771  C CA  . PRO C 108 ? 0.6103 0.4472 0.3382 0.0251  -0.0064 -0.0641 108 PRO C CA  
6772  C C   . PRO C 108 ? 0.6878 0.5036 0.3859 0.0317  0.0045  -0.0773 108 PRO C C   
6773  O O   . PRO C 108 ? 0.7204 0.5460 0.4358 0.0394  0.0212  -0.0823 108 PRO C O   
6774  C CB  . PRO C 108 ? 0.5503 0.3966 0.3135 0.0259  -0.0227 -0.0637 108 PRO C CB  
6775  C CG  . PRO C 108 ? 0.5629 0.3904 0.3066 0.0210  -0.0445 -0.0644 108 PRO C CG  
6776  C CD  . PRO C 108 ? 0.6122 0.4317 0.3258 0.0158  -0.0458 -0.0573 108 PRO C CD  
6777  N N   . VAL C 109 ? 0.7087 0.4948 0.3613 0.0293  -0.0056 -0.0831 109 VAL C N   
6778  C CA  . VAL C 109 ? 0.7193 0.4798 0.3355 0.0349  0.0044  -0.0972 109 VAL C CA  
6779  C C   . VAL C 109 ? 0.7379 0.4943 0.3239 0.0365  0.0301  -0.0966 109 VAL C C   
6780  O O   . VAL C 109 ? 0.7374 0.4946 0.3241 0.0445  0.0529  -0.1044 109 VAL C O   
6781  C CB  . VAL C 109 ? 0.7006 0.4283 0.2743 0.0305  -0.0186 -0.1050 109 VAL C CB  
6782  C CG1 . VAL C 109 ? 0.7609 0.4570 0.2852 0.0353  -0.0064 -0.1204 109 VAL C CG1 
6783  C CG2 . VAL C 109 ? 0.6972 0.4275 0.3019 0.0282  -0.0418 -0.1075 109 VAL C CG2 
6784  N N   . THR C 110 ? 0.7443 0.4953 0.3040 0.0291  0.0272  -0.0868 110 THR C N   
6785  C CA  . THR C 110 ? 0.7864 0.5288 0.3107 0.0286  0.0514  -0.0846 110 THR C CA  
6786  C C   . THR C 110 ? 0.7691 0.5442 0.3328 0.0264  0.0710  -0.0736 110 THR C C   
6787  O O   . THR C 110 ? 0.8017 0.5771 0.3497 0.0264  0.0968  -0.0721 110 THR C O   
6788  C CB  . THR C 110 ? 0.8463 0.5617 0.3164 0.0219  0.0390  -0.0785 110 THR C CB  
6789  O OG1 . THR C 110 ? 0.8013 0.5320 0.2966 0.0152  0.0233  -0.0637 110 THR C OG1 
6790  C CG2 . THR C 110 ? 0.9068 0.5914 0.3389 0.0225  0.0152  -0.0897 110 THR C CG2 
6791  N N   . GLN C 111 ? 0.7303 0.5320 0.3443 0.0239  0.0586  -0.0663 111 GLN C N   
6792  C CA  . GLN C 111 ? 0.7539 0.5874 0.4085 0.0199  0.0714  -0.0561 111 GLN C CA  
6793  C C   . GLN C 111 ? 0.7840 0.6108 0.4163 0.0097  0.0750  -0.0435 111 GLN C C   
6794  O O   . GLN C 111 ? 0.7613 0.6098 0.4201 0.0042  0.0888  -0.0357 111 GLN C O   
6795  C CB  . GLN C 111 ? 0.8371 0.6894 0.5128 0.0264  0.0996  -0.0615 111 GLN C CB  
6796  C CG  . GLN C 111 ? 0.9210 0.7844 0.6291 0.0376  0.0977  -0.0712 111 GLN C CG  
6797  C CD  . GLN C 111 ? 0.9716 0.8612 0.7308 0.0368  0.0811  -0.0655 111 GLN C CD  
6798  O OE1 . GLN C 111 ? 1.0107 0.8906 0.7718 0.0372  0.0591  -0.0671 111 GLN C OE1 
6799  N NE2 . GLN C 111 ? 0.9622 0.8851 0.7624 0.0347  0.0916  -0.0587 111 GLN C NE2 
6800  N N   . GLU C 112 ? 0.8227 0.6185 0.4061 0.0071  0.0619  -0.0414 112 GLU C N   
6801  C CA  . GLU C 112 ? 0.8260 0.6119 0.3890 -0.0014 0.0600  -0.0276 112 GLU C CA  
6802  C C   . GLU C 112 ? 0.7677 0.5717 0.3722 -0.0059 0.0423  -0.0187 112 GLU C C   
6803  O O   . GLU C 112 ? 0.7306 0.5423 0.3598 -0.0025 0.0229  -0.0226 112 GLU C O   
6804  C CB  . GLU C 112 ? 0.9147 0.6630 0.4165 -0.0013 0.0448  -0.0270 112 GLU C CB  
6805  C CG  . GLU C 112 ? 1.0233 0.7448 0.4673 0.0009  0.0633  -0.0329 112 GLU C CG  
6806  C CD  . GLU C 112 ? 1.1235 0.8087 0.5096 0.0025  0.0402  -0.0363 112 GLU C CD  
6807  O OE1 . GLU C 112 ? 1.1200 0.8052 0.5193 0.0047  0.0129  -0.0419 112 GLU C OE1 
6808  O OE2 . GLU C 112 ? 1.2131 0.8697 0.5402 0.0010  0.0485  -0.0328 112 GLU C OE2 
6809  N N   . SER C 113 ? 0.7585 0.5667 0.3688 -0.0139 0.0499  -0.0068 113 SER C N   
6810  C CA  . SER C 113 ? 0.6878 0.5035 0.3248 -0.0178 0.0325  0.0015  113 SER C CA  
6811  C C   . SER C 113 ? 0.6790 0.4713 0.2831 -0.0238 0.0314  0.0146  113 SER C C   
6812  O O   . SER C 113 ? 0.6884 0.4650 0.2577 -0.0275 0.0492  0.0190  113 SER C O   
6813  C CB  . SER C 113 ? 0.6845 0.5331 0.3752 -0.0216 0.0410  0.0020  113 SER C CB  
6814  O OG  . SER C 113 ? 0.7615 0.6162 0.4530 -0.0295 0.0641  0.0074  113 SER C OG  
6815  N N   . GLY C 114 ? 0.6501 0.4387 0.2650 -0.0243 0.0114  0.0216  114 GLY C N   
6816  C CA  . GLY C 114 ? 0.7014 0.4651 0.2867 -0.0279 0.0070  0.0350  114 GLY C CA  
6817  C C   . GLY C 114 ? 0.6742 0.4460 0.2938 -0.0296 -0.0054 0.0413  114 GLY C C   
6818  O O   . GLY C 114 ? 0.6275 0.4183 0.2831 -0.0259 -0.0173 0.0351  114 GLY C O   
6819  N N   . LEU C 115 ? 0.6893 0.4440 0.2958 -0.0349 -0.0015 0.0537  115 LEU C N   
6820  C CA  . LEU C 115 ? 0.6593 0.4180 0.2960 -0.0364 -0.0100 0.0591  115 LEU C CA  
6821  C C   . LEU C 115 ? 0.6795 0.4239 0.3079 -0.0273 -0.0359 0.0638  115 LEU C C   
6822  O O   . LEU C 115 ? 0.7336 0.4507 0.3226 -0.0245 -0.0431 0.0732  115 LEU C O   
6823  C CB  . LEU C 115 ? 0.6756 0.4197 0.3042 -0.0464 0.0058  0.0701  115 LEU C CB  
6824  C CG  . LEU C 115 ? 0.7061 0.4588 0.3729 -0.0493 0.0010  0.0711  115 LEU C CG  
6825  C CD1 . LEU C 115 ? 0.6891 0.4745 0.3979 -0.0567 0.0131  0.0613  115 LEU C CD1 
6826  C CD2 . LEU C 115 ? 0.7818 0.5055 0.4327 -0.0539 0.0035  0.0846  115 LEU C CD2 
6827  N N   . GLY C 116 ? 0.6328 0.3961 0.2987 -0.0225 -0.0495 0.0578  116 GLY C N   
6828  C CA  . GLY C 116 ? 0.6235 0.3799 0.2931 -0.0140 -0.0730 0.0617  116 GLY C CA  
6829  C C   . GLY C 116 ? 0.5959 0.3509 0.2907 -0.0135 -0.0751 0.0684  116 GLY C C   
6830  O O   . GLY C 116 ? 0.5827 0.3398 0.2893 -0.0210 -0.0594 0.0693  116 GLY C O   
6831  N N   . GLU C 117 ? 0.6107 0.3616 0.3143 -0.0047 -0.0945 0.0727  117 GLU C N   
6832  C CA  . GLU C 117 ? 0.5873 0.3350 0.3148 -0.0019 -0.0961 0.0783  117 GLU C CA  
6833  C C   . GLU C 117 ? 0.5181 0.2905 0.2880 0.0029  -0.1043 0.0703  117 GLU C C   
6834  O O   . GLU C 117 ? 0.5026 0.2849 0.2795 0.0087  -0.1196 0.0670  117 GLU C O   
6835  C CB  . GLU C 117 ? 0.6520 0.3737 0.3576 0.0061  -0.1099 0.0918  117 GLU C CB  
6836  C CG  . GLU C 117 ? 0.6836 0.3947 0.4077 0.0098  -0.1085 0.0989  117 GLU C CG  
6837  C CD  . GLU C 117 ? 0.7774 0.4644 0.4833 0.0207  -0.1251 0.1129  117 GLU C CD  
6838  O OE1 . GLU C 117 ? 0.7900 0.4850 0.4986 0.0294  -0.1458 0.1134  117 GLU C OE1 
6839  O OE2 . GLU C 117 ? 0.8372 0.4970 0.5271 0.0207  -0.1184 0.1238  117 GLU C OE2 
6840  N N   . LEU C 118 ? 0.4802 0.2611 0.2772 0.0001  -0.0942 0.0673  118 LEU C N   
6841  C CA  . LEU C 118 ? 0.4563 0.2578 0.2905 0.0048  -0.0996 0.0609  118 LEU C CA  
6842  C C   . LEU C 118 ? 0.4917 0.2889 0.3368 0.0163  -0.1170 0.0674  118 LEU C C   
6843  O O   . LEU C 118 ? 0.5234 0.2998 0.3561 0.0212  -0.1210 0.0775  118 LEU C O   
6844  C CB  . LEU C 118 ? 0.4266 0.2322 0.2805 0.0000  -0.0859 0.0573  118 LEU C CB  
6845  C CG  . LEU C 118 ? 0.3969 0.2229 0.2847 0.0036  -0.0873 0.0503  118 LEU C CG  
6846  C CD1 . LEU C 118 ? 0.3900 0.2379 0.2859 0.0009  -0.0875 0.0419  118 LEU C CD1 
6847  C CD2 . LEU C 118 ? 0.3965 0.2197 0.2952 -0.0006 -0.0753 0.0473  118 LEU C CD2 
6848  N N   . ALA C 119 ? 0.5178 0.3350 0.3877 0.0207  -0.1275 0.0621  119 ALA C N   
6849  C CA  . ALA C 119 ? 0.5325 0.3530 0.4204 0.0310  -0.1454 0.0672  119 ALA C CA  
6850  C C   . ALA C 119 ? 0.5153 0.3583 0.4471 0.0344  -0.1444 0.0619  119 ALA C C   
6851  O O   . ALA C 119 ? 0.5155 0.3722 0.4586 0.0286  -0.1337 0.0534  119 ALA C O   
6852  C CB  . ALA C 119 ? 0.5622 0.3833 0.4326 0.0317  -0.1633 0.0668  119 ALA C CB  
6853  N N   . GLN C 120 ? 0.5138 0.3609 0.4706 0.0444  -0.1555 0.0674  120 GLN C N   
6854  C CA  . GLN C 120 ? 0.5031 0.3720 0.5032 0.0482  -0.1531 0.0635  120 GLN C CA  
6855  C C   . GLN C 120 ? 0.5289 0.4114 0.5549 0.0561  -0.1740 0.0676  120 GLN C C   
6856  O O   . GLN C 120 ? 0.5431 0.4153 0.5644 0.0644  -0.1869 0.0768  120 GLN C O   
6857  C CB  . GLN C 120 ? 0.5300 0.3909 0.5425 0.0528  -0.1378 0.0652  120 GLN C CB  
6858  C CG  . GLN C 120 ? 0.5425 0.4222 0.5954 0.0574  -0.1307 0.0615  120 GLN C CG  
6859  C CD  . GLN C 120 ? 0.5971 0.4629 0.6561 0.0635  -0.1160 0.0631  120 GLN C CD  
6860  O OE1 . GLN C 120 ? 0.6027 0.4563 0.6432 0.0568  -0.1011 0.0583  120 GLN C OE1 
6861  N NE2 . GLN C 120 ? 0.5870 0.4549 0.6733 0.0765  -0.1204 0.0691  120 GLN C NE2 
6862  N N   . ASP C 121 ? 0.4963 0.4016 0.5500 0.0531  -0.1782 0.0614  121 ASP C N   
6863  C CA  . ASP C 121 ? 0.4597 0.3821 0.5443 0.0582  -0.1986 0.0641  121 ASP C CA  
6864  C C   . ASP C 121 ? 0.3899 0.3372 0.5125 0.0532  -0.1940 0.0568  121 ASP C C   
6865  O O   . ASP C 121 ? 0.3742 0.3224 0.4932 0.0470  -0.1764 0.0507  121 ASP C O   
6866  C CB  . ASP C 121 ? 0.4606 0.3757 0.5134 0.0537  -0.2154 0.0632  121 ASP C CB  
6867  C CG  . ASP C 121 ? 0.4526 0.3790 0.5240 0.0589  -0.2307 0.0671  121 ASP C CG  
6868  O OD1 . ASP C 121 ? 0.4209 0.3689 0.5378 0.0630  -0.2305 0.0677  121 ASP C OD1 
6869  O OD2 . ASP C 121 ? 0.4991 0.4124 0.5385 0.0588  -0.2428 0.0698  121 ASP C OD2 
6870  N N   . VAL C 122 ? 0.4077 0.3748 0.5625 0.0535  -0.2051 0.0564  122 VAL C N   
6871  C CA  . VAL C 122 ? 0.3631 0.3522 0.5546 0.0475  -0.2022 0.0508  122 VAL C CA  
6872  C C   . VAL C 122 ? 0.3954 0.3811 0.5671 0.0362  -0.2085 0.0426  122 VAL C C   
6873  O O   . VAL C 122 ? 0.4646 0.4406 0.6085 0.0328  -0.2225 0.0404  122 VAL C O   
6874  C CB  . VAL C 122 ? 0.3256 0.3362 0.5568 0.0491  -0.2119 0.0525  122 VAL C CB  
6875  C CG1 . VAL C 122 ? 0.3085 0.3379 0.5726 0.0399  -0.2099 0.0466  122 VAL C CG1 
6876  C CG2 . VAL C 122 ? 0.3319 0.3496 0.5910 0.0612  -0.2029 0.0597  122 VAL C CG2 
6877  N N   . LEU C 123 ? 0.3507 0.3421 0.5329 0.0305  -0.1951 0.0376  123 LEU C N   
6878  C CA  . LEU C 123 ? 0.3452 0.3364 0.5202 0.0202  -0.1998 0.0295  123 LEU C CA  
6879  C C   . LEU C 123 ? 0.3404 0.3522 0.5624 0.0159  -0.1958 0.0283  123 LEU C C   
6880  O O   . LEU C 123 ? 0.3069 0.3275 0.5520 0.0193  -0.1777 0.0316  123 LEU C O   
6881  C CB  . LEU C 123 ? 0.2873 0.2629 0.4254 0.0161  -0.1835 0.0242  123 LEU C CB  
6882  C CG  . LEU C 123 ? 0.3828 0.3543 0.5108 0.0072  -0.1842 0.0156  123 LEU C CG  
6883  C CD1 . LEU C 123 ? 0.3739 0.3271 0.4564 0.0060  -0.1789 0.0112  123 LEU C CD1 
6884  C CD2 . LEU C 123 ? 0.2983 0.2795 0.4524 0.0036  -0.1683 0.0143  123 LEU C CD2 
6885  N N   . ALA C 124 ? 0.3324 0.3487 0.5642 0.0074  -0.2095 0.0230  124 ALA C N   
6886  C CA  . ALA C 124 ? 0.3150 0.3485 0.5901 0.0006  -0.2048 0.0217  124 ALA C CA  
6887  C C   . ALA C 124 ? 0.3452 0.3694 0.6095 -0.0103 -0.2055 0.0136  124 ALA C C   
6888  O O   . ALA C 124 ? 0.3504 0.3562 0.5756 -0.0132 -0.2143 0.0071  124 ALA C O   
6889  C CB  . ALA C 124 ? 0.2905 0.3386 0.5952 -0.0004 -0.2167 0.0234  124 ALA C CB  
6890  N N   . ILE C 125 ? 0.3654 0.3990 0.6601 -0.0158 -0.1914 0.0141  125 ILE C N   
6891  C CA  . ILE C 125 ? 0.3800 0.4015 0.6650 -0.0252 -0.1867 0.0078  125 ILE C CA  
6892  C C   . ILE C 125 ? 0.3594 0.3961 0.6924 -0.0335 -0.1800 0.0099  125 ILE C C   
6893  O O   . ILE C 125 ? 0.3374 0.3920 0.7039 -0.0299 -0.1679 0.0171  125 ILE C O   
6894  C CB  . ILE C 125 ? 0.3124 0.3174 0.5611 -0.0210 -0.1663 0.0077  125 ILE C CB  
6895  C CG1 . ILE C 125 ? 0.2916 0.2803 0.5246 -0.0281 -0.1635 0.0012  125 ILE C CG1 
6896  C CG2 . ILE C 125 ? 0.3243 0.3390 0.5899 -0.0158 -0.1444 0.0152  125 ILE C CG2 
6897  C CD1 . ILE C 125 ? 0.3071 0.2828 0.5081 -0.0230 -0.1467 0.0015  125 ILE C CD1 
6898  N N   . HIS C 126 ? 0.3608 0.3888 0.6967 -0.0447 -0.1861 0.0037  126 HIS C N   
6899  C CA  . HIS C 126 ? 0.3583 0.3985 0.7397 -0.0548 -0.1791 0.0060  126 HIS C CA  
6900  C C   . HIS C 126 ? 0.3265 0.3647 0.7113 -0.0525 -0.1501 0.0130  126 HIS C C   
6901  O O   . HIS C 126 ? 0.3036 0.3228 0.6502 -0.0482 -0.1385 0.0124  126 HIS C O   
6902  C CB  . HIS C 126 ? 0.3428 0.3659 0.7142 -0.0661 -0.1882 -0.0025 126 HIS C CB  
6903  C CG  . HIS C 126 ? 0.3544 0.3811 0.7251 -0.0686 -0.2090 -0.0076 126 HIS C CG  
6904  N ND1 . HIS C 126 ? 0.3835 0.4325 0.7963 -0.0722 -0.2127 -0.0041 126 HIS C ND1 
6905  C CD2 . HIS C 126 ? 0.3605 0.3714 0.6933 -0.0681 -0.2269 -0.0158 126 HIS C CD2 
6906  C CE1 . HIS C 126 ? 0.4079 0.4552 0.8092 -0.0742 -0.2340 -0.0098 126 HIS C CE1 
6907  N NE2 . HIS C 126 ? 0.3979 0.4213 0.7494 -0.0719 -0.2423 -0.0169 126 HIS C NE2 
6908  N N   . SER C 127 ? 0.3193 0.3780 0.7501 -0.0553 -0.1384 0.0199  127 SER C N   
6909  C CA  . SER C 127 ? 0.3143 0.3682 0.7493 -0.0567 -0.1115 0.0263  127 SER C CA  
6910  C C   . SER C 127 ? 0.3184 0.3649 0.7723 -0.0719 -0.1131 0.0241  127 SER C C   
6911  O O   . SER C 127 ? 0.3208 0.3595 0.7710 -0.0796 -0.1343 0.0157  127 SER C O   
6912  C CB  . SER C 127 ? 0.2965 0.3733 0.7675 -0.0515 -0.0934 0.0350  127 SER C CB  
6913  O OG  . SER C 127 ? 0.2936 0.3971 0.8199 -0.0572 -0.1039 0.0359  127 SER C OG  
6914  N N   . THR C 128 ? 0.3405 0.3852 0.8098 -0.0765 -0.0903 0.0314  128 THR C N   
6915  C CA  . THR C 128 ? 0.3760 0.4141 0.8702 -0.0924 -0.0900 0.0309  128 THR C CA  
6916  C C   . THR C 128 ? 0.4000 0.4613 0.9410 -0.0963 -0.0734 0.0389  128 THR C C   
6917  O O   . THR C 128 ? 0.4197 0.4964 0.9755 -0.0891 -0.0560 0.0465  128 THR C O   
6918  C CB  . THR C 128 ? 0.3696 0.3762 0.8288 -0.0937 -0.0755 0.0332  128 THR C CB  
6919  O OG1 . THR C 128 ? 0.3888 0.3961 0.8447 -0.0880 -0.0479 0.0444  128 THR C OG1 
6920  C CG2 . THR C 128 ? 0.3258 0.3101 0.7312 -0.0846 -0.0863 0.0259  128 THR C CG2 
6921  N N   . HIS C 129 ? 0.4084 0.4714 0.9707 -0.1074 -0.0775 0.0365  129 HIS C N   
6922  C CA  . HIS C 129 ? 0.4136 0.4971 1.0195 -0.1124 -0.0604 0.0437  129 HIS C CA  
6923  C C   . HIS C 129 ? 0.4252 0.4900 1.0318 -0.1264 -0.0524 0.0444  129 HIS C C   
6924  O O   . HIS C 129 ? 0.4128 0.4716 1.0211 -0.1359 -0.0705 0.0362  129 HIS C O   
6925  C CB  . HIS C 129 ? 0.4560 0.5689 1.0979 -0.1116 -0.0770 0.0404  129 HIS C CB  
6926  C CG  . HIS C 129 ? 0.5177 0.6545 1.2076 -0.1154 -0.0587 0.0476  129 HIS C CG  
6927  N ND1 . HIS C 129 ? 0.5395 0.6854 1.2416 -0.1083 -0.0300 0.0573  129 HIS C ND1 
6928  C CD2 . HIS C 129 ? 0.5561 0.7099 1.2846 -0.1256 -0.0648 0.0462  129 HIS C CD2 
6929  C CE1 . HIS C 129 ? 0.5722 0.7389 1.3175 -0.1133 -0.0181 0.0615  129 HIS C CE1 
6930  N NE2 . HIS C 129 ? 0.5785 0.7517 1.3427 -0.1243 -0.0393 0.0552  129 HIS C NE2 
6931  N N   . GLY C 130 ? 0.4630 0.5152 1.0631 -0.1275 -0.0250 0.0543  130 GLY C N   
6932  C CA  . GLY C 130 ? 0.5040 0.5317 1.0957 -0.1392 -0.0161 0.0564  130 GLY C CA  
6933  C C   . GLY C 130 ? 0.4961 0.4916 1.0464 -0.1401 -0.0328 0.0481  130 GLY C C   
6934  O O   . GLY C 130 ? 0.4484 0.4293 0.9641 -0.1301 -0.0338 0.0482  130 GLY C O   
6935  N N   . SER C 131 ? 0.5061 0.4903 1.0600 -0.1520 -0.0456 0.0404  131 SER C N   
6936  C CA  . SER C 131 ? 0.5068 0.4585 1.0222 -0.1530 -0.0602 0.0311  131 SER C CA  
6937  C C   . SER C 131 ? 0.5371 0.4947 1.0423 -0.1505 -0.0898 0.0170  131 SER C C   
6938  O O   . SER C 131 ? 0.5894 0.5208 1.0617 -0.1508 -0.1022 0.0074  131 SER C O   
6939  C CB  . SER C 131 ? 0.5251 0.4536 1.0425 -0.1673 -0.0551 0.0303  131 SER C CB  
6940  O OG  . SER C 131 ? 0.4947 0.4383 1.0419 -0.1800 -0.0705 0.0220  131 SER C OG  
6941  N N   . LYS C 132 ? 0.5089 0.4991 1.0396 -0.1471 -0.1004 0.0159  132 LYS C N   
6942  C CA  . LYS C 132 ? 0.4784 0.4736 0.9964 -0.1443 -0.1282 0.0042  132 LYS C CA  
6943  C C   . LYS C 132 ? 0.4802 0.4864 0.9828 -0.1291 -0.1320 0.0060  132 LYS C C   
6944  O O   . LYS C 132 ? 0.5102 0.5233 1.0180 -0.1219 -0.1135 0.0157  132 LYS C O   
6945  C CB  . LYS C 132 ? 0.4536 0.4751 1.0107 -0.1528 -0.1415 0.0013  132 LYS C CB  
6946  C CG  . LYS C 132 ? 0.5379 0.5504 1.1136 -0.1699 -0.1378 -0.0007 132 LYS C CG  
6947  C CD  . LYS C 132 ? 0.6447 0.6496 1.2112 -0.1791 -0.1639 -0.0145 132 LYS C CD  
6948  C CE  . LYS C 132 ? 0.7047 0.7227 1.2566 -0.1690 -0.1873 -0.0205 132 LYS C CE  
6949  N NZ  . LYS C 132 ? 0.7786 0.7843 1.3132 -0.1781 -0.2118 -0.0343 132 LYS C NZ  
6950  N N   . LEU C 133 ? 0.4397 0.4457 0.9207 -0.1243 -0.1550 -0.0030 133 LEU C N   
6951  C CA  . LEU C 133 ? 0.4181 0.4386 0.8905 -0.1108 -0.1602 -0.0007 133 LEU C CA  
6952  C C   . LEU C 133 ? 0.3734 0.4288 0.8900 -0.1074 -0.1568 0.0071  133 LEU C C   
6953  O O   . LEU C 133 ? 0.4011 0.4721 0.9485 -0.1146 -0.1645 0.0059  133 LEU C O   
6954  C CB  . LEU C 133 ? 0.4358 0.4463 0.8721 -0.1069 -0.1849 -0.0113 133 LEU C CB  
6955  C CG  . LEU C 133 ? 0.4437 0.4212 0.8299 -0.1051 -0.1887 -0.0198 133 LEU C CG  
6956  C CD1 . LEU C 133 ? 0.4838 0.4550 0.8369 -0.1014 -0.2114 -0.0294 133 LEU C CD1 
6957  C CD2 . LEU C 133 ? 0.3677 0.3377 0.7364 -0.0960 -0.1735 -0.0142 133 LEU C CD2 
6958  N N   . GLY C 134 ? 0.3342 0.4012 0.8536 -0.0961 -0.1453 0.0144  134 GLY C N   
6959  C CA  . GLY C 134 ? 0.3269 0.4241 0.8853 -0.0903 -0.1398 0.0214  134 GLY C CA  
6960  C C   . GLY C 134 ? 0.3412 0.4477 0.8878 -0.0784 -0.1572 0.0198  134 GLY C C   
6961  O O   . GLY C 134 ? 0.3242 0.4146 0.8323 -0.0764 -0.1757 0.0127  134 GLY C O   
6962  N N   . PRO C 135 ? 0.3606 0.4907 0.9373 -0.0697 -0.1495 0.0268  135 PRO C N   
6963  C CA  . PRO C 135 ? 0.4156 0.5534 0.9830 -0.0578 -0.1652 0.0267  135 PRO C CA  
6964  C C   . PRO C 135 ? 0.4613 0.5813 0.9821 -0.0480 -0.1674 0.0255  135 PRO C C   
6965  O O   . PRO C 135 ? 0.4487 0.5586 0.9549 -0.0469 -0.1515 0.0272  135 PRO C O   
6966  C CB  . PRO C 135 ? 0.3659 0.5297 0.9770 -0.0501 -0.1491 0.0352  135 PRO C CB  
6967  C CG  . PRO C 135 ? 0.3453 0.5096 0.9735 -0.0548 -0.1203 0.0401  135 PRO C CG  
6968  C CD  . PRO C 135 ? 0.3429 0.4910 0.9608 -0.0697 -0.1236 0.0353  135 PRO C CD  
6969  N N   . MET C 136 ? 0.2785 0.3946 0.7756 -0.0414 -0.1872 0.0230  136 MET C N   
6970  C CA  . MET C 136 ? 0.3193 0.4202 0.7744 -0.0317 -0.1888 0.0227  136 MET C CA  
6971  C C   . MET C 136 ? 0.3365 0.4482 0.8072 -0.0207 -0.1692 0.0305  136 MET C C   
6972  O O   . MET C 136 ? 0.3265 0.4580 0.8352 -0.0163 -0.1620 0.0358  136 MET C O   
6973  C CB  . MET C 136 ? 0.3380 0.4325 0.7657 -0.0265 -0.2113 0.0204  136 MET C CB  
6974  C CG  . MET C 136 ? 0.3728 0.4584 0.7866 -0.0363 -0.2313 0.0125  136 MET C CG  
6975  S SD  . MET C 136 ? 0.6034 0.6571 0.9615 -0.0411 -0.2332 0.0034  136 MET C SD  
6976  C CE  . MET C 136 ? 0.5382 0.5790 0.8500 -0.0288 -0.2397 0.0053  136 MET C CE  
6977  N N   . VAL C 137 ? 0.3563 0.4548 0.7979 -0.0160 -0.1601 0.0307  137 VAL C N   
6978  C CA  . VAL C 137 ? 0.3302 0.4295 0.7677 -0.0038 -0.1409 0.0363  137 VAL C CA  
6979  C C   . VAL C 137 ? 0.2996 0.3805 0.6896 0.0046  -0.1494 0.0350  137 VAL C C   
6980  O O   . VAL C 137 ? 0.2873 0.3518 0.6412 0.0001  -0.1618 0.0296  137 VAL C O   
6981  C CB  . VAL C 137 ? 0.3362 0.4255 0.7609 -0.0059 -0.1126 0.0374  137 VAL C CB  
6982  C CG1 . VAL C 137 ? 0.3166 0.4247 0.7908 -0.0127 -0.0998 0.0412  137 VAL C CG1 
6983  C CG2 . VAL C 137 ? 0.2194 0.2856 0.6005 -0.0126 -0.1139 0.0320  137 VAL C CG2 
6984  N N   . LYS C 138 ? 0.3110 0.3931 0.7015 0.0166  -0.1415 0.0398  138 LYS C N   
6985  C CA  . LYS C 138 ? 0.3110 0.3758 0.6614 0.0242  -0.1499 0.0400  138 LYS C CA  
6986  C C   . LYS C 138 ? 0.3120 0.3586 0.6268 0.0287  -0.1288 0.0397  138 LYS C C   
6987  O O   . LYS C 138 ? 0.3054 0.3549 0.6318 0.0314  -0.1075 0.0413  138 LYS C O   
6988  C CB  . LYS C 138 ? 0.3252 0.3998 0.6969 0.0344  -0.1616 0.0457  138 LYS C CB  
6989  C CG  . LYS C 138 ? 0.3641 0.4497 0.7512 0.0289  -0.1808 0.0444  138 LYS C CG  
6990  C CD  . LYS C 138 ? 0.3867 0.4787 0.7855 0.0396  -0.1881 0.0501  138 LYS C CD  
6991  C CE  . LYS C 138 ? 0.4127 0.5177 0.8292 0.0343  -0.2087 0.0491  138 LYS C CE  
6992  N NZ  . LYS C 138 ? 0.4411 0.5529 0.8676 0.0452  -0.2185 0.0552  138 LYS C NZ  
6993  N N   . VAL C 139 ? 0.3231 0.3505 0.5933 0.0286  -0.1352 0.0373  139 VAL C N   
6994  C CA  . VAL C 139 ? 0.3260 0.3367 0.5646 0.0335  -0.1214 0.0377  139 VAL C CA  
6995  C C   . VAL C 139 ? 0.3500 0.3543 0.5825 0.0419  -0.1335 0.0424  139 VAL C C   
6996  O O   . VAL C 139 ? 0.3627 0.3575 0.5701 0.0402  -0.1493 0.0421  139 VAL C O   
6997  C CB  . VAL C 139 ? 0.3925 0.3871 0.5878 0.0270  -0.1181 0.0325  139 VAL C CB  
6998  C CG1 . VAL C 139 ? 0.3865 0.3667 0.5545 0.0301  -0.1043 0.0325  139 VAL C CG1 
6999  C CG2 . VAL C 139 ? 0.3950 0.3941 0.5952 0.0194  -0.1102 0.0289  139 VAL C CG2 
7000  N N   . PRO C 140 ? 0.3745 0.3825 0.6293 0.0518  -0.1257 0.0471  140 PRO C N   
7001  C CA  . PRO C 140 ? 0.4153 0.4178 0.6707 0.0617  -0.1391 0.0534  140 PRO C CA  
7002  C C   . PRO C 140 ? 0.4246 0.3998 0.6324 0.0627  -0.1380 0.0541  140 PRO C C   
7003  O O   . PRO C 140 ? 0.4423 0.4084 0.6380 0.0677  -0.1537 0.0597  140 PRO C O   
7004  C CB  . PRO C 140 ? 0.4341 0.4470 0.7283 0.0728  -0.1261 0.0574  140 PRO C CB  
7005  C CG  . PRO C 140 ? 0.4035 0.4324 0.7227 0.0670  -0.1096 0.0535  140 PRO C CG  
7006  C CD  . PRO C 140 ? 0.3641 0.3811 0.6459 0.0554  -0.1043 0.0473  140 PRO C CD  
7007  N N   . GLN C 141 ? 0.4171 0.3797 0.5986 0.0575  -0.1205 0.0493  141 GLN C N   
7008  C CA  . GLN C 141 ? 0.4681 0.4070 0.6078 0.0557  -0.1186 0.0495  141 GLN C CA  
7009  C C   . GLN C 141 ? 0.3818 0.3173 0.4923 0.0445  -0.1175 0.0435  141 GLN C C   
7010  O O   . GLN C 141 ? 0.3635 0.2901 0.4543 0.0399  -0.1041 0.0398  141 GLN C O   
7011  C CB  . GLN C 141 ? 0.5369 0.4610 0.6693 0.0594  -0.0997 0.0487  141 GLN C CB  
7012  C CG  . GLN C 141 ? 0.6122 0.5315 0.7661 0.0726  -0.0976 0.0545  141 GLN C CG  
7013  C CD  . GLN C 141 ? 0.7118 0.6490 0.9052 0.0784  -0.0861 0.0532  141 GLN C CD  
7014  O OE1 . GLN C 141 ? 0.7367 0.6845 0.9349 0.0717  -0.0755 0.0477  141 GLN C OE1 
7015  N NE2 . GLN C 141 ? 0.7753 0.7152 0.9975 0.0916  -0.0869 0.0588  141 GLN C NE2 
7016  N N   . PHE C 142 ? 0.3706 0.3136 0.4799 0.0402  -0.1318 0.0421  142 PHE C N   
7017  C CA  . PHE C 142 ? 0.3357 0.2752 0.4190 0.0313  -0.1307 0.0362  142 PHE C CA  
7018  C C   . PHE C 142 ? 0.3604 0.2809 0.4049 0.0297  -0.1318 0.0378  142 PHE C C   
7019  O O   . PHE C 142 ? 0.3658 0.2771 0.3993 0.0335  -0.1443 0.0432  142 PHE C O   
7020  C CB  . PHE C 142 ? 0.2926 0.2424 0.3855 0.0274  -0.1451 0.0330  142 PHE C CB  
7021  C CG  . PHE C 142 ? 0.3379 0.2836 0.4077 0.0199  -0.1420 0.0261  142 PHE C CG  
7022  C CD1 . PHE C 142 ? 0.2949 0.2477 0.3741 0.0162  -0.1295 0.0220  142 PHE C CD1 
7023  C CD2 . PHE C 142 ? 0.3592 0.2927 0.3966 0.0175  -0.1504 0.0242  142 PHE C CD2 
7024  C CE1 . PHE C 142 ? 0.3363 0.2853 0.3966 0.0113  -0.1266 0.0163  142 PHE C CE1 
7025  C CE2 . PHE C 142 ? 0.3414 0.2713 0.3598 0.0122  -0.1455 0.0175  142 PHE C CE2 
7026  C CZ  . PHE C 142 ? 0.3440 0.2822 0.3757 0.0097  -0.1339 0.0137  142 PHE C CZ  
7027  N N   . LEU C 143 ? 0.3655 0.2807 0.3901 0.0238  -0.1189 0.0337  143 LEU C N   
7028  C CA  . LEU C 143 ? 0.3882 0.2877 0.3792 0.0202  -0.1161 0.0348  143 LEU C CA  
7029  C C   . LEU C 143 ? 0.4222 0.3211 0.3918 0.0151  -0.1203 0.0307  143 LEU C C   
7030  O O   . LEU C 143 ? 0.4317 0.3413 0.4080 0.0119  -0.1171 0.0244  143 LEU C O   
7031  C CB  . LEU C 143 ? 0.3986 0.2941 0.3833 0.0159  -0.0996 0.0326  143 LEU C CB  
7032  C CG  . LEU C 143 ? 0.4120 0.3008 0.4088 0.0202  -0.0924 0.0351  143 LEU C CG  
7033  C CD1 . LEU C 143 ? 0.3978 0.2841 0.3870 0.0137  -0.0782 0.0302  143 LEU C CD1 
7034  C CD2 . LEU C 143 ? 0.3984 0.2685 0.3850 0.0255  -0.0974 0.0430  143 LEU C CD2 
7035  N N   . PHE C 144 ? 0.4553 0.3393 0.3968 0.0150  -0.1260 0.0345  144 PHE C N   
7036  C CA  . PHE C 144 ? 0.4349 0.3145 0.3510 0.0114  -0.1292 0.0304  144 PHE C CA  
7037  C C   . PHE C 144 ? 0.4661 0.3257 0.3463 0.0100  -0.1269 0.0361  144 PHE C C   
7038  O O   . PHE C 144 ? 0.4896 0.3384 0.3668 0.0117  -0.1242 0.0434  144 PHE C O   
7039  C CB  . PHE C 144 ? 0.4463 0.3297 0.3686 0.0138  -0.1474 0.0282  144 PHE C CB  
7040  C CG  . PHE C 144 ? 0.4536 0.3288 0.3725 0.0194  -0.1640 0.0360  144 PHE C CG  
7041  C CD1 . PHE C 144 ? 0.4334 0.3171 0.3845 0.0254  -0.1687 0.0414  144 PHE C CD1 
7042  C CD2 . PHE C 144 ? 0.4904 0.3487 0.3730 0.0195  -0.1749 0.0385  144 PHE C CD2 
7043  C CE1 . PHE C 144 ? 0.4462 0.3238 0.3976 0.0323  -0.1851 0.0496  144 PHE C CE1 
7044  C CE2 . PHE C 144 ? 0.5169 0.3672 0.3950 0.0258  -0.1927 0.0471  144 PHE C CE2 
7045  C CZ  . PHE C 144 ? 0.4931 0.3541 0.4078 0.0326  -0.1985 0.0530  144 PHE C CZ  
7046  N N   . SER C 145 ? 0.4661 0.3184 0.3177 0.0071  -0.1271 0.0329  145 SER C N   
7047  C CA  . SER C 145 ? 0.4911 0.3232 0.3055 0.0051  -0.1224 0.0388  145 SER C CA  
7048  C C   . SER C 145 ? 0.5587 0.3753 0.3440 0.0088  -0.1401 0.0419  145 SER C C   
7049  O O   . SER C 145 ? 0.5590 0.3798 0.3417 0.0092  -0.1505 0.0347  145 SER C O   
7050  C CB  . SER C 145 ? 0.4831 0.3177 0.2837 -0.0015 -0.1040 0.0333  145 SER C CB  
7051  O OG  . SER C 145 ? 0.5268 0.3419 0.2903 -0.0044 -0.0967 0.0390  145 SER C OG  
7052  N N   . CYS C 146 ? 0.5968 0.3940 0.3600 0.0115  -0.1448 0.0529  146 CYS C N   
7053  C CA  . CYS C 146 ? 0.5857 0.3634 0.3098 0.0142  -0.1598 0.0575  146 CYS C CA  
7054  C C   . CYS C 146 ? 0.5994 0.3619 0.2822 0.0081  -0.1430 0.0565  146 CYS C C   
7055  O O   . CYS C 146 ? 0.6165 0.3666 0.2861 0.0051  -0.1287 0.0644  146 CYS C O   
7056  C CB  . CYS C 146 ? 0.5742 0.3359 0.2914 0.0211  -0.1720 0.0716  146 CYS C CB  
7057  S SG  . CYS C 146 ? 0.6744 0.4531 0.4354 0.0308  -0.1973 0.0740  146 CYS C SG  
7058  N N   . ALA C 147 ? 0.6227 0.3857 0.2869 0.0059  -0.1427 0.0466  147 ALA C N   
7059  C CA  . ALA C 147 ? 0.6955 0.4477 0.3250 0.0007  -0.1226 0.0437  147 ALA C CA  
7060  C C   . ALA C 147 ? 0.7701 0.4921 0.3414 0.0018  -0.1286 0.0502  147 ALA C C   
7061  O O   . ALA C 147 ? 0.8111 0.5225 0.3674 0.0068  -0.1530 0.0537  147 ALA C O   
7062  C CB  . ALA C 147 ? 0.6894 0.4562 0.3291 -0.0009 -0.1153 0.0288  147 ALA C CB  
7063  N N   . PRO C 148 ? 0.7501 0.4586 0.2884 -0.0032 -0.1063 0.0525  148 PRO C N   
7064  C CA  . PRO C 148 ? 0.8006 0.4778 0.2767 -0.0025 -0.1088 0.0581  148 PRO C CA  
7065  C C   . PRO C 148 ? 0.8420 0.5176 0.3006 0.0002  -0.1222 0.0453  148 PRO C C   
7066  O O   . PRO C 148 ? 0.8179 0.5067 0.2905 -0.0010 -0.1163 0.0320  148 PRO C O   
7067  C CB  . PRO C 148 ? 0.8093 0.4806 0.2656 -0.0095 -0.0765 0.0592  148 PRO C CB  
7068  C CG  . PRO C 148 ? 0.7513 0.4553 0.2613 -0.0130 -0.0607 0.0497  148 PRO C CG  
7069  C CD  . PRO C 148 ? 0.7119 0.4337 0.2692 -0.0098 -0.0780 0.0504  148 PRO C CD  
7070  N N   . SER C 149 ? 0.9036 0.5672 0.3414 0.0034  -0.1376 0.0483  149 SER C N   
7071  C CA  . SER C 149 ? 0.9497 0.6128 0.3770 0.0050  -0.1527 0.0361  149 SER C CA  
7072  C C   . SER C 149 ? 0.9193 0.5742 0.3163 0.0021  -0.1343 0.0228  149 SER C C   
7073  O O   . SER C 149 ? 0.9247 0.5844 0.3275 0.0024  -0.1430 0.0090  149 SER C O   
7074  C CB  . SER C 149 ? 1.0761 0.7243 0.4779 0.0081  -0.1695 0.0438  149 SER C CB  
7075  O OG  . SER C 149 ? 1.1876 0.8128 0.5423 0.0064  -0.1514 0.0512  149 SER C OG  
7076  N N   . PHE C 150 ? 0.9029 0.5452 0.2695 -0.0006 -0.1076 0.0269  150 PHE C N   
7077  C CA  . PHE C 150 ? 0.9027 0.5371 0.2404 -0.0019 -0.0869 0.0148  150 PHE C CA  
7078  C C   . PHE C 150 ? 0.8620 0.5134 0.2279 -0.0017 -0.0798 0.0009  150 PHE C C   
7079  O O   . PHE C 150 ? 0.9310 0.5777 0.2816 -0.0005 -0.0699 -0.0128 150 PHE C O   
7080  C CB  . PHE C 150 ? 1.0107 0.6339 0.3210 -0.0056 -0.0559 0.0232  150 PHE C CB  
7081  C CG  . PHE C 150 ? 0.9837 0.6231 0.3223 -0.0095 -0.0342 0.0256  150 PHE C CG  
7082  C CD1 . PHE C 150 ? 0.9691 0.6212 0.3190 -0.0097 -0.0136 0.0128  150 PHE C CD1 
7083  C CD2 . PHE C 150 ? 0.9624 0.6049 0.3198 -0.0129 -0.0344 0.0403  150 PHE C CD2 
7084  C CE1 . PHE C 150 ? 0.9239 0.6061 0.3275 -0.0132 0.0052  0.0143  150 PHE C CE1 
7085  C CE2 . PHE C 150 ? 0.9028 0.5703 0.3062 -0.0176 -0.0149 0.0407  150 PHE C CE2 
7086  C CZ  . PHE C 150 ? 0.8850 0.5747 0.3140 -0.0180 0.0040  0.0278  150 PHE C CZ  
7087  N N   . LEU C 151 ? 0.8384 0.5083 0.2449 -0.0024 -0.0836 0.0045  151 LEU C N   
7088  C CA  . LEU C 151 ? 0.8323 0.5294 0.2864 -0.0022 -0.0689 -0.0062 151 LEU C CA  
7089  C C   . LEU C 151 ? 0.8799 0.5773 0.3400 0.0007  -0.0854 -0.0214 151 LEU C C   
7090  O O   . LEU C 151 ? 0.8818 0.5866 0.3537 0.0025  -0.0712 -0.0335 151 LEU C O   
7091  C CB  . LEU C 151 ? 0.7555 0.4806 0.2687 -0.0039 -0.0683 0.0017  151 LEU C CB  
7092  C CG  . LEU C 151 ? 0.7066 0.4598 0.2651 -0.0046 -0.0481 -0.0047 151 LEU C CG  
7093  C CD1 . LEU C 151 ? 0.6792 0.4308 0.2200 -0.0069 -0.0180 -0.0052 151 LEU C CD1 
7094  C CD2 . LEU C 151 ? 0.6573 0.4329 0.2650 -0.0068 -0.0509 0.0030  151 LEU C CD2 
7095  N N   . ALA C 152 ? 0.9018 0.5893 0.3520 0.0012  -0.1154 -0.0207 152 ALA C N   
7096  C CA  . ALA C 152 ? 0.9026 0.5935 0.3685 0.0018  -0.1318 -0.0343 152 ALA C CA  
7097  C C   . ALA C 152 ? 0.9648 0.6347 0.3898 0.0017  -0.1338 -0.0426 152 ALA C C   
7098  O O   . ALA C 152 ? 0.9750 0.6433 0.4069 0.0008  -0.1484 -0.0536 152 ALA C O   
7099  C CB  . ALA C 152 ? 0.8624 0.5691 0.3692 0.0012  -0.1589 -0.0289 152 ALA C CB  
7100  N N   . GLN C 153 ? 0.9651 0.6181 0.3471 0.0019  -0.1188 -0.0372 153 GLN C N   
7101  C CA  . GLN C 153 ? 0.9745 0.6065 0.3147 0.0019  -0.1228 -0.0439 153 GLN C CA  
7102  C C   . GLN C 153 ? 0.9724 0.5948 0.2957 0.0034  -0.1048 -0.0611 153 GLN C C   
7103  O O   . GLN C 153 ? 1.0199 0.6244 0.3109 0.0032  -0.1093 -0.0700 153 GLN C O   
7104  C CB  . GLN C 153 ? 1.0060 0.6214 0.3045 0.0018  -0.1138 -0.0316 153 GLN C CB  
7105  C CG  . GLN C 153 ? 1.0245 0.6405 0.3282 0.0018  -0.1389 -0.0180 153 GLN C CG  
7106  C CD  . GLN C 153 ? 1.1190 0.7163 0.3811 0.0020  -0.1296 -0.0050 153 GLN C CD  
7107  O OE1 . GLN C 153 ? 1.1675 0.7542 0.4015 0.0011  -0.1018 -0.0047 153 GLN C OE1 
7108  N NE2 . GLN C 153 ? 1.1550 0.7486 0.4141 0.0034  -0.1520 0.0060  153 GLN C NE2 
7109  N N   . LYS C 154 ? 0.9441 0.5778 0.2889 0.0055  -0.0845 -0.0663 154 LYS C N   
7110  C CA  . LYS C 154 ? 0.9983 0.6230 0.3299 0.0091  -0.0646 -0.0824 154 LYS C CA  
7111  C C   . LYS C 154 ? 0.9645 0.6031 0.3369 0.0117  -0.0634 -0.0922 154 LYS C C   
7112  O O   . LYS C 154 ? 0.9167 0.5735 0.3207 0.0120  -0.0603 -0.0857 154 LYS C O   
7113  C CB  . LYS C 154 ? 1.0503 0.6701 0.3562 0.0115  -0.0291 -0.0799 154 LYS C CB  
7114  C CG  . LYS C 154 ? 1.1606 0.7590 0.4165 0.0098  -0.0270 -0.0753 154 LYS C CG  
7115  C CD  . LYS C 154 ? 1.2431 0.8344 0.4719 0.0121  0.0092  -0.0758 154 LYS C CD  
7116  C CE  . LYS C 154 ? 1.3620 0.9262 0.5392 0.0124  0.0067  -0.0821 154 LYS C CE  
7117  N NZ  . LYS C 154 ? 1.4308 0.9830 0.5707 0.0132  0.0373  -0.0788 154 LYS C NZ  
7118  N N   . GLY C 155 ? 1.0324 0.6603 0.4022 0.0135  -0.0659 -0.1078 155 GLY C N   
7119  C CA  . GLY C 155 ? 1.0447 0.6799 0.4476 0.0178  -0.0593 -0.1188 155 GLY C CA  
7120  C C   . GLY C 155 ? 1.0308 0.6748 0.4734 0.0143  -0.0854 -0.1216 155 GLY C C   
7121  O O   . GLY C 155 ? 1.0710 0.7147 0.5359 0.0179  -0.0805 -0.1320 155 GLY C O   
7122  N N   . LEU C 156 ? 0.9507 0.6029 0.4051 0.0079  -0.1116 -0.1118 156 LEU C N   
7123  C CA  . LEU C 156 ? 0.8343 0.5004 0.3338 0.0038  -0.1339 -0.1119 156 LEU C CA  
7124  C C   . LEU C 156 ? 0.8291 0.4840 0.3264 -0.0017 -0.1539 -0.1210 156 LEU C C   
7125  O O   . LEU C 156 ? 0.8656 0.5027 0.3236 -0.0031 -0.1565 -0.1253 156 LEU C O   
7126  C CB  . LEU C 156 ? 0.8011 0.4878 0.3256 0.0010  -0.1485 -0.0952 156 LEU C CB  
7127  C CG  . LEU C 156 ? 0.7794 0.4811 0.3119 0.0043  -0.1292 -0.0830 156 LEU C CG  
7128  C CD1 . LEU C 156 ? 0.7851 0.5058 0.3477 0.0018  -0.1449 -0.0677 156 LEU C CD1 
7129  C CD2 . LEU C 156 ? 0.7323 0.4535 0.3043 0.0088  -0.1055 -0.0850 156 LEU C CD2 
7130  N N   . PRO C 157 ? 0.7857 0.4508 0.3254 -0.0055 -0.1674 -0.1241 157 PRO C N   
7131  C CA  . PRO C 157 ? 0.8321 0.4897 0.3742 -0.0127 -0.1876 -0.1312 157 PRO C CA  
7132  C C   . PRO C 157 ? 0.8878 0.5493 0.4173 -0.0168 -0.2078 -0.1222 157 PRO C C   
7133  O O   . PRO C 157 ? 0.8625 0.5364 0.3943 -0.0145 -0.2091 -0.1083 157 PRO C O   
7134  C CB  . PRO C 157 ? 0.7813 0.4556 0.3786 -0.0167 -0.1971 -0.1305 157 PRO C CB  
7135  C CG  . PRO C 157 ? 0.7478 0.4273 0.3605 -0.0097 -0.1771 -0.1301 157 PRO C CG  
7136  C CD  . PRO C 157 ? 0.7686 0.4509 0.3543 -0.0039 -0.1640 -0.1217 157 PRO C CD  
7137  N N   . ASN C 158 ? 0.9437 0.5936 0.4599 -0.0226 -0.2237 -0.1303 158 ASN C N   
7138  C CA  . ASN C 158 ? 1.0239 0.6732 0.5211 -0.0254 -0.2430 -0.1238 158 ASN C CA  
7139  C C   . ASN C 158 ? 0.9648 0.6424 0.5076 -0.0269 -0.2605 -0.1088 158 ASN C C   
7140  O O   . ASN C 158 ? 0.9105 0.6058 0.5024 -0.0304 -0.2668 -0.1085 158 ASN C O   
7141  C CB  . ASN C 158 ? 1.1608 0.7932 0.6397 -0.0323 -0.2575 -0.1377 158 ASN C CB  
7142  C CG  . ASN C 158 ? 1.3069 0.9326 0.7538 -0.0343 -0.2762 -0.1337 158 ASN C CG  
7143  O OD1 . ASN C 158 ? 1.3401 0.9833 0.8141 -0.0378 -0.2985 -0.1255 158 ASN C OD1 
7144  N ND2 . ASN C 158 ? 1.3928 0.9932 0.7820 -0.0316 -0.2667 -0.1393 158 ASN C ND2 
7145  N N   . ASN C 159 ? 0.9747 0.6551 0.5009 -0.0235 -0.2657 -0.0960 159 ASN C N   
7146  C CA  . ASN C 159 ? 0.9902 0.6945 0.5538 -0.0227 -0.2808 -0.0811 159 ASN C CA  
7147  C C   . ASN C 159 ? 0.9039 0.6298 0.5106 -0.0193 -0.2696 -0.0719 159 ASN C C   
7148  O O   . ASN C 159 ? 0.9008 0.6471 0.5429 -0.0181 -0.2799 -0.0604 159 ASN C O   
7149  C CB  . ASN C 159 ? 1.1162 0.8324 0.7104 -0.0293 -0.3062 -0.0837 159 ASN C CB  
7150  C CG  . ASN C 159 ? 1.3236 1.0262 0.8796 -0.0309 -0.3249 -0.0846 159 ASN C CG  
7151  O OD1 . ASN C 159 ? 1.4267 1.1048 0.9275 -0.0289 -0.3173 -0.0884 159 ASN C OD1 
7152  N ND2 . ASN C 159 ? 1.3647 1.0835 0.9504 -0.0347 -0.3490 -0.0814 159 ASN C ND2 
7153  N N   . VAL C 160 ? 0.8282 0.5496 0.4321 -0.0173 -0.2487 -0.0774 160 VAL C N   
7154  C CA  . VAL C 160 ? 0.7421 0.4817 0.3803 -0.0142 -0.2375 -0.0697 160 VAL C CA  
7155  C C   . VAL C 160 ? 0.7651 0.5041 0.3832 -0.0090 -0.2289 -0.0567 160 VAL C C   
7156  O O   . VAL C 160 ? 0.8265 0.5464 0.3972 -0.0070 -0.2186 -0.0573 160 VAL C O   
7157  C CB  . VAL C 160 ? 0.7233 0.4571 0.3629 -0.0132 -0.2189 -0.0803 160 VAL C CB  
7158  C CG1 . VAL C 160 ? 0.6844 0.4319 0.3423 -0.0090 -0.2046 -0.0725 160 VAL C CG1 
7159  C CG2 . VAL C 160 ? 0.7103 0.4488 0.3844 -0.0186 -0.2273 -0.0894 160 VAL C CG2 
7160  N N   . GLN C 161 ? 0.7307 0.4895 0.3843 -0.0071 -0.2322 -0.0446 161 GLN C N   
7161  C CA  . GLN C 161 ? 0.8022 0.5590 0.4397 -0.0029 -0.2274 -0.0309 161 GLN C CA  
7162  C C   . GLN C 161 ? 0.7464 0.5130 0.3996 -0.0005 -0.2108 -0.0247 161 GLN C C   
7163  O O   . GLN C 161 ? 0.7193 0.4880 0.3724 0.0022  -0.2086 -0.0121 161 GLN C O   
7164  C CB  . GLN C 161 ? 0.8819 0.6501 0.5425 -0.0015 -0.2469 -0.0205 161 GLN C CB  
7165  C CG  . GLN C 161 ? 1.0221 0.7774 0.6544 -0.0027 -0.2631 -0.0227 161 GLN C CG  
7166  C CD  . GLN C 161 ? 1.1239 0.8963 0.7920 -0.0018 -0.2841 -0.0156 161 GLN C CD  
7167  O OE1 . GLN C 161 ? 1.1341 0.9271 0.8504 -0.0041 -0.2902 -0.0180 161 GLN C OE1 
7168  N NE2 . GLN C 161 ? 1.1983 0.9630 0.8445 0.0019  -0.2946 -0.0064 161 GLN C NE2 
7169  N N   . GLY C 162 ? 0.7214 0.4928 0.3876 -0.0016 -0.1996 -0.0335 162 GLY C N   
7170  C CA  . GLY C 162 ? 0.5658 0.3549 0.2611 0.0003  -0.1771 -0.0271 162 GLY C CA  
7171  C C   . GLY C 162 ? 0.5347 0.3367 0.2629 -0.0003 -0.1674 -0.0358 162 GLY C C   
7172  O O   . GLY C 162 ? 0.6032 0.3953 0.3231 -0.0019 -0.1734 -0.0472 162 GLY C O   
7173  N N   . ALA C 163 ? 0.4927 0.3148 0.2567 0.0009  -0.1536 -0.0302 163 ALA C N   
7174  C CA  . ALA C 163 ? 0.4843 0.3183 0.2783 0.0014  -0.1434 -0.0361 163 ALA C CA  
7175  C C   . ALA C 163 ? 0.4472 0.3025 0.2848 0.0014  -0.1428 -0.0284 163 ALA C C   
7176  O O   . ALA C 163 ? 0.4649 0.3264 0.3082 0.0019  -0.1425 -0.0191 163 ALA C O   
7177  C CB  . ALA C 163 ? 0.4917 0.3254 0.2734 0.0042  -0.1201 -0.0396 163 ALA C CB  
7178  N N   . LEU C 164 ? 0.4753 0.3391 0.3418 0.0009  -0.1425 -0.0322 164 LEU C N   
7179  C CA  . LEU C 164 ? 0.5115 0.3941 0.4147 0.0014  -0.1371 -0.0254 164 LEU C CA  
7180  C C   . LEU C 164 ? 0.4664 0.3566 0.3784 0.0040  -0.1193 -0.0270 164 LEU C C   
7181  O O   . LEU C 164 ? 0.4553 0.3394 0.3641 0.0055  -0.1153 -0.0343 164 LEU C O   
7182  C CB  . LEU C 164 ? 0.5765 0.4648 0.5091 -0.0014 -0.1503 -0.0255 164 LEU C CB  
7183  C CG  . LEU C 164 ? 0.6494 0.5290 0.5848 -0.0038 -0.1534 -0.0349 164 LEU C CG  
7184  C CD1 . LEU C 164 ? 0.6797 0.5707 0.6468 -0.0034 -0.1435 -0.0321 164 LEU C CD1 
7185  C CD2 . LEU C 164 ? 0.6858 0.5595 0.6245 -0.0091 -0.1742 -0.0387 164 LEU C CD2 
7186  N N   . GLY C 165 ? 0.4455 0.3484 0.3683 0.0049  -0.1092 -0.0204 165 GLY C N   
7187  C CA  . GLY C 165 ? 0.3801 0.2921 0.3103 0.0074  -0.0950 -0.0213 165 GLY C CA  
7188  C C   . GLY C 165 ? 0.3873 0.3109 0.3467 0.0079  -0.0941 -0.0178 165 GLY C C   
7189  O O   . GLY C 165 ? 0.3587 0.2880 0.3320 0.0061  -0.0977 -0.0122 165 GLY C O   
7190  N N   . LEU C 166 ? 0.3830 0.3085 0.3501 0.0111  -0.0883 -0.0207 166 LEU C N   
7191  C CA  . LEU C 166 ? 0.3790 0.3127 0.3689 0.0121  -0.0863 -0.0166 166 LEU C CA  
7192  C C   . LEU C 166 ? 0.3566 0.3027 0.3504 0.0157  -0.0761 -0.0143 166 LEU C C   
7193  O O   . LEU C 166 ? 0.3418 0.2920 0.3479 0.0188  -0.0736 -0.0118 166 LEU C O   
7194  C CB  . LEU C 166 ? 0.4062 0.3292 0.4031 0.0129  -0.0901 -0.0204 166 LEU C CB  
7195  C CG  . LEU C 166 ? 0.4208 0.3332 0.4201 0.0079  -0.1023 -0.0235 166 LEU C CG  
7196  C CD1 . LEU C 166 ? 0.4793 0.3791 0.4841 0.0081  -0.1033 -0.0282 166 LEU C CD1 
7197  C CD2 . LEU C 166 ? 0.4233 0.3451 0.4431 0.0042  -0.1065 -0.0167 166 LEU C CD2 
7198  N N   . GLY C 167 ? 0.3266 0.2788 0.3101 0.0149  -0.0708 -0.0146 167 GLY C N   
7199  C CA  . GLY C 167 ? 0.2992 0.2662 0.2889 0.0170  -0.0627 -0.0132 167 GLY C CA  
7200  C C   . GLY C 167 ? 0.3159 0.2939 0.3168 0.0144  -0.0629 -0.0076 167 GLY C C   
7201  O O   . GLY C 167 ? 0.3545 0.3281 0.3577 0.0114  -0.0669 -0.0046 167 GLY C O   
7202  N N   . GLN C 168 ? 0.3307 0.3234 0.3392 0.0160  -0.0586 -0.0066 168 GLN C N   
7203  C CA  . GLN C 168 ? 0.3168 0.3192 0.3315 0.0128  -0.0596 -0.0027 168 GLN C CA  
7204  C C   . GLN C 168 ? 0.3184 0.3233 0.3267 0.0051  -0.0571 -0.0030 168 GLN C C   
7205  O O   . GLN C 168 ? 0.3023 0.3197 0.3139 0.0025  -0.0530 -0.0042 168 GLN C O   
7206  C CB  . GLN C 168 ? 0.3079 0.3254 0.3335 0.0177  -0.0591 -0.0014 168 GLN C CB  
7207  C CG  . GLN C 168 ? 0.2916 0.3026 0.3218 0.0251  -0.0617 0.0011  168 GLN C CG  
7208  C CD  . GLN C 168 ? 0.3544 0.3569 0.3818 0.0224  -0.0645 0.0054  168 GLN C CD  
7209  O OE1 . GLN C 168 ? 0.4049 0.4139 0.4306 0.0198  -0.0657 0.0081  168 GLN C OE1 
7210  N NE2 . GLN C 168 ? 0.3359 0.3240 0.3629 0.0223  -0.0652 0.0056  168 GLN C NE2 
7211  N N   . ALA C 169 ? 0.3464 0.3392 0.3475 0.0016  -0.0592 -0.0017 169 ALA C N   
7212  C CA  . ALA C 169 ? 0.3453 0.3338 0.3376 -0.0050 -0.0569 -0.0012 169 ALA C CA  
7213  C C   . ALA C 169 ? 0.3594 0.3368 0.3507 -0.0057 -0.0603 0.0013  169 ALA C C   
7214  O O   . ALA C 169 ? 0.3688 0.3421 0.3659 -0.0015 -0.0640 0.0023  169 ALA C O   
7215  C CB  . ALA C 169 ? 0.3220 0.3032 0.3016 -0.0057 -0.0544 -0.0025 169 ALA C CB  
7216  N N   . PRO C 170 ? 0.3763 0.3488 0.3626 -0.0110 -0.0580 0.0023  170 PRO C N   
7217  C CA  . PRO C 170 ? 0.3752 0.3380 0.3625 -0.0106 -0.0587 0.0041  170 PRO C CA  
7218  C C   . PRO C 170 ? 0.3924 0.3451 0.3815 -0.0062 -0.0630 0.0068  170 PRO C C   
7219  O O   . PRO C 170 ? 0.4244 0.3747 0.4222 -0.0033 -0.0629 0.0082  170 PRO C O   
7220  C CB  . PRO C 170 ? 0.3881 0.3444 0.3670 -0.0176 -0.0547 0.0036  170 PRO C CB  
7221  C CG  . PRO C 170 ? 0.3986 0.3593 0.3720 -0.0221 -0.0522 0.0031  170 PRO C CG  
7222  C CD  . PRO C 170 ? 0.3914 0.3676 0.3727 -0.0183 -0.0532 0.0012  170 PRO C CD  
7223  N N   . ILE C 171 ? 0.3506 0.2976 0.3317 -0.0056 -0.0667 0.0077  171 ILE C N   
7224  C CA  . ILE C 171 ? 0.3163 0.2563 0.3015 -0.0012 -0.0744 0.0103  171 ILE C CA  
7225  C C   . ILE C 171 ? 0.3638 0.3058 0.3490 0.0010  -0.0810 0.0079  171 ILE C C   
7226  O O   . ILE C 171 ? 0.3580 0.2928 0.3384 0.0026  -0.0896 0.0090  171 ILE C O   
7227  C CB  . ILE C 171 ? 0.3312 0.2573 0.3045 -0.0014 -0.0770 0.0144  171 ILE C CB  
7228  C CG1 . ILE C 171 ? 0.3333 0.2535 0.2850 -0.0054 -0.0746 0.0144  171 ILE C CG1 
7229  C CG2 . ILE C 171 ? 0.2983 0.2182 0.2743 -0.0024 -0.0710 0.0161  171 ILE C CG2 
7230  C CD1 . ILE C 171 ? 0.3463 0.2497 0.2814 -0.0039 -0.0804 0.0200  171 ILE C CD1 
7231  N N   . SER C 172 ? 0.3819 0.3321 0.3718 0.0013  -0.0780 0.0046  172 SER C N   
7232  C CA  . SER C 172 ? 0.3803 0.3293 0.3721 0.0035  -0.0833 0.0014  172 SER C CA  
7233  C C   . SER C 172 ? 0.3878 0.3361 0.3967 0.0047  -0.0904 0.0032  172 SER C C   
7234  O O   . SER C 172 ? 0.3918 0.3432 0.4133 0.0052  -0.0880 0.0069  172 SER C O   
7235  C CB  . SER C 172 ? 0.3607 0.3171 0.3569 0.0051  -0.0778 -0.0013 172 SER C CB  
7236  O OG  . SER C 172 ? 0.3569 0.3199 0.3666 0.0057  -0.0745 0.0016  172 SER C OG  
7237  N N   . LEU C 173 ? 0.3802 0.3241 0.3905 0.0048  -0.0985 0.0002  173 LEU C N   
7238  C CA  . LEU C 173 ? 0.3728 0.3184 0.4037 0.0043  -0.1063 0.0018  173 LEU C CA  
7239  C C   . LEU C 173 ? 0.3830 0.3361 0.4353 0.0044  -0.0986 0.0045  173 LEU C C   
7240  O O   . LEU C 173 ? 0.3923 0.3507 0.4631 0.0047  -0.0979 0.0085  173 LEU C O   
7241  C CB  . LEU C 173 ? 0.3617 0.2999 0.3887 0.0024  -0.1174 -0.0036 173 LEU C CB  
7242  C CG  . LEU C 173 ? 0.3462 0.2886 0.4003 -0.0003 -0.1256 -0.0029 173 LEU C CG  
7243  C CD1 . LEU C 173 ? 0.3273 0.2767 0.3969 0.0008  -0.1329 0.0023  173 LEU C CD1 
7244  C CD2 . LEU C 173 ? 0.3622 0.2944 0.4087 -0.0037 -0.1368 -0.0101 173 LEU C CD2 
7245  N N   . GLN C 174 ? 0.3315 0.2844 0.3808 0.0049  -0.0923 0.0029  174 GLN C N   
7246  C CA  . GLN C 174 ? 0.3105 0.2671 0.3750 0.0050  -0.0851 0.0067  174 GLN C CA  
7247  C C   . GLN C 174 ? 0.3121 0.2740 0.3755 0.0062  -0.0765 0.0106  174 GLN C C   
7248  O O   . GLN C 174 ? 0.3136 0.2780 0.3905 0.0062  -0.0709 0.0144  174 GLN C O   
7249  C CB  . GLN C 174 ? 0.3137 0.2662 0.3731 0.0067  -0.0817 0.0052  174 GLN C CB  
7250  C CG  . GLN C 174 ? 0.3520 0.3089 0.3981 0.0101  -0.0752 0.0059  174 GLN C CG  
7251  C CD  . GLN C 174 ? 0.3285 0.2860 0.3597 0.0111  -0.0768 0.0010  174 GLN C CD  
7252  O OE1 . GLN C 174 ? 0.3435 0.2949 0.3684 0.0098  -0.0825 -0.0029 174 GLN C OE1 
7253  N NE2 . GLN C 174 ? 0.3313 0.2966 0.3564 0.0130  -0.0720 0.0015  174 GLN C NE2 
7254  N N   . ASN C 175 ? 0.3223 0.2850 0.3694 0.0067  -0.0745 0.0093  175 ASN C N   
7255  C CA  . ASN C 175 ? 0.3623 0.3271 0.4056 0.0066  -0.0673 0.0114  175 ASN C CA  
7256  C C   . ASN C 175 ? 0.3609 0.3240 0.4152 0.0073  -0.0665 0.0136  175 ASN C C   
7257  O O   . ASN C 175 ? 0.3612 0.3245 0.4201 0.0082  -0.0586 0.0157  175 ASN C O   
7258  C CB  A ASN C 175 ? 0.3965 0.3625 0.4231 0.0049  -0.0662 0.0089  175 ASN C CB  
7259  C CB  B ASN C 175 ? 0.3919 0.3576 0.4187 0.0049  -0.0663 0.0090  175 ASN C CB  
7260  C CG  A ASN C 175 ? 0.5331 0.5056 0.5546 0.0057  -0.0648 0.0077  175 ASN C CG  
7261  C CG  B ASN C 175 ? 0.3985 0.3630 0.4198 0.0032  -0.0603 0.0096  175 ASN C CG  
7262  O OD1 A ASN C 175 ? 0.5392 0.5132 0.5648 0.0079  -0.0629 0.0100  175 ASN C OD1 
7263  O OD1 B ASN C 175 ? 0.3904 0.3545 0.4149 0.0043  -0.0552 0.0113  175 ASN C OD1 
7264  N ND2 A ASN C 175 ? 0.4968 0.4732 0.5103 0.0044  -0.0652 0.0049  175 ASN C ND2 
7265  N ND2 B ASN C 175 ? 0.4209 0.3825 0.4319 0.0001  -0.0602 0.0079  175 ASN C ND2 
7266  N N   . GLN C 176 ? 0.3345 0.2956 0.3930 0.0077  -0.0747 0.0135  176 GLN C N   
7267  C CA  . GLN C 176 ? 0.2935 0.2547 0.3666 0.0102  -0.0754 0.0165  176 GLN C CA  
7268  C C   . GLN C 176 ? 0.2767 0.2453 0.3776 0.0110  -0.0743 0.0190  176 GLN C C   
7269  O O   . GLN C 176 ? 0.2715 0.2430 0.3879 0.0139  -0.0675 0.0218  176 GLN C O   
7270  C CB  . GLN C 176 ? 0.2849 0.2415 0.3526 0.0112  -0.0867 0.0169  176 GLN C CB  
7271  C CG  . GLN C 176 ? 0.2799 0.2274 0.3232 0.0102  -0.0845 0.0165  176 GLN C CG  
7272  C CD  . GLN C 176 ? 0.2927 0.2321 0.3285 0.0123  -0.0943 0.0194  176 GLN C CD  
7273  O OE1 . GLN C 176 ? 0.3431 0.2800 0.3899 0.0167  -0.0960 0.0235  176 GLN C OE1 
7274  N NE2 . GLN C 176 ? 0.2995 0.2336 0.3156 0.0099  -0.1002 0.0177  176 GLN C NE2 
7275  N N   . LEU C 177 ? 0.2845 0.2554 0.3928 0.0081  -0.0796 0.0178  177 LEU C N   
7276  C CA  . LEU C 177 ? 0.2964 0.2741 0.4323 0.0065  -0.0771 0.0203  177 LEU C CA  
7277  C C   . LEU C 177 ? 0.3158 0.2932 0.4517 0.0070  -0.0610 0.0234  177 LEU C C   
7278  O O   . LEU C 177 ? 0.2834 0.2664 0.4403 0.0077  -0.0523 0.0270  177 LEU C O   
7279  C CB  . LEU C 177 ? 0.2951 0.2708 0.4353 0.0020  -0.0868 0.0173  177 LEU C CB  
7280  C CG  . LEU C 177 ? 0.2887 0.2632 0.4277 0.0008  -0.1041 0.0138  177 LEU C CG  
7281  C CD1 . LEU C 177 ? 0.3062 0.2737 0.4413 -0.0040 -0.1113 0.0088  177 LEU C CD1 
7282  C CD2 . LEU C 177 ? 0.2704 0.2561 0.4402 0.0011  -0.1118 0.0169  177 LEU C CD2 
7283  N N   . PHE C 178 ? 0.3241 0.2954 0.4363 0.0068  -0.0571 0.0223  178 PHE C N   
7284  C CA  . PHE C 178 ? 0.3044 0.2731 0.4088 0.0075  -0.0442 0.0254  178 PHE C CA  
7285  C C   . PHE C 178 ? 0.2980 0.2668 0.4024 0.0101  -0.0343 0.0264  178 PHE C C   
7286  O O   . PHE C 178 ? 0.3418 0.3107 0.4551 0.0108  -0.0222 0.0299  178 PHE C O   
7287  C CB  . PHE C 178 ? 0.3268 0.2914 0.4053 0.0081  -0.0450 0.0239  178 PHE C CB  
7288  C CG  . PHE C 178 ? 0.3231 0.2855 0.4002 0.0076  -0.0514 0.0231  178 PHE C CG  
7289  C CD1 . PHE C 178 ? 0.3090 0.2690 0.4036 0.0053  -0.0534 0.0244  178 PHE C CD1 
7290  C CD2 . PHE C 178 ? 0.2857 0.2479 0.3453 0.0094  -0.0548 0.0208  178 PHE C CD2 
7291  C CE1 . PHE C 178 ? 0.3108 0.2645 0.4018 0.0053  -0.0584 0.0227  178 PHE C CE1 
7292  C CE2 . PHE C 178 ? 0.2665 0.2255 0.3252 0.0108  -0.0589 0.0197  178 PHE C CE2 
7293  C CZ  . PHE C 178 ? 0.2683 0.2210 0.3407 0.0091  -0.0606 0.0204  178 PHE C CZ  
7294  N N   . SER C 179 ? 0.2965 0.2630 0.3897 0.0117  -0.0380 0.0232  179 SER C N   
7295  C CA  . SER C 179 ? 0.3287 0.2902 0.4161 0.0144  -0.0282 0.0225  179 SER C CA  
7296  C C   . SER C 179 ? 0.3642 0.3303 0.4791 0.0187  -0.0239 0.0249  179 SER C C   
7297  O O   . SER C 179 ? 0.3636 0.3263 0.4804 0.0219  -0.0101 0.0254  179 SER C O   
7298  C CB  . SER C 179 ? 0.4057 0.3605 0.4713 0.0135  -0.0329 0.0184  179 SER C CB  
7299  O OG  . SER C 179 ? 0.4853 0.4403 0.5583 0.0147  -0.0422 0.0184  179 SER C OG  
7300  N N   . HIS C 180 ? 0.3166 0.2904 0.4531 0.0192  -0.0355 0.0261  180 HIS C N   
7301  C CA  . HIS C 180 ? 0.2976 0.2796 0.4658 0.0240  -0.0338 0.0291  180 HIS C CA  
7302  C C   . HIS C 180 ? 0.3005 0.2919 0.4940 0.0229  -0.0218 0.0325  180 HIS C C   
7303  O O   . HIS C 180 ? 0.3268 0.3228 0.5405 0.0279  -0.0097 0.0345  180 HIS C O   
7304  C CB  . HIS C 180 ? 0.2853 0.2744 0.4695 0.0242  -0.0525 0.0299  180 HIS C CB  
7305  C CG  . HIS C 180 ? 0.2651 0.2648 0.4838 0.0305  -0.0541 0.0335  180 HIS C CG  
7306  N ND1 . HIS C 180 ? 0.2827 0.2760 0.5002 0.0387  -0.0508 0.0347  180 HIS C ND1 
7307  C CD2 . HIS C 180 ? 0.2822 0.2990 0.5404 0.0302  -0.0590 0.0365  180 HIS C CD2 
7308  C CE1 . HIS C 180 ? 0.2813 0.2884 0.5368 0.0447  -0.0534 0.0387  180 HIS C CE1 
7309  N NE2 . HIS C 180 ? 0.2922 0.3155 0.5744 0.0392  -0.0590 0.0397  180 HIS C NE2 
7310  N N   . PHE C 181 ? 0.3159 0.3088 0.5088 0.0167  -0.0238 0.0333  181 PHE C N   
7311  C CA  . PHE C 181 ? 0.2862 0.2872 0.5059 0.0137  -0.0133 0.0376  181 PHE C CA  
7312  C C   . PHE C 181 ? 0.3420 0.3330 0.5400 0.0124  0.0038  0.0400  181 PHE C C   
7313  O O   . PHE C 181 ? 0.3719 0.3667 0.5880 0.0099  0.0164  0.0447  181 PHE C O   
7314  C CB  . PHE C 181 ? 0.2280 0.2355 0.4669 0.0067  -0.0271 0.0378  181 PHE C CB  
7315  C CG  . PHE C 181 ? 0.2601 0.2795 0.5252 0.0074  -0.0441 0.0365  181 PHE C CG  
7316  C CD1 . PHE C 181 ? 0.2419 0.2782 0.5490 0.0095  -0.0409 0.0399  181 PHE C CD1 
7317  C CD2 . PHE C 181 ? 0.2623 0.2766 0.5108 0.0060  -0.0634 0.0323  181 PHE C CD2 
7318  C CE1 . PHE C 181 ? 0.2619 0.3104 0.5939 0.0108  -0.0594 0.0395  181 PHE C CE1 
7319  C CE2 . PHE C 181 ? 0.2136 0.2370 0.4815 0.0068  -0.0809 0.0316  181 PHE C CE2 
7320  C CZ  . PHE C 181 ? 0.2565 0.2972 0.5661 0.0092  -0.0803 0.0354  181 PHE C CZ  
7321  N N   . GLY C 182 ? 0.3357 0.3142 0.4956 0.0137  0.0043  0.0372  182 GLY C N   
7322  C CA  . GLY C 182 ? 0.3077 0.2757 0.4421 0.0129  0.0169  0.0397  182 GLY C CA  
7323  C C   . GLY C 182 ? 0.3237 0.2891 0.4570 0.0082  0.0140  0.0439  182 GLY C C   
7324  O O   . GLY C 182 ? 0.3117 0.2711 0.4401 0.0069  0.0273  0.0496  182 GLY C O   
7325  N N   . LEU C 183 ? 0.3067 0.2740 0.4424 0.0060  -0.0025 0.0412  183 LEU C N   
7326  C CA  . LEU C 183 ? 0.3002 0.2622 0.4355 0.0023  -0.0061 0.0442  183 LEU C CA  
7327  C C   . LEU C 183 ? 0.3241 0.2753 0.4254 0.0048  -0.0062 0.0457  183 LEU C C   
7328  O O   . LEU C 183 ? 0.3273 0.2779 0.4063 0.0078  -0.0090 0.0423  183 LEU C O   
7329  C CB  . LEU C 183 ? 0.2853 0.2508 0.4332 -0.0003 -0.0231 0.0394  183 LEU C CB  
7330  C CG  . LEU C 183 ? 0.3072 0.2843 0.4878 -0.0029 -0.0300 0.0374  183 LEU C CG  
7331  C CD1 . LEU C 183 ? 0.3057 0.2814 0.4857 -0.0053 -0.0482 0.0316  183 LEU C CD1 
7332  C CD2 . LEU C 183 ? 0.3169 0.2992 0.5289 -0.0079 -0.0205 0.0427  183 LEU C CD2 
7333  N N   . LYS C 184 ? 0.3089 0.2515 0.4079 0.0033  -0.0038 0.0512  184 LYS C N   
7334  C CA  . LYS C 184 ? 0.3413 0.2756 0.4135 0.0069  -0.0084 0.0529  184 LYS C CA  
7335  C C   . LYS C 184 ? 0.3320 0.2715 0.4027 0.0086  -0.0235 0.0454  184 LYS C C   
7336  O O   . LYS C 184 ? 0.3019 0.2445 0.3905 0.0059  -0.0306 0.0410  184 LYS C O   
7337  C CB  . LYS C 184 ? 0.4145 0.3355 0.4865 0.0060  -0.0033 0.0613  184 LYS C CB  
7338  C CG  . LYS C 184 ? 0.5063 0.4190 0.5581 0.0114  -0.0115 0.0633  184 LYS C CG  
7339  C CD  . LYS C 184 ? 0.6072 0.5028 0.6500 0.0123  -0.0036 0.0744  184 LYS C CD  
7340  C CE  . LYS C 184 ? 0.6826 0.5697 0.7105 0.0197  -0.0130 0.0770  184 LYS C CE  
7341  N NZ  . LYS C 184 ? 0.6879 0.5880 0.7114 0.0248  -0.0261 0.0684  184 LYS C NZ  
7342  N N   . ARG C 185 ? 0.3393 0.2800 0.3882 0.0126  -0.0282 0.0439  185 ARG C N   
7343  C CA  . ARG C 185 ? 0.3237 0.2704 0.3705 0.0143  -0.0394 0.0373  185 ARG C CA  
7344  C C   . ARG C 185 ? 0.3330 0.2730 0.3821 0.0171  -0.0441 0.0383  185 ARG C C   
7345  O O   . ARG C 185 ? 0.3326 0.2716 0.3698 0.0224  -0.0466 0.0407  185 ARG C O   
7346  C CB  . ARG C 185 ? 0.3327 0.2857 0.3603 0.0163  -0.0418 0.0352  185 ARG C CB  
7347  C CG  . ARG C 185 ? 0.3285 0.2831 0.3506 0.0137  -0.0363 0.0332  185 ARG C CG  
7348  C CD  . ARG C 185 ? 0.3327 0.2926 0.3373 0.0133  -0.0407 0.0291  185 ARG C CD  
7349  N NE  . ARG C 185 ? 0.3720 0.3395 0.3826 0.0119  -0.0478 0.0233  185 ARG C NE  
7350  C CZ  . ARG C 185 ? 0.4097 0.3772 0.4249 0.0091  -0.0474 0.0193  185 ARG C CZ  
7351  N NH1 . ARG C 185 ? 0.4073 0.3794 0.4241 0.0076  -0.0530 0.0153  185 ARG C NH1 
7352  N NH2 . ARG C 185 ? 0.4264 0.3884 0.4442 0.0084  -0.0404 0.0199  185 ARG C NH2 
7353  N N   . GLN C 186 ? 0.3630 0.2981 0.4286 0.0138  -0.0463 0.0360  186 GLN C N   
7354  C CA  . GLN C 186 ? 0.3490 0.2727 0.4173 0.0157  -0.0495 0.0357  186 GLN C CA  
7355  C C   . GLN C 186 ? 0.3404 0.2624 0.4228 0.0106  -0.0560 0.0284  186 GLN C C   
7356  O O   . GLN C 186 ? 0.3553 0.2815 0.4530 0.0046  -0.0554 0.0283  186 GLN C O   
7357  C CB  . GLN C 186 ? 0.3844 0.2948 0.4547 0.0151  -0.0416 0.0451  186 GLN C CB  
7358  C CG  . GLN C 186 ? 0.4283 0.3222 0.5010 0.0172  -0.0437 0.0458  186 GLN C CG  
7359  C CD  . GLN C 186 ? 0.4812 0.3598 0.5589 0.0138  -0.0346 0.0556  186 GLN C CD  
7360  O OE1 . GLN C 186 ? 0.4892 0.3602 0.5853 0.0057  -0.0331 0.0545  186 GLN C OE1 
7361  N NE2 . GLN C 186 ? 0.5230 0.3966 0.5839 0.0190  -0.0286 0.0656  186 GLN C NE2 
7362  N N   . PHE C 187 ? 0.3641 0.2802 0.4415 0.0131  -0.0624 0.0218  187 PHE C N   
7363  C CA  . PHE C 187 ? 0.3605 0.2699 0.4476 0.0074  -0.0695 0.0145  187 PHE C CA  
7364  C C   . PHE C 187 ? 0.3962 0.2873 0.4787 0.0099  -0.0713 0.0106  187 PHE C C   
7365  O O   . PHE C 187 ? 0.3944 0.2821 0.4655 0.0184  -0.0685 0.0115  187 PHE C O   
7366  C CB  . PHE C 187 ? 0.3394 0.2584 0.4207 0.0063  -0.0771 0.0073  187 PHE C CB  
7367  C CG  . PHE C 187 ? 0.3634 0.2836 0.4260 0.0127  -0.0778 0.0024  187 PHE C CG  
7368  C CD1 . PHE C 187 ? 0.3505 0.2832 0.4049 0.0167  -0.0735 0.0054  187 PHE C CD1 
7369  C CD2 . PHE C 187 ? 0.3864 0.2952 0.4401 0.0140  -0.0821 -0.0059 187 PHE C CD2 
7370  C CE1 . PHE C 187 ? 0.3525 0.2894 0.3949 0.0215  -0.0731 0.0012  187 PHE C CE1 
7371  C CE2 . PHE C 187 ? 0.3899 0.3013 0.4286 0.0201  -0.0799 -0.0102 187 PHE C CE2 
7372  C CZ  . PHE C 187 ? 0.3550 0.2820 0.3905 0.0236  -0.0752 -0.0062 187 PHE C CZ  
7373  N N   . SER C 188 ? 0.4143 0.2936 0.5074 0.0026  -0.0765 0.0058  188 SER C N   
7374  C CA  . SER C 188 ? 0.4015 0.2583 0.4914 0.0035  -0.0773 0.0016  188 SER C CA  
7375  C C   . SER C 188 ? 0.4116 0.2597 0.4953 -0.0006 -0.0878 -0.0115 188 SER C C   
7376  O O   . SER C 188 ? 0.4251 0.2811 0.5169 -0.0086 -0.0962 -0.0150 188 SER C O   
7377  C CB  . SER C 188 ? 0.4135 0.2577 0.5205 -0.0036 -0.0727 0.0084  188 SER C CB  
7378  O OG  . SER C 188 ? 0.4285 0.2772 0.5352 0.0007  -0.0622 0.0211  188 SER C OG  
7379  N N   . VAL C 189 ? 0.4072 0.2392 0.4748 0.0061  -0.0871 -0.0185 189 VAL C N   
7380  C CA  . VAL C 189 ? 0.4130 0.2325 0.4663 0.0038  -0.0953 -0.0321 189 VAL C CA  
7381  C C   . VAL C 189 ? 0.4288 0.2179 0.4804 0.0016  -0.0961 -0.0391 189 VAL C C   
7382  O O   . VAL C 189 ? 0.4864 0.2616 0.5339 0.0107  -0.0875 -0.0368 189 VAL C O   
7383  C CB  . VAL C 189 ? 0.4034 0.2285 0.4351 0.0143  -0.0914 -0.0368 189 VAL C CB  
7384  C CG1 . VAL C 189 ? 0.3899 0.2002 0.4009 0.0118  -0.0986 -0.0510 189 VAL C CG1 
7385  C CG2 . VAL C 189 ? 0.3864 0.2389 0.4198 0.0160  -0.0894 -0.0295 189 VAL C CG2 
7386  N N   . CYS C 190 ? 0.4396 0.2177 0.4950 -0.0104 -0.1074 -0.0476 190 CYS C N   
7387  C CA  . CYS C 190 ? 0.4526 0.1983 0.5032 -0.0148 -0.1103 -0.0574 190 CYS C CA  
7388  C C   . CYS C 190 ? 0.5980 0.3328 0.6287 -0.0208 -0.1238 -0.0734 190 CYS C C   
7389  O O   . CYS C 190 ? 0.5984 0.3361 0.6403 -0.0342 -0.1378 -0.0772 190 CYS C O   
7390  C CB  . CYS C 190 ? 0.4583 0.1967 0.5370 -0.0273 -0.1112 -0.0513 190 CYS C CB  
7391  S SG  . CYS C 190 ? 0.5994 0.2934 0.6754 -0.0290 -0.1065 -0.0565 190 CYS C SG  
7392  N N   . LEU C 191 ? 0.5879 0.3112 0.5889 -0.0107 -0.1198 -0.0827 191 LEU C N   
7393  C CA  . LEU C 191 ? 0.5924 0.3011 0.5662 -0.0154 -0.1313 -0.0983 191 LEU C CA  
7394  C C   . LEU C 191 ? 0.6726 0.3441 0.6391 -0.0236 -0.1378 -0.1120 191 LEU C C   
7395  O O   . LEU C 191 ? 0.6690 0.3179 0.6382 -0.0183 -0.1273 -0.1125 191 LEU C O   
7396  C CB  . LEU C 191 ? 0.5594 0.2678 0.5024 -0.0019 -0.1216 -0.1034 191 LEU C CB  
7397  C CG  . LEU C 191 ? 0.5156 0.2577 0.4644 0.0054  -0.1144 -0.0912 191 LEU C CG  
7398  C CD1 . LEU C 191 ? 0.5089 0.2496 0.4283 0.0164  -0.1043 -0.0975 191 LEU C CD1 
7399  C CD2 . LEU C 191 ? 0.5164 0.2815 0.4770 -0.0046 -0.1273 -0.0848 191 LEU C CD2 
7400  N N   . SER C 192 ? 0.6997 0.3634 0.6564 -0.0365 -0.1562 -0.1232 192 SER C N   
7401  C CA  . SER C 192 ? 0.7082 0.3453 0.6549 -0.0453 -0.1605 -0.1354 192 SER C CA  
7402  C C   . SER C 192 ? 0.7537 0.3677 0.6546 -0.0375 -0.1568 -0.1508 192 SER C C   
7403  O O   . SER C 192 ? 0.7705 0.3935 0.6463 -0.0344 -0.1618 -0.1540 192 SER C O   
7404  C CB  . SER C 192 ? 0.6878 0.3408 0.6517 -0.0627 -0.1782 -0.1355 192 SER C CB  
7405  O OG  . SER C 192 ? 0.6817 0.3112 0.6330 -0.0720 -0.1828 -0.1483 192 SER C OG  
7406  N N   . ARG C 193 ? 0.7048 0.2882 0.5951 -0.0342 -0.1463 -0.1593 193 ARG C N   
7407  C CA  . ARG C 193 ? 0.7682 0.3254 0.6178 -0.0260 -0.1382 -0.1747 193 ARG C CA  
7408  C C   . ARG C 193 ? 0.8160 0.3681 0.6390 -0.0377 -0.1527 -0.1871 193 ARG C C   
7409  O O   . ARG C 193 ? 0.8142 0.3525 0.5980 -0.0313 -0.1479 -0.1984 193 ARG C O   
7410  C CB  . ARG C 193 ? 0.9072 0.4331 0.7606 -0.0216 -0.1244 -0.1793 193 ARG C CB  
7411  C CG  . ARG C 193 ? 1.0577 0.5555 0.8750 -0.0103 -0.1113 -0.1946 193 ARG C CG  
7412  C CD  . ARG C 193 ? 1.1996 0.6631 1.0188 -0.0135 -0.1043 -0.2032 193 ARG C CD  
7413  N NE  . ARG C 193 ? 1.2971 0.7562 1.1513 -0.0127 -0.0977 -0.1905 193 ARG C NE  
7414  C CZ  . ARG C 193 ? 1.3727 0.8291 1.2384 0.0052  -0.0816 -0.1808 193 ARG C CZ  
7415  N NH1 . ARG C 193 ? 1.3926 0.8545 1.2422 0.0243  -0.0702 -0.1824 193 ARG C NH1 
7416  N NH2 . ARG C 193 ? 1.3891 0.8394 1.2833 0.0042  -0.0769 -0.1681 193 ARG C NH2 
7417  N N   . TYR C 194 ? 0.8399 0.4045 0.6859 -0.0546 -0.1696 -0.1842 194 TYR C N   
7418  C CA  . TYR C 194 ? 0.9035 0.4629 0.7322 -0.0678 -0.1862 -0.1953 194 TYR C CA  
7419  C C   . TYR C 194 ? 0.8816 0.4709 0.7081 -0.0722 -0.2038 -0.1892 194 TYR C C   
7420  O O   . TYR C 194 ? 0.7563 0.3751 0.6160 -0.0742 -0.2095 -0.1750 194 TYR C O   
7421  C CB  . TYR C 194 ? 0.9407 0.4928 0.7990 -0.0840 -0.1932 -0.1971 194 TYR C CB  
7422  C CG  . TYR C 194 ? 0.9631 0.4888 0.8327 -0.0798 -0.1751 -0.1976 194 TYR C CG  
7423  C CD1 . TYR C 194 ? 1.0367 0.5256 0.8766 -0.0743 -0.1638 -0.2126 194 TYR C CD1 
7424  C CD2 . TYR C 194 ? 0.9163 0.4534 0.8258 -0.0803 -0.1683 -0.1823 194 TYR C CD2 
7425  C CE1 . TYR C 194 ? 1.0760 0.5397 0.9271 -0.0686 -0.1468 -0.2118 194 TYR C CE1 
7426  C CE2 . TYR C 194 ? 0.9558 0.4672 0.8736 -0.0752 -0.1516 -0.1805 194 TYR C CE2 
7427  C CZ  . TYR C 194 ? 1.0594 0.5341 0.9488 -0.0689 -0.1412 -0.1949 194 TYR C CZ  
7428  O OH  . TYR C 194 ? 1.1205 0.5689 1.0192 -0.0623 -0.1244 -0.1919 194 TYR C OH  
7429  N N   . SER C 195 ? 0.9358 0.5159 0.7233 -0.0736 -0.2123 -0.1996 195 SER C N   
7430  C CA  . SER C 195 ? 0.9445 0.5481 0.7239 -0.0762 -0.2291 -0.1938 195 SER C CA  
7431  C C   . SER C 195 ? 0.8870 0.5126 0.7039 -0.0912 -0.2498 -0.1884 195 SER C C   
7432  O O   . SER C 195 ? 0.8404 0.4937 0.6705 -0.0919 -0.2621 -0.1778 195 SER C O   
7433  C CB  . SER C 195 ? 1.0781 0.6608 0.8027 -0.0742 -0.2319 -0.2070 195 SER C CB  
7434  O OG  . SER C 195 ? 1.1265 0.7265 0.8320 -0.0704 -0.2404 -0.1995 195 SER C OG  
7435  N N   . THR C 196 ? 0.8894 0.5030 0.7268 -0.1025 -0.2516 -0.1949 196 THR C N   
7436  C CA  . THR C 196 ? 0.9035 0.5352 0.7756 -0.1183 -0.2704 -0.1926 196 THR C CA  
7437  C C   . THR C 196 ? 0.8321 0.4911 0.7611 -0.1224 -0.2679 -0.1773 196 THR C C   
7438  O O   . THR C 196 ? 0.8179 0.4956 0.7805 -0.1348 -0.2815 -0.1743 196 THR C O   
7439  C CB  . THR C 196 ? 0.9986 0.6024 0.8635 -0.1312 -0.2743 -0.2087 196 THR C CB  
7440  O OG1 . THR C 196 ? 1.0186 0.6016 0.8970 -0.1301 -0.2550 -0.2099 196 THR C OG1 
7441  C CG2 . THR C 196 ? 0.9536 0.5300 0.7612 -0.1283 -0.2775 -0.2251 196 THR C CG2 
7442  N N   . SER C 197 ? 0.7935 0.4549 0.7339 -0.1121 -0.2502 -0.1679 197 SER C N   
7443  C CA  . SER C 197 ? 0.7888 0.4759 0.7799 -0.1149 -0.2461 -0.1527 197 SER C CA  
7444  C C   . SER C 197 ? 0.7888 0.4892 0.7811 -0.1005 -0.2341 -0.1411 197 SER C C   
7445  O O   . SER C 197 ? 0.8088 0.4915 0.7681 -0.0886 -0.2231 -0.1453 197 SER C O   
7446  C CB  . SER C 197 ? 0.8289 0.4988 0.8440 -0.1233 -0.2352 -0.1537 197 SER C CB  
7447  O OG  . SER C 197 ? 0.8648 0.5034 0.8559 -0.1135 -0.2174 -0.1586 197 SER C OG  
7448  N N   . ASN C 198 ? 0.7301 0.4624 0.7615 -0.1018 -0.2361 -0.1270 198 ASN C N   
7449  C CA  . ASN C 198 ? 0.6877 0.4367 0.7235 -0.0901 -0.2275 -0.1158 198 ASN C CA  
7450  C C   . ASN C 198 ? 0.6301 0.3706 0.6799 -0.0847 -0.2084 -0.1093 198 ASN C C   
7451  O O   . ASN C 198 ? 0.5703 0.3023 0.6429 -0.0919 -0.2018 -0.1077 198 ASN C O   
7452  C CB  . ASN C 198 ? 0.6475 0.4335 0.7197 -0.0930 -0.2365 -0.1035 198 ASN C CB  
7453  C CG  . ASN C 198 ? 0.6640 0.4604 0.7187 -0.0929 -0.2543 -0.1061 198 ASN C CG  
7454  O OD1 . ASN C 198 ? 0.6993 0.4771 0.7095 -0.0887 -0.2581 -0.1151 198 ASN C OD1 
7455  N ND2 . ASN C 198 ? 0.6548 0.4796 0.7444 -0.0974 -0.2648 -0.0979 198 ASN C ND2 
7456  N N   . GLY C 199 ? 0.4554 0.4753 0.5235 0.0127  -0.2176 -0.1625 199 GLY C N   
7457  C CA  . GLY C 199 ? 0.4466 0.4446 0.5246 0.0061  -0.1982 -0.1506 199 GLY C CA  
7458  C C   . GLY C 199 ? 0.4227 0.4223 0.5074 0.0068  -0.1964 -0.1304 199 GLY C C   
7459  O O   . GLY C 199 ? 0.4473 0.4649 0.5392 0.0120  -0.2099 -0.1253 199 GLY C O   
7460  N N   . ALA C 200 ? 0.4210 0.4024 0.5025 0.0028  -0.1808 -0.1188 200 ALA C N   
7461  C CA  . ALA C 200 ? 0.4040 0.3862 0.4942 0.0048  -0.1687 -0.0967 200 ALA C CA  
7462  C C   . ALA C 200 ? 0.3876 0.3516 0.4406 0.0072  -0.1466 -0.0802 200 ALA C C   
7463  O O   . ALA C 200 ? 0.3929 0.3428 0.4251 0.0046  -0.1375 -0.0832 200 ALA C O   
7464  C CB  . ALA C 200 ? 0.3432 0.3282 0.4940 -0.0033 -0.1590 -0.0932 200 ALA C CB  
7465  N N   . ILE C 201 ? 0.3940 0.3596 0.4435 0.0128  -0.1402 -0.0643 201 ILE C N   
7466  C CA  . ILE C 201 ? 0.3725 0.3223 0.4038 0.0139  -0.1197 -0.0513 201 ILE C CA  
7467  C C   . ILE C 201 ? 0.3360 0.2885 0.4021 0.0136  -0.1064 -0.0451 201 ILE C C   
7468  O O   . ILE C 201 ? 0.3442 0.3109 0.4405 0.0172  -0.1136 -0.0433 201 ILE C O   
7469  C CB  . ILE C 201 ? 0.4258 0.3727 0.4271 0.0218  -0.1217 -0.0400 201 ILE C CB  
7470  C CG1 . ILE C 201 ? 0.4707 0.4235 0.4384 0.0254  -0.1347 -0.0430 201 ILE C CG1 
7471  C CG2 . ILE C 201 ? 0.4092 0.3384 0.3950 0.0209  -0.1035 -0.0333 201 ILE C CG2 
7472  C CD1 . ILE C 201 ? 0.5038 0.4450 0.4468 0.0214  -0.1260 -0.0493 201 ILE C CD1 
7473  N N   . LEU C 202 ? 0.3571 0.2986 0.4182 0.0110  -0.0867 -0.0414 202 LEU C N   
7474  C CA  . LEU C 202 ? 0.3579 0.3045 0.4450 0.0127  -0.0697 -0.0359 202 LEU C CA  
7475  C C   . LEU C 202 ? 0.3479 0.2838 0.4080 0.0191  -0.0572 -0.0329 202 LEU C C   
7476  O O   . LEU C 202 ? 0.3411 0.2642 0.3678 0.0179  -0.0554 -0.0336 202 LEU C O   
7477  C CB  . LEU C 202 ? 0.3760 0.3237 0.4831 0.0060  -0.0560 -0.0330 202 LEU C CB  
7478  C CG  . LEU C 202 ? 0.3886 0.3503 0.5497 -0.0008 -0.0626 -0.0356 202 LEU C CG  
7479  C CD1 . LEU C 202 ? 0.3856 0.3472 0.5471 -0.0054 -0.0877 -0.0499 202 LEU C CD1 
7480  C CD2 . LEU C 202 ? 0.3878 0.3484 0.5717 -0.0064 -0.0427 -0.0255 202 LEU C CD2 
7481  N N   . PHE C 203 ? 0.3477 0.2894 0.4266 0.0263  -0.0499 -0.0321 203 PHE C N   
7482  C CA  . PHE C 203 ? 0.3435 0.2747 0.4033 0.0332  -0.0398 -0.0353 203 PHE C CA  
7483  C C   . PHE C 203 ? 0.3451 0.2846 0.4142 0.0385  -0.0178 -0.0374 203 PHE C C   
7484  O O   . PHE C 203 ? 0.3434 0.2981 0.4492 0.0420  -0.0104 -0.0353 203 PHE C O   
7485  C CB  . PHE C 203 ? 0.3669 0.2949 0.4396 0.0402  -0.0496 -0.0347 203 PHE C CB  
7486  C CG  . PHE C 203 ? 0.3658 0.2899 0.4257 0.0377  -0.0684 -0.0280 203 PHE C CG  
7487  C CD1 . PHE C 203 ? 0.3606 0.2995 0.4361 0.0369  -0.0840 -0.0238 203 PHE C CD1 
7488  C CD2 . PHE C 203 ? 0.3862 0.2948 0.4195 0.0371  -0.0705 -0.0261 203 PHE C CD2 
7489  C CE1 . PHE C 203 ? 0.3825 0.3221 0.4382 0.0373  -0.1002 -0.0178 203 PHE C CE1 
7490  C CE2 . PHE C 203 ? 0.3950 0.3036 0.4147 0.0364  -0.0837 -0.0165 203 PHE C CE2 
7491  C CZ  . PHE C 203 ? 0.4081 0.3328 0.4344 0.0375  -0.0980 -0.0123 203 PHE C CZ  
7492  N N   . GLY C 204 ? 0.3671 0.2995 0.4023 0.0402  -0.0071 -0.0412 204 GLY C N   
7493  C CA  . GLY C 204 ? 0.3738 0.3172 0.4055 0.0476  0.0152  -0.0424 204 GLY C CA  
7494  C C   . GLY C 204 ? 0.3937 0.3408 0.4066 0.0429  0.0243  -0.0313 204 GLY C C   
7495  O O   . GLY C 204 ? 0.3813 0.3202 0.3886 0.0339  0.0124  -0.0258 204 GLY C O   
7496  N N   . ASP C 205 ? 0.4527 0.4135 0.4569 0.0507  0.0466  -0.0270 205 ASP C N   
7497  C CA  . ASP C 205 ? 0.5040 0.4702 0.4889 0.0494  0.0586  -0.0109 205 ASP C CA  
7498  C C   . ASP C 205 ? 0.4853 0.4592 0.5151 0.0401  0.0646  0.0082  205 ASP C C   
7499  O O   . ASP C 205 ? 0.4736 0.4643 0.5424 0.0420  0.0800  0.0154  205 ASP C O   
7500  C CB  . ASP C 205 ? 0.5671 0.5495 0.5230 0.0636  0.0821  -0.0103 205 ASP C CB  
7501  C CG  . ASP C 205 ? 0.6103 0.5987 0.5352 0.0653  0.0923  0.0092  205 ASP C CG  
7502  O OD1 . ASP C 205 ? 0.5921 0.5686 0.5193 0.0553  0.0800  0.0200  205 ASP C OD1 
7503  O OD2 . ASP C 205 ? 0.6537 0.6604 0.5517 0.0784  0.1135  0.0143  205 ASP C OD2 
7504  N N   . ILE C 206 ? 0.4880 0.4515 0.5171 0.0310  0.0551  0.0169  206 ILE C N   
7505  C CA  . ILE C 206 ? 0.5277 0.4959 0.6084 0.0214  0.0586  0.0308  206 ILE C CA  
7506  C C   . ILE C 206 ? 0.5847 0.5660 0.6729 0.0248  0.0860  0.0566  206 ILE C C   
7507  O O   . ILE C 206 ? 0.6250 0.6125 0.7656 0.0173  0.0946  0.0721  206 ILE C O   
7508  C CB  . ILE C 206 ? 0.5289 0.4795 0.6125 0.0111  0.0376  0.0266  206 ILE C CB  
7509  C CG1 . ILE C 206 ? 0.5765 0.5161 0.6094 0.0151  0.0362  0.0296  206 ILE C CG1 
7510  C CG2 . ILE C 206 ? 0.5364 0.4797 0.6195 0.0080  0.0132  0.0061  206 ILE C CG2 
7511  C CD1 . ILE C 206 ? 0.6115 0.5349 0.6463 0.0074  0.0189  0.0249  206 ILE C CD1 
7512  N N   . ASN C 207 ? 0.6286 0.6170 0.6671 0.0373  0.1004  0.0613  207 ASN C N   
7513  C CA  . ASN C 207 ? 0.6735 0.6774 0.7064 0.0439  0.1277  0.0902  207 ASN C CA  
7514  C C   . ASN C 207 ? 0.6769 0.7063 0.7048 0.0573  0.1553  0.0938  207 ASN C C   
7515  O O   . ASN C 207 ? 0.7094 0.7556 0.7041 0.0696  0.1784  0.1122  207 ASN C O   
7516  C CB  . ASN C 207 ? 0.7872 0.7844 0.7616 0.0503  0.1225  0.0961  207 ASN C CB  
7517  C CG  . ASN C 207 ? 0.8591 0.8334 0.8458 0.0385  0.1002  0.0961  207 ASN C CG  
7518  O OD1 . ASN C 207 ? 0.8998 0.8681 0.9386 0.0279  0.1016  0.1097  207 ASN C OD1 
7519  N ND2 . ASN C 207 ? 0.8642 0.8260 0.8088 0.0401  0.0796  0.0784  207 ASN C ND2 
7520  N N   . ASP C 208 ? 0.6656 0.7002 0.7286 0.0562  0.1536  0.0774  208 ASP C N   
7521  C CA  . ASP C 208 ? 0.7088 0.7675 0.7746 0.0700  0.1793  0.0752  208 ASP C CA  
7522  C C   . ASP C 208 ? 0.7374 0.8164 0.8763 0.0647  0.2020  0.0990  208 ASP C C   
7523  O O   . ASP C 208 ? 0.7542 0.8285 0.9540 0.0517  0.1865  0.0942  208 ASP C O   
7524  C CB  . ASP C 208 ? 0.6868 0.7382 0.7504 0.0743  0.1629  0.0419  208 ASP C CB  
7525  C CG  . ASP C 208 ? 0.7033 0.7784 0.7730 0.0909  0.1894  0.0342  208 ASP C CG  
7526  O OD1 . ASP C 208 ? 0.7312 0.8325 0.8152 0.0982  0.2225  0.0555  208 ASP C OD1 
7527  O OD2 . ASP C 208 ? 0.7059 0.7735 0.7690 0.0976  0.1783  0.0069  208 ASP C OD2 
7528  N N   . PRO C 209 ? 0.7467 0.8502 0.8808 0.0748  0.2384  0.1270  209 PRO C N   
7529  C CA  . PRO C 209 ? 0.7288 0.8568 0.9362 0.0713  0.2680  0.1555  209 PRO C CA  
7530  C C   . PRO C 209 ? 0.7036 0.8428 0.9744 0.0690  0.2652  0.1378  209 PRO C C   
7531  O O   . PRO C 209 ? 0.7309 0.8837 1.0837 0.0586  0.2743  0.1547  209 PRO C O   
7532  C CB  . PRO C 209 ? 0.7643 0.9213 0.9270 0.0916  0.3093  0.1782  209 PRO C CB  
7533  C CG  . PRO C 209 ? 0.7801 0.9242 0.8493 0.1015  0.2964  0.1692  209 PRO C CG  
7534  C CD  . PRO C 209 ? 0.7599 0.8693 0.8161 0.0895  0.2515  0.1371  209 PRO C CD  
7535  N N   . ASN C 210 ? 0.6638 0.7989 0.9035 0.0791  0.2531  0.1055  210 ASN C N   
7536  C CA  . ASN C 210 ? 0.6568 0.8007 0.9590 0.0775  0.2460  0.0904  210 ASN C CA  
7537  C C   . ASN C 210 ? 0.6412 0.7670 0.9913 0.0574  0.2088  0.0845  210 ASN C C   
7538  O O   . ASN C 210 ? 0.6463 0.7864 1.0743 0.0496  0.2053  0.0877  210 ASN C O   
7539  C CB  . ASN C 210 ? 0.6871 0.8248 0.9498 0.0925  0.2375  0.0574  210 ASN C CB  
7540  C CG  . ASN C 210 ? 0.7823 0.9429 1.0076 0.1151  0.2745  0.0549  210 ASN C CG  
7541  O OD1 . ASN C 210 ? 0.8008 0.9819 1.0628 0.1265  0.2928  0.0472  210 ASN C OD1 
7542  N ND2 . ASN C 210 ? 0.8402 0.9993 0.9912 0.1234  0.2847  0.0595  210 ASN C ND2 
7543  N N   . ASN C 211 ? 0.6539 0.7516 0.9599 0.0493  0.1825  0.0774  211 ASN C N   
7544  C CA  . ASN C 211 ? 0.6489 0.7294 0.9855 0.0332  0.1461  0.0666  211 ASN C CA  
7545  C C   . ASN C 211 ? 0.6587 0.7367 1.0355 0.0186  0.1477  0.0867  211 ASN C C   
7546  O O   . ASN C 211 ? 0.6626 0.7255 1.0605 0.0055  0.1187  0.0765  211 ASN C O   
7547  C CB  . ASN C 211 ? 0.6520 0.7039 0.9229 0.0330  0.1172  0.0465  211 ASN C CB  
7548  C CG  . ASN C 211 ? 0.6751 0.7236 0.9084 0.0464  0.1135  0.0261  211 ASN C CG  
7549  O OD1 . ASN C 211 ? 0.6584 0.7206 0.9271 0.0530  0.1167  0.0191  211 ASN C OD1 
7550  N ND2 . ASN C 211 ? 0.6806 0.7099 0.8482 0.0504  0.1048  0.0158  211 ASN C ND2 
7551  N N   . ASN C 212 ? 0.6678 0.7621 1.0600 0.0217  0.1828  0.1156  212 ASN C N   
7552  C CA  . ASN C 212 ? 0.6654 0.7536 1.0942 0.0092  0.1883  0.1398  212 ASN C CA  
7553  C C   . ASN C 212 ? 0.5879 0.6812 1.1137 -0.0075 0.1726  0.1358  212 ASN C C   
7554  O O   . ASN C 212 ? 0.5711 0.6498 1.1343 -0.0217 0.1598  0.1399  212 ASN C O   
7555  C CB  . ASN C 212 ? 0.7413 0.8501 1.1680 0.0184  0.2331  0.1777  212 ASN C CB  
7556  C CG  . ASN C 212 ? 0.7865 0.8821 1.2263 0.0098  0.2392  0.2068  212 ASN C CG  
7557  O OD1 . ASN C 212 ? 0.7772 0.8479 1.1668 0.0086  0.2194  0.1996  212 ASN C OD1 
7558  N ND2 . ASN C 212 ? 0.8300 0.9401 1.3386 0.0050  0.2639  0.2388  212 ASN C ND2 
7559  N N   . ASN C 213 ? 0.5401 0.6538 1.1086 -0.0054 0.1701  0.1242  213 ASN C N   
7560  C CA  . ASN C 213 ? 0.5000 0.6239 1.1649 -0.0205 0.1534  0.1194  213 ASN C CA  
7561  C C   . ASN C 213 ? 0.4225 0.5236 1.0754 -0.0301 0.1058  0.0884  213 ASN C C   
7562  O O   . ASN C 213 ? 0.4110 0.5066 1.1220 -0.0452 0.0880  0.0836  213 ASN C O   
7563  C CB  . ASN C 213 ? 0.5570 0.7123 1.2732 -0.0139 0.1619  0.1159  213 ASN C CB  
7564  C CG  . ASN C 213 ? 0.6453 0.8221 1.3777 -0.0043 0.2083  0.1457  213 ASN C CG  
7565  O OD1 . ASN C 213 ? 0.7056 0.8758 1.4524 -0.0087 0.2251  0.1710  213 ASN C OD1 
7566  N ND2 . ASN C 213 ? 0.6662 0.8635 1.3844 0.0118  0.2258  0.1409  213 ASN C ND2 
7567  N N   . TYR C 214 ? 0.3742 0.4619 0.9518 -0.0207 0.0866  0.0674  214 TYR C N   
7568  C CA  . TYR C 214 ? 0.3495 0.4195 0.9069 -0.0267 0.0443  0.0401  214 TYR C CA  
7569  C C   . TYR C 214 ? 0.3849 0.4266 0.9034 -0.0332 0.0344  0.0372  214 TYR C C   
7570  O O   . TYR C 214 ? 0.3985 0.4299 0.9308 -0.0421 0.0044  0.0175  214 TYR C O   
7571  C CB  . TYR C 214 ? 0.3131 0.3797 0.8113 -0.0141 0.0296  0.0236  214 TYR C CB  
7572  C CG  . TYR C 214 ? 0.2826 0.3393 0.7663 -0.0182 -0.0117 -0.0002 214 TYR C CG  
7573  C CD1 . TYR C 214 ? 0.2655 0.3410 0.8074 -0.0225 -0.0372 -0.0125 214 TYR C CD1 
7574  C CD2 . TYR C 214 ? 0.3095 0.3417 0.7221 -0.0168 -0.0250 -0.0097 214 TYR C CD2 
7575  C CE1 . TYR C 214 ? 0.2723 0.3432 0.7945 -0.0237 -0.0748 -0.0336 214 TYR C CE1 
7576  C CE2 . TYR C 214 ? 0.2835 0.3106 0.6793 -0.0185 -0.0593 -0.0294 214 TYR C CE2 
7577  C CZ  . TYR C 214 ? 0.3059 0.3529 0.7527 -0.0212 -0.0840 -0.0413 214 TYR C CZ  
7578  O OH  . TYR C 214 ? 0.3313 0.3778 0.7555 -0.0204 -0.1183 -0.0605 214 TYR C OH  
7579  N N   . ILE C 215 ? 0.3928 0.4238 0.8607 -0.0271 0.0586  0.0550  215 ILE C N   
7580  C CA  . ILE C 215 ? 0.3990 0.4042 0.8272 -0.0305 0.0501  0.0536  215 ILE C CA  
7581  C C   . ILE C 215 ? 0.4058 0.4074 0.8879 -0.0399 0.0665  0.0764  215 ILE C C   
7582  O O   . ILE C 215 ? 0.4182 0.3996 0.8797 -0.0419 0.0645  0.0811  215 ILE C O   
7583  C CB  . ILE C 215 ? 0.3945 0.3902 0.7357 -0.0177 0.0611  0.0586  215 ILE C CB  
7584  C CG1 . ILE C 215 ? 0.4435 0.4568 0.7780 -0.0079 0.0981  0.0845  215 ILE C CG1 
7585  C CG2 . ILE C 215 ? 0.3546 0.3487 0.6509 -0.0103 0.0427  0.0358  215 ILE C CG2 
7586  C CD1 . ILE C 215 ? 0.4819 0.4898 0.8046 -0.0070 0.1186  0.1123  215 ILE C CD1 
7587  N N   . HIS C 216 ? 0.4525 0.4742 1.0116 -0.0455 0.0831  0.0920  216 HIS C N   
7588  C CA  . HIS C 216 ? 0.5197 0.5400 1.1394 -0.0538 0.1049  0.1212  216 HIS C CA  
7589  C C   . HIS C 216 ? 0.5113 0.5064 1.1535 -0.0632 0.0785  0.1046  216 HIS C C   
7590  O O   . HIS C 216 ? 0.4866 0.4688 1.1263 -0.0610 0.0899  0.1235  216 HIS C O   
7591  C CB  . HIS C 216 ? 0.5740 0.6191 1.2718 -0.0555 0.1195  0.1335  216 HIS C CB  
7592  C CG  . HIS C 216 ? 0.6569 0.6987 1.3901 -0.0534 0.1406  0.1634  216 HIS C CG  
7593  N ND1 . HIS C 216 ? 0.6948 0.7242 1.4863 -0.0602 0.1222  0.1540  216 HIS C ND1 
7594  C CD2 . HIS C 216 ? 0.7127 0.7642 1.4304 -0.0431 0.1780  0.2022  216 HIS C CD2 
7595  C CE1 . HIS C 216 ? 0.7510 0.7817 1.5700 -0.0558 0.1480  0.1879  216 HIS C CE1 
7596  N NE2 . HIS C 216 ? 0.7646 0.8089 1.5369 -0.0452 0.1814  0.2184  216 HIS C NE2 
7597  N N   . ASN C 217 ? 0.5394 0.5311 1.1929 -0.0684 0.0420  0.0669  217 ASN C N   
7598  C CA  . ASN C 217 ? 0.5964 0.5697 1.2582 -0.0711 0.0167  0.0440  217 ASN C CA  
7599  C C   . ASN C 217 ? 0.5856 0.5338 1.1822 -0.0686 0.0118  0.0397  217 ASN C C   
7600  O O   . ASN C 217 ? 0.6116 0.5458 1.2135 -0.0687 -0.0006 0.0269  217 ASN C O   
7601  C CB  . ASN C 217 ? 0.6466 0.6271 1.3226 -0.0728 -0.0201 0.0047  217 ASN C CB  
7602  C CG  . ASN C 217 ? 0.6917 0.6580 1.3757 -0.0732 -0.0432 -0.0210 217 ASN C CG  
7603  O OD1 . ASN C 217 ? 0.7010 0.6656 1.4440 -0.0754 -0.0385 -0.0156 217 ASN C OD1 
7604  N ND2 . ASN C 217 ? 0.7180 0.6743 1.3421 -0.0698 -0.0657 -0.0477 217 ASN C ND2 
7605  N N   . SER C 218 ? 0.5158 0.4597 1.0484 -0.0634 0.0219  0.0491  218 SER C N   
7606  C CA  . SER C 218 ? 0.4305 0.3531 0.8949 -0.0568 0.0163  0.0447  218 SER C CA  
7607  C C   . SER C 218 ? 0.4187 0.3366 0.8560 -0.0495 0.0453  0.0819  218 SER C C   
7608  O O   . SER C 218 ? 0.4331 0.3377 0.8137 -0.0426 0.0418  0.0813  218 SER C O   
7609  C CB  . SER C 218 ? 0.3879 0.3134 0.7752 -0.0475 0.0010  0.0240  218 SER C CB  
7610  O OG  . SER C 218 ? 0.3955 0.3330 0.7408 -0.0375 0.0226  0.0439  218 SER C OG  
7611  N N   . LEU C 219 ? 0.4298 0.3617 0.9076 -0.0500 0.0741  0.1157  219 LEU C N   
7612  C CA  . LEU C 219 ? 0.4457 0.3807 0.8847 -0.0392 0.1025  0.1536  219 LEU C CA  
7613  C C   . LEU C 219 ? 0.4665 0.3799 0.9041 -0.0383 0.1012  0.1674  219 LEU C C   
7614  O O   . LEU C 219 ? 0.4579 0.3701 0.8386 -0.0271 0.1128  0.1893  219 LEU C O   
7615  C CB  . LEU C 219 ? 0.4841 0.4428 0.9697 -0.0383 0.1363  0.1894  219 LEU C CB  
7616  C CG  . LEU C 219 ? 0.4684 0.4539 0.9257 -0.0299 0.1487  0.1855  219 LEU C CG  
7617  C CD1 . LEU C 219 ? 0.4700 0.4812 0.9814 -0.0284 0.1833  0.2192  219 LEU C CD1 
7618  C CD2 . LEU C 219 ? 0.4576 0.4451 0.8134 -0.0132 0.1521  0.1838  219 LEU C CD2 
7619  N N   . ASP C 220 ? 0.4674 0.3724 0.9569 -0.0449 0.0844  0.1499  220 ASP C N   
7620  C CA  . ASP C 220 ? 0.5241 0.4146 1.0081 -0.0407 0.0816  0.1575  220 ASP C CA  
7621  C C   . ASP C 220 ? 0.4689 0.3397 0.8915 -0.0374 0.0636  0.1371  220 ASP C C   
7622  O O   . ASP C 220 ? 0.4788 0.3424 0.8654 -0.0289 0.0689  0.1552  220 ASP C O   
7623  C CB  . ASP C 220 ? 0.6288 0.5149 1.1837 -0.0472 0.0684  0.1401  220 ASP C CB  
7624  C CG  . ASP C 220 ? 0.7340 0.6365 1.3600 -0.0488 0.0859  0.1634  220 ASP C CG  
7625  O OD1 . ASP C 220 ? 0.7851 0.6991 1.4045 -0.0413 0.1130  0.2043  220 ASP C OD1 
7626  O OD2 . ASP C 220 ? 0.7573 0.6620 1.4443 -0.0559 0.0718  0.1401  220 ASP C OD2 
7627  N N   . VAL C 221 ? 0.4058 0.2708 0.8170 -0.0427 0.0413  0.0997  221 VAL C N   
7628  C CA  . VAL C 221 ? 0.4024 0.2513 0.7578 -0.0385 0.0236  0.0770  221 VAL C CA  
7629  C C   . VAL C 221 ? 0.4594 0.3199 0.7381 -0.0262 0.0339  0.0937  221 VAL C C   
7630  O O   . VAL C 221 ? 0.5034 0.3558 0.7403 -0.0190 0.0286  0.0935  221 VAL C O   
7631  C CB  . VAL C 221 ? 0.3967 0.2493 0.7431 -0.0427 -0.0014 0.0347  221 VAL C CB  
7632  C CG1 . VAL C 221 ? 0.3272 0.1736 0.6067 -0.0351 -0.0164 0.0133  221 VAL C CG1 
7633  C CG2 . VAL C 221 ? 0.4055 0.2622 0.8103 -0.0494 -0.0151 0.0117  221 VAL C CG2 
7634  N N   . LEU C 222 ? 0.4813 0.3619 0.7446 -0.0232 0.0473  0.1049  222 LEU C N   
7635  C CA  . LEU C 222 ? 0.4784 0.3716 0.6701 -0.0108 0.0557  0.1145  222 LEU C CA  
7636  C C   . LEU C 222 ? 0.5347 0.4288 0.7065 -0.0015 0.0716  0.1494  222 LEU C C   
7637  O O   . LEU C 222 ? 0.5365 0.4331 0.6478 0.0083  0.0666  0.1486  222 LEU C O   
7638  C CB  . LEU C 222 ? 0.4595 0.3746 0.6471 -0.0081 0.0696  0.1178  222 LEU C CB  
7639  C CG  . LEU C 222 ? 0.4087 0.3279 0.6056 -0.0134 0.0534  0.0869  222 LEU C CG  
7640  C CD1 . LEU C 222 ? 0.3980 0.3397 0.5906 -0.0074 0.0708  0.0937  222 LEU C CD1 
7641  C CD2 . LEU C 222 ? 0.3890 0.2980 0.5351 -0.0107 0.0307  0.0601  222 LEU C CD2 
7642  N N   . HIS C 223 ? 0.5794 0.4722 0.8062 -0.0046 0.0894  0.1808  223 HIS C N   
7643  C CA  . HIS C 223 ? 0.6774 0.5733 0.8930 0.0054  0.1067  0.2225  223 HIS C CA  
7644  C C   . HIS C 223 ? 0.6663 0.5445 0.8601 0.0096  0.0891  0.2171  223 HIS C C   
7645  O O   . HIS C 223 ? 0.7022 0.5882 0.8534 0.0222  0.0933  0.2401  223 HIS C O   
7646  C CB  . HIS C 223 ? 0.7729 0.6755 1.0622 0.0001  0.1226  0.2452  223 HIS C CB  
7647  C CG  . HIS C 223 ? 0.8682 0.7841 1.1470 0.0121  0.1374  0.2817  223 HIS C CG  
7648  N ND1 . HIS C 223 ? 0.9093 0.8514 1.1413 0.0260  0.1581  0.3096  223 HIS C ND1 
7649  C CD2 . HIS C 223 ? 0.8928 0.8013 1.2034 0.0133  0.1340  0.2936  223 HIS C CD2 
7650  C CE1 . HIS C 223 ? 0.9339 0.8839 1.1684 0.0350  0.1653  0.3380  223 HIS C CE1 
7651  N NE2 . HIS C 223 ? 0.9223 0.8515 1.2067 0.0271  0.1517  0.3308  223 HIS C NE2 
7652  N N   . ASP C 224 ? 0.6178 0.4757 0.8396 0.0004  0.0685  0.1844  224 ASP C N   
7653  C CA  . ASP C 224 ? 0.5978 0.4381 0.8154 0.0037  0.0540  0.1771  224 ASP C CA  
7654  C C   . ASP C 224 ? 0.5363 0.3778 0.6955 0.0070  0.0338  0.1430  224 ASP C C   
7655  O O   . ASP C 224 ? 0.5246 0.3528 0.6865 0.0085  0.0214  0.1299  224 ASP C O   
7656  C CB  . ASP C 224 ? 0.6275 0.4557 0.9106 -0.0063 0.0451  0.1554  224 ASP C CB  
7657  C CG  . ASP C 224 ? 0.6423 0.4806 0.9827 -0.0086 0.0610  0.1806  224 ASP C CG  
7658  O OD1 . ASP C 224 ? 0.6343 0.4863 0.9605 0.0001  0.0781  0.2184  224 ASP C OD1 
7659  O OD2 . ASP C 224 ? 0.6312 0.4666 1.0311 -0.0180 0.0556  0.1616  224 ASP C OD2 
7660  N N   . LEU C 225 ? 0.4828 0.3397 0.5960 0.0083  0.0319  0.1290  225 LEU C N   
7661  C CA  . LEU C 225 ? 0.4530 0.3108 0.5192 0.0106  0.0149  0.1012  225 LEU C CA  
7662  C C   . LEU C 225 ? 0.4653 0.3254 0.4966 0.0208  0.0099  0.1123  225 LEU C C   
7663  O O   . LEU C 225 ? 0.4590 0.3303 0.4711 0.0298  0.0191  0.1402  225 LEU C O   
7664  C CB  . LEU C 225 ? 0.4463 0.3190 0.4757 0.0113  0.0151  0.0882  225 LEU C CB  
7665  C CG  . LEU C 225 ? 0.4191 0.2926 0.4714 0.0028  0.0114  0.0674  225 LEU C CG  
7666  C CD1 . LEU C 225 ? 0.4404 0.3258 0.4512 0.0067  0.0089  0.0546  225 LEU C CD1 
7667  C CD2 . LEU C 225 ? 0.3838 0.2440 0.4573 -0.0039 -0.0052 0.0421  225 LEU C CD2 
7668  N N   . VAL C 226 ? 0.4685 0.3211 0.4914 0.0203  -0.0049 0.0901  226 VAL C N   
7669  C CA  . VAL C 226 ? 0.4619 0.3184 0.4591 0.0287  -0.0131 0.0949  226 VAL C CA  
7670  C C   . VAL C 226 ? 0.4576 0.3231 0.4144 0.0283  -0.0240 0.0716  226 VAL C C   
7671  O O   . VAL C 226 ? 0.4408 0.3020 0.4003 0.0216  -0.0279 0.0489  226 VAL C O   
7672  C CB  . VAL C 226 ? 0.4574 0.2983 0.4913 0.0289  -0.0184 0.0903  226 VAL C CB  
7673  C CG1 . VAL C 226 ? 0.5029 0.3499 0.5154 0.0359  -0.0293 0.0859  226 VAL C CG1 
7674  C CG2 . VAL C 226 ? 0.4952 0.3274 0.5693 0.0318  -0.0084 0.1196  226 VAL C CG2 
7675  N N   . TYR C 227 ? 0.4864 0.3651 0.4085 0.0360  -0.0298 0.0776  227 TYR C N   
7676  C CA  . TYR C 227 ? 0.5194 0.4058 0.4114 0.0350  -0.0401 0.0561  227 TYR C CA  
7677  C C   . TYR C 227 ? 0.4796 0.3700 0.3678 0.0379  -0.0537 0.0496  227 TYR C C   
7678  O O   . TYR C 227 ? 0.4781 0.3722 0.3731 0.0448  -0.0572 0.0655  227 TYR C O   
7679  C CB  . TYR C 227 ? 0.5742 0.4754 0.4305 0.0408  -0.0375 0.0595  227 TYR C CB  
7680  C CG  . TYR C 227 ? 0.5917 0.4929 0.4535 0.0382  -0.0225 0.0632  227 TYR C CG  
7681  C CD1 . TYR C 227 ? 0.5933 0.4910 0.4580 0.0318  -0.0227 0.0432  227 TYR C CD1 
7682  C CD2 . TYR C 227 ? 0.6480 0.5543 0.5174 0.0427  -0.0074 0.0900  227 TYR C CD2 
7683  C CE1 . TYR C 227 ? 0.6350 0.5356 0.5108 0.0301  -0.0097 0.0467  227 TYR C CE1 
7684  C CE2 . TYR C 227 ? 0.6786 0.5880 0.5606 0.0402  0.0081  0.0949  227 TYR C CE2 
7685  C CZ  . TYR C 227 ? 0.6901 0.5971 0.5761 0.0338  0.0062  0.0718  227 TYR C CZ  
7686  O OH  . TYR C 227 ? 0.7375 0.6503 0.6425 0.0319  0.0212  0.0773  227 TYR C OH  
7687  N N   . THR C 228 ? 0.4158 0.3070 0.2977 0.0331  -0.0608 0.0290  228 THR C N   
7688  C CA  . THR C 228 ? 0.4260 0.3239 0.3110 0.0345  -0.0726 0.0225  228 THR C CA  
7689  C C   . THR C 228 ? 0.4095 0.3131 0.2792 0.0309  -0.0801 0.0055  228 THR C C   
7690  O O   . THR C 228 ? 0.4305 0.3283 0.2947 0.0263  -0.0747 -0.0033 228 THR C O   
7691  C CB  . THR C 228 ? 0.4111 0.3010 0.3245 0.0315  -0.0697 0.0168  228 THR C CB  
7692  O OG1 . THR C 228 ? 0.4474 0.3471 0.3722 0.0344  -0.0785 0.0158  228 THR C OG1 
7693  C CG2 . THR C 228 ? 0.3821 0.2659 0.2947 0.0244  -0.0652 0.0014  228 THR C CG2 
7694  N N   . PRO C 229 ? 0.3814 0.2966 0.2499 0.0332  -0.0938 0.0004  229 PRO C N   
7695  C CA  . PRO C 229 ? 0.4037 0.3215 0.2659 0.0292  -0.1012 -0.0175 229 PRO C CA  
7696  C C   . PRO C 229 ? 0.3760 0.2840 0.2584 0.0204  -0.0954 -0.0255 229 PRO C C   
7697  O O   . PRO C 229 ? 0.3959 0.3018 0.2978 0.0180  -0.0903 -0.0212 229 PRO C O   
7698  C CB  . PRO C 229 ? 0.3790 0.3123 0.2461 0.0326  -0.1197 -0.0225 229 PRO C CB  
7699  C CG  . PRO C 229 ? 0.4098 0.3519 0.2667 0.0424  -0.1217 -0.0035 229 PRO C CG  
7700  C CD  . PRO C 229 ? 0.3908 0.3188 0.2641 0.0405  -0.1050 0.0103  229 PRO C CD  
7701  N N   . LEU C 230 ? 0.3860 0.2891 0.2621 0.0174  -0.0949 -0.0362 230 LEU C N   
7702  C CA  . LEU C 230 ? 0.3710 0.2661 0.2640 0.0108  -0.0898 -0.0396 230 LEU C CA  
7703  C C   . LEU C 230 ? 0.3768 0.2745 0.2910 0.0066  -0.1001 -0.0500 230 LEU C C   
7704  O O   . LEU C 230 ? 0.3816 0.2821 0.2902 0.0084  -0.1110 -0.0637 230 LEU C O   
7705  C CB  . LEU C 230 ? 0.4041 0.2909 0.2856 0.0108  -0.0821 -0.0417 230 LEU C CB  
7706  C CG  . LEU C 230 ? 0.3844 0.2639 0.2791 0.0064  -0.0777 -0.0419 230 LEU C CG  
7707  C CD1 . LEU C 230 ? 0.3590 0.2391 0.2595 0.0049  -0.0711 -0.0325 230 LEU C CD1 
7708  C CD2 . LEU C 230 ? 0.3891 0.2641 0.2742 0.0086  -0.0728 -0.0445 230 LEU C CD2 
7709  N N   . THR C 231 ? 0.4040 0.3022 0.3452 0.0015  -0.0965 -0.0442 231 THR C N   
7710  C CA  . THR C 231 ? 0.4114 0.3106 0.3856 -0.0045 -0.1034 -0.0504 231 THR C CA  
7711  C C   . THR C 231 ? 0.4068 0.2976 0.3964 -0.0088 -0.0914 -0.0407 231 THR C C   
7712  O O   . THR C 231 ? 0.3906 0.2803 0.3655 -0.0066 -0.0791 -0.0291 231 THR C O   
7713  C CB  . THR C 231 ? 0.3850 0.2979 0.3899 -0.0068 -0.1099 -0.0478 231 THR C CB  
7714  O OG1 . THR C 231 ? 0.3670 0.2848 0.3696 -0.0039 -0.0970 -0.0333 231 THR C OG1 
7715  C CG2 . THR C 231 ? 0.3686 0.2924 0.3652 -0.0024 -0.1290 -0.0598 231 THR C CG2 
7716  N N   . ILE C 232 ? 0.4092 0.2946 0.4296 -0.0141 -0.0966 -0.0463 232 ILE C N   
7717  C CA  . ILE C 232 ? 0.3992 0.2752 0.4371 -0.0169 -0.0867 -0.0344 232 ILE C CA  
7718  C C   . ILE C 232 ? 0.3675 0.2468 0.4571 -0.0243 -0.0844 -0.0244 232 ILE C C   
7719  O O   . ILE C 232 ? 0.3562 0.2373 0.4786 -0.0294 -0.0976 -0.0383 232 ILE C O   
7720  C CB  . ILE C 232 ? 0.3935 0.2555 0.4289 -0.0154 -0.0922 -0.0480 232 ILE C CB  
7721  C CG1 . ILE C 232 ? 0.3746 0.2372 0.3644 -0.0080 -0.0922 -0.0565 232 ILE C CG1 
7722  C CG2 . ILE C 232 ? 0.4013 0.2534 0.4575 -0.0166 -0.0826 -0.0316 232 ILE C CG2 
7723  C CD1 . ILE C 232 ? 0.3418 0.2069 0.3069 -0.0048 -0.0805 -0.0404 232 ILE C CD1 
7724  N N   . SER C 233 ? 0.3753 0.2579 0.4739 -0.0246 -0.0678 0.0000  233 SER C N   
7725  C CA  . SER C 233 ? 0.3814 0.2683 0.5353 -0.0317 -0.0608 0.0159  233 SER C CA  
7726  C C   . SER C 233 ? 0.4327 0.3025 0.6280 -0.0370 -0.0644 0.0168  233 SER C C   
7727  O O   . SER C 233 ? 0.4493 0.3046 0.6261 -0.0334 -0.0700 0.0067  233 SER C O   
7728  C CB  . SER C 233 ? 0.3920 0.2917 0.5378 -0.0276 -0.0383 0.0451  233 SER C CB  
7729  O OG  . SER C 233 ? 0.4188 0.3113 0.5420 -0.0224 -0.0301 0.0603  233 SER C OG  
7730  N N   . LYS C 234 ? 0.4107 0.2825 0.6689 -0.0453 -0.0600 0.0298  234 LYS C N   
7731  C CA  . LYS C 234 ? 0.4343 0.2877 0.7460 -0.0512 -0.0627 0.0326  234 LYS C CA  
7732  C C   . LYS C 234 ? 0.4269 0.2722 0.7214 -0.0446 -0.0474 0.0605  234 LYS C C   
7733  O O   . LYS C 234 ? 0.3916 0.2238 0.7100 -0.0440 -0.0499 0.0596  234 LYS C O   
7734  C CB  . LYS C 234 ? 0.4869 0.3516 0.8722 -0.0602 -0.0575 0.0452  234 LYS C CB  
7735  C CG  . LYS C 234 ? 0.5528 0.4308 0.9654 -0.0653 -0.0760 0.0172  234 LYS C CG  
7736  C CD  . LYS C 234 ? 0.6420 0.5352 1.1293 -0.0715 -0.0679 0.0336  234 LYS C CD  
7737  C CE  . LYS C 234 ? 0.7015 0.6115 1.2181 -0.0752 -0.0855 0.0114  234 LYS C CE  
7738  N NZ  . LYS C 234 ? 0.7410 0.6687 1.3284 -0.0804 -0.0724 0.0344  234 LYS C NZ  
7739  N N   . GLN C 235 ? 0.4379 0.2983 0.6825 -0.0364 -0.0327 0.0809  235 GLN C N   
7740  C CA  . GLN C 235 ? 0.4438 0.3025 0.6664 -0.0282 -0.0209 0.1082  235 GLN C CA  
7741  C C   . GLN C 235 ? 0.4432 0.2966 0.6081 -0.0198 -0.0307 0.0900  235 GLN C C   
7742  O O   . GLN C 235 ? 0.4520 0.3069 0.5920 -0.0117 -0.0256 0.1077  235 GLN C O   
7743  C CB  . GLN C 235 ? 0.5002 0.3821 0.7013 -0.0224 0.0005  0.1397  235 GLN C CB  
7744  C CG  . GLN C 235 ? 0.6333 0.5234 0.8974 -0.0296 0.0162  0.1670  235 GLN C CG  
7745  C CD  . GLN C 235 ? 0.7811 0.6591 1.0990 -0.0325 0.0192  0.1867  235 GLN C CD  
7746  O OE1 . GLN C 235 ? 0.8187 0.6918 1.1136 -0.0242 0.0199  0.1989  235 GLN C OE1 
7747  N NE2 . GLN C 235 ? 0.8273 0.7097 1.2128 -0.0417 0.0187  0.1823  235 GLN C NE2 
7748  N N   . GLY C 236 ? 0.4075 0.2572 0.5536 -0.0214 -0.0450 0.0563  236 GLY C N   
7749  C CA  . GLY C 236 ? 0.4079 0.2532 0.5098 -0.0147 -0.0528 0.0389  236 GLY C CA  
7750  C C   . GLY C 236 ? 0.3564 0.2161 0.4039 -0.0087 -0.0492 0.0386  236 GLY C C   
7751  O O   . GLY C 236 ? 0.3559 0.2142 0.3731 -0.0033 -0.0530 0.0314  236 GLY C O   
7752  N N   . GLU C 237 ? 0.3526 0.2263 0.3943 -0.0097 -0.0421 0.0445  237 GLU C N   
7753  C CA  . GLU C 237 ? 0.3452 0.2309 0.3429 -0.0037 -0.0384 0.0414  237 GLU C CA  
7754  C C   . GLU C 237 ? 0.3571 0.2416 0.3393 -0.0046 -0.0477 0.0181  237 GLU C C   
7755  O O   . GLU C 237 ? 0.3783 0.2602 0.3815 -0.0094 -0.0553 0.0072  237 GLU C O   
7756  C CB  . GLU C 237 ? 0.3546 0.2571 0.3543 -0.0016 -0.0236 0.0582  237 GLU C CB  
7757  C CG  . GLU C 237 ? 0.4027 0.3111 0.4158 0.0009  -0.0106 0.0880  237 GLU C CG  
7758  C CD  . GLU C 237 ? 0.5226 0.4472 0.5597 -0.0002 0.0063  0.1055  237 GLU C CD  
7759  O OE1 . GLU C 237 ? 0.5148 0.4370 0.5974 -0.0091 0.0039  0.1010  237 GLU C OE1 
7760  O OE2 . GLU C 237 ? 0.6000 0.5422 0.6120 0.0087  0.0220  0.1235  237 GLU C OE2 
7761  N N   . TYR C 238 ? 0.3820 0.2697 0.3296 0.0006  -0.0477 0.0119  238 TYR C N   
7762  C CA  . TYR C 238 ? 0.3903 0.2767 0.3236 0.0010  -0.0539 -0.0039 238 TYR C CA  
7763  C C   . TYR C 238 ? 0.3883 0.2845 0.3217 0.0027  -0.0488 -0.0036 238 TYR C C   
7764  O O   . TYR C 238 ? 0.3689 0.2730 0.2903 0.0073  -0.0399 0.0012  238 TYR C O   
7765  C CB  . TYR C 238 ? 0.3789 0.2624 0.2881 0.0046  -0.0562 -0.0099 238 TYR C CB  
7766  C CG  . TYR C 238 ? 0.3859 0.2616 0.2987 0.0046  -0.0605 -0.0111 238 TYR C CG  
7767  C CD1 . TYR C 238 ? 0.3752 0.2443 0.2932 0.0034  -0.0655 -0.0220 238 TYR C CD1 
7768  C CD2 . TYR C 238 ? 0.4096 0.2870 0.3204 0.0076  -0.0595 -0.0014 238 TYR C CD2 
7769  C CE1 . TYR C 238 ? 0.3686 0.2313 0.2932 0.0051  -0.0673 -0.0254 238 TYR C CE1 
7770  C CE2 . TYR C 238 ? 0.3955 0.2662 0.3163 0.0088  -0.0633 -0.0019 238 TYR C CE2 
7771  C CZ  . TYR C 238 ? 0.3703 0.2331 0.2996 0.0075  -0.0661 -0.0149 238 TYR C CZ  
7772  O OH  . TYR C 238 ? 0.3992 0.2562 0.3412 0.0104  -0.0677 -0.0176 238 TYR C OH  
7773  N N   . PHE C 239 ? 0.3883 0.2854 0.3342 0.0007  -0.0553 -0.0103 239 PHE C N   
7774  C CA  . PHE C 239 ? 0.3615 0.2681 0.3161 0.0031  -0.0523 -0.0099 239 PHE C CA  
7775  C C   . PHE C 239 ? 0.3866 0.2904 0.3318 0.0058  -0.0607 -0.0175 239 PHE C C   
7776  O O   . PHE C 239 ? 0.4131 0.3118 0.3501 0.0047  -0.0699 -0.0228 239 PHE C O   
7777  C CB  . PHE C 239 ? 0.3465 0.2623 0.3378 -0.0012 -0.0531 -0.0048 239 PHE C CB  
7778  C CG  . PHE C 239 ? 0.3412 0.2652 0.3483 -0.0018 -0.0381 0.0100  239 PHE C CG  
7779  C CD1 . PHE C 239 ? 0.3262 0.2446 0.3410 -0.0055 -0.0355 0.0194  239 PHE C CD1 
7780  C CD2 . PHE C 239 ? 0.3582 0.2970 0.3746 0.0026  -0.0248 0.0167  239 PHE C CD2 
7781  C CE1 . PHE C 239 ? 0.3456 0.2735 0.3737 -0.0046 -0.0193 0.0392  239 PHE C CE1 
7782  C CE2 . PHE C 239 ? 0.3533 0.3034 0.3803 0.0040  -0.0071 0.0338  239 PHE C CE2 
7783  C CZ  . PHE C 239 ? 0.3525 0.2977 0.3843 0.0003  -0.0044 0.0470  239 PHE C CZ  
7784  N N   . ILE C 240 ? 0.3843 0.2919 0.3308 0.0106  -0.0561 -0.0171 240 ILE C N   
7785  C CA  . ILE C 240 ? 0.4042 0.3117 0.3529 0.0140  -0.0637 -0.0176 240 ILE C CA  
7786  C C   . ILE C 240 ? 0.3888 0.3079 0.3641 0.0177  -0.0623 -0.0141 240 ILE C C   
7787  O O   . ILE C 240 ? 0.4146 0.3419 0.4048 0.0179  -0.0522 -0.0123 240 ILE C O   
7788  C CB  . ILE C 240 ? 0.4500 0.3474 0.3844 0.0176  -0.0607 -0.0189 240 ILE C CB  
7789  C CG1 . ILE C 240 ? 0.4359 0.3319 0.3733 0.0210  -0.0505 -0.0242 240 ILE C CG1 
7790  C CG2 . ILE C 240 ? 0.4404 0.3298 0.3555 0.0145  -0.0626 -0.0209 240 ILE C CG2 
7791  C CD1 . ILE C 240 ? 0.4069 0.2923 0.3452 0.0236  -0.0496 -0.0280 240 ILE C CD1 
7792  N N   . GLN C 241 ? 0.3898 0.3121 0.3722 0.0219  -0.0715 -0.0108 241 GLN C N   
7793  C CA  . GLN C 241 ? 0.3819 0.3168 0.3949 0.0267  -0.0723 -0.0066 241 GLN C CA  
7794  C C   . GLN C 241 ? 0.4343 0.3629 0.4532 0.0349  -0.0648 -0.0046 241 GLN C C   
7795  O O   . GLN C 241 ? 0.4552 0.3755 0.4661 0.0386  -0.0701 0.0011  241 GLN C O   
7796  C CB  . GLN C 241 ? 0.3362 0.2828 0.3595 0.0277  -0.0913 -0.0035 241 GLN C CB  
7797  C CG  . GLN C 241 ? 0.3687 0.3304 0.4288 0.0342  -0.0943 0.0028  241 GLN C CG  
7798  C CD  . GLN C 241 ? 0.4370 0.4104 0.5315 0.0311  -0.0822 0.0012  241 GLN C CD  
7799  O OE1 . GLN C 241 ? 0.4369 0.4107 0.5322 0.0230  -0.0778 -0.0019 241 GLN C OE1 
7800  N NE2 . GLN C 241 ? 0.4667 0.4499 0.5921 0.0388  -0.0743 0.0054  241 GLN C NE2 
7801  N N   . VAL C 242 ? 0.4143 0.3476 0.4504 0.0387  -0.0512 -0.0087 242 VAL C N   
7802  C CA  . VAL C 242 ? 0.3607 0.2884 0.4118 0.0478  -0.0432 -0.0120 242 VAL C CA  
7803  C C   . VAL C 242 ? 0.3906 0.3345 0.4823 0.0550  -0.0430 -0.0062 242 VAL C C   
7804  O O   . VAL C 242 ? 0.3892 0.3493 0.4985 0.0549  -0.0337 -0.0075 242 VAL C O   
7805  C CB  . VAL C 242 ? 0.3271 0.2505 0.3647 0.0498  -0.0274 -0.0264 242 VAL C CB  
7806  C CG1 . VAL C 242 ? 0.3169 0.2353 0.3756 0.0601  -0.0193 -0.0358 242 VAL C CG1 
7807  C CG2 . VAL C 242 ? 0.3372 0.2466 0.3420 0.0437  -0.0306 -0.0319 242 VAL C CG2 
7808  N N   . ASN C 243 ? 0.3505 0.2923 0.4606 0.0616  -0.0528 0.0032  243 ASN C N   
7809  C CA  . ASN C 243 ? 0.3674 0.3262 0.5214 0.0700  -0.0554 0.0103  243 ASN C CA  
7810  C C   . ASN C 243 ? 0.3809 0.3389 0.5643 0.0805  -0.0369 0.0010  243 ASN C C   
7811  O O   . ASN C 243 ? 0.3830 0.3602 0.6038 0.0865  -0.0311 0.0023  243 ASN C O   
7812  C CB  . ASN C 243 ? 0.3816 0.3407 0.5437 0.0758  -0.0740 0.0272  243 ASN C CB  
7813  C CG  . ASN C 243 ? 0.3924 0.3668 0.5400 0.0702  -0.0950 0.0336  243 ASN C CG  
7814  O OD1 . ASN C 243 ? 0.4046 0.3859 0.5432 0.0606  -0.0959 0.0246  243 ASN C OD1 
7815  N ND2 . ASN C 243 ? 0.4123 0.3921 0.5579 0.0772  -0.1125 0.0493  243 ASN C ND2 
7816  N N   . ALA C 244 ? 0.3631 0.3001 0.5328 0.0832  -0.0277 -0.0107 244 ALA C N   
7817  C CA  . ALA C 244 ? 0.3398 0.2733 0.5337 0.0945  -0.0112 -0.0264 244 ALA C CA  
7818  C C   . ALA C 244 ? 0.3363 0.2492 0.5033 0.0931  -0.0042 -0.0466 244 ALA C C   
7819  O O   . ALA C 244 ? 0.3334 0.2309 0.4765 0.0848  -0.0135 -0.0436 244 ALA C O   
7820  C CB  . ALA C 244 ? 0.3364 0.2651 0.5766 0.1059  -0.0160 -0.0167 244 ALA C CB  
7821  N N   . ILE C 245 ? 0.3811 0.2969 0.5536 0.1022  0.0122  -0.0690 245 ILE C N   
7822  C CA  . ILE C 245 ? 0.3944 0.2913 0.5533 0.1044  0.0157  -0.0944 245 ILE C CA  
7823  C C   . ILE C 245 ? 0.3901 0.2731 0.5984 0.1166  0.0189  -0.1037 245 ILE C C   
7824  O O   . ILE C 245 ? 0.4225 0.3188 0.6604 0.1285  0.0304  -0.1075 245 ILE C O   
7825  C CB  . ILE C 245 ? 0.4239 0.3344 0.5487 0.1085  0.0303  -0.1176 245 ILE C CB  
7826  C CG1 . ILE C 245 ? 0.4370 0.3628 0.5219 0.0977  0.0289  -0.1024 245 ILE C CG1 
7827  C CG2 . ILE C 245 ? 0.4208 0.3131 0.5306 0.1101  0.0273  -0.1472 245 ILE C CG2 
7828  C CD1 . ILE C 245 ? 0.5066 0.4534 0.5615 0.1044  0.0467  -0.1144 245 ILE C CD1 
7829  N N   . ARG C 246 ? 0.3970 0.2534 0.6212 0.1138  0.0094  -0.1046 246 ARG C N   
7830  C CA  . ARG C 246 ? 0.4197 0.2631 0.6880 0.1203  0.0111  -0.1062 246 ARG C CA  
7831  C C   . ARG C 246 ? 0.4509 0.2862 0.7108 0.1208  0.0170  -0.1402 246 ARG C C   
7832  O O   . ARG C 246 ? 0.5066 0.3343 0.7392 0.1116  0.0112  -0.1527 246 ARG C O   
7833  C CB  . ARG C 246 ? 0.4856 0.3126 0.7721 0.1125  -0.0015 -0.0771 246 ARG C CB  
7834  C CG  . ARG C 246 ? 0.5388 0.3548 0.8703 0.1163  0.0002  -0.0735 246 ARG C CG  
7835  C CD  . ARG C 246 ? 0.6233 0.4219 0.9678 0.1063  -0.0075 -0.0536 246 ARG C CD  
7836  N NE  . ARG C 246 ? 0.6888 0.4918 1.0324 0.1055  -0.0156 -0.0129 246 ARG C NE  
7837  C CZ  . ARG C 246 ? 0.7560 0.5515 1.0881 0.0966  -0.0205 0.0080  246 ARG C CZ  
7838  N NH1 . ARG C 246 ? 0.7755 0.5585 1.1043 0.0864  -0.0188 -0.0072 246 ARG C NH1 
7839  N NH2 . ARG C 246 ? 0.7795 0.5834 1.1030 0.0986  -0.0274 0.0442  246 ARG C NH2 
7840  N N   . VAL C 247 ? 0.4783 0.3172 0.7621 0.1319  0.0272  -0.1556 247 VAL C N   
7841  C CA  . VAL C 247 ? 0.5160 0.3449 0.8009 0.1330  0.0292  -0.1866 247 VAL C CA  
7842  C C   . VAL C 247 ? 0.5712 0.3866 0.9135 0.1369  0.0284  -0.1800 247 VAL C C   
7843  O O   . VAL C 247 ? 0.5487 0.3727 0.9174 0.1491  0.0376  -0.1779 247 VAL C O   
7844  C CB  . VAL C 247 ? 0.5409 0.3879 0.7942 0.1449  0.0439  -0.2174 247 VAL C CB  
7845  C CG1 . VAL C 247 ? 0.5858 0.4226 0.8374 0.1461  0.0421  -0.2509 247 VAL C CG1 
7846  C CG2 . VAL C 247 ? 0.5199 0.3836 0.7191 0.1416  0.0460  -0.2177 247 VAL C CG2 
7847  N N   . ASN C 248 ? 0.4220 0.2663 0.8352 0.0302  0.0751  0.0640  248 ASN C N   
7848  C CA  . ASN C 248 ? 0.4446 0.2927 0.8942 0.0414  0.0942  0.0871  248 ASN C CA  
7849  C C   . ASN C 248 ? 0.4113 0.2814 0.8252 0.0654  0.1183  0.1168  248 ASN C C   
7850  O O   . ASN C 248 ? 0.3906 0.2852 0.7888 0.0768  0.1318  0.1442  248 ASN C O   
7851  C CB  . ASN C 248 ? 0.4859 0.2995 0.9453 0.0399  0.0782  0.0567  248 ASN C CB  
7852  C CG  . ASN C 248 ? 0.4844 0.2790 0.9891 0.0235  0.0493  0.0313  248 ASN C CG  
7853  O OD1 . ASN C 248 ? 0.4430 0.2591 0.9995 0.0129  0.0489  0.0467  248 ASN C OD1 
7854  N ND2 . ASN C 248 ? 0.5287 0.2843 1.0144 0.0267  0.0245  -0.0070 248 ASN C ND2 
7855  N N   . LYS C 249 ? 0.4410 0.3047 0.8373 0.0783  0.1212  0.1106  249 LYS C N   
7856  C CA  . LYS C 249 ? 0.4563 0.3487 0.8199 0.1041  0.1346  0.1346  249 LYS C CA  
7857  C C   . LYS C 249 ? 0.4108 0.3192 0.7352 0.1091  0.1213  0.1146  249 LYS C C   
7858  O O   . LYS C 249 ? 0.3974 0.3344 0.7047 0.1285  0.1222  0.1243  249 LYS C O   
7859  C CB  . LYS C 249 ? 0.5095 0.4001 0.8912 0.1179  0.1503  0.1505  249 LYS C CB  
7860  C CG  . LYS C 249 ? 0.5652 0.4434 1.0044 0.1089  0.1641  0.1663  249 LYS C CG  
7861  C CD  . LYS C 249 ? 0.6126 0.4919 1.0660 0.1265  0.1842  0.1883  249 LYS C CD  
7862  C CE  . LYS C 249 ? 0.6466 0.5076 1.1771 0.1137  0.1932  0.1943  249 LYS C CE  
7863  N NZ  . LYS C 249 ? 0.6220 0.4976 1.1979 0.1005  0.1985  0.2079  249 LYS C NZ  
7864  N N   . HIS C 250 ? 0.3645 0.2654 0.6702 0.0866  0.1051  0.0843  250 HIS C N   
7865  C CA  . HIS C 250 ? 0.3891 0.3155 0.6603 0.0823  0.0947  0.0675  250 HIS C CA  
7866  C C   . HIS C 250 ? 0.3770 0.3222 0.6231 0.0709  0.0812  0.0644  250 HIS C C   
7867  O O   . HIS C 250 ? 0.3926 0.3208 0.6353 0.0560  0.0764  0.0562  250 HIS C O   
7868  C CB  . HIS C 250 ? 0.3679 0.2695 0.6296 0.0763  0.0939  0.0410  250 HIS C CB  
7869  C CG  . HIS C 250 ? 0.3887 0.2704 0.6664 0.0938  0.1063  0.0414  250 HIS C CG  
7870  N ND1 . HIS C 250 ? 0.4124 0.2600 0.6725 0.1015  0.1071  0.0171  250 HIS C ND1 
7871  C CD2 . HIS C 250 ? 0.3871 0.2745 0.6917 0.1107  0.1188  0.0636  250 HIS C CD2 
7872  C CE1 . HIS C 250 ? 0.4769 0.3089 0.7550 0.1202  0.1193  0.0226  250 HIS C CE1 
7873  N NE2 . HIS C 250 ? 0.4326 0.2899 0.7419 0.1241  0.1274  0.0522  250 HIS C NE2 
7874  N N   . LEU C 251 ? 0.3740 0.3524 0.6065 0.0787  0.0707  0.0675  251 LEU C N   
7875  C CA  . LEU C 251 ? 0.3514 0.3415 0.5594 0.0714  0.0542  0.0609  251 LEU C CA  
7876  C C   . LEU C 251 ? 0.3238 0.3299 0.5363 0.0561  0.0416  0.0431  251 LEU C C   
7877  O O   . LEU C 251 ? 0.3200 0.3508 0.5565 0.0622  0.0344  0.0433  251 LEU C O   
7878  C CB  . LEU C 251 ? 0.3605 0.3680 0.5469 0.0991  0.0449  0.0759  251 LEU C CB  
7879  C CG  . LEU C 251 ? 0.3830 0.3745 0.5668 0.1182  0.0674  0.1048  251 LEU C CG  
7880  C CD1 . LEU C 251 ? 0.3741 0.3660 0.5786 0.1413  0.0846  0.1270  251 LEU C CD1 
7881  C CD2 . LEU C 251 ? 0.4205 0.4181 0.5598 0.1435  0.0622  0.1163  251 LEU C CD2 
7882  N N   . VAL C 252 ? 0.3051 0.2983 0.5035 0.0377  0.0399  0.0317  252 VAL C N   
7883  C CA  . VAL C 252 ? 0.2982 0.3022 0.5063 0.0239  0.0350  0.0218  252 VAL C CA  
7884  C C   . VAL C 252 ? 0.3031 0.3182 0.5050 0.0209  0.0110  0.0156  252 VAL C C   
7885  O O   . VAL C 252 ? 0.3494 0.3507 0.5194 0.0207  0.0065  0.0141  252 VAL C O   
7886  C CB  . VAL C 252 ? 0.2908 0.2701 0.4792 0.0134  0.0483  0.0139  252 VAL C CB  
7887  C CG1 . VAL C 252 ? 0.2996 0.2892 0.5001 0.0053  0.0535  0.0136  252 VAL C CG1 
7888  C CG2 . VAL C 252 ? 0.2920 0.2506 0.4762 0.0242  0.0639  0.0117  252 VAL C CG2 
7889  N N   . ILE C 253 ? 0.3183 0.3576 0.5566 0.0214  -0.0071 0.0114  253 ILE C N   
7890  C CA  . ILE C 253 ? 0.3538 0.3988 0.5905 0.0236  -0.0408 -0.0024 253 ILE C CA  
7891  C C   . ILE C 253 ? 0.4117 0.4553 0.6834 0.0001  -0.0414 -0.0083 253 ILE C C   
7892  O O   . ILE C 253 ? 0.3948 0.4567 0.7304 -0.0094 -0.0340 -0.0013 253 ILE C O   
7893  C CB  . ILE C 253 ? 0.3462 0.4171 0.6159 0.0406  -0.0742 -0.0097 253 ILE C CB  
7894  C CG1 . ILE C 253 ? 0.4134 0.4907 0.6593 0.0679  -0.0668 0.0034  253 ILE C CG1 
7895  C CG2 . ILE C 253 ? 0.3546 0.4203 0.6069 0.0511  -0.1185 -0.0329 253 ILE C CG2 
7896  C CD1 . ILE C 253 ? 0.4666 0.5217 0.6454 0.0871  -0.0528 0.0141  253 ILE C CD1 
7897  N N   . PRO C 254 ? 0.4966 0.5190 0.7322 -0.0069 -0.0442 -0.0155 254 PRO C N   
7898  C CA  . PRO C 254 ? 0.5657 0.5836 0.8351 -0.0264 -0.0420 -0.0174 254 PRO C CA  
7899  C C   . PRO C 254 ? 0.7148 0.7485 1.0564 -0.0314 -0.0772 -0.0298 254 PRO C C   
7900  O O   . PRO C 254 ? 0.7733 0.7962 1.0988 -0.0235 -0.1156 -0.0519 254 PRO C O   
7901  C CB  . PRO C 254 ? 0.5398 0.5321 0.7501 -0.0263 -0.0446 -0.0244 254 PRO C CB  
7902  C CG  . PRO C 254 ? 0.5040 0.4896 0.6609 -0.0106 -0.0350 -0.0182 254 PRO C CG  
7903  C CD  . PRO C 254 ? 0.5083 0.5114 0.6781 0.0060  -0.0456 -0.0168 254 PRO C CD  
7904  N N   . THR C 255 ? 0.7745 0.8324 1.1987 -0.0407 -0.0644 -0.0152 255 THR C N   
7905  C CA  . THR C 255 ? 0.7945 0.8742 1.3289 -0.0513 -0.0928 -0.0196 255 THR C CA  
7906  C C   . THR C 255 ? 0.8471 0.9399 1.3908 -0.0346 -0.1487 -0.0459 255 THR C C   
7907  O O   . THR C 255 ? 0.8381 0.9571 1.4044 -0.0230 -0.1491 -0.0384 255 THR C O   
7908  C CB  . THR C 255 ? 0.7741 0.8345 1.3440 -0.0677 -0.1036 -0.0261 255 THR C CB  
7909  O OG1 . THR C 255 ? 0.7805 0.8130 1.2783 -0.0596 -0.1395 -0.0564 255 THR C OG1 
7910  C CG2 . THR C 255 ? 0.7631 0.8127 1.3202 -0.0760 -0.0472 0.0038  255 THR C CG2 
7911  N N   . GLY C 271 ? 1.4506 1.1200 1.0362 0.4471  -0.4428 -0.3105 271 GLY C N   
7912  C CA  . GLY C 271 ? 1.4320 1.0849 1.0142 0.4323  -0.4317 -0.3017 271 GLY C CA  
7913  C C   . GLY C 271 ? 1.3296 0.9923 1.0285 0.3614  -0.4538 -0.3134 271 GLY C C   
7914  O O   . GLY C 271 ? 1.3094 0.9475 1.0416 0.3631  -0.4961 -0.3411 271 GLY C O   
7915  N N   . GLU C 272 ? 1.2457 0.9449 1.0088 0.3018  -0.4207 -0.2894 272 GLU C N   
7916  C CA  . GLU C 272 ? 1.1540 0.8699 1.0337 0.2338  -0.4206 -0.2873 272 GLU C CA  
7917  C C   . GLU C 272 ? 0.9625 0.6945 0.8209 0.2034  -0.3617 -0.2513 272 GLU C C   
7918  O O   . GLU C 272 ? 0.9478 0.6853 0.7282 0.2306  -0.3330 -0.2326 272 GLU C O   
7919  C CB  . GLU C 272 ? 1.1839 0.9268 1.1671 0.2050  -0.4439 -0.2961 272 GLU C CB  
7920  C CG  . GLU C 272 ? 1.1391 0.9194 1.2220 0.1404  -0.4088 -0.2684 272 GLU C CG  
7921  C CD  . GLU C 272 ? 1.1769 0.9544 1.3373 0.0987  -0.3942 -0.2585 272 GLU C CD  
7922  O OE1 . GLU C 272 ? 1.2376 0.9859 1.3929 0.1129  -0.4197 -0.2775 272 GLU C OE1 
7923  O OE2 . GLU C 272 ? 1.1392 0.9428 1.3637 0.0552  -0.3548 -0.2299 272 GLU C OE2 
7924  N N   . ILE C 273 ? 0.8670 0.6034 0.7908 0.1538  -0.3413 -0.2400 273 ILE C N   
7925  C CA  . ILE C 273 ? 0.8097 0.5515 0.7066 0.1321  -0.2894 -0.2109 273 ILE C CA  
7926  C C   . ILE C 273 ? 0.7694 0.5414 0.6849 0.1110  -0.2647 -0.1924 273 ILE C C   
7927  O O   . ILE C 273 ? 0.7525 0.5490 0.7449 0.0875  -0.2771 -0.1947 273 ILE C O   
7928  C CB  . ILE C 273 ? 0.7961 0.5325 0.7594 0.0882  -0.2700 -0.2013 273 ILE C CB  
7929  C CG1 . ILE C 273 ? 0.8845 0.5890 0.8333 0.1069  -0.2950 -0.2206 273 ILE C CG1 
7930  C CG2 . ILE C 273 ? 0.7136 0.4470 0.6425 0.0748  -0.2216 -0.1748 273 ILE C CG2 
7931  C CD1 . ILE C 273 ? 0.8768 0.5731 0.8770 0.0713  -0.2700 -0.2075 273 ILE C CD1 
7932  N N   . GLY C 274 ? 0.7568 0.5317 0.6082 0.1224  -0.2244 -0.1672 274 GLY C N   
7933  C CA  . GLY C 274 ? 0.7304 0.5455 0.6085 0.1023  -0.1845 -0.1323 274 GLY C CA  
7934  C C   . GLY C 274 ? 0.6692 0.5030 0.6354 0.0494  -0.1639 -0.1188 274 GLY C C   
7935  O O   . GLY C 274 ? 0.7215 0.5394 0.7233 0.0280  -0.1656 -0.1244 274 GLY C O   
7936  N N   . GLY C 275 ? 0.5513 0.4159 0.5474 0.0342  -0.1413 -0.0987 275 GLY C N   
7937  C CA  . GLY C 275 ? 0.4693 0.3504 0.5349 -0.0035 -0.1193 -0.0845 275 GLY C CA  
7938  C C   . GLY C 275 ? 0.4379 0.3236 0.4839 -0.0143 -0.0781 -0.0589 275 GLY C C   
7939  O O   . GLY C 275 ? 0.4567 0.3498 0.5399 -0.0357 -0.0578 -0.0471 275 GLY C O   
7940  N N   . ALA C 276 ? 0.4004 0.2819 0.3916 0.0047  -0.0661 -0.0489 276 ALA C N   
7941  C CA  . ALA C 276 ? 0.3507 0.2381 0.3373 -0.0054 -0.0369 -0.0288 276 ALA C CA  
7942  C C   . ALA C 276 ? 0.3994 0.2702 0.3589 -0.0005 -0.0317 -0.0256 276 ALA C C   
7943  O O   . ALA C 276 ? 0.4087 0.2705 0.3294 0.0243  -0.0330 -0.0228 276 ALA C O   
7944  C CB  . ALA C 276 ? 0.3395 0.2405 0.3163 0.0074  -0.0229 -0.0124 276 ALA C CB  
7945  N N   . LEU C 277 ? 0.3848 0.2517 0.3616 -0.0189 -0.0220 -0.0224 277 LEU C N   
7946  C CA  . LEU C 277 ? 0.4045 0.2580 0.3604 -0.0152 -0.0153 -0.0171 277 LEU C CA  
7947  C C   . LEU C 277 ? 0.4312 0.2982 0.3773 -0.0095 -0.0014 -0.0004 277 LEU C C   
7948  O O   . LEU C 277 ? 0.4107 0.2921 0.3759 -0.0181 0.0036  0.0042  277 LEU C O   
7949  C CB  . LEU C 277 ? 0.4036 0.2496 0.3814 -0.0311 -0.0065 -0.0141 277 LEU C CB  
7950  C CG  . LEU C 277 ? 0.3198 0.1540 0.2768 -0.0265 0.0031  -0.0052 277 LEU C CG  
7951  C CD1 . LEU C 277 ? 0.3502 0.1587 0.2952 -0.0169 -0.0091 -0.0155 277 LEU C CD1 
7952  C CD2 . LEU C 277 ? 0.3614 0.1938 0.3317 -0.0341 0.0196  0.0060  277 LEU C CD2 
7953  N N   . ILE C 278 ? 0.4540 0.3147 0.3779 0.0063  0.0031  0.0082  278 ILE C N   
7954  C CA  . ILE C 278 ? 0.4211 0.2970 0.3584 0.0089  0.0145  0.0267  278 ILE C CA  
7955  C C   . ILE C 278 ? 0.4249 0.2934 0.3555 0.0050  0.0158  0.0282  278 ILE C C   
7956  O O   . ILE C 278 ? 0.4291 0.2786 0.3353 0.0136  0.0160  0.0249  278 ILE C O   
7957  C CB  . ILE C 278 ? 0.4283 0.3096 0.3571 0.0355  0.0268  0.0463  278 ILE C CB  
7958  C CG1 . ILE C 278 ? 0.3605 0.2477 0.2881 0.0471  0.0285  0.0490  278 ILE C CG1 
7959  C CG2 . ILE C 278 ? 0.4359 0.3381 0.4092 0.0338  0.0378  0.0693  278 ILE C CG2 
7960  C CD1 . ILE C 278 ? 0.3979 0.2850 0.2989 0.0869  0.0465  0.0723  278 ILE C CD1 
7961  N N   . THR C 279 ? 0.4388 0.3190 0.3884 -0.0045 0.0132  0.0303  279 THR C N   
7962  C CA  . THR C 279 ? 0.4610 0.3355 0.3976 -0.0027 0.0128  0.0321  279 THR C CA  
7963  C C   . THR C 279 ? 0.4669 0.3595 0.4291 -0.0015 0.0011  0.0353  279 THR C C   
7964  O O   . THR C 279 ? 0.4440 0.3482 0.4382 -0.0077 -0.0086 0.0309  279 THR C O   
7965  C CB  . THR C 279 ? 0.4633 0.3234 0.3829 -0.0087 0.0163  0.0243  279 THR C CB  
7966  O OG1 . THR C 279 ? 0.4929 0.3465 0.3934 0.0006  0.0199  0.0314  279 THR C OG1 
7967  C CG2 . THR C 279 ? 0.4216 0.2898 0.3483 -0.0139 0.0118  0.0161  279 THR C CG2 
7968  N N   . THR C 280 ? 0.4622 0.3557 0.4163 0.0076  -0.0019 0.0413  280 THR C N   
7969  C CA  . THR C 280 ? 0.4206 0.3310 0.4041 0.0114  -0.0240 0.0388  280 THR C CA  
7970  C C   . THR C 280 ? 0.4577 0.3577 0.3986 0.0230  -0.0361 0.0269  280 THR C C   
7971  O O   . THR C 280 ? 0.4985 0.4088 0.4526 0.0332  -0.0631 0.0192  280 THR C O   
7972  C CB  . THR C 280 ? 0.3820 0.3101 0.4019 0.0200  -0.0229 0.0586  280 THR C CB  
7973  O OG1 . THR C 280 ? 0.4207 0.3339 0.3966 0.0316  -0.0059 0.0679  280 THR C OG1 
7974  C CG2 . THR C 280 ? 0.3528 0.2954 0.4210 0.0189  -0.0075 0.0782  280 THR C CG2 
7975  N N   . THR C 281 ? 0.4404 0.3202 0.3348 0.0260  -0.0171 0.0274  281 THR C N   
7976  C CA  . THR C 281 ? 0.4960 0.3645 0.3426 0.0474  -0.0165 0.0279  281 THR C CA  
7977  C C   . THR C 281 ? 0.5384 0.3986 0.3529 0.0594  -0.0215 0.0140  281 THR C C   
7978  O O   . THR C 281 ? 0.5934 0.4406 0.3559 0.0859  -0.0111 0.0200  281 THR C O   
7979  C CB  . THR C 281 ? 0.4975 0.3475 0.3217 0.0515  0.0139  0.0471  281 THR C CB  
7980  O OG1 . THR C 281 ? 0.4822 0.3212 0.3234 0.0336  0.0318  0.0484  281 THR C OG1 
7981  C CG2 . THR C 281 ? 0.5053 0.3592 0.3442 0.0522  0.0138  0.0575  281 THR C CG2 
7982  N N   . HIS C 282 ? 0.5016 0.3672 0.3430 0.0460  -0.0339 -0.0013 282 HIS C N   
7983  C CA  . HIS C 282 ? 0.5431 0.3991 0.3528 0.0643  -0.0496 -0.0213 282 HIS C CA  
7984  C C   . HIS C 282 ? 0.5111 0.3759 0.3736 0.0496  -0.0819 -0.0425 282 HIS C C   
7985  O O   . HIS C 282 ? 0.5085 0.3871 0.4286 0.0241  -0.0753 -0.0329 282 HIS C O   
7986  C CB  . HIS C 282 ? 0.6318 0.4757 0.4142 0.0689  -0.0160 -0.0116 282 HIS C CB  
7987  C CG  . HIS C 282 ? 0.6812 0.5330 0.5126 0.0378  0.0009  -0.0042 282 HIS C CG  
7988  N ND1 . HIS C 282 ? 0.7025 0.5626 0.5714 0.0211  -0.0140 -0.0174 282 HIS C ND1 
7989  C CD2 . HIS C 282 ? 0.6812 0.5316 0.5313 0.0243  0.0278  0.0135  282 HIS C CD2 
7990  C CE1 . HIS C 282 ? 0.6755 0.5409 0.5727 0.0025  0.0032  -0.0077 282 HIS C CE1 
7991  N NE2 . HIS C 282 ? 0.6674 0.5265 0.5561 0.0031  0.0243  0.0076  282 HIS C NE2 
7992  N N   . PRO C 283 ? 0.5360 0.3901 0.3805 0.0703  -0.1185 -0.0710 283 PRO C N   
7993  C CA  . PRO C 283 ? 0.4982 0.3571 0.4133 0.0548  -0.1542 -0.0919 283 PRO C CA  
7994  C C   . PRO C 283 ? 0.4910 0.3459 0.4311 0.0373  -0.1379 -0.0921 283 PRO C C   
7995  O O   . PRO C 283 ? 0.4785 0.3485 0.4916 0.0120  -0.1331 -0.0799 283 PRO C O   
7996  C CB  . PRO C 283 ? 0.5564 0.3951 0.4327 0.0887  -0.2041 -0.1302 283 PRO C CB  
7997  C CG  . PRO C 283 ? 0.6227 0.4427 0.3885 0.1270  -0.1805 -0.1256 283 PRO C CG  
7998  C CD  . PRO C 283 ? 0.5927 0.4278 0.3547 0.1140  -0.1335 -0.0857 283 PRO C CD  
7999  N N   . TYR C 284 ? 0.5137 0.3503 0.3941 0.0543  -0.1231 -0.0993 284 TYR C N   
8000  C CA  . TYR C 284 ? 0.5154 0.3479 0.4217 0.0418  -0.1138 -0.1028 284 TYR C CA  
8001  C C   . TYR C 284 ? 0.5196 0.3670 0.4355 0.0223  -0.0696 -0.0730 284 TYR C C   
8002  O O   . TYR C 284 ? 0.5480 0.4010 0.4406 0.0227  -0.0463 -0.0540 284 TYR C O   
8003  C CB  . TYR C 284 ? 0.5719 0.3758 0.4123 0.0758  -0.1233 -0.1279 284 TYR C CB  
8004  C CG  . TYR C 284 ? 0.6259 0.4082 0.4427 0.1042  -0.1780 -0.1663 284 TYR C CG  
8005  C CD1 . TYR C 284 ? 0.6221 0.4057 0.5237 0.0862  -0.2243 -0.1882 284 TYR C CD1 
8006  C CD2 . TYR C 284 ? 0.7015 0.4634 0.4180 0.1527  -0.1841 -0.1780 284 TYR C CD2 
8007  C CE1 . TYR C 284 ? 0.6712 0.4508 0.5769 0.1100  -0.2691 -0.2111 284 TYR C CE1 
8008  C CE2 . TYR C 284 ? 0.7738 0.5289 0.4841 0.1798  -0.2318 -0.2031 284 TYR C CE2 
8009  C CZ  . TYR C 284 ? 0.7559 0.5188 0.5625 0.1573  -0.2766 -0.2223 284 TYR C CZ  
8010  O OH  . TYR C 284 ? 0.8512 0.6043 0.6610 0.1863  -0.3254 -0.2486 284 TYR C OH  
8011  N N   . THR C 285 ? 0.5012 0.3534 0.4568 0.0066  -0.0622 -0.0702 285 THR C N   
8012  C CA  . THR C 285 ? 0.4542 0.3194 0.4187 -0.0070 -0.0308 -0.0489 285 THR C CA  
8013  C C   . THR C 285 ? 0.4628 0.3215 0.3883 0.0066  -0.0073 -0.0448 285 THR C C   
8014  O O   . THR C 285 ? 0.5115 0.3571 0.4149 0.0237  -0.0089 -0.0570 285 THR C O   
8015  C CB  . THR C 285 ? 0.3995 0.2733 0.4154 -0.0210 -0.0306 -0.0447 285 THR C CB  
8016  O OG1 . THR C 285 ? 0.3927 0.2763 0.4557 -0.0300 -0.0406 -0.0360 285 THR C OG1 
8017  C CG2 . THR C 285 ? 0.3322 0.2180 0.3502 -0.0279 -0.0080 -0.0293 285 THR C CG2 
8018  N N   . VAL C 286 ? 0.4491 0.3160 0.3749 0.0007  0.0153  -0.0259 286 VAL C N   
8019  C CA  . VAL C 286 ? 0.4884 0.3529 0.3984 0.0139  0.0434  -0.0122 286 VAL C CA  
8020  C C   . VAL C 286 ? 0.4844 0.3644 0.4432 -0.0028 0.0557  -0.0025 286 VAL C C   
8021  O O   . VAL C 286 ? 0.4613 0.3509 0.4524 -0.0218 0.0471  -0.0011 286 VAL C O   
8022  C CB  . VAL C 286 ? 0.4447 0.3049 0.3376 0.0211  0.0600  0.0053  286 VAL C CB  
8023  C CG1 . VAL C 286 ? 0.4633 0.3235 0.3619 0.0355  0.0981  0.0309  286 VAL C CG1 
8024  C CG2 . VAL C 286 ? 0.4850 0.3318 0.3238 0.0440  0.0440  -0.0052 286 VAL C CG2 
8025  N N   . LEU C 287 ? 0.4996 0.3811 0.4602 0.0100  0.0732  0.0029  287 LEU C N   
8026  C CA  . LEU C 287 ? 0.4734 0.3733 0.4881 -0.0026 0.0825  0.0126  287 LEU C CA  
8027  C C   . LEU C 287 ? 0.4947 0.4023 0.5389 0.0063  0.1164  0.0397  287 LEU C C   
8028  O O   . LEU C 287 ? 0.5482 0.4450 0.5540 0.0351  0.1429  0.0533  287 LEU C O   
8029  C CB  . LEU C 287 ? 0.4432 0.3434 0.4563 0.0043  0.0776  0.0018  287 LEU C CB  
8030  C CG  . LEU C 287 ? 0.3998 0.2904 0.4016 -0.0016 0.0499  -0.0185 287 LEU C CG  
8031  C CD1 . LEU C 287 ? 0.4295 0.3126 0.4316 0.0093  0.0488  -0.0279 287 LEU C CD1 
8032  C CD2 . LEU C 287 ? 0.3324 0.2375 0.3672 -0.0216 0.0372  -0.0155 287 LEU C CD2 
8033  N N   . SER C 288 ? 0.4622 0.3877 0.5785 -0.0138 0.1154  0.0490  288 SER C N   
8034  C CA  . SER C 288 ? 0.4663 0.4038 0.6428 -0.0088 0.1485  0.0799  288 SER C CA  
8035  C C   . SER C 288 ? 0.4832 0.4287 0.6534 0.0149  0.1745  0.0919  288 SER C C   
8036  O O   . SER C 288 ? 0.4447 0.3912 0.5935 0.0155  0.1572  0.0723  288 SER C O   
8037  C CB  . SER C 288 ? 0.4455 0.4003 0.7169 -0.0361 0.1295  0.0797  288 SER C CB  
8038  O OG  . SER C 288 ? 0.4361 0.4063 0.7220 -0.0426 0.1052  0.0623  288 SER C OG  
8039  N N   . HIS C 289 ? 0.5283 0.4786 0.7219 0.0376  0.2204  0.1286  289 HIS C N   
8040  C CA  . HIS C 289 ? 0.5694 0.5201 0.7334 0.0744  0.2543  0.1443  289 HIS C CA  
8041  C C   . HIS C 289 ? 0.5788 0.5507 0.7904 0.0636  0.2425  0.1360  289 HIS C C   
8042  O O   . HIS C 289 ? 0.5823 0.5419 0.7355 0.0849  0.2410  0.1207  289 HIS C O   
8043  C CB  . HIS C 289 ? 0.5901 0.5468 0.7898 0.1027  0.3082  0.1939  289 HIS C CB  
8044  C CG  . HIS C 289 ? 0.6262 0.5742 0.7794 0.1492  0.3375  0.2104  289 HIS C CG  
8045  N ND1 . HIS C 289 ? 0.6844 0.5999 0.7098 0.1932  0.3414  0.1947  289 HIS C ND1 
8046  C CD2 . HIS C 289 ? 0.6382 0.6002 0.8514 0.1611  0.3577  0.2388  289 HIS C CD2 
8047  C CE1 . HIS C 289 ? 0.7480 0.6558 0.7514 0.2294  0.3629  0.2133  289 HIS C CE1 
8048  N NE2 . HIS C 289 ? 0.7223 0.6592 0.8391 0.2107  0.3784  0.2440  289 HIS C NE2 
8049  N N   . SER C 290 ? 0.5766 0.5775 0.8946 0.0324  0.2288  0.1426  290 SER C N   
8050  C CA  . SER C 290 ? 0.5746 0.5996 0.9427 0.0253  0.2155  0.1370  290 SER C CA  
8051  C C   . SER C 290 ? 0.5299 0.5395 0.8282 0.0186  0.1752  0.0967  290 SER C C   
8052  O O   . SER C 290 ? 0.5375 0.5496 0.8223 0.0310  0.1765  0.0914  290 SER C O   
8053  C CB  . SER C 290 ? 0.5669 0.6221 1.0584 -0.0036 0.1921  0.1426  290 SER C CB  
8054  O OG  . SER C 290 ? 0.5609 0.6078 1.0536 -0.0315 0.1476  0.1140  290 SER C OG  
8055  N N   . ILE C 291 ? 0.4599 0.4534 0.7209 0.0013  0.1436  0.0730  291 ILE C N   
8056  C CA  . ILE C 291 ? 0.4402 0.4201 0.6488 -0.0026 0.1137  0.0448  291 ILE C CA  
8057  C C   . ILE C 291 ? 0.4475 0.3988 0.5797 0.0207  0.1239  0.0349  291 ILE C C   
8058  O O   . ILE C 291 ? 0.4286 0.3712 0.5428 0.0262  0.1134  0.0210  291 ILE C O   
8059  C CB  . ILE C 291 ? 0.4304 0.4021 0.6243 -0.0215 0.0834  0.0286  291 ILE C CB  
8060  C CG1 . ILE C 291 ? 0.4098 0.4016 0.6711 -0.0381 0.0617  0.0280  291 ILE C CG1 
8061  C CG2 . ILE C 291 ? 0.4259 0.3851 0.5761 -0.0208 0.0632  0.0104  291 ILE C CG2 
8062  C CD1 . ILE C 291 ? 0.4324 0.4113 0.6716 -0.0483 0.0338  0.0117  291 ILE C CD1 
8063  N N   . PHE C 292 ? 0.4707 0.4045 0.5592 0.0372  0.1411  0.0407  292 PHE C N   
8064  C CA  . PHE C 292 ? 0.4847 0.3867 0.4944 0.0662  0.1412  0.0244  292 PHE C CA  
8065  C C   . PHE C 292 ? 0.5458 0.4421 0.5438 0.0943  0.1599  0.0265  292 PHE C C   
8066  O O   . PHE C 292 ? 0.6004 0.4717 0.5611 0.1054  0.1406  0.0004  292 PHE C O   
8067  C CB  . PHE C 292 ? 0.5029 0.3895 0.4620 0.0903  0.1602  0.0352  292 PHE C CB  
8068  C CG  . PHE C 292 ? 0.5782 0.4287 0.4454 0.1318  0.1548  0.0143  292 PHE C CG  
8069  C CD1 . PHE C 292 ? 0.5814 0.4089 0.4106 0.1272  0.1122  -0.0208 292 PHE C CD1 
8070  C CD2 . PHE C 292 ? 0.6657 0.5037 0.4874 0.1800  0.1898  0.0284  292 PHE C CD2 
8071  C CE1 . PHE C 292 ? 0.6478 0.4376 0.3967 0.1683  0.0944  -0.0492 292 PHE C CE1 
8072  C CE2 . PHE C 292 ? 0.7519 0.5488 0.4747 0.2274  0.1767  0.0010  292 PHE C CE2 
8073  C CZ  . PHE C 292 ? 0.7218 0.4935 0.4101 0.2199  0.1237  -0.0416 292 PHE C CZ  
8074  N N   . GLU C 293 ? 0.5562 0.4756 0.5974 0.1059  0.1972  0.0588  293 GLU C N   
8075  C CA  . GLU C 293 ? 0.5950 0.5098 0.6224 0.1401  0.2236  0.0672  293 GLU C CA  
8076  C C   . GLU C 293 ? 0.5628 0.4792 0.6124 0.1259  0.1985  0.0470  293 GLU C C   
8077  O O   . GLU C 293 ? 0.6003 0.4869 0.6003 0.1519  0.1954  0.0281  293 GLU C O   
8078  C CB  . GLU C 293 ? 0.6540 0.6051 0.7575 0.1482  0.2699  0.1140  293 GLU C CB  
8079  C CG  . GLU C 293 ? 0.7781 0.7253 0.8621 0.1792  0.3145  0.1483  293 GLU C CG  
8080  C CD  . GLU C 293 ? 0.9436 0.8532 0.9216 0.2346  0.3317  0.1506  293 GLU C CD  
8081  O OE1 . GLU C 293 ? 0.9969 0.9124 0.9931 0.2559  0.3591  0.1831  293 GLU C OE1 
8082  O OE2 . GLU C 293 ? 1.0192 0.8911 0.8966 0.2562  0.3104  0.1188  293 GLU C OE2 
8083  N N   . VAL C 294 ? 0.4741 0.4207 0.5939 0.0885  0.1780  0.0492  294 VAL C N   
8084  C CA  . VAL C 294 ? 0.4045 0.3576 0.5500 0.0787  0.1588  0.0386  294 VAL C CA  
8085  C C   . VAL C 294 ? 0.4136 0.3335 0.5154 0.0734  0.1291  0.0088  294 VAL C C   
8086  O O   . VAL C 294 ? 0.4929 0.3926 0.5827 0.0864  0.1256  -0.0028 294 VAL C O   
8087  C CB  . VAL C 294 ? 0.3544 0.3467 0.5745 0.0498  0.1409  0.0478  294 VAL C CB  
8088  C CG1 . VAL C 294 ? 0.3626 0.3605 0.5965 0.0470  0.1221  0.0398  294 VAL C CG1 
8089  C CG2 . VAL C 294 ? 0.3245 0.3517 0.6171 0.0531  0.1653  0.0768  294 VAL C CG2 
8090  N N   . PHE C 295 ? 0.4207 0.3335 0.5073 0.0555  0.1091  -0.0015 295 PHE C N   
8091  C CA  . PHE C 295 ? 0.4265 0.3144 0.4967 0.0474  0.0821  -0.0231 295 PHE C CA  
8092  C C   . PHE C 295 ? 0.5021 0.3467 0.5235 0.0727  0.0749  -0.0479 295 PHE C C   
8093  O O   . PHE C 295 ? 0.5631 0.3865 0.5983 0.0728  0.0588  -0.0627 295 PHE C O   
8094  C CB  . PHE C 295 ? 0.4164 0.3085 0.4830 0.0272  0.0661  -0.0251 295 PHE C CB  
8095  C CG  . PHE C 295 ? 0.4514 0.3209 0.5146 0.0203  0.0414  -0.0422 295 PHE C CG  
8096  C CD1 . PHE C 295 ? 0.4491 0.3251 0.5528 0.0085  0.0336  -0.0352 295 PHE C CD1 
8097  C CD2 . PHE C 295 ? 0.4909 0.3332 0.5170 0.0302  0.0264  -0.0626 295 PHE C CD2 
8098  C CE1 . PHE C 295 ? 0.4477 0.3065 0.5726 0.0018  0.0162  -0.0428 295 PHE C CE1 
8099  C CE2 . PHE C 295 ? 0.5072 0.3318 0.5540 0.0219  -0.0011 -0.0782 295 PHE C CE2 
8100  C CZ  . PHE C 295 ? 0.4790 0.3131 0.5845 0.0053  -0.0038 -0.0657 295 PHE C CZ  
8101  N N   . THR C 296 ? 0.5432 0.3710 0.5080 0.0988  0.0851  -0.0530 296 THR C N   
8102  C CA  . THR C 296 ? 0.6186 0.3985 0.5228 0.1309  0.0667  -0.0857 296 THR C CA  
8103  C C   . THR C 296 ? 0.6727 0.4325 0.5701 0.1563  0.0761  -0.0930 296 THR C C   
8104  O O   . THR C 296 ? 0.7395 0.4553 0.6138 0.1731  0.0481  -0.1272 296 THR C O   
8105  C CB  . THR C 296 ? 0.7464 0.5100 0.5722 0.1672  0.0776  -0.0880 296 THR C CB  
8106  O OG1 . THR C 296 ? 0.8225 0.6073 0.6421 0.1897  0.1271  -0.0527 296 THR C OG1 
8107  C CG2 . THR C 296 ? 0.7346 0.5126 0.5650 0.1443  0.0653  -0.0836 296 THR C CG2 
8108  N N   . GLN C 297 ? 0.6454 0.4358 0.5679 0.1615  0.1137  -0.0617 297 GLN C N   
8109  C CA  . GLN C 297 ? 0.6572 0.4351 0.5796 0.1864  0.1289  -0.0617 297 GLN C CA  
8110  C C   . GLN C 297 ? 0.6275 0.4066 0.6116 0.1583  0.1078  -0.0679 297 GLN C C   
8111  O O   . GLN C 297 ? 0.6729 0.4141 0.6484 0.1754  0.0965  -0.0892 297 GLN C O   
8112  C CB  . GLN C 297 ? 0.7140 0.5324 0.6622 0.1997  0.1767  -0.0204 297 GLN C CB  
8113  C CG  . GLN C 297 ? 0.8332 0.6442 0.7803 0.2333  0.2021  -0.0127 297 GLN C CG  
8114  C CD  . GLN C 297 ? 0.9829 0.7420 0.8367 0.2803  0.1969  -0.0390 297 GLN C CD  
8115  O OE1 . GLN C 297 ? 1.0786 0.8299 0.8686 0.3053  0.2053  -0.0344 297 GLN C OE1 
8116  N NE2 . GLN C 297 ? 0.9979 0.7278 0.8491 0.2882  0.1786  -0.0624 297 GLN C NE2 
8117  N N   . VAL C 298 ? 0.5527 0.3714 0.5962 0.1209  0.1037  -0.0483 298 VAL C N   
8118  C CA  . VAL C 298 ? 0.4980 0.3183 0.5934 0.1021  0.0898  -0.0463 298 VAL C CA  
8119  C C   . VAL C 298 ? 0.5294 0.3044 0.6250 0.0982  0.0588  -0.0754 298 VAL C C   
8120  O O   . VAL C 298 ? 0.5059 0.2574 0.6354 0.1001  0.0513  -0.0813 298 VAL C O   
8121  C CB  . VAL C 298 ? 0.4624 0.3257 0.5996 0.0733  0.0868  -0.0239 298 VAL C CB  
8122  C CG1 . VAL C 298 ? 0.4471 0.3044 0.6251 0.0627  0.0756  -0.0184 298 VAL C CG1 
8123  C CG2 . VAL C 298 ? 0.4403 0.3471 0.6029 0.0761  0.1059  0.0002  298 VAL C CG2 
8124  N N   . PHE C 299 ? 0.5938 0.3573 0.6619 0.0927  0.0394  -0.0922 299 PHE C N   
8125  C CA  . PHE C 299 ? 0.6266 0.3504 0.7086 0.0884  0.0027  -0.1223 299 PHE C CA  
8126  C C   . PHE C 299 ? 0.7296 0.3990 0.7758 0.1224  -0.0133 -0.1584 299 PHE C C   
8127  O O   . PHE C 299 ? 0.7805 0.4294 0.8668 0.1131  -0.0329 -0.1675 299 PHE C O   
8128  C CB  . PHE C 299 ? 0.6301 0.3557 0.6858 0.0808  -0.0170 -0.1338 299 PHE C CB  
8129  C CG  . PHE C 299 ? 0.6908 0.3909 0.7865 0.0686  -0.0580 -0.1576 299 PHE C CG  
8130  C CD1 . PHE C 299 ? 0.7989 0.4697 0.8569 0.0877  -0.0878 -0.1896 299 PHE C CD1 
8131  C CD2 . PHE C 299 ? 0.6216 0.3488 0.7917 0.0366  -0.0603 -0.1337 299 PHE C CD2 
8132  C CE1 . PHE C 299 ? 0.8120 0.4827 0.9220 0.0718  -0.1253 -0.2015 299 PHE C CE1 
8133  C CE2 . PHE C 299 ? 0.6326 0.3616 0.8508 0.0238  -0.0895 -0.1403 299 PHE C CE2 
8134  C CZ  . PHE C 299 ? 0.7253 0.4268 0.9218 0.0394  -0.1246 -0.1757 299 PHE C CZ  
8135  N N   . ALA C 300 ? 0.7576 0.4158 0.7217 0.1599  0.0018  -0.1666 300 ALA C N   
8136  C CA  . ALA C 300 ? 0.8023 0.4230 0.7175 0.1923  -0.0086 -0.1932 300 ALA C CA  
8137  C C   . ALA C 300 ? 0.8376 0.4444 0.7949 0.1941  0.0018  -0.1891 300 ALA C C   
8138  O O   . ALA C 300 ? 0.9099 0.4827 0.8585 0.2045  -0.0193 -0.2135 300 ALA C O   
8139  C CB  . ALA C 300 ? 0.8492 0.4750 0.6755 0.2348  0.0190  -0.1864 300 ALA C CB  
8140  N N   . ASN C 301 ? 0.7965 0.4307 0.7968 0.1880  0.0330  -0.1574 301 ASN C N   
8141  C CA  . ASN C 301 ? 0.7753 0.4040 0.8231 0.1904  0.0467  -0.1456 301 ASN C CA  
8142  C C   . ASN C 301 ? 0.7317 0.3529 0.8502 0.1560  0.0225  -0.1417 301 ASN C C   
8143  O O   . ASN C 301 ? 0.7433 0.3518 0.8892 0.1602  0.0278  -0.1342 301 ASN C O   
8144  C CB  . ASN C 301 ? 0.7191 0.4114 0.7952 0.1809  0.0879  -0.0976 301 ASN C CB  
8145  C CG  . ASN C 301 ? 0.7500 0.4612 0.7731 0.2129  0.1222  -0.0837 301 ASN C CG  
8146  O OD1 . ASN C 301 ? 0.8330 0.5109 0.7873 0.2489  0.1214  -0.1056 301 ASN C OD1 
8147  N ND2 . ASN C 301 ? 0.6807 0.4525 0.7432 0.1993  0.1489  -0.0448 301 ASN C ND2 
8148  N N   . ASN C 302 ? 0.7106 0.3467 0.8631 0.1242  0.0010  -0.1403 302 ASN C N   
8149  C CA  . ASN C 302 ? 0.7229 0.3636 0.9530 0.0955  -0.0146 -0.1285 302 ASN C CA  
8150  C C   . ASN C 302 ? 0.8254 0.4361 1.0630 0.0901  -0.0572 -0.1628 302 ASN C C   
8151  O O   . ASN C 302 ? 0.8402 0.4663 1.1553 0.0648  -0.0740 -0.1541 302 ASN C O   
8152  C CB  . ASN C 302 ? 0.6223 0.3110 0.9014 0.0680  -0.0023 -0.0941 302 ASN C CB  
8153  C CG  . ASN C 302 ? 0.5451 0.2682 0.8401 0.0718  0.0347  -0.0563 302 ASN C CG  
8154  O OD1 . ASN C 302 ? 0.5112 0.2479 0.8544 0.0679  0.0483  -0.0286 302 ASN C OD1 
8155  N ND2 . ASN C 302 ? 0.4784 0.2213 0.7332 0.0818  0.0519  -0.0527 302 ASN C ND2 
8156  N N   . MET C 303 ? 0.8342 0.4388 0.8137 0.1292  0.1004  -0.0587 303 MET C N   
8157  C CA  . MET C 303 ? 0.8600 0.4286 0.8137 0.0959  0.0961  -0.0718 303 MET C CA  
8158  C C   . MET C 303 ? 0.9657 0.4759 0.8699 0.1239  0.0964  -0.0946 303 MET C C   
8159  O O   . MET C 303 ? 0.9791 0.5037 0.8848 0.1684  0.1045  -0.1001 303 MET C O   
8160  C CB  . MET C 303 ? 0.7396 0.3855 0.7317 0.0719  0.0939  -0.0734 303 MET C CB  
8161  C CG  . MET C 303 ? 0.6348 0.3309 0.6696 0.0429  0.0920  -0.0552 303 MET C CG  
8162  S SD  . MET C 303 ? 0.8896 0.5325 0.9123 -0.0059 0.0875  -0.0546 303 MET C SD  
8163  C CE  . MET C 303 ? 0.8481 0.5099 0.8732 -0.0316 0.0692  -0.0820 303 MET C CE  
8164  N N   . PRO C 304 ? 1.0404 0.4870 0.9033 0.0989  0.0871  -0.1112 304 PRO C N   
8165  C CA  . PRO C 304 ? 1.0973 0.4848 0.9045 0.1278  0.0863  -0.1365 304 PRO C CA  
8166  C C   . PRO C 304 ? 1.0356 0.4920 0.8554 0.1496  0.0960  -0.1463 304 PRO C C   
8167  O O   . PRO C 304 ? 0.9598 0.4534 0.7887 0.1239  0.0888  -0.1499 304 PRO C O   
8168  C CB  . PRO C 304 ? 1.1681 0.4817 0.9372 0.0851  0.0693  -0.1540 304 PRO C CB  
8169  C CG  . PRO C 304 ? 1.1250 0.5018 0.9502 0.0346  0.0628  -0.1418 304 PRO C CG  
8170  C CD  . PRO C 304 ? 1.0634 0.4887 0.9310 0.0434  0.0766  -0.1113 304 PRO C CD  
8171  N N   . LYS C 305 ? 1.0606 0.5339 0.8805 0.1981  0.1135  -0.1504 305 LYS C N   
8172  C CA  . LYS C 305 ? 1.0185 0.5599 0.8553 0.2181  0.1346  -0.1550 305 LYS C CA  
8173  C C   . LYS C 305 ? 1.0967 0.5992 0.8697 0.2201  0.1339  -0.1767 305 LYS C C   
8174  O O   . LYS C 305 ? 1.0988 0.6472 0.8712 0.2248  0.1505  -0.1761 305 LYS C O   
8175  C CB  . LYS C 305 ? 0.9775 0.5692 0.8494 0.2586  0.1501  -0.1559 305 LYS C CB  
8176  C CG  . LYS C 305 ? 0.8683 0.5285 0.8126 0.2590  0.1502  -0.1381 305 LYS C CG  
8177  C CD  . LYS C 305 ? 0.8348 0.5657 0.8301 0.2896  0.1578  -0.1458 305 LYS C CD  
8178  C CE  . LYS C 305 ? 0.7478 0.5465 0.8137 0.2880  0.1488  -0.1345 305 LYS C CE  
8179  N NZ  . LYS C 305 ? 0.6681 0.5207 0.7695 0.2594  0.1606  -0.1205 305 LYS C NZ  
8180  N N   . GLN C 306 ? 1.1686 0.5801 0.8809 0.2181  0.1152  -0.1963 306 GLN C N   
8181  C CA  . GLN C 306 ? 1.2316 0.6060 0.8796 0.2199  0.1069  -0.2202 306 GLN C CA  
8182  C C   . GLN C 306 ? 1.2386 0.5884 0.8757 0.1718  0.0744  -0.2290 306 GLN C C   
8183  O O   . GLN C 306 ? 1.3439 0.6262 0.9211 0.1651  0.0523  -0.2572 306 GLN C O   
8184  C CB  . GLN C 306 ? 1.3012 0.6237 0.9062 0.2437  0.1030  -0.2361 306 GLN C CB  
8185  C CG  . GLN C 306 ? 1.2576 0.6213 0.9046 0.2784  0.1222  -0.2235 306 GLN C CG  
8186  C CD  . GLN C 306 ? 1.1930 0.6450 0.8730 0.3067  0.1551  -0.2197 306 GLN C CD  
8187  O OE1 . GLN C 306 ? 1.1571 0.6421 0.8309 0.2988  0.1689  -0.2174 306 GLN C OE1 
8188  N NE2 . GLN C 306 ? 1.1902 0.6779 0.9036 0.3385  0.1681  -0.2201 306 GLN C NE2 
8189  N N   . ALA C 307 ? 1.1427 0.5549 0.8473 0.1366  0.0687  -0.2061 307 ALA C N   
8190  C CA  . ALA C 307 ? 1.1144 0.5436 0.8362 0.0911  0.0399  -0.2120 307 ALA C CA  
8191  C C   . ALA C 307 ? 1.0650 0.5760 0.8087 0.0952  0.0436  -0.2001 307 ALA C C   
8192  O O   . ALA C 307 ? 1.0568 0.5957 0.8116 0.0698  0.0177  -0.2074 307 ALA C O   
8193  C CB  . ALA C 307 ? 1.0483 0.4819 0.8254 0.0503  0.0343  -0.1955 307 ALA C CB  
8194  N N   . GLN C 308 ? 1.0407 0.5878 0.7913 0.1280  0.0760  -0.1833 308 GLN C N   
8195  C CA  . GLN C 308 ? 1.0071 0.6174 0.7718 0.1332  0.0881  -0.1672 308 GLN C CA  
8196  C C   . GLN C 308 ? 1.0877 0.6714 0.7746 0.1496  0.0795  -0.1852 308 GLN C C   
8197  O O   . GLN C 308 ? 1.1946 0.7180 0.8157 0.1701  0.0781  -0.2086 308 GLN C O   
8198  C CB  . GLN C 308 ? 0.9844 0.6341 0.7806 0.1580  0.1289  -0.1484 308 GLN C CB  
8199  C CG  . GLN C 308 ? 0.9652 0.6377 0.8275 0.1526  0.1331  -0.1345 308 GLN C CG  
8200  C CD  . GLN C 308 ? 0.9709 0.6959 0.8776 0.1756  0.1667  -0.1229 308 GLN C CD  
8201  O OE1 . GLN C 308 ? 1.0043 0.7507 0.8981 0.1896  0.1944  -0.1222 308 GLN C OE1 
8202  N NE2 . GLN C 308 ? 0.9337 0.6798 0.8928 0.1787  0.1650  -0.1145 308 GLN C NE2 
8203  N N   . VAL C 309 ? 1.0538 0.6760 0.7395 0.1453  0.0719  -0.1747 309 VAL C N   
8204  C CA  . VAL C 309 ? 1.0931 0.6883 0.6928 0.1680  0.0628  -0.1871 309 VAL C CA  
8205  C C   . VAL C 309 ? 1.0556 0.6821 0.6484 0.1827  0.0953  -0.1585 309 VAL C C   
8206  O O   . VAL C 309 ? 0.9765 0.6529 0.6425 0.1675  0.1126  -0.1340 309 VAL C O   
8207  C CB  . VAL C 309 ? 1.1180 0.7154 0.7079 0.1499  0.0075  -0.2094 309 VAL C CB  
8208  C CG1 . VAL C 309 ? 1.1805 0.7400 0.7804 0.1257  -0.0222 -0.2397 309 VAL C CG1 
8209  C CG2 . VAL C 309 ? 1.0283 0.6969 0.6940 0.1266  -0.0047 -0.1895 309 VAL C CG2 
8210  N N   . LYS C 310 ? 1.1442 0.7329 0.6423 0.2120  0.1040  -0.1617 310 LYS C N   
8211  C CA  . LYS C 310 ? 1.1684 0.7687 0.6449 0.2231  0.1362  -0.1326 310 LYS C CA  
8212  C C   . LYS C 310 ? 1.0980 0.7460 0.6331 0.2017  0.1088  -0.1179 310 LYS C C   
8213  O O   . LYS C 310 ? 1.1057 0.7623 0.6393 0.1960  0.0576  -0.1351 310 LYS C O   
8214  C CB  . LYS C 310 ? 1.3179 0.8573 0.6641 0.2589  0.1390  -0.1370 310 LYS C CB  
8215  C CG  . LYS C 310 ? 1.3596 0.8941 0.6757 0.2677  0.1836  -0.1014 310 LYS C CG  
8216  C CD  . LYS C 310 ? 1.4861 0.9456 0.6545 0.3071  0.1926  -0.0986 310 LYS C CD  
8217  C CE  . LYS C 310 ? 1.5245 0.9693 0.6390 0.3227  0.1239  -0.1127 310 LYS C CE  
8218  N NZ  . LYS C 310 ? 1.6719 1.0494 0.6595 0.3593  0.1289  -0.0984 310 LYS C NZ  
8219  N N   . ALA C 311 ? 1.0418 0.7265 0.6374 0.1891  0.1418  -0.0901 311 ALA C N   
8220  C CA  . ALA C 311 ? 0.9973 0.7209 0.6393 0.1749  0.1228  -0.0742 311 ALA C CA  
8221  C C   . ALA C 311 ? 1.0686 0.7580 0.6213 0.2002  0.1052  -0.0700 311 ALA C C   
8222  O O   . ALA C 311 ? 1.1234 0.7563 0.5806 0.2259  0.1320  -0.0635 311 ALA C O   
8223  C CB  . ALA C 311 ? 0.9469 0.7028 0.6556 0.1599  0.1627  -0.0487 311 ALA C CB  
8224  N N   . VAL C 312 ? 1.0661 0.7885 0.6457 0.1969  0.0613  -0.0738 312 VAL C N   
8225  C CA  . VAL C 312 ? 1.1493 0.8442 0.6462 0.2287  0.0319  -0.0747 312 VAL C CA  
8226  C C   . VAL C 312 ? 1.0759 0.8052 0.6171 0.2261  0.0244  -0.0552 312 VAL C C   
8227  O O   . VAL C 312 ? 0.9512 0.7389 0.5941 0.1976  0.0236  -0.0521 312 VAL C O   
8228  C CB  . VAL C 312 ? 1.3363 1.0408 0.8113 0.2389  -0.0308 -0.1133 312 VAL C CB  
8229  C CG1 . VAL C 312 ? 1.4456 1.0982 0.8546 0.2480  -0.0258 -0.1351 312 VAL C CG1 
8230  C CG2 . VAL C 312 ? 1.2052 0.9879 0.7990 0.2033  -0.0638 -0.1302 312 VAL C CG2 
8231  N N   . GLY C 313 ? 1.1530 0.8352 0.6066 0.2595  0.0226  -0.0404 313 GLY C N   
8232  C CA  . GLY C 313 ? 1.0947 0.7953 0.5728 0.2657  0.0125  -0.0239 313 GLY C CA  
8233  C C   . GLY C 313 ? 1.0215 0.7151 0.5441 0.2398  0.0664  0.0055  313 GLY C C   
8234  O O   . GLY C 313 ? 1.0457 0.6925 0.5326 0.2328  0.1171  0.0211  313 GLY C O   
8235  N N   . PRO C 314 ? 0.9495 0.6933 0.5528 0.2258  0.0556  0.0106  314 PRO C N   
8236  C CA  . PRO C 314 ? 0.9180 0.6607 0.5713 0.2005  0.0970  0.0323  314 PRO C CA  
8237  C C   . PRO C 314 ? 0.8546 0.6493 0.6040 0.1644  0.1155  0.0250  314 PRO C C   
8238  O O   . PRO C 314 ? 0.8411 0.6405 0.6361 0.1437  0.1477  0.0374  314 PRO C O   
8239  C CB  . PRO C 314 ? 0.8715 0.6458 0.5602 0.2095  0.0677  0.0345  314 PRO C CB  
8240  C CG  . PRO C 314 ? 0.8243 0.6658 0.5522 0.2165  0.0171  0.0073  314 PRO C CG  
8241  C CD  . PRO C 314 ? 0.9128 0.7208 0.5650 0.2349  0.0030  -0.0072 314 PRO C CD  
8242  N N   . PHE C 315 ? 0.8312 0.6581 0.6056 0.1588  0.0936  0.0033  315 PHE C N   
8243  C CA  . PHE C 315 ? 0.7642 0.6344 0.6223 0.1314  0.1017  -0.0044 315 PHE C CA  
8244  C C   . PHE C 315 ? 0.8277 0.6729 0.6731 0.1272  0.1401  -0.0040 315 PHE C C   
8245  O O   . PHE C 315 ? 0.9284 0.7266 0.6963 0.1445  0.1542  -0.0050 315 PHE C O   
8246  C CB  . PHE C 315 ? 0.7290 0.6347 0.6179 0.1238  0.0632  -0.0274 315 PHE C CB  
8247  C CG  . PHE C 315 ? 0.6898 0.6372 0.6038 0.1280  0.0267  -0.0328 315 PHE C CG  
8248  C CD1 . PHE C 315 ? 0.6089 0.5946 0.5826 0.1188  0.0296  -0.0214 315 PHE C CD1 
8249  C CD2 . PHE C 315 ? 0.7395 0.6918 0.6175 0.1451  -0.0120 -0.0523 315 PHE C CD2 
8250  C CE1 . PHE C 315 ? 0.5853 0.6158 0.5845 0.1269  0.0001  -0.0278 315 PHE C CE1 
8251  C CE2 . PHE C 315 ? 0.7352 0.7404 0.6478 0.1524  -0.0455 -0.0609 315 PHE C CE2 
8252  C CZ  . PHE C 315 ? 0.6586 0.7041 0.6328 0.1436  -0.0367 -0.0478 315 PHE C CZ  
8253  N N   . GLY C 316 ? 0.7687 0.6466 0.6869 0.1089  0.1559  -0.0045 316 GLY C N   
8254  C CA  . GLY C 316 ? 0.7638 0.6335 0.6870 0.1086  0.1930  -0.0069 316 GLY C CA  
8255  C C   . GLY C 316 ? 0.7311 0.6053 0.6682 0.1103  0.1827  -0.0261 316 GLY C C   
8256  O O   . GLY C 316 ? 0.7405 0.6000 0.6611 0.1205  0.2091  -0.0333 316 GLY C O   
8257  N N   . LEU C 317 ? 0.6860 0.5766 0.6508 0.1005  0.1471  -0.0346 317 LEU C N   
8258  C CA  . LEU C 317 ? 0.6687 0.5493 0.6432 0.0985  0.1377  -0.0508 317 LEU C CA  
8259  C C   . LEU C 317 ? 0.7176 0.5875 0.6729 0.0891  0.0994  -0.0658 317 LEU C C   
8260  O O   . LEU C 317 ? 0.6848 0.5860 0.6807 0.0721  0.0785  -0.0629 317 LEU C O   
8261  C CB  . LEU C 317 ? 0.5902 0.5003 0.6336 0.0896  0.1415  -0.0450 317 LEU C CB  
8262  C CG  . LEU C 317 ? 0.5921 0.4799 0.6407 0.0919  0.1353  -0.0571 317 LEU C CG  
8263  C CD1 . LEU C 317 ? 0.6330 0.4929 0.6456 0.1145  0.1570  -0.0695 317 LEU C CD1 
8264  C CD2 . LEU C 317 ? 0.5527 0.4675 0.6575 0.0910  0.1374  -0.0481 317 LEU C CD2 
8265  N N   . CYS C 318 ? 0.7961 0.6249 0.6906 0.0999  0.0906  -0.0846 318 CYS C N   
8266  C CA  . CYS C 318 ? 0.8222 0.6439 0.7029 0.0882  0.0504  -0.1060 318 CYS C CA  
8267  C C   . CYS C 318 ? 0.8412 0.6168 0.7019 0.0832  0.0437  -0.1281 318 CYS C C   
8268  O O   . CYS C 318 ? 0.8747 0.6144 0.7028 0.1027  0.0682  -0.1305 318 CYS C O   
8269  C CB  . CYS C 318 ? 0.8892 0.6984 0.7033 0.1081  0.0317  -0.1142 318 CYS C CB  
8270  S SG  . CYS C 318 ? 0.8554 0.7054 0.6874 0.1151  0.0334  -0.0892 318 CYS C SG  
8271  N N   . TYR C 319 ? 0.8426 0.6195 0.7255 0.0564  0.0120  -0.1458 319 TYR C N   
8272  C CA  . TYR C 319 ? 0.8896 0.6105 0.7541 0.0441  0.0030  -0.1678 319 TYR C CA  
8273  C C   . TYR C 319 ? 0.9718 0.6762 0.8086 0.0307  -0.0383 -0.2022 319 TYR C C   
8274  O O   . TYR C 319 ? 0.9726 0.7252 0.8228 0.0277  -0.0645 -0.2086 319 TYR C O   
8275  C CB  . TYR C 319 ? 0.8555 0.5793 0.7796 0.0139  0.0097  -0.1567 319 TYR C CB  
8276  C CG  . TYR C 319 ? 0.8290 0.5577 0.7739 0.0311  0.0426  -0.1305 319 TYR C CG  
8277  C CD1 . TYR C 319 ? 0.7334 0.5227 0.7248 0.0328  0.0545  -0.1061 319 TYR C CD1 
8278  C CD2 . TYR C 319 ? 0.9113 0.5837 0.8287 0.0491  0.0577  -0.1339 319 TYR C CD2 
8279  C CE1 . TYR C 319 ? 0.7124 0.5106 0.7268 0.0484  0.0779  -0.0882 319 TYR C CE1 
8280  C CE2 . TYR C 319 ? 0.8994 0.5856 0.8414 0.0693  0.0808  -0.1154 319 TYR C CE2 
8281  C CZ  . TYR C 319 ? 0.8181 0.5696 0.8109 0.0672  0.0896  -0.0937 319 TYR C CZ  
8282  O OH  . TYR C 319 ? 0.8182 0.5871 0.8388 0.0876  0.1066  -0.0811 319 TYR C OH  
8283  N N   . ASP C 320 ? 1.0615 0.6963 0.8578 0.0260  -0.0471 -0.2273 320 ASP C N   
8284  C CA  . ASP C 320 ? 1.1341 0.7509 0.9210 0.0005  -0.0906 -0.2659 320 ASP C CA  
8285  C C   . ASP C 320 ? 1.0624 0.7165 0.9393 -0.0533 -0.0976 -0.2636 320 ASP C C   
8286  O O   . ASP C 320 ? 1.0223 0.6440 0.9216 -0.0718 -0.0726 -0.2473 320 ASP C O   
8287  C CB  . ASP C 320 ? 1.2713 0.7903 0.9830 0.0108  -0.0958 -0.2943 320 ASP C CB  
8288  C CG  . ASP C 320 ? 1.3537 0.8434 1.0716 -0.0298 -0.1393 -0.3364 320 ASP C CG  
8289  O OD1 . ASP C 320 ? 1.3741 0.9159 1.1109 -0.0409 -0.1790 -0.3594 320 ASP C OD1 
8290  O OD2 . ASP C 320 ? 1.4092 0.8212 1.1126 -0.0496 -0.1348 -0.3482 320 ASP C OD2 
8291  N N   . SER C 321 ? 1.0494 0.7687 0.9729 -0.0761 -0.1316 -0.2823 321 SER C N   
8292  C CA  . SER C 321 ? 1.0229 0.8007 1.0422 -0.1253 -0.1311 -0.2780 321 SER C CA  
8293  C C   . SER C 321 ? 1.1246 0.8394 1.1580 -0.1765 -0.1325 -0.2985 321 SER C C   
8294  O O   . SER C 321 ? 1.1221 0.8568 1.2214 -0.2204 -0.1142 -0.2864 321 SER C O   
8295  C CB  . SER C 321 ? 1.0065 0.8829 1.0768 -0.1286 -0.1685 -0.2970 321 SER C CB  
8296  O OG  . SER C 321 ? 0.9659 0.9140 1.1371 -0.1742 -0.1633 -0.2943 321 SER C OG  
8297  N N   . ARG C 322 ? 1.2260 0.8572 1.1903 -0.1707 -0.1520 -0.3296 322 ARG C N   
8298  C CA  . ARG C 322 ? 1.3260 0.8735 1.2865 -0.2176 -0.1551 -0.3525 322 ARG C CA  
8299  C C   . ARG C 322 ? 1.3707 0.8272 1.2979 -0.2146 -0.1108 -0.3204 322 ARG C C   
8300  O O   . ARG C 322 ? 1.4333 0.8430 1.3861 -0.2637 -0.0969 -0.3182 322 ARG C O   
8301  C CB  . ARG C 322 ? 1.4213 0.9012 1.3058 -0.2043 -0.1951 -0.4003 322 ARG C CB  
8302  C CG  . ARG C 322 ? 1.5076 0.9435 1.4172 -0.2674 -0.2250 -0.4455 322 ARG C CG  
8303  C CD  . ARG C 322 ? 1.5982 1.0012 1.4326 -0.2438 -0.2671 -0.4895 322 ARG C CD  
8304  N NE  . ARG C 322 ? 1.6958 1.0513 1.5322 -0.2967 -0.2759 -0.5190 322 ARG C NE  
8305  C CZ  . ARG C 322 ? 1.7798 1.1221 1.5717 -0.2903 -0.3134 -0.5598 322 ARG C CZ  
8306  N NH1 . ARG C 322 ? 1.8810 1.1776 1.6802 -0.3438 -0.3189 -0.5887 322 ARG C NH1 
8307  N NH2 . ARG C 322 ? 1.7766 1.1466 1.5110 -0.2301 -0.3434 -0.5710 322 ARG C NH2 
8308  N N   . LYS C 323 ? 1.3314 0.7625 1.2012 -0.1565 -0.0884 -0.2969 323 LYS C N   
8309  C CA  . LYS C 323 ? 1.3352 0.6875 1.1687 -0.1381 -0.0533 -0.2705 323 LYS C CA  
8310  C C   . LYS C 323 ? 1.2850 0.6864 1.1743 -0.1447 -0.0219 -0.2275 323 LYS C C   
8311  O O   . LYS C 323 ? 1.3322 0.6674 1.2080 -0.1532 0.0005  -0.2088 323 LYS C O   
8312  C CB  . LYS C 323 ? 1.3252 0.6465 1.0866 -0.0721 -0.0436 -0.2697 323 LYS C CB  
8313  C CG  . LYS C 323 ? 1.4148 0.6727 1.1035 -0.0595 -0.0716 -0.3124 323 LYS C CG  
8314  C CD  . LYS C 323 ? 1.4309 0.6570 1.0460 0.0063  -0.0539 -0.3122 323 LYS C CD  
8315  C CE  . LYS C 323 ? 1.5009 0.7034 1.0467 0.0250  -0.0834 -0.3512 323 LYS C CE  
8316  N NZ  . LYS C 323 ? 1.4664 0.7123 0.9751 0.0794  -0.0632 -0.3392 323 LYS C NZ  
8317  N N   . ILE C 324 ? 1.2249 0.7339 1.1672 -0.1372 -0.0218 -0.2124 324 ILE C N   
8318  C CA  . ILE C 324 ? 1.1641 0.7234 1.1581 -0.1441 0.0035  -0.1765 324 ILE C CA  
8319  C C   . ILE C 324 ? 1.2045 0.8064 1.2644 -0.2035 -0.0042 -0.1860 324 ILE C C   
8320  O O   . ILE C 324 ? 1.2398 0.8918 1.3282 -0.2211 -0.0342 -0.2155 324 ILE C O   
8321  C CB  . ILE C 324 ? 1.0590 0.7036 1.0734 -0.1055 0.0095  -0.1566 324 ILE C CB  
8322  C CG1 . ILE C 324 ? 1.0069 0.7419 1.0666 -0.1181 -0.0141 -0.1690 324 ILE C CG1 
8323  C CG2 . ILE C 324 ? 1.0734 0.6877 1.0301 -0.0550 0.0145  -0.1593 324 ILE C CG2 
8324  C CD1 . ILE C 324 ? 0.9180 0.7244 0.9967 -0.0868 -0.0057 -0.1464 324 ILE C CD1 
8325  N N   . SER C 325 ? 1.2093 0.7872 1.2903 -0.2341 0.0230  -0.1638 325 SER C N   
8326  C CA  . SER C 325 ? 1.1947 0.8168 1.3466 -0.2960 0.0266  -0.1712 325 SER C CA  
8327  C C   . SER C 325 ? 1.2242 0.8057 1.3765 -0.3170 0.0684  -0.1362 325 SER C C   
8328  O O   . SER C 325 ? 1.1685 0.8170 1.3546 -0.3061 0.0865  -0.1103 325 SER C O   
8329  C CB  . SER C 325 ? 1.2343 0.8093 1.3870 -0.3428 0.0033  -0.2123 325 SER C CB  
8330  O OG  . SER C 325 ? 1.1885 0.8286 1.3562 -0.3290 -0.0398 -0.2476 325 SER C OG  
8331  N N   . GLY C 326 ? 1.3093 0.7727 1.4141 -0.3442 0.0834  -0.1352 326 GLY C N   
8332  C CA  . GLY C 326 ? 1.3261 0.7361 1.3959 -0.3386 0.1174  -0.0932 326 GLY C CA  
8333  C C   . GLY C 326 ? 1.3320 0.6503 1.3147 -0.2784 0.1183  -0.0816 326 GLY C C   
8334  O O   . GLY C 326 ? 1.4344 0.6603 1.3579 -0.2679 0.1076  -0.0909 326 GLY C O   
8335  N N   . GLY C 327 ? 1.1997 0.5661 1.1827 -0.2292 0.1228  -0.0629 327 GLY C N   
8336  C CA  . GLY C 327 ? 1.0475 0.5379 1.0993 -0.2291 0.1270  -0.0504 327 GLY C CA  
8337  C C   . GLY C 327 ? 0.9223 0.4776 0.9772 -0.1697 0.1142  -0.0440 327 GLY C C   
8338  O O   . GLY C 327 ? 0.9587 0.4795 0.9732 -0.1295 0.1023  -0.0523 327 GLY C O   
8339  N N   . ALA C 328 ? 0.8048 0.4564 0.9115 -0.1668 0.1180  -0.0321 328 ALA C N   
8340  C CA  . ALA C 328 ? 0.7218 0.4307 0.8354 -0.1186 0.1116  -0.0221 328 ALA C CA  
8341  C C   . ALA C 328 ? 0.7606 0.4442 0.8493 -0.0950 0.1301  0.0065  328 ALA C C   
8342  O O   . ALA C 328 ? 0.8675 0.5114 0.9416 -0.1191 0.1514  0.0223  328 ALA C O   
8343  C CB  . ALA C 328 ? 0.6388 0.4544 0.8121 -0.1243 0.1007  -0.0288 328 ALA C CB  
8344  N N   . PRO C 329 ? 0.7053 0.4066 0.7851 -0.0483 0.1228  0.0118  329 PRO C N   
8345  C CA  . PRO C 329 ? 0.7277 0.3991 0.7766 -0.0206 0.1323  0.0335  329 PRO C CA  
8346  C C   . PRO C 329 ? 0.6702 0.4008 0.7473 -0.0271 0.1421  0.0490  329 PRO C C   
8347  O O   . PRO C 329 ? 0.6286 0.4351 0.7570 -0.0452 0.1388  0.0416  329 PRO C O   
8348  C CB  . PRO C 329 ? 0.7064 0.3936 0.7534 0.0284  0.1169  0.0258  329 PRO C CB  
8349  C CG  . PRO C 329 ? 0.6349 0.3856 0.7231 0.0220  0.1080  0.0086  329 PRO C CG  
8350  C CD  . PRO C 329 ? 0.6553 0.3927 0.7460 -0.0189 0.1076  -0.0029 329 PRO C CD  
8351  N N   . SER C 330 ? 0.7088 0.3989 0.7443 -0.0083 0.1532  0.0692  330 SER C N   
8352  C CA  . SER C 330 ? 0.6841 0.4237 0.7324 -0.0009 0.1608  0.0826  330 SER C CA  
8353  C C   . SER C 330 ? 0.5883 0.4024 0.6755 0.0286  0.1387  0.0718  330 SER C C   
8354  O O   . SER C 330 ? 0.5712 0.3743 0.6463 0.0644  0.1219  0.0661  330 SER C O   
8355  C CB  . SER C 330 ? 0.7543 0.4210 0.7302 0.0245  0.1726  0.1047  330 SER C CB  
8356  O OG  . SER C 330 ? 0.8734 0.4431 0.7951 0.0027  0.1938  0.1165  330 SER C OG  
8357  N N   . VAL C 331 ? 0.4769 0.4050 0.7554 0.0805  -0.0468 -0.1187 331 VAL C N   
8358  C CA  . VAL C 331 ? 0.4568 0.4294 0.7156 0.0776  -0.0306 -0.1166 331 VAL C CA  
8359  C C   . VAL C 331 ? 0.4410 0.4095 0.6718 0.0704  -0.0304 -0.0783 331 VAL C C   
8360  O O   . VAL C 331 ? 0.4922 0.4548 0.7050 0.0585  -0.0285 -0.0614 331 VAL C O   
8361  C CB  . VAL C 331 ? 0.4391 0.4389 0.6706 0.0611  -0.0143 -0.1342 331 VAL C CB  
8362  C CG1 . VAL C 331 ? 0.4129 0.4400 0.6140 0.0530  -0.0021 -0.1274 331 VAL C CG1 
8363  C CG2 . VAL C 331 ? 0.4726 0.4856 0.7248 0.0642  -0.0089 -0.1783 331 VAL C CG2 
8364  N N   . ASP C 332 ? 0.3639 0.3400 0.5953 0.0784  -0.0334 -0.0685 332 ASP C N   
8365  C CA  . ASP C 332 ? 0.3259 0.2958 0.5285 0.0725  -0.0331 -0.0375 332 ASP C CA  
8366  C C   . ASP C 332 ? 0.3110 0.3051 0.4932 0.0701  -0.0244 -0.0404 332 ASP C C   
8367  O O   . ASP C 332 ? 0.3100 0.3283 0.5125 0.0747  -0.0252 -0.0592 332 ASP C O   
8368  C CB  . ASP C 332 ? 0.4039 0.3435 0.6139 0.0771  -0.0523 -0.0147 332 ASP C CB  
8369  C CG  . ASP C 332 ? 0.4676 0.3676 0.6874 0.0707  -0.0643 -0.0064 332 ASP C CG  
8370  O OD1 . ASP C 332 ? 0.4960 0.3999 0.7125 0.0577  -0.0547 -0.0109 332 ASP C OD1 
8371  O OD2 . ASP C 332 ? 0.5187 0.3789 0.7465 0.0766  -0.0875 0.0061  332 ASP C OD2 
8372  N N   . LEU C 333 ? 0.3526 0.3415 0.4963 0.0623  -0.0168 -0.0247 333 LEU C N   
8373  C CA  . LEU C 333 ? 0.3077 0.3017 0.4223 0.0564  -0.0126 -0.0224 333 LEU C CA  
8374  C C   . LEU C 333 ? 0.3788 0.3648 0.4901 0.0592  -0.0222 -0.0040 333 LEU C C   
8375  O O   . LEU C 333 ? 0.3260 0.2974 0.4239 0.0586  -0.0221 0.0136  333 LEU C O   
8376  C CB  . LEU C 333 ? 0.3150 0.2935 0.3851 0.0511  -0.0047 -0.0175 333 LEU C CB  
8377  C CG  . LEU C 333 ? 0.3362 0.3137 0.3968 0.0468  -0.0015 -0.0288 333 LEU C CG  
8378  C CD1 . LEU C 333 ? 0.3977 0.3482 0.4122 0.0485  -0.0033 -0.0208 333 LEU C CD1 
8379  C CD2 . LEU C 333 ? 0.3244 0.3209 0.3864 0.0321  0.0042  -0.0489 333 LEU C CD2 
8380  N N   . ILE C 334 ? 0.3851 0.3879 0.5083 0.0593  -0.0305 -0.0097 334 ILE C N   
8381  C CA  . ILE C 334 ? 0.4115 0.4078 0.5245 0.0593  -0.0448 0.0082  334 ILE C CA  
8382  C C   . ILE C 334 ? 0.3995 0.3902 0.4626 0.0451  -0.0363 0.0125  334 ILE C C   
8383  O O   . ILE C 334 ? 0.3677 0.3700 0.4182 0.0336  -0.0298 -0.0013 334 ILE C O   
8384  C CB  . ILE C 334 ? 0.4206 0.4428 0.5783 0.0706  -0.0653 -0.0018 334 ILE C CB  
8385  C CG1 . ILE C 334 ? 0.4291 0.4492 0.6374 0.0898  -0.0743 -0.0154 334 ILE C CG1 
8386  C CG2 . ILE C 334 ? 0.4778 0.4850 0.6208 0.0715  -0.0890 0.0226  334 ILE C CG2 
8387  C CD1 . ILE C 334 ? 0.3712 0.3415 0.5713 0.0926  -0.0854 0.0082  334 ILE C CD1 
8388  N N   . LEU C 335 ? 0.4296 0.3995 0.4595 0.0424  -0.0351 0.0300  335 LEU C N   
8389  C CA  . LEU C 335 ? 0.4577 0.4133 0.4374 0.0333  -0.0257 0.0288  335 LEU C CA  
8390  C C   . LEU C 335 ? 0.5361 0.4949 0.4958 0.0228  -0.0399 0.0372  335 LEU C C   
8391  O O   . LEU C 335 ? 0.5999 0.5624 0.5733 0.0248  -0.0568 0.0530  335 LEU C O   
8392  C CB  . LEU C 335 ? 0.4606 0.4042 0.4197 0.0386  -0.0117 0.0336  335 LEU C CB  
8393  C CG  . LEU C 335 ? 0.4403 0.3886 0.4261 0.0491  -0.0040 0.0266  335 LEU C CG  
8394  C CD1 . LEU C 335 ? 0.4861 0.4409 0.4637 0.0551  0.0086  0.0274  335 LEU C CD1 
8395  C CD2 . LEU C 335 ? 0.4198 0.3555 0.3931 0.0500  -0.0021 0.0120  335 LEU C CD2 
8396  N N   . ASP C 336 ? 0.5824 0.5343 0.5064 0.0094  -0.0378 0.0277  336 ASP C N   
8397  C CA  . ASP C 336 ? 0.6499 0.6093 0.5527 -0.0047 -0.0540 0.0330  336 ASP C CA  
8398  C C   . ASP C 336 ? 0.6710 0.6156 0.5369 -0.0076 -0.0571 0.0503  336 ASP C C   
8399  O O   . ASP C 336 ? 0.6375 0.5635 0.4715 -0.0056 -0.0374 0.0475  336 ASP C O   
8400  C CB  . ASP C 336 ? 0.7374 0.6833 0.5981 -0.0255 -0.0497 0.0179  336 ASP C CB  
8401  C CG  . ASP C 336 ? 0.8285 0.7926 0.6731 -0.0445 -0.0702 0.0206  336 ASP C CG  
8402  O OD1 . ASP C 336 ? 0.7957 0.8021 0.6867 -0.0403 -0.0923 0.0264  336 ASP C OD1 
8403  O OD2 . ASP C 336 ? 0.9275 0.8624 0.7132 -0.0615 -0.0673 0.0149  336 ASP C OD2 
8404  N N   . LYS C 337 ? 0.7814 0.7382 0.6530 -0.0121 -0.0832 0.0668  337 LYS C N   
8405  C CA  . LYS C 337 ? 0.9128 0.8545 0.7330 -0.0256 -0.0905 0.0862  337 LYS C CA  
8406  C C   . LYS C 337 ? 0.9677 0.8962 0.7793 -0.0246 -0.0755 0.1004  337 LYS C C   
8407  O O   . LYS C 337 ? 1.0473 0.9680 0.8062 -0.0419 -0.0669 0.1099  337 LYS C O   
8408  C CB  . LYS C 337 ? 0.9774 0.9065 0.7333 -0.0432 -0.0772 0.0716  337 LYS C CB  
8409  C CG  . LYS C 337 ? 1.0352 0.9743 0.7662 -0.0619 -0.1050 0.0748  337 LYS C CG  
8410  C CD  . LYS C 337 ? 1.0819 1.0310 0.8283 -0.0604 -0.1419 0.1052  337 LYS C CD  
8411  C CE  . LYS C 337 ? 1.0895 1.0579 0.8204 -0.0753 -0.1782 0.1094  337 LYS C CE  
8412  N NZ  . LYS C 337 ? 1.0743 1.0498 0.8358 -0.0628 -0.2244 0.1375  337 LYS C NZ  
8413  N N   . ASN C 338 ? 0.9209 0.8520 0.7821 -0.0090 -0.0702 0.0990  338 ASN C N   
8414  C CA  . ASN C 338 ? 0.9183 0.8447 0.7728 -0.0138 -0.0525 0.1080  338 ASN C CA  
8415  C C   . ASN C 338 ? 0.9641 0.8718 0.8360 -0.0173 -0.0772 0.1348  338 ASN C C   
8416  O O   . ASN C 338 ? 0.9901 0.8915 0.9023 -0.0016 -0.1050 0.1371  338 ASN C O   
8417  C CB  . ASN C 338 ? 0.8514 0.7891 0.7397 0.0021  -0.0287 0.0870  338 ASN C CB  
8418  C CG  . ASN C 338 ? 0.8207 0.7723 0.6969 -0.0046 -0.0037 0.0858  338 ASN C CG  
8419  O OD1 . ASN C 338 ? 0.8531 0.8054 0.7081 -0.0258 -0.0036 0.1054  338 ASN C OD1 
8420  N ND2 . ASN C 338 ? 0.7784 0.7433 0.6657 0.0115  0.0163  0.0621  338 ASN C ND2 
8421  N N   . ASP C 339 ? 0.9999 0.8990 0.8401 -0.0392 -0.0672 0.1527  339 ASP C N   
8422  C CA  . ASP C 339 ? 1.0759 0.9419 0.9204 -0.0503 -0.0884 0.1808  339 ASP C CA  
8423  C C   . ASP C 339 ? 1.0251 0.8990 0.9266 -0.0349 -0.0755 0.1645  339 ASP C C   
8424  O O   . ASP C 339 ? 1.0291 0.8710 0.9496 -0.0376 -0.0927 0.1784  339 ASP C O   
8425  C CB  . ASP C 339 ? 1.2081 1.0663 0.9896 -0.0914 -0.0773 0.2052  339 ASP C CB  
8426  C CG  . ASP C 339 ? 1.3673 1.2075 1.0809 -0.1126 -0.0975 0.2274  339 ASP C CG  
8427  O OD1 . ASP C 339 ? 1.4098 1.2359 1.1329 -0.0935 -0.1314 0.2305  339 ASP C OD1 
8428  O OD2 . ASP C 339 ? 1.4581 1.3051 1.1083 -0.1509 -0.0792 0.2399  339 ASP C OD2 
8429  N N   . ALA C 340 ? 0.9746 0.8844 0.8973 -0.0196 -0.0482 0.1346  340 ALA C N   
8430  C CA  . ALA C 340 ? 0.9066 0.8319 0.8702 -0.0108 -0.0321 0.1189  340 ALA C CA  
8431  C C   . ALA C 340 ? 0.7733 0.7118 0.7730 0.0156  -0.0282 0.0917  340 ALA C C   
8432  O O   . ALA C 340 ? 0.7676 0.7086 0.7620 0.0253  -0.0324 0.0810  340 ALA C O   
8433  C CB  . ALA C 340 ? 0.9924 0.9533 0.9395 -0.0261 -0.0006 0.1125  340 ALA C CB  
8434  N N   . VAL C 341 ? 0.6332 0.5790 0.6654 0.0198  -0.0214 0.0827  341 VAL C N   
8435  C CA  . VAL C 341 ? 0.4994 0.4469 0.5683 0.0361  -0.0252 0.0640  341 VAL C CA  
8436  C C   . VAL C 341 ? 0.4051 0.3750 0.4837 0.0387  -0.0082 0.0502  341 VAL C C   
8437  O O   . VAL C 341 ? 0.4152 0.4015 0.4919 0.0270  0.0017  0.0565  341 VAL C O   
8438  C CB  . VAL C 341 ? 0.4719 0.3926 0.5698 0.0370  -0.0466 0.0701  341 VAL C CB  
8439  C CG1 . VAL C 341 ? 0.4548 0.3813 0.5885 0.0476  -0.0448 0.0473  341 VAL C CG1 
8440  C CG2 . VAL C 341 ? 0.4779 0.3831 0.5773 0.0463  -0.0706 0.0770  341 VAL C CG2 
8441  N N   . TRP C 342 ? 0.3539 0.3291 0.4399 0.0512  -0.0058 0.0318  342 TRP C N   
8442  C CA  . TRP C 342 ? 0.3253 0.3173 0.4224 0.0555  0.0008  0.0211  342 TRP C CA  
8443  C C   . TRP C 342 ? 0.3431 0.3309 0.4694 0.0527  -0.0072 0.0124  342 TRP C C   
8444  O O   . TRP C 342 ? 0.3486 0.3321 0.4763 0.0572  -0.0097 -0.0019 342 TRP C O   
8445  C CB  . TRP C 342 ? 0.3468 0.3349 0.4194 0.0681  0.0036  0.0095  342 TRP C CB  
8446  C CG  . TRP C 342 ? 0.3300 0.3369 0.4095 0.0786  0.0051  0.0025  342 TRP C CG  
8447  C CD1 . TRP C 342 ? 0.3444 0.3820 0.4561 0.0739  0.0057  0.0016  342 TRP C CD1 
8448  C CD2 . TRP C 342 ? 0.3723 0.3678 0.4274 0.0967  0.0013  -0.0057 342 TRP C CD2 
8449  N NE1 . TRP C 342 ? 0.3572 0.4172 0.4747 0.0905  0.0026  -0.0084 342 TRP C NE1 
8450  C CE2 . TRP C 342 ? 0.3676 0.3964 0.4495 0.1082  -0.0023 -0.0125 342 TRP C CE2 
8451  C CE3 . TRP C 342 ? 0.4126 0.3684 0.4240 0.1033  -0.0027 -0.0081 342 TRP C CE3 
8452  C CZ2 . TRP C 342 ? 0.4172 0.4405 0.4880 0.1341  -0.0135 -0.0220 342 TRP C CZ2 
8453  C CZ3 . TRP C 342 ? 0.4670 0.4027 0.4578 0.1254  -0.0133 -0.0155 342 TRP C CZ3 
8454  C CH2 . TRP C 342 ? 0.4505 0.4199 0.4732 0.1444  -0.0204 -0.0225 342 TRP C CH2 
8455  N N   . ARG C 343 ? 0.3341 0.3232 0.4797 0.0405  -0.0098 0.0190  343 ARG C N   
8456  C CA  . ARG C 343 ? 0.3385 0.3136 0.5088 0.0359  -0.0191 0.0086  343 ARG C CA  
8457  C C   . ARG C 343 ? 0.3387 0.3357 0.5145 0.0375  -0.0165 -0.0087 343 ARG C C   
8458  O O   . ARG C 343 ? 0.3743 0.3993 0.5467 0.0385  -0.0117 -0.0067 343 ARG C O   
8459  C CB  . ARG C 343 ? 0.3806 0.3369 0.5590 0.0151  -0.0259 0.0244  343 ARG C CB  
8460  C CG  . ARG C 343 ? 0.4228 0.3474 0.6222 0.0107  -0.0394 0.0121  343 ARG C CG  
8461  C CD  . ARG C 343 ? 0.4873 0.3620 0.6810 -0.0070 -0.0550 0.0334  343 ARG C CD  
8462  N NE  . ARG C 343 ? 0.5293 0.3712 0.7145 0.0088  -0.0697 0.0451  343 ARG C NE  
8463  C CZ  . ARG C 343 ? 0.6302 0.4266 0.7926 -0.0063 -0.0864 0.0743  343 ARG C CZ  
8464  N NH1 . ARG C 343 ? 0.6951 0.4744 0.8374 -0.0439 -0.0854 0.0946  343 ARG C NH1 
8465  N NH2 . ARG C 343 ? 0.6627 0.4326 0.8193 0.0120  -0.1060 0.0842  343 ARG C NH2 
8466  N N   . ILE C 344 ? 0.3200 0.3080 0.5023 0.0399  -0.0207 -0.0283 344 ILE C N   
8467  C CA  . ILE C 344 ? 0.3773 0.3819 0.5543 0.0365  -0.0219 -0.0430 344 ILE C CA  
8468  C C   . ILE C 344 ? 0.4064 0.4030 0.6045 0.0233  -0.0290 -0.0569 344 ILE C C   
8469  O O   . ILE C 344 ? 0.4366 0.4078 0.6473 0.0250  -0.0321 -0.0712 344 ILE C O   
8470  C CB  . ILE C 344 ? 0.4321 0.4357 0.5831 0.0406  -0.0185 -0.0576 344 ILE C CB  
8471  C CG1 . ILE C 344 ? 0.4606 0.4595 0.5863 0.0484  -0.0133 -0.0451 344 ILE C CG1 
8472  C CG2 . ILE C 344 ? 0.4280 0.4421 0.5587 0.0342  -0.0248 -0.0657 344 ILE C CG2 
8473  C CD1 . ILE C 344 ? 0.4799 0.4758 0.5745 0.0416  -0.0087 -0.0569 344 ILE C CD1 
8474  N N   . SER C 345 ? 0.3903 0.4097 0.5953 0.0114  -0.0335 -0.0556 345 SER C N   
8475  C CA  . SER C 345 ? 0.4115 0.4232 0.6324 -0.0081 -0.0419 -0.0689 345 SER C CA  
8476  C C   . SER C 345 ? 0.4396 0.4444 0.6467 -0.0079 -0.0446 -0.0976 345 SER C C   
8477  O O   . SER C 345 ? 0.4719 0.4937 0.6527 -0.0013 -0.0431 -0.1014 345 SER C O   
8478  C CB  . SER C 345 ? 0.3689 0.4246 0.6044 -0.0235 -0.0462 -0.0617 345 SER C CB  
8479  O OG  . SER C 345 ? 0.4261 0.4843 0.6683 -0.0435 -0.0571 -0.0795 345 SER C OG  
8480  N N   . SER C 346 ? 0.4566 0.4319 0.6748 -0.0176 -0.0494 -0.1186 346 SER C N   
8481  C CA  . SER C 346 ? 0.4709 0.4449 0.6740 -0.0197 -0.0479 -0.1531 346 SER C CA  
8482  C C   . SER C 346 ? 0.5269 0.5312 0.7098 -0.0374 -0.0568 -0.1568 346 SER C C   
8483  O O   . SER C 346 ? 0.5557 0.5683 0.7086 -0.0440 -0.0561 -0.1786 346 SER C O   
8484  C CB  . SER C 346 ? 0.4915 0.4212 0.7138 -0.0211 -0.0526 -0.1809 346 SER C CB  
8485  O OG  . SER C 346 ? 0.5210 0.4334 0.7488 -0.0462 -0.0658 -0.1814 346 SER C OG  
8486  N N   . GLU C 347 ? 0.5641 0.5930 0.7616 -0.0449 -0.0656 -0.1343 347 GLU C N   
8487  C CA  . GLU C 347 ? 0.6153 0.6828 0.8051 -0.0573 -0.0808 -0.1359 347 GLU C CA  
8488  C C   . GLU C 347 ? 0.5978 0.6849 0.7588 -0.0373 -0.0844 -0.1217 347 GLU C C   
8489  O O   . GLU C 347 ? 0.6185 0.7271 0.7580 -0.0399 -0.1026 -0.1225 347 GLU C O   
8490  C CB  . GLU C 347 ? 0.6486 0.7477 0.8772 -0.0731 -0.0873 -0.1216 347 GLU C CB  
8491  C CG  . GLU C 347 ? 0.7596 0.8873 0.9988 -0.1024 -0.1048 -0.1358 347 GLU C CG  
8492  C CD  . GLU C 347 ? 0.8338 1.0107 1.1166 -0.1233 -0.1065 -0.1218 347 GLU C CD  
8493  O OE1 . GLU C 347 ? 0.8305 0.9829 1.1260 -0.1350 -0.0935 -0.1083 347 GLU C OE1 
8494  O OE2 . GLU C 347 ? 0.8904 1.1341 1.1938 -0.1309 -0.1221 -0.1248 347 GLU C OE2 
8495  N N   . ASN C 348 ? 0.5613 0.6330 0.7169 -0.0183 -0.0709 -0.1083 348 ASN C N   
8496  C CA  . ASN C 348 ? 0.5740 0.6448 0.6935 -0.0022 -0.0749 -0.0952 348 ASN C CA  
8497  C C   . ASN C 348 ? 0.5933 0.6384 0.6638 -0.0101 -0.0671 -0.1076 348 ASN C C   
8498  O O   . ASN C 348 ? 0.6561 0.6950 0.6773 -0.0162 -0.0800 -0.1047 348 ASN C O   
8499  C CB  . ASN C 348 ? 0.5791 0.6497 0.7144 0.0179  -0.0652 -0.0751 348 ASN C CB  
8500  C CG  . ASN C 348 ? 0.6214 0.6811 0.7195 0.0365  -0.0740 -0.0619 348 ASN C CG  
8501  O OD1 . ASN C 348 ? 0.6604 0.6898 0.7094 0.0309  -0.0745 -0.0631 348 ASN C OD1 
8502  N ND2 . ASN C 348 ? 0.6062 0.6900 0.7257 0.0569  -0.0815 -0.0516 348 ASN C ND2 
8503  N N   . PHE C 349 ? 0.5387 0.5715 0.6213 -0.0120 -0.0478 -0.1224 349 PHE C N   
8504  C CA  . PHE C 349 ? 0.5468 0.5734 0.5907 -0.0213 -0.0346 -0.1366 349 PHE C CA  
8505  C C   . PHE C 349 ? 0.6070 0.6414 0.6294 -0.0432 -0.0294 -0.1707 349 PHE C C   
8506  O O   . PHE C 349 ? 0.6325 0.6733 0.6157 -0.0588 -0.0158 -0.1851 349 PHE C O   
8507  C CB  . PHE C 349 ? 0.5225 0.5472 0.5943 -0.0090 -0.0171 -0.1390 349 PHE C CB  
8508  C CG  . PHE C 349 ? 0.5335 0.5541 0.6588 0.0004  -0.0135 -0.1571 349 PHE C CG  
8509  C CD1 . PHE C 349 ? 0.5980 0.6231 0.7334 -0.0048 -0.0061 -0.1958 349 PHE C CD1 
8510  C CD2 . PHE C 349 ? 0.5280 0.5345 0.6879 0.0145  -0.0189 -0.1361 349 PHE C CD2 
8511  C CE1 . PHE C 349 ? 0.6481 0.6535 0.8311 0.0097  -0.0093 -0.2131 349 PHE C CE1 
8512  C CE2 . PHE C 349 ? 0.5810 0.5656 0.7794 0.0221  -0.0229 -0.1469 349 PHE C CE2 
8513  C CZ  . PHE C 349 ? 0.6319 0.6109 0.8437 0.0227  -0.0205 -0.1855 349 PHE C CZ  
8514  N N   . MET C 350 ? 0.7086 0.4382 0.6162 0.0652  -0.0678 -0.1433 350 MET C N   
8515  C CA  . MET C 350 ? 0.7594 0.4735 0.6350 0.0727  -0.0713 -0.1678 350 MET C CA  
8516  C C   . MET C 350 ? 0.7839 0.5138 0.6364 0.0722  -0.0930 -0.1821 350 MET C C   
8517  O O   . MET C 350 ? 0.7878 0.5297 0.6641 0.0598  -0.1091 -0.1885 350 MET C O   
8518  C CB  . MET C 350 ? 0.8065 0.4922 0.7007 0.0660  -0.0688 -0.1885 350 MET C CB  
8519  C CG  . MET C 350 ? 0.8304 0.4969 0.7419 0.0716  -0.0466 -0.1749 350 MET C CG  
8520  S SD  . MET C 350 ? 0.8058 0.4727 0.6879 0.0933  -0.0268 -0.1623 350 MET C SD  
8521  C CE  . MET C 350 ? 0.6823 0.3297 0.5191 0.1026  -0.0301 -0.1944 350 MET C CE  
8522  N N   . VAL C 351 ? 0.7921 0.5237 0.5984 0.0872  -0.0927 -0.1856 351 VAL C N   
8523  C CA  . VAL C 351 ? 0.7964 0.5447 0.5734 0.0922  -0.1128 -0.1950 351 VAL C CA  
8524  C C   . VAL C 351 ? 0.8584 0.5945 0.6007 0.0991  -0.1241 -0.2275 351 VAL C C   
8525  O O   . VAL C 351 ? 0.8755 0.5908 0.5930 0.1092  -0.1096 -0.2350 351 VAL C O   
8526  C CB  . VAL C 351 ? 0.6494 0.4101 0.3940 0.1066  -0.1038 -0.1706 351 VAL C CB  
8527  C CG1 . VAL C 351 ? 0.6714 0.4489 0.3842 0.1152  -0.1241 -0.1758 351 VAL C CG1 
8528  C CG2 . VAL C 351 ? 0.6203 0.3920 0.3987 0.0990  -0.0925 -0.1419 351 VAL C CG2 
8529  N N   . GLN C 352 ? 0.9078 0.6603 0.6469 0.0954  -0.1504 -0.2469 352 GLN C N   
8530  C CA  . GLN C 352 ? 0.9700 0.7269 0.6902 0.0960  -0.1604 -0.2715 352 GLN C CA  
8531  C C   . GLN C 352 ? 1.0156 0.7850 0.6761 0.1180  -0.1661 -0.2678 352 GLN C C   
8532  O O   . GLN C 352 ? 1.0690 0.8630 0.7201 0.1201  -0.1872 -0.2769 352 GLN C O   
8533  C CB  . GLN C 352 ? 1.0162 0.7932 0.7797 0.0762  -0.1811 -0.2890 352 GLN C CB  
8534  C CG  . GLN C 352 ? 1.1550 0.9353 0.9046 0.0735  -0.1919 -0.3178 352 GLN C CG  
8535  C CD  . GLN C 352 ? 1.2856 1.0310 1.0357 0.0685  -0.1722 -0.3311 352 GLN C CD  
8536  O OE1 . GLN C 352 ? 1.3065 1.0334 1.0996 0.0528  -0.1600 -0.3303 352 GLN C OE1 
8537  N NE2 . GLN C 352 ? 1.3751 1.1100 1.0762 0.0833  -0.1671 -0.3417 352 GLN C NE2 
8538  N N   . ALA C 353 ? 1.0182 0.7717 0.6412 0.1352  -0.1448 -0.2508 353 ALA C N   
8539  C CA  . ALA C 353 ? 1.0416 0.7994 0.6044 0.1580  -0.1403 -0.2420 353 ALA C CA  
8540  C C   . ALA C 353 ? 1.1134 0.8828 0.6484 0.1636  -0.1564 -0.2642 353 ALA C C   
8541  O O   . ALA C 353 ? 1.1572 0.9450 0.6590 0.1780  -0.1676 -0.2574 353 ALA C O   
8542  C CB  . ALA C 353 ? 1.0229 0.7568 0.5611 0.1704  -0.1091 -0.2295 353 ALA C CB  
8543  N N   . GLN C 354 ? 1.1321 0.8884 0.6783 0.1535  -0.1555 -0.2898 354 GLN C N   
8544  C CA  . GLN C 354 ? 1.1687 0.9329 0.6883 0.1570  -0.1699 -0.3148 354 GLN C CA  
8545  C C   . GLN C 354 ? 1.1541 0.9121 0.7191 0.1326  -0.1788 -0.3438 354 GLN C C   
8546  O O   . GLN C 354 ? 1.1349 0.8750 0.7411 0.1182  -0.1660 -0.3410 354 GLN C O   
8547  C CB  . GLN C 354 ? 1.2337 0.9792 0.6999 0.1763  -0.1496 -0.3141 354 GLN C CB  
8548  C CG  . GLN C 354 ? 1.2773 1.0345 0.6903 0.2013  -0.1469 -0.2918 354 GLN C CG  
8549  C CD  . GLN C 354 ? 1.3415 1.0777 0.7094 0.2194  -0.1191 -0.2845 354 GLN C CD  
8550  O OE1 . GLN C 354 ? 1.3764 1.0945 0.7437 0.2154  -0.1093 -0.3043 354 GLN C OE1 
8551  N NE2 . GLN C 354 ? 1.3502 1.0877 0.6822 0.2391  -0.1038 -0.2552 354 GLN C NE2 
8552  N N   . ASP C 355 ? 1.1860 0.9564 0.7432 0.1282  -0.1982 -0.3708 355 ASP C N   
8553  C CA  . ASP C 355 ? 1.2345 0.9936 0.8310 0.1044  -0.2026 -0.3999 355 ASP C CA  
8554  C C   . ASP C 355 ? 1.2588 0.9769 0.8553 0.1013  -0.1750 -0.4061 355 ASP C C   
8555  O O   . ASP C 355 ? 1.2980 1.0010 0.8482 0.1188  -0.1602 -0.4064 355 ASP C O   
8556  C CB  . ASP C 355 ? 1.3369 1.1133 0.9139 0.1034  -0.2260 -0.4297 355 ASP C CB  
8557  C CG  . ASP C 355 ? 1.4607 1.2308 0.9689 0.1273  -0.2210 -0.4338 355 ASP C CG  
8558  O OD1 . ASP C 355 ? 1.4765 1.2371 0.9518 0.1468  -0.2019 -0.4082 355 ASP C OD1 
8559  O OD2 . ASP C 355 ? 1.5456 1.3197 1.0327 0.1264  -0.2350 -0.4625 355 ASP C OD2 
8560  N N   . GLY C 356 ? 1.2347 0.9351 0.8843 0.0802  -0.1666 -0.4095 356 GLY C N   
8561  C CA  . GLY C 356 ? 1.2370 0.8973 0.8960 0.0771  -0.1389 -0.4116 356 GLY C CA  
8562  C C   . GLY C 356 ? 1.1853 0.8340 0.8242 0.0967  -0.1147 -0.3848 356 GLY C C   
8563  O O   . GLY C 356 ? 1.2065 0.8268 0.8377 0.1029  -0.0910 -0.3870 356 GLY C O   
8564  N N   . VAL C 357 ? 1.1066 0.7776 0.7378 0.1071  -0.1198 -0.3593 357 VAL C N   
8565  C CA  . VAL C 357 ? 1.0354 0.6976 0.6549 0.1230  -0.0972 -0.3319 357 VAL C CA  
8566  C C   . VAL C 357 ? 0.9371 0.6097 0.5950 0.1151  -0.1004 -0.3091 357 VAL C C   
8567  O O   . VAL C 357 ? 0.9032 0.6007 0.5638 0.1121  -0.1204 -0.3043 357 VAL C O   
8568  C CB  . VAL C 357 ? 1.0694 0.7426 0.6301 0.1467  -0.0940 -0.3208 357 VAL C CB  
8569  C CG1 . VAL C 357 ? 0.9633 0.6280 0.5191 0.1603  -0.0679 -0.2916 357 VAL C CG1 
8570  C CG2 . VAL C 357 ? 1.0651 0.7277 0.5857 0.1553  -0.0904 -0.3441 357 VAL C CG2 
8571  N N   . SER C 358 ? 0.8934 0.5479 0.5821 0.1124  -0.0808 -0.2951 358 SER C N   
8572  C CA  . SER C 358 ? 0.8859 0.5484 0.6115 0.1049  -0.0827 -0.2737 358 SER C CA  
8573  C C   . SER C 358 ? 0.9125 0.5708 0.6272 0.1209  -0.0621 -0.2466 358 SER C C   
8574  O O   . SER C 358 ? 0.9179 0.5590 0.6351 0.1287  -0.0402 -0.2423 358 SER C O   
8575  C CB  . SER C 358 ? 0.9322 0.5801 0.7118 0.0850  -0.0793 -0.2789 358 SER C CB  
8576  O OG  . SER C 358 ? 0.9405 0.5962 0.7565 0.0777  -0.0800 -0.2575 358 SER C OG  
8577  N N   . CYS C 359 ? 0.8630 0.5431 0.5728 0.1236  -0.0664 -0.2249 359 CYS C N   
8578  C CA  . CYS C 359 ? 0.7934 0.4821 0.4983 0.1340  -0.0439 -0.1953 359 CYS C CA  
8579  C C   . CYS C 359 ? 0.7256 0.4291 0.4773 0.1233  -0.0375 -0.1684 359 CYS C C   
8580  O O   . CYS C 359 ? 0.6766 0.3913 0.4556 0.1097  -0.0520 -0.1649 359 CYS C O   
8581  C CB  . CYS C 359 ? 0.7707 0.4740 0.4309 0.1465  -0.0456 -0.1860 359 CYS C CB  
8582  S SG  . CYS C 359 ? 0.9742 0.6613 0.5657 0.1668  -0.0460 -0.2116 359 CYS C SG  
8583  N N   . LEU C 360 ? 0.7159 0.4215 0.4770 0.1304  -0.0156 -0.1503 360 LEU C N   
8584  C CA  . LEU C 360 ? 0.6977 0.4213 0.4973 0.1227  -0.0101 -0.1259 360 LEU C CA  
8585  C C   . LEU C 360 ? 0.7409 0.4860 0.5322 0.1203  -0.0142 -0.1098 360 LEU C C   
8586  O O   . LEU C 360 ? 0.7696 0.5188 0.5337 0.1306  -0.0025 -0.1024 360 LEU C O   
8587  C CB  . LEU C 360 ? 0.7213 0.4461 0.5352 0.1322  0.0124  -0.1140 360 LEU C CB  
8588  C CG  . LEU C 360 ? 0.6875 0.4351 0.5396 0.1265  0.0176  -0.0910 360 LEU C CG  
8589  C CD1 . LEU C 360 ? 0.6567 0.4015 0.5406 0.1149  0.0058  -0.0894 360 LEU C CD1 
8590  C CD2 . LEU C 360 ? 0.6751 0.4277 0.5399 0.1389  0.0381  -0.0832 360 LEU C CD2 
8591  N N   . GLY C 361 ? 0.7211 0.4774 0.5360 0.1074  -0.0287 -0.1042 361 GLY C N   
8592  C CA  . GLY C 361 ? 0.7085 0.4809 0.5158 0.1048  -0.0357 -0.0923 361 GLY C CA  
8593  C C   . GLY C 361 ? 0.6826 0.4706 0.5074 0.1024  -0.0226 -0.0694 361 GLY C C   
8594  O O   . GLY C 361 ? 0.6568 0.4565 0.4973 0.0940  -0.0297 -0.0596 361 GLY C O   
8595  N N   . PHE C 362 ? 0.6917 0.4807 0.5149 0.1096  -0.0030 -0.0625 362 PHE C N   
8596  C CA  . PHE C 362 ? 0.6444 0.4498 0.4838 0.1068  0.0107  -0.0443 362 PHE C CA  
8597  C C   . PHE C 362 ? 0.6774 0.4787 0.4860 0.1181  0.0286  -0.0398 362 PHE C C   
8598  O O   . PHE C 362 ? 0.7435 0.5334 0.5300 0.1295  0.0370  -0.0487 362 PHE C O   
8599  C CB  . PHE C 362 ? 0.6108 0.4284 0.4872 0.1043  0.0194  -0.0389 362 PHE C CB  
8600  C CG  . PHE C 362 ? 0.5820 0.4022 0.4860 0.0958  0.0059  -0.0396 362 PHE C CG  
8601  C CD1 . PHE C 362 ? 0.5883 0.3912 0.4920 0.0972  -0.0015 -0.0518 362 PHE C CD1 
8602  C CD2 . PHE C 362 ? 0.5336 0.3718 0.4637 0.0865  0.0028  -0.0286 362 PHE C CD2 
8603  C CE1 . PHE C 362 ? 0.5434 0.3460 0.4728 0.0901  -0.0097 -0.0498 362 PHE C CE1 
8604  C CE2 . PHE C 362 ? 0.4951 0.3347 0.4463 0.0810  -0.0070 -0.0274 362 PHE C CE2 
8605  C CZ  . PHE C 362 ? 0.5103 0.3317 0.4614 0.0830  -0.0121 -0.0365 362 PHE C CZ  
8606  N N   . VAL C 363 ? 0.6438 0.4519 0.4506 0.1154  0.0367  -0.0254 363 VAL C N   
8607  C CA  . VAL C 363 ? 0.6100 0.4112 0.3862 0.1261  0.0568  -0.0176 363 VAL C CA  
8608  C C   . VAL C 363 ? 0.5840 0.3998 0.3914 0.1195  0.0793  -0.0032 363 VAL C C   
8609  O O   . VAL C 363 ? 0.5539 0.3852 0.3999 0.1060  0.0748  0.0011  363 VAL C O   
8610  C CB  . VAL C 363 ? 0.6331 0.4238 0.3718 0.1320  0.0489  -0.0131 363 VAL C CB  
8611  C CG1 . VAL C 363 ? 0.6395 0.4224 0.3536 0.1373  0.0240  -0.0313 363 VAL C CG1 
8612  C CG2 . VAL C 363 ? 0.6120 0.4109 0.3755 0.1198  0.0434  -0.0016 363 VAL C CG2 
8613  N N   . ASP C 364 ? 0.6126 0.4247 0.4045 0.1291  0.1040  0.0022  364 ASP C N   
8614  C CA  . ASP C 364 ? 0.6030 0.4305 0.4279 0.1226  0.1286  0.0138  364 ASP C CA  
8615  C C   . ASP C 364 ? 0.6400 0.4621 0.4632 0.1153  0.1375  0.0282  364 ASP C C   
8616  O O   . ASP C 364 ? 0.6693 0.4709 0.4489 0.1262  0.1455  0.0362  364 ASP C O   
8617  C CB  . ASP C 364 ? 0.6389 0.4632 0.4482 0.1364  0.1547  0.0148  364 ASP C CB  
8618  C CG  . ASP C 364 ? 0.6292 0.4767 0.4851 0.1286  0.1800  0.0234  364 ASP C CG  
8619  O OD1 . ASP C 364 ? 0.6087 0.4709 0.5021 0.1120  0.1794  0.0293  364 ASP C OD1 
8620  O OD2 . ASP C 364 ? 0.6449 0.4972 0.5018 0.1389  0.2004  0.0225  364 ASP C OD2 
8621  N N   . GLY C 365 ? 0.6267 0.4660 0.4955 0.0982  0.1358  0.0311  365 GLY C N   
8622  C CA  . GLY C 365 ? 0.6285 0.4610 0.5039 0.0887  0.1461  0.0431  365 GLY C CA  
8623  C C   . GLY C 365 ? 0.6649 0.4998 0.5587 0.0844  0.1803  0.0539  365 GLY C C   
8624  O O   . GLY C 365 ? 0.7080 0.5327 0.6090 0.0759  0.1936  0.0642  365 GLY C O   
8625  N N   . GLY C 366 ? 0.6793 0.5266 0.5832 0.0901  0.1964  0.0515  366 GLY C N   
8626  C CA  . GLY C 366 ? 0.6907 0.5441 0.6179 0.0857  0.2313  0.0610  366 GLY C CA  
8627  C C   . GLY C 366 ? 0.6903 0.5777 0.6873 0.0646  0.2332  0.0550  366 GLY C C   
8628  O O   . GLY C 366 ? 0.6203 0.5271 0.6428 0.0561  0.2068  0.0438  366 GLY C O   
8629  N N   . VAL C 367 ? 0.7963 0.6910 0.8237 0.0562  0.2654  0.0624  367 VAL C N   
8630  C CA  . VAL C 367 ? 0.8446 0.7779 0.9437 0.0361  0.2700  0.0540  367 VAL C CA  
8631  C C   . VAL C 367 ? 0.8900 0.8176 1.0142 0.0148  0.2695  0.0538  367 VAL C C   
8632  O O   . VAL C 367 ? 0.9198 0.8800 1.1015 -0.0041 0.2642  0.0419  367 VAL C O   
8633  C CB  . VAL C 367 ? 0.8862 0.8360 1.0166 0.0358  0.3072  0.0594  367 VAL C CB  
8634  C CG1 . VAL C 367 ? 0.8728 0.8764 1.0774 0.0222  0.3014  0.0451  367 VAL C CG1 
8635  C CG2 . VAL C 367 ? 0.8979 0.8332 0.9810 0.0611  0.3189  0.0653  367 VAL C CG2 
8636  N N   . HIS C 368 ? 0.8812 0.7677 0.9620 0.0188  0.2746  0.0661  368 HIS C N   
8637  C CA  . HIS C 368 ? 0.8525 0.7274 0.9525 0.0008  0.2744  0.0658  368 HIS C CA  
8638  C C   . HIS C 368 ? 0.8349 0.6929 0.8975 0.0078  0.2423  0.0637  368 HIS C C   
8639  O O   . HIS C 368 ? 0.8764 0.7038 0.9171 0.0075  0.2460  0.0728  368 HIS C O   
8640  C CB  . HIS C 368 ? 0.9135 0.7530 1.0016 -0.0005 0.3128  0.0846  368 HIS C CB  
8641  C CG  . HIS C 368 ? 0.9873 0.8391 1.1051 -0.0039 0.3495  0.0902  368 HIS C CG  
8642  N ND1 . HIS C 368 ? 0.9870 0.8788 1.1786 -0.0256 0.3577  0.0767  368 HIS C ND1 
8643  C CD2 . HIS C 368 ? 1.0580 0.8901 1.1418 0.0130  0.3803  0.1076  368 HIS C CD2 
8644  C CE1 . HIS C 368 ? 1.0355 0.9321 1.2420 -0.0232 0.3936  0.0860  368 HIS C CE1 
8645  N NE2 . HIS C 368 ? 1.0793 0.9381 1.2185 0.0007  0.4075  0.1050  368 HIS C NE2 
8646  N N   . ALA C 369 ? 0.7790 0.6561 0.8346 0.0154  0.2127  0.0528  369 ALA C N   
8647  C CA  . ALA C 369 ? 0.7089 0.5751 0.7369 0.0204  0.1827  0.0495  369 ALA C CA  
8648  C C   . ALA C 369 ? 0.7289 0.6033 0.7900 0.0018  0.1717  0.0410  369 ALA C C   
8649  O O   . ALA C 369 ? 0.7317 0.6328 0.8417 -0.0144 0.1762  0.0310  369 ALA C O   
8650  C CB  . ALA C 369 ? 0.6340 0.5173 0.6528 0.0311  0.1582  0.0399  369 ALA C CB  
8651  N N   . ARG C 370 ? 0.7655 0.6190 0.8004 0.0052  0.1567  0.0437  370 ARG C N   
8652  C CA  . ARG C 370 ? 0.7685 0.6222 0.8253 -0.0095 0.1478  0.0365  370 ARG C CA  
8653  C C   . ARG C 370 ? 0.6427 0.5322 0.7305 -0.0180 0.1241  0.0195  370 ARG C C   
8654  O O   . ARG C 370 ? 0.6174 0.5234 0.7424 -0.0346 0.1246  0.0083  370 ARG C O   
8655  C CB  . ARG C 370 ? 0.8695 0.6942 0.8873 0.0010  0.1368  0.0448  370 ARG C CB  
8656  C CG  . ARG C 370 ? 0.9201 0.7454 0.9519 -0.0089 0.1215  0.0363  370 ARG C CG  
8657  C CD  . ARG C 370 ? 0.9780 0.7971 1.0432 -0.0276 0.1400  0.0315  370 ARG C CD  
8658  N NE  . ARG C 370 ? 0.9853 0.8045 1.0620 -0.0365 0.1265  0.0207  370 ARG C NE  
8659  C CZ  . ARG C 370 ? 0.9747 0.8222 1.0843 -0.0508 0.1145  0.0021  370 ARG C CZ  
8660  N NH1 . ARG C 370 ? 0.9655 0.8470 1.1037 -0.0576 0.1123  -0.0076 370 ARG C NH1 
8661  N NH2 . ARG C 370 ? 0.9621 0.8054 1.0750 -0.0565 0.1043  -0.0071 370 ARG C NH2 
8662  N N   . ALA C 371 ? 0.5495 0.4504 0.6213 -0.0058 0.1045  0.0174  371 ALA C N   
8663  C CA  . ALA C 371 ? 0.4518 0.3844 0.5463 -0.0085 0.0835  0.0054  371 ALA C CA  
8664  C C   . ALA C 371 ? 0.4494 0.3951 0.5387 0.0046  0.0805  0.0060  371 ALA C C   
8665  O O   . ALA C 371 ? 0.4894 0.4167 0.5517 0.0156  0.0910  0.0138  371 ALA C O   
8666  C CB  . ALA C 371 ? 0.4241 0.3495 0.5030 -0.0067 0.0620  0.0032  371 ALA C CB  
8667  N N   . GLY C 372 ? 0.4298 0.4067 0.5436 0.0048  0.0672  -0.0022 372 GLY C N   
8668  C CA  . GLY C 372 ? 0.4187 0.4081 0.5315 0.0185  0.0645  -0.0019 372 GLY C CA  
8669  C C   . GLY C 372 ? 0.4072 0.3718 0.4824 0.0312  0.0529  0.0018  372 GLY C C   
8670  O O   . GLY C 372 ? 0.4097 0.3645 0.4676 0.0432  0.0582  0.0037  372 GLY C O   
8671  N N   . ILE C 373 ? 0.4112 0.3666 0.4763 0.0277  0.0376  0.0012  373 ILE C N   
8672  C CA  . ILE C 373 ? 0.3994 0.3328 0.4354 0.0356  0.0255  0.0031  373 ILE C CA  
8673  C C   . ILE C 373 ? 0.3790 0.2933 0.3986 0.0303  0.0225  0.0062  373 ILE C C   
8674  O O   . ILE C 373 ? 0.3695 0.2897 0.4027 0.0208  0.0201  0.0048  373 ILE C O   
8675  C CB  . ILE C 373 ? 0.3664 0.3109 0.4113 0.0391  0.0096  0.0007  373 ILE C CB  
8676  C CG1 . ILE C 373 ? 0.3515 0.3154 0.4133 0.0475  0.0126  -0.0006 373 ILE C CG1 
8677  C CG2 . ILE C 373 ? 0.3776 0.2997 0.3995 0.0446  -0.0003 0.0013  373 ILE C CG2 
8678  C CD1 . ILE C 373 ? 0.3329 0.3098 0.4049 0.0528  -0.0004 0.0000  373 ILE C CD1 
8679  N N   . ALA C 374 ? 0.4082 0.3003 0.3979 0.0379  0.0224  0.0095  374 ALA C N   
8680  C CA  . ALA C 374 ? 0.4265 0.3034 0.4011 0.0368  0.0160  0.0129  374 ALA C CA  
8681  C C   . ALA C 374 ? 0.4371 0.3057 0.3945 0.0440  0.0000  0.0098  374 ALA C C   
8682  O O   . ALA C 374 ? 0.4456 0.3030 0.3790 0.0532  -0.0005 0.0084  374 ALA C O   
8683  C CB  . ALA C 374 ? 0.4212 0.2807 0.3768 0.0395  0.0315  0.0210  374 ALA C CB  
8684  N N   . LEU C 375 ? 0.4382 0.3129 0.4088 0.0395  -0.0125 0.0075  375 LEU C N   
8685  C CA  . LEU C 375 ? 0.4165 0.2858 0.3809 0.0428  -0.0264 0.0036  375 LEU C CA  
8686  C C   . LEU C 375 ? 0.5102 0.3701 0.4577 0.0463  -0.0320 0.0059  375 LEU C C   
8687  O O   . LEU C 375 ? 0.5219 0.3815 0.4737 0.0432  -0.0301 0.0112  375 LEU C O   
8688  C CB  . LEU C 375 ? 0.3662 0.2452 0.3519 0.0374  -0.0337 0.0030  375 LEU C CB  
8689  C CG  . LEU C 375 ? 0.3480 0.2401 0.3497 0.0369  -0.0296 0.0029  375 LEU C CG  
8690  C CD1 . LEU C 375 ? 0.3296 0.2308 0.3455 0.0339  -0.0353 0.0051  375 LEU C CD1 
8691  C CD2 . LEU C 375 ? 0.3640 0.2510 0.3619 0.0442  -0.0284 -0.0005 375 LEU C CD2 
8692  N N   . GLY C 376 ? 0.5499 0.4027 0.4778 0.0540  -0.0396 0.0007  376 GLY C N   
8693  C CA  . GLY C 376 ? 0.5511 0.3986 0.4587 0.0616  -0.0464 0.0028  376 GLY C CA  
8694  C C   . GLY C 376 ? 0.5045 0.3589 0.4209 0.0610  -0.0647 -0.0046 376 GLY C C   
8695  O O   . GLY C 376 ? 0.4606 0.3214 0.4024 0.0524  -0.0691 -0.0084 376 GLY C O   
8696  N N   . ALA C 377 ? 0.5098 0.3642 0.4058 0.0709  -0.0748 -0.0064 377 ALA C N   
8697  C CA  . ALA C 377 ? 0.4747 0.3413 0.3837 0.0704  -0.0934 -0.0145 377 ALA C CA  
8698  C C   . ALA C 377 ? 0.4951 0.3647 0.4200 0.0629  -0.1032 -0.0307 377 ALA C C   
8699  O O   . ALA C 377 ? 0.4991 0.3777 0.4546 0.0539  -0.1097 -0.0346 377 ALA C O   
8700  C CB  . ALA C 377 ? 0.4773 0.3469 0.3579 0.0856  -0.1040 -0.0143 377 ALA C CB  
8701  N N   A HIS C 378 ? 0.5099 0.3697 0.4155 0.0664  -0.1015 -0.0396 378 HIS C N   
8702  N N   B HIS C 378 ? 0.5109 0.3708 0.4153 0.0669  -0.1019 -0.0398 378 HIS C N   
8703  C CA  A HIS C 378 ? 0.4969 0.3539 0.4160 0.0598  -0.1091 -0.0567 378 HIS C CA  
8704  C CA  B HIS C 378 ? 0.4990 0.3547 0.4152 0.0606  -0.1079 -0.0565 378 HIS C CA  
8705  C C   A HIS C 378 ? 0.4720 0.3255 0.4233 0.0483  -0.0993 -0.0524 378 HIS C C   
8706  C C   B HIS C 378 ? 0.4769 0.3302 0.4272 0.0486  -0.0992 -0.0525 378 HIS C C   
8707  O O   A HIS C 378 ? 0.4703 0.3231 0.4457 0.0399  -0.1047 -0.0618 378 HIS C O   
8708  O O   B HIS C 378 ? 0.4699 0.3232 0.4443 0.0402  -0.1053 -0.0620 378 HIS C O   
8709  C CB  A HIS C 378 ? 0.5270 0.3714 0.4145 0.0683  -0.1073 -0.0678 378 HIS C CB  
8710  C CB  B HIS C 378 ? 0.5268 0.3684 0.4119 0.0690  -0.1015 -0.0638 378 HIS C CB  
8711  C CG  A HIS C 378 ? 0.5419 0.3915 0.3990 0.0794  -0.1233 -0.0791 378 HIS C CG  
8712  C CG  B HIS C 378 ? 0.5496 0.3842 0.4362 0.0663  -0.1112 -0.0859 378 HIS C CG  
8713  N ND1 A HIS C 378 ? 0.6040 0.4448 0.4341 0.0861  -0.1287 -0.0972 378 HIS C ND1 
8714  N ND1 B HIS C 378 ? 0.5844 0.4283 0.4740 0.0646  -0.1317 -0.1034 378 HIS C ND1 
8715  C CD2 A HIS C 378 ? 0.5218 0.3856 0.3691 0.0871  -0.1358 -0.0752 378 HIS C CD2 
8716  C CD2 B HIS C 378 ? 0.5554 0.3739 0.4419 0.0653  -0.1028 -0.0949 378 HIS C CD2 
8717  C CE1 A HIS C 378 ? 0.6013 0.4527 0.4044 0.0974  -0.1455 -0.1046 378 HIS C CE1 
8718  C CE1 B HIS C 378 ? 0.5831 0.4152 0.4752 0.0605  -0.1353 -0.1239 378 HIS C CE1 
8719  N NE2 A HIS C 378 ? 0.5284 0.3945 0.3422 0.0990  -0.1502 -0.0904 378 HIS C NE2 
8720  N NE2 B HIS C 378 ? 0.5650 0.3794 0.4539 0.0617  -0.1170 -0.1183 378 HIS C NE2 
8721  N N   . HIS C 379 ? 0.4622 0.3139 0.4142 0.0484  -0.0846 -0.0385 379 HIS C N   
8722  C CA  . HIS C 379 ? 0.4521 0.3040 0.4301 0.0410  -0.0767 -0.0323 379 HIS C CA  
8723  C C   . HIS C 379 ? 0.4553 0.3166 0.4587 0.0335  -0.0817 -0.0286 379 HIS C C   
8724  O O   . HIS C 379 ? 0.4695 0.3279 0.4949 0.0274  -0.0796 -0.0291 379 HIS C O   
8725  C CB  . HIS C 379 ? 0.4377 0.2930 0.4125 0.0429  -0.0633 -0.0201 379 HIS C CB  
8726  C CG  . HIS C 379 ? 0.4112 0.2710 0.4075 0.0387  -0.0576 -0.0135 379 HIS C CG  
8727  N ND1 . HIS C 379 ? 0.4355 0.2903 0.4374 0.0415  -0.0518 -0.0141 379 HIS C ND1 
8728  C CD2 . HIS C 379 ? 0.4058 0.2745 0.4162 0.0342  -0.0565 -0.0057 379 HIS C CD2 
8729  C CE1 . HIS C 379 ? 0.4282 0.2897 0.4454 0.0400  -0.0484 -0.0058 379 HIS C CE1 
8730  N NE2 . HIS C 379 ? 0.4342 0.3043 0.4556 0.0351  -0.0513 -0.0014 379 HIS C NE2 
8731  N N   . LEU C 380 ? 0.4099 0.2805 0.4099 0.0353  -0.0859 -0.0236 380 LEU C N   
8732  C CA  . LEU C 380 ? 0.3811 0.2622 0.4044 0.0301  -0.0883 -0.0189 380 LEU C CA  
8733  C C   . LEU C 380 ? 0.3701 0.2590 0.4144 0.0255  -0.1005 -0.0296 380 LEU C C   
8734  O O   . LEU C 380 ? 0.3938 0.2902 0.4653 0.0191  -0.0990 -0.0267 380 LEU C O   
8735  C CB  . LEU C 380 ? 0.3807 0.2670 0.3935 0.0355  -0.0869 -0.0100 380 LEU C CB  
8736  C CG  . LEU C 380 ? 0.3567 0.2371 0.3571 0.0367  -0.0738 -0.0008 380 LEU C CG  
8737  C CD1 . LEU C 380 ? 0.3667 0.2461 0.3555 0.0427  -0.0721 0.0060  380 LEU C CD1 
8738  C CD2 . LEU C 380 ? 0.3242 0.2080 0.3413 0.0302  -0.0661 0.0038  380 LEU C CD2 
8739  N N   . GLU C 381 ? 0.3986 0.2877 0.4308 0.0289  -0.1124 -0.0428 381 GLU C N   
8740  C CA  . GLU C 381 ? 0.4185 0.3198 0.4726 0.0239  -0.1271 -0.0572 381 GLU C CA  
8741  C C   . GLU C 381 ? 0.4233 0.3183 0.5119 0.0105  -0.1216 -0.0629 381 GLU C C   
8742  O O   . GLU C 381 ? 0.4320 0.3080 0.5163 0.0084  -0.1115 -0.0631 381 GLU C O   
8743  C CB  . GLU C 381 ? 0.4004 0.3019 0.4290 0.0311  -0.1416 -0.0733 381 GLU C CB  
8744  C CG  . GLU C 381 ? 0.4256 0.3370 0.4252 0.0458  -0.1492 -0.0669 381 GLU C CG  
8745  C CD  . GLU C 381 ? 0.4920 0.3985 0.4520 0.0574  -0.1583 -0.0781 381 GLU C CD  
8746  O OE1 . GLU C 381 ? 0.5162 0.4119 0.4720 0.0532  -0.1599 -0.0938 381 GLU C OE1 
8747  O OE2 . GLU C 381 ? 0.5387 0.4504 0.4693 0.0724  -0.1625 -0.0704 381 GLU C OE2 
8748  N N   . GLU C 382 ? 0.4116 0.3224 0.5358 0.0025  -0.1263 -0.0659 382 GLU C N   
8749  C CA  . GLU C 382 ? 0.4268 0.3319 0.5895 -0.0112 -0.1182 -0.0693 382 GLU C CA  
8750  C C   . GLU C 382 ? 0.3847 0.2742 0.5485 -0.0117 -0.0969 -0.0502 382 GLU C C   
8751  O O   . GLU C 382 ? 0.4007 0.2746 0.5831 -0.0190 -0.0856 -0.0496 382 GLU C O   
8752  C CB  . GLU C 382 ? 0.4584 0.3495 0.6251 -0.0179 -0.1239 -0.0903 382 GLU C CB  
8753  C CG  . GLU C 382 ? 0.4765 0.3870 0.6453 -0.0182 -0.1475 -0.1132 382 GLU C CG  
8754  C CD  . GLU C 382 ? 0.4637 0.4051 0.6731 -0.0248 -0.1571 -0.1164 382 GLU C CD  
8755  O OE1 . GLU C 382 ? 0.4707 0.4123 0.7206 -0.0367 -0.1442 -0.1105 382 GLU C OE1 
8756  O OE2 . GLU C 382 ? 0.4441 0.4106 0.6459 -0.0168 -0.1768 -0.1246 382 GLU C OE2 
8757  N N   . ASN C 383 ? 0.3872 0.2809 0.5303 -0.0031 -0.0917 -0.0351 383 ASN C N   
8758  C CA  . ASN C 383 ? 0.3989 0.2861 0.5424 -0.0020 -0.0752 -0.0181 383 ASN C CA  
8759  C C   . ASN C 383 ? 0.3541 0.2576 0.5042 0.0001  -0.0735 -0.0090 383 ASN C C   
8760  O O   . ASN C 383 ? 0.3542 0.2687 0.4941 0.0053  -0.0829 -0.0112 383 ASN C O   
8761  C CB  . ASN C 383 ? 0.4215 0.2979 0.5336 0.0061  -0.0698 -0.0115 383 ASN C CB  
8762  C CG  . ASN C 383 ? 0.4418 0.3003 0.5486 0.0064  -0.0673 -0.0179 383 ASN C CG  
8763  O OD1 . ASN C 383 ? 0.4466 0.2923 0.5682 0.0036  -0.0573 -0.0140 383 ASN C OD1 
8764  N ND2 . ASN C 383 ? 0.4596 0.3149 0.5432 0.0117  -0.0736 -0.0259 383 ASN C ND2 
8765  N N   . LEU C 384 ? 0.3738 0.2768 0.5383 -0.0020 -0.0598 0.0023  384 LEU C N   
8766  C CA  . LEU C 384 ? 0.3545 0.2695 0.5200 0.0018  -0.0549 0.0112  384 LEU C CA  
8767  C C   . LEU C 384 ? 0.4005 0.3089 0.5357 0.0091  -0.0480 0.0202  384 LEU C C   
8768  O O   . LEU C 384 ? 0.4354 0.3350 0.5634 0.0105  -0.0386 0.0273  384 LEU C O   
8769  C CB  . LEU C 384 ? 0.3344 0.2546 0.5320 -0.0036 -0.0426 0.0176  384 LEU C CB  
8770  C CG  . LEU C 384 ? 0.3343 0.2652 0.5309 0.0020  -0.0347 0.0268  384 LEU C CG  
8771  C CD1 . LEU C 384 ? 0.3069 0.2556 0.5116 0.0053  -0.0470 0.0203  384 LEU C CD1 
8772  C CD2 . LEU C 384 ? 0.3301 0.2628 0.5532 -0.0017 -0.0173 0.0359  384 LEU C CD2 
8773  N N   . VAL C 385 ? 0.3997 0.3127 0.5180 0.0141  -0.0528 0.0194  385 VAL C N   
8774  C CA  . VAL C 385 ? 0.3771 0.2856 0.4709 0.0183  -0.0479 0.0233  385 VAL C CA  
8775  C C   . VAL C 385 ? 0.3502 0.2635 0.4414 0.0214  -0.0420 0.0271  385 VAL C C   
8776  O O   . VAL C 385 ? 0.3482 0.2644 0.4409 0.0240  -0.0456 0.0254  385 VAL C O   
8777  C CB  . VAL C 385 ? 0.3624 0.2661 0.4374 0.0203  -0.0548 0.0180  385 VAL C CB  
8778  C CG1 . VAL C 385 ? 0.3633 0.2652 0.4210 0.0218  -0.0492 0.0198  385 VAL C CG1 
8779  C CG2 . VAL C 385 ? 0.3532 0.2509 0.4290 0.0186  -0.0596 0.0126  385 VAL C CG2 
8780  N N   . VAL C 386 ? 0.3570 0.2701 0.4423 0.0228  -0.0326 0.0322  386 VAL C N   
8781  C CA  . VAL C 386 ? 0.3292 0.2451 0.4111 0.0262  -0.0252 0.0341  386 VAL C CA  
8782  C C   . VAL C 386 ? 0.3454 0.2577 0.4051 0.0273  -0.0248 0.0292  386 VAL C C   
8783  O O   . VAL C 386 ? 0.3791 0.2929 0.4267 0.0275  -0.0246 0.0285  386 VAL C O   
8784  C CB  . VAL C 386 ? 0.3299 0.2483 0.4168 0.0283  -0.0135 0.0418  386 VAL C CB  
8785  C CG1 . VAL C 386 ? 0.3386 0.2590 0.4185 0.0331  -0.0047 0.0420  386 VAL C CG1 
8786  C CG2 . VAL C 386 ? 0.3173 0.2390 0.4333 0.0244  -0.0114 0.0457  386 VAL C CG2 
8787  N N   . PHE C 387 ? 0.3336 0.2415 0.3901 0.0283  -0.0242 0.0256  387 PHE C N   
8788  C CA  . PHE C 387 ? 0.3633 0.2654 0.4040 0.0269  -0.0217 0.0187  387 PHE C CA  
8789  C C   . PHE C 387 ? 0.3848 0.2869 0.4196 0.0299  -0.0129 0.0166  387 PHE C C   
8790  O O   . PHE C 387 ? 0.3846 0.2813 0.4239 0.0335  -0.0071 0.0170  387 PHE C O   
8791  C CB  . PHE C 387 ? 0.3619 0.2532 0.4008 0.0267  -0.0225 0.0168  387 PHE C CB  
8792  C CG  . PHE C 387 ? 0.3976 0.2880 0.4349 0.0251  -0.0296 0.0177  387 PHE C CG  
8793  C CD1 . PHE C 387 ? 0.3834 0.2778 0.4288 0.0279  -0.0370 0.0214  387 PHE C CD1 
8794  C CD2 . PHE C 387 ? 0.4222 0.3089 0.4511 0.0205  -0.0285 0.0132  387 PHE C CD2 
8795  C CE1 . PHE C 387 ? 0.3666 0.2590 0.4061 0.0276  -0.0431 0.0203  387 PHE C CE1 
8796  C CE2 . PHE C 387 ? 0.4019 0.2872 0.4275 0.0205  -0.0325 0.0143  387 PHE C CE2 
8797  C CZ  . PHE C 387 ? 0.3917 0.2786 0.4198 0.0247  -0.0398 0.0178  387 PHE C CZ  
8798  N N   . ASP C 388 ? 0.3790 0.2881 0.4022 0.0305  -0.0120 0.0147  388 ASP C N   
8799  C CA  . ASP C 388 ? 0.4020 0.3120 0.4130 0.0351  -0.0040 0.0115  388 ASP C CA  
8800  C C   . ASP C 388 ? 0.4376 0.3432 0.4356 0.0310  -0.0046 -0.0039 388 ASP C C   
8801  O O   . ASP C 388 ? 0.4851 0.4002 0.4716 0.0292  -0.0102 -0.0118 388 ASP C O   
8802  C CB  . ASP C 388 ? 0.4441 0.3640 0.4449 0.0406  -0.0025 0.0182  388 ASP C CB  
8803  C CG  . ASP C 388 ? 0.5197 0.4404 0.5042 0.0483  0.0078  0.0175  388 ASP C CG  
8804  O OD1 . ASP C 388 ? 0.5761 0.4898 0.5564 0.0483  0.0127  0.0083  388 ASP C OD1 
8805  O OD2 . ASP C 388 ? 0.5372 0.4635 0.5112 0.0558  0.0127  0.0269  388 ASP C OD2 
8806  N N   . LEU C 389 ? 0.4018 0.2932 0.4035 0.0300  0.0015  -0.0086 389 LEU C N   
8807  C CA  . LEU C 389 ? 0.4210 0.3031 0.4161 0.0232  0.0028  -0.0240 389 LEU C CA  
8808  C C   . LEU C 389 ? 0.4544 0.3401 0.4317 0.0251  0.0058  -0.0374 389 LEU C C   
8809  O O   . LEU C 389 ? 0.5027 0.3890 0.4747 0.0176  0.0028  -0.0543 389 LEU C O   
8810  C CB  . LEU C 389 ? 0.4405 0.3009 0.4441 0.0233  0.0109  -0.0230 389 LEU C CB  
8811  C CG  . LEU C 389 ? 0.4054 0.2645 0.4213 0.0254  0.0067  -0.0091 389 LEU C CG  
8812  C CD1 . LEU C 389 ? 0.4223 0.2636 0.4430 0.0318  0.0145  -0.0040 389 LEU C CD1 
8813  C CD2 . LEU C 389 ? 0.3824 0.2427 0.3991 0.0172  0.0009  -0.0114 389 LEU C CD2 
8814  N N   . GLU C 390 ? 0.4433 0.3328 0.4119 0.0350  0.0120  -0.0309 390 GLU C N   
8815  C CA  . GLU C 390 ? 0.4683 0.3603 0.4135 0.0396  0.0158  -0.0436 390 GLU C CA  
8816  C C   . GLU C 390 ? 0.4576 0.3704 0.3867 0.0399  0.0040  -0.0494 390 GLU C C   
8817  O O   . GLU C 390 ? 0.4800 0.3986 0.3898 0.0399  0.0006  -0.0676 390 GLU C O   
8818  C CB  . GLU C 390 ? 0.4885 0.3789 0.4272 0.0519  0.0289  -0.0330 390 GLU C CB  
8819  C CG  . GLU C 390 ? 0.5444 0.4179 0.4990 0.0543  0.0405  -0.0300 390 GLU C CG  
8820  C CD  . GLU C 390 ? 0.6613 0.5337 0.6087 0.0666  0.0562  -0.0253 390 GLU C CD  
8821  O OE1 . GLU C 390 ? 0.6594 0.5444 0.5930 0.0733  0.0592  -0.0178 390 GLU C OE1 
8822  O OE2 . GLU C 390 ? 0.7319 0.5897 0.6871 0.0710  0.0673  -0.0278 390 GLU C OE2 
8823  N N   . ARG C 391 ? 0.4475 0.3719 0.3844 0.0412  -0.0028 -0.0349 391 ARG C N   
8824  C CA  . ARG C 391 ? 0.4545 0.4000 0.3776 0.0449  -0.0140 -0.0370 391 ARG C CA  
8825  C C   . ARG C 391 ? 0.4356 0.3899 0.3761 0.0349  -0.0256 -0.0419 391 ARG C C   
8826  O O   . ARG C 391 ? 0.4468 0.4213 0.3816 0.0386  -0.0359 -0.0428 391 ARG C O   
8827  C CB  . ARG C 391 ? 0.4558 0.4071 0.3710 0.0574  -0.0101 -0.0157 391 ARG C CB  
8828  C CG  . ARG C 391 ? 0.5217 0.4668 0.4190 0.0687  0.0045  -0.0087 391 ARG C CG  
8829  C CD  . ARG C 391 ? 0.6142 0.5657 0.4983 0.0820  0.0099  0.0113  391 ARG C CD  
8830  N NE  . ARG C 391 ? 0.7902 0.7601 0.6551 0.0882  -0.0044 0.0070  391 ARG C NE  
8831  C CZ  . ARG C 391 ? 0.9168 0.8950 0.7600 0.1039  -0.0028 0.0218  391 ARG C CZ  
8832  N NH1 . ARG C 391 ? 0.9488 0.9153 0.7867 0.1135  0.0153  0.0428  391 ARG C NH1 
8833  N NH2 . ARG C 391 ? 0.9572 0.9561 0.7853 0.1108  -0.0184 0.0162  391 ARG C NH2 
8834  N N   . SER C 392 ? 0.4131 0.3528 0.3737 0.0244  -0.0227 -0.0439 392 SER C N   
8835  C CA  . SER C 392 ? 0.3812 0.3266 0.3590 0.0149  -0.0296 -0.0474 392 SER C CA  
8836  C C   . SER C 392 ? 0.3708 0.3296 0.3528 0.0204  -0.0364 -0.0335 392 SER C C   
8837  O O   . SER C 392 ? 0.3849 0.3629 0.3698 0.0198  -0.0453 -0.0389 392 SER C O   
8838  C CB  . SER C 392 ? 0.3813 0.3406 0.3598 0.0063  -0.0364 -0.0701 392 SER C CB  
8839  O OG  . SER C 392 ? 0.3674 0.3263 0.3679 -0.0055 -0.0369 -0.0745 392 SER C OG  
8840  N N   . ARG C 393 ? 0.3520 0.3006 0.3373 0.0257  -0.0317 -0.0168 393 ARG C N   
8841  C CA  . ARG C 393 ? 0.3389 0.2938 0.3287 0.0308  -0.0356 -0.0043 393 ARG C CA  
8842  C C   . ARG C 393 ? 0.3670 0.3063 0.3702 0.0289  -0.0314 0.0063  393 ARG C C   
8843  O O   . ARG C 393 ? 0.3738 0.3016 0.3812 0.0275  -0.0257 0.0076  393 ARG C O   
8844  C CB  . ARG C 393 ? 0.3552 0.3188 0.3290 0.0433  -0.0348 0.0050  393 ARG C CB  
8845  C CG  . ARG C 393 ? 0.3662 0.3175 0.3355 0.0478  -0.0234 0.0140  393 ARG C CG  
8846  C CD  . ARG C 393 ? 0.4249 0.3828 0.3734 0.0616  -0.0188 0.0241  393 ARG C CD  
8847  N NE  . ARG C 393 ? 0.4627 0.4086 0.4131 0.0649  -0.0042 0.0351  393 ARG C NE  
8848  C CZ  . ARG C 393 ? 0.4874 0.4313 0.4266 0.0761  0.0066  0.0506  393 ARG C CZ  
8849  N NH1 . ARG C 393 ? 0.4844 0.4362 0.4048 0.0878  0.0040  0.0586  393 ARG C NH1 
8850  N NH2 . ARG C 393 ? 0.5187 0.4533 0.4670 0.0766  0.0217  0.0593  393 ARG C NH2 
8851  N N   . VAL C 394 ? 0.3709 0.3114 0.3814 0.0299  -0.0350 0.0125  394 VAL C N   
8852  C CA  . VAL C 394 ? 0.4033 0.3318 0.4254 0.0285  -0.0337 0.0197  394 VAL C CA  
8853  C C   . VAL C 394 ? 0.3684 0.2957 0.3928 0.0345  -0.0310 0.0307  394 VAL C C   
8854  O O   . VAL C 394 ? 0.3627 0.2971 0.3803 0.0407  -0.0324 0.0341  394 VAL C O   
8855  C CB  . VAL C 394 ? 0.4774 0.4029 0.5048 0.0242  -0.0380 0.0160  394 VAL C CB  
8856  C CG1 . VAL C 394 ? 0.5085 0.4237 0.5444 0.0239  -0.0392 0.0204  394 VAL C CG1 
8857  C CG2 . VAL C 394 ? 0.5161 0.4381 0.5423 0.0183  -0.0365 0.0079  394 VAL C CG2 
8858  N N   . GLY C 395 ? 0.3694 0.2885 0.4059 0.0333  -0.0262 0.0365  395 GLY C N   
8859  C CA  . GLY C 395 ? 0.3555 0.2689 0.4005 0.0363  -0.0203 0.0469  395 GLY C CA  
8860  C C   . GLY C 395 ? 0.3287 0.2336 0.3921 0.0302  -0.0239 0.0447  395 GLY C C   
8861  O O   . GLY C 395 ? 0.3429 0.2484 0.4127 0.0254  -0.0299 0.0376  395 GLY C O   
8862  N N   . PHE C 396 ? 0.3441 0.2402 0.4142 0.0317  -0.0203 0.0502  396 PHE C N   
8863  C CA  . PHE C 396 ? 0.3712 0.2583 0.4591 0.0250  -0.0242 0.0443  396 PHE C CA  
8864  C C   . PHE C 396 ? 0.3939 0.2679 0.4972 0.0246  -0.0133 0.0525  396 PHE C C   
8865  O O   . PHE C 396 ? 0.4236 0.2937 0.5178 0.0326  -0.0028 0.0650  396 PHE C O   
8866  C CB  . PHE C 396 ? 0.3935 0.2782 0.4712 0.0260  -0.0327 0.0364  396 PHE C CB  
8867  C CG  . PHE C 396 ? 0.4198 0.3044 0.4843 0.0347  -0.0296 0.0421  396 PHE C CG  
8868  C CD1 . PHE C 396 ? 0.4354 0.3062 0.5048 0.0391  -0.0235 0.0477  396 PHE C CD1 
8869  C CD2 . PHE C 396 ? 0.3840 0.2830 0.4336 0.0391  -0.0327 0.0414  396 PHE C CD2 
8870  C CE1 . PHE C 396 ? 0.4378 0.3111 0.4958 0.0504  -0.0212 0.0544  396 PHE C CE1 
8871  C CE2 . PHE C 396 ? 0.3801 0.2857 0.4212 0.0484  -0.0323 0.0457  396 PHE C CE2 
8872  C CZ  . PHE C 396 ? 0.4086 0.3020 0.4530 0.0556  -0.0267 0.0534  396 PHE C CZ  
8873  N N   . ASN C 397 ? 0.3764 0.2432 0.5032 0.0157  -0.0150 0.0452  397 ASN C N   
8874  C CA  . ASN C 397 ? 0.4090 0.2597 0.5561 0.0125  -0.0020 0.0517  397 ASN C CA  
8875  C C   . ASN C 397 ? 0.4003 0.2332 0.5348 0.0204  0.0031  0.0569  397 ASN C C   
8876  O O   . ASN C 397 ? 0.4263 0.2574 0.5502 0.0221  -0.0067 0.0475  397 ASN C O   
8877  C CB  . ASN C 397 ? 0.4180 0.2682 0.5980 -0.0011 -0.0070 0.0381  397 ASN C CB  
8878  C CG  . ASN C 397 ? 0.3786 0.2328 0.5509 -0.0036 -0.0253 0.0205  397 ASN C CG  
8879  O OD1 . ASN C 397 ? 0.3707 0.2391 0.5272 -0.0002 -0.0361 0.0167  397 ASN C OD1 
8880  N ND2 . ASN C 397 ? 0.4000 0.2391 0.5822 -0.0087 -0.0274 0.0096  397 ASN C ND2 
8881  N N   . SER C 398 ? 0.4065 0.2261 0.5401 0.0276  0.0197  0.0736  398 SER C N   
8882  C CA  . SER C 398 ? 0.4082 0.2114 0.5289 0.0391  0.0256  0.0816  398 SER C CA  
8883  C C   . SER C 398 ? 0.4815 0.2575 0.6252 0.0316  0.0336  0.0763  398 SER C C   
8884  O O   . SER C 398 ? 0.5500 0.3126 0.6822 0.0401  0.0386  0.0796  398 SER C O   
8885  C CB  . SER C 398 ? 0.4103 0.2115 0.5126 0.0549  0.0394  0.1038  398 SER C CB  
8886  O OG  . SER C 398 ? 0.4676 0.2588 0.5851 0.0504  0.0570  0.1145  398 SER C OG  
8887  N N   . ASN C 399 ? 0.4800 0.2545 0.6532 0.0150  0.0345  0.0657  399 ASN C N   
8888  C CA  . ASN C 399 ? 0.4868 0.2447 0.6791 0.0041  0.0371  0.0518  399 ASN C CA  
8889  C C   . ASN C 399 ? 0.5048 0.2741 0.7160 -0.0097 0.0182  0.0285  399 ASN C C   
8890  O O   . ASN C 399 ? 0.5079 0.2999 0.7192 -0.0112 0.0080  0.0271  399 ASN C O   
8891  C CB  . ASN C 399 ? 0.4899 0.2375 0.7041 -0.0026 0.0576  0.0606  399 ASN C CB  
8892  C CG  . ASN C 399 ? 0.4907 0.2278 0.6819 0.0140  0.0756  0.0850  399 ASN C CG  
8893  O OD1 . ASN C 399 ? 0.5045 0.2243 0.6818 0.0230  0.0809  0.0890  399 ASN C OD1 
8894  N ND2 . ASN C 399 ? 0.4965 0.2450 0.6819 0.0197  0.0845  0.1011  399 ASN C ND2 
8895  N N   . SER C 400 ? 0.5173 0.2757 0.7373 -0.0177 0.0123  0.0092  400 SER C N   
8896  C CA  . SER C 400 ? 0.4805 0.2528 0.7135 -0.0284 -0.0085 -0.0146 400 SER C CA  
8897  C C   . SER C 400 ? 0.4816 0.2724 0.7512 -0.0419 -0.0089 -0.0181 400 SER C C   
8898  O O   . SER C 400 ? 0.4764 0.2627 0.7674 -0.0474 0.0094  -0.0084 400 SER C O   
8899  C CB  . SER C 400 ? 0.4842 0.2420 0.7172 -0.0340 -0.0142 -0.0366 400 SER C CB  
8900  O OG  . SER C 400 ? 0.5444 0.2930 0.8060 -0.0467 -0.0026 -0.0420 400 SER C OG  
8901  N N   . LEU C 401 ? 0.4770 0.2938 0.7494 -0.0449 -0.0287 -0.0304 401 LEU C N   
8902  C CA  . LEU C 401 ? 0.4721 0.3110 0.7846 -0.0569 -0.0312 -0.0361 401 LEU C CA  
8903  C C   . LEU C 401 ? 0.5035 0.3371 0.8513 -0.0723 -0.0276 -0.0529 401 LEU C C   
8904  O O   . LEU C 401 ? 0.4898 0.3311 0.8730 -0.0816 -0.0141 -0.0487 401 LEU C O   
8905  C CB  . LEU C 401 ? 0.4474 0.3188 0.7506 -0.0535 -0.0549 -0.0470 401 LEU C CB  
8906  C CG  . LEU C 401 ? 0.4106 0.2955 0.6813 -0.0393 -0.0563 -0.0309 401 LEU C CG  
8907  C CD1 . LEU C 401 ? 0.3825 0.2966 0.6557 -0.0374 -0.0765 -0.0418 401 LEU C CD1 
8908  C CD2 . LEU C 401 ? 0.3710 0.2567 0.6536 -0.0381 -0.0361 -0.0101 401 LEU C CD2 
8909  N N   . LYS C 402 ? 0.5242 0.3452 0.8570 -0.0731 -0.0370 -0.0710 402 LYS C N   
8910  C CA  . LYS C 402 ? 0.4351 0.2530 0.7932 -0.0866 -0.0362 -0.0904 402 LYS C CA  
8911  C C   . LYS C 402 ? 0.5398 0.3338 0.9132 -0.0905 -0.0071 -0.0746 402 LYS C C   
8912  O O   . LYS C 402 ? 0.5483 0.3455 0.9585 -0.1044 -0.0003 -0.0839 402 LYS C O   
8913  C CB  . LYS C 402 ? 0.4542 0.2591 0.7839 -0.0837 -0.0507 -0.1116 402 LYS C CB  
8914  C CG  . LYS C 402 ? 0.5743 0.3682 0.9207 -0.0961 -0.0495 -0.1332 402 LYS C CG  
8915  C CD  . LYS C 402 ? 0.8427 0.6261 1.1534 -0.0900 -0.0653 -0.1544 402 LYS C CD  
8916  C CE  . LYS C 402 ? 0.9008 0.6677 1.2217 -0.1015 -0.0639 -0.1778 402 LYS C CE  
8917  N NZ  . LYS C 402 ? 0.9434 0.6866 1.2939 -0.1120 -0.0391 -0.1694 402 LYS C NZ  
8918  N N   . SER C 403 ? 0.5351 0.3078 0.8815 -0.0774 0.0101  -0.0498 403 SER C N   
8919  C CA  . SER C 403 ? 0.5447 0.2951 0.9005 -0.0773 0.0380  -0.0318 403 SER C CA  
8920  C C   . SER C 403 ? 0.5359 0.3028 0.9246 -0.0833 0.0522  -0.0188 403 SER C C   
8921  O O   . SER C 403 ? 0.5261 0.2791 0.9344 -0.0876 0.0747  -0.0095 403 SER C O   
8922  C CB  . SER C 403 ? 0.5135 0.2418 0.8283 -0.0581 0.0502  -0.0084 403 SER C CB  
8923  O OG  . SER C 403 ? 0.5036 0.2452 0.8060 -0.0477 0.0552  0.0135  403 SER C OG  
8924  N N   . TYR C 404 ? 0.5136 0.3096 0.9101 -0.0834 0.0399  -0.0189 404 TYR C N   
8925  C CA  . TYR C 404 ? 0.4965 0.3120 0.9268 -0.0889 0.0520  -0.0091 404 TYR C CA  
8926  C C   . TYR C 404 ? 0.5155 0.3569 0.9938 -0.1062 0.0398  -0.0335 404 TYR C C   
8927  O O   . TYR C 404 ? 0.5120 0.3739 1.0259 -0.1122 0.0482  -0.0294 404 TYR C O   
8928  C CB  . TYR C 404 ? 0.4049 0.2379 0.8190 -0.0785 0.0466  0.0047  404 TYR C CB  
8929  C CG  . TYR C 404 ? 0.4730 0.2878 0.8408 -0.0602 0.0576  0.0290  404 TYR C CG  
8930  C CD1 . TYR C 404 ? 0.4807 0.2873 0.8428 -0.0524 0.0833  0.0533  404 TYR C CD1 
8931  C CD2 . TYR C 404 ? 0.3868 0.1949 0.7157 -0.0495 0.0420  0.0270  404 TYR C CD2 
8932  C CE1 . TYR C 404 ? 0.4621 0.2570 0.7790 -0.0339 0.0903  0.0737  404 TYR C CE1 
8933  C CE2 . TYR C 404 ? 0.4321 0.2296 0.7213 -0.0324 0.0497  0.0471  404 TYR C CE2 
8934  C CZ  . TYR C 404 ? 0.4487 0.2407 0.7311 -0.0245 0.0725  0.0697  404 TYR C CZ  
8935  O OH  . TYR C 404 ? 0.4591 0.2453 0.7001 -0.0060 0.0774  0.0878  404 TYR C OH  
8936  N N   . GLY C 405 ? 0.4540 0.2962 0.9313 -0.1129 0.0195  -0.0592 405 GLY C N   
8937  C CA  . GLY C 405 ? 0.4599 0.3320 0.9757 -0.1267 0.0016  -0.0854 405 GLY C CA  
8938  C C   . GLY C 405 ? 0.5516 0.4610 1.0679 -0.1220 -0.0236 -0.0922 405 GLY C C   
8939  O O   . GLY C 405 ? 0.4275 0.3702 0.9788 -0.1301 -0.0373 -0.1087 405 GLY C O   
8940  N N   . LYS C 406 ? 0.5047 0.4090 0.9818 -0.1080 -0.0305 -0.0802 406 LYS C N   
8941  C CA  . LYS C 406 ? 0.4393 0.3753 0.9150 -0.1014 -0.0515 -0.0821 406 LYS C CA  
8942  C C   . LYS C 406 ? 0.4393 0.3766 0.8767 -0.0929 -0.0789 -0.0971 406 LYS C C   
8943  O O   . LYS C 406 ? 0.4475 0.3573 0.8530 -0.0897 -0.0787 -0.1016 406 LYS C O   
8944  C CB  . LYS C 406 ? 0.3703 0.3027 0.8355 -0.0920 -0.0364 -0.0543 406 LYS C CB  
8945  C CG  . LYS C 406 ? 0.3849 0.3126 0.8773 -0.0963 -0.0062 -0.0361 406 LYS C CG  
8946  C CD  . LYS C 406 ? 0.4106 0.3750 0.9552 -0.1056 -0.0083 -0.0449 406 LYS C CD  
8947  C CE  . LYS C 406 ? 0.4643 0.4194 1.0370 -0.1113 0.0239  -0.0302 406 LYS C CE  
8948  N NZ  . LYS C 406 ? 0.4862 0.4148 1.0243 -0.0990 0.0474  -0.0013 406 LYS C NZ  
8949  N N   . THR C 407 ? 0.4438 0.4148 0.8840 -0.0873 -0.1012 -0.1036 407 THR C N   
8950  C CA  . THR C 407 ? 0.3988 0.3760 0.7893 -0.0718 -0.1233 -0.1096 407 THR C CA  
8951  C C   . THR C 407 ? 0.3723 0.3679 0.7420 -0.0558 -0.1239 -0.0902 407 THR C C   
8952  O O   . THR C 407 ? 0.3378 0.3464 0.7349 -0.0573 -0.1112 -0.0769 407 THR C O   
8953  C CB  . THR C 407 ? 0.3612 0.3642 0.7639 -0.0754 -0.1522 -0.1396 407 THR C CB  
8954  O OG1 . THR C 407 ? 0.4630 0.5084 0.9005 -0.0749 -0.1619 -0.1415 407 THR C OG1 
8955  C CG2 . THR C 407 ? 0.3944 0.3824 0.8124 -0.0892 -0.1444 -0.1563 407 THR C CG2 
8956  N N   . CYS C 408 ? 0.3977 0.3921 0.7187 -0.0402 -0.1364 -0.0884 408 CYS C N   
8957  C CA  . CYS C 408 ? 0.4062 0.4139 0.7069 -0.0251 -0.1367 -0.0719 408 CYS C CA  
8958  C C   . CYS C 408 ? 0.4007 0.4479 0.7317 -0.0217 -0.1535 -0.0796 408 CYS C C   
8959  O O   . CYS C 408 ? 0.3707 0.4308 0.7005 -0.0110 -0.1496 -0.0653 408 CYS C O   
8960  C CB  . CYS C 408 ? 0.4207 0.4127 0.6634 -0.0102 -0.1420 -0.0670 408 CYS C CB  
8961  S SG  . CYS C 408 ? 0.3843 0.3424 0.5936 -0.0073 -0.1177 -0.0463 408 CYS C SG  
8962  N N   . SER C 409 ? 0.4595 0.5268 0.8190 -0.0303 -0.1724 -0.1035 409 SER C N   
8963  C CA  . SER C 409 ? 0.4583 0.5708 0.8549 -0.0276 -0.1917 -0.1142 409 SER C CA  
8964  C C   . SER C 409 ? 0.4093 0.5418 0.8715 -0.0418 -0.1781 -0.1118 409 SER C C   
8965  O O   . SER C 409 ? 0.4297 0.5987 0.9215 -0.0353 -0.1853 -0.1101 409 SER C O   
8966  C CB  . SER C 409 ? 0.5305 0.6608 0.9302 -0.0309 -0.2188 -0.1435 409 SER C CB  
8967  O OG  . SER C 409 ? 0.5671 0.6838 0.9071 -0.0155 -0.2333 -0.1468 409 SER C OG  
8968  N N   . ASN C 410 ? 0.3889 0.4980 0.8758 -0.0601 -0.1573 -0.1112 410 ASN C N   
8969  C CA  . ASN C 410 ? 0.3071 0.4315 0.8532 -0.0733 -0.1392 -0.1073 410 ASN C CA  
8970  C C   . ASN C 410 ? 0.3191 0.4177 0.8639 -0.0743 -0.1060 -0.0807 410 ASN C C   
8971  O O   . ASN C 410 ? 0.3599 0.4662 0.9524 -0.0854 -0.0869 -0.0753 410 ASN C O   
8972  C CB  . ASN C 410 ? 0.3388 0.4593 0.9110 -0.0909 -0.1363 -0.1269 410 ASN C CB  
8973  C CG  . ASN C 410 ? 0.4265 0.5009 0.9771 -0.0995 -0.1218 -0.1270 410 ASN C CG  
8974  O OD1 . ASN C 410 ? 0.3978 0.4419 0.9307 -0.0973 -0.1023 -0.1070 410 ASN C OD1 
8975  N ND2 . ASN C 410 ? 0.4669 0.5361 1.0176 -0.1083 -0.1309 -0.1496 410 ASN C ND2 
8976  N N   . LEU C 411 ? 0.3282 0.3967 0.8144 -0.0611 -0.0976 -0.0636 411 LEU C N   
8977  C CA  . LEU C 411 ? 0.3354 0.3831 0.8122 -0.0585 -0.0683 -0.0395 411 LEU C CA  
8978  C C   . LEU C 411 ? 0.3256 0.4018 0.8292 -0.0521 -0.0605 -0.0292 411 LEU C C   
8979  O O   . LEU C 411 ? 0.3285 0.4020 0.8574 -0.0570 -0.0354 -0.0162 411 LEU C O   
8980  C CB  . LEU C 411 ? 0.3482 0.3672 0.7596 -0.0444 -0.0655 -0.0265 411 LEU C CB  
8981  C CG  . LEU C 411 ? 0.3953 0.3769 0.7817 -0.0471 -0.0484 -0.0170 411 LEU C CG  
8982  C CD1 . LEU C 411 ? 0.3936 0.3596 0.7247 -0.0318 -0.0447 -0.0025 411 LEU C CD1 
8983  C CD2 . LEU C 411 ? 0.4000 0.3727 0.8203 -0.0564 -0.0219 -0.0055 411 LEU C CD2 
8984  N N   . PHE C 412 ? 0.3481 0.4511 0.8451 -0.0396 -0.0813 -0.0346 412 PHE C N   
8985  C CA  . PHE C 412 ? 0.3069 0.4402 0.8282 -0.0295 -0.0780 -0.0267 412 PHE C CA  
8986  C C   . PHE C 412 ? 0.2796 0.4588 0.8437 -0.0293 -0.1035 -0.0447 412 PHE C C   
8987  O O   . PHE C 412 ? 0.3157 0.5007 0.8698 -0.0306 -0.1283 -0.0621 412 PHE C O   
8988  C CB  . PHE C 412 ? 0.2750 0.3940 0.7413 -0.0092 -0.0770 -0.0126 412 PHE C CB  
8989  C CG  . PHE C 412 ? 0.2472 0.3262 0.6684 -0.0086 -0.0586 0.0006  412 PHE C CG  
8990  C CD1 . PHE C 412 ? 0.2677 0.3364 0.6945 -0.0099 -0.0317 0.0152  412 PHE C CD1 
8991  C CD2 . PHE C 412 ? 0.2542 0.3081 0.6282 -0.0063 -0.0680 -0.0021 412 PHE C CD2 
8992  C CE1 . PHE C 412 ? 0.2597 0.2958 0.6440 -0.0077 -0.0176 0.0261  412 PHE C CE1 
8993  C CE2 . PHE C 412 ? 0.2705 0.2936 0.6077 -0.0053 -0.0531 0.0086  412 PHE C CE2 
8994  C CZ  . PHE C 412 ? 0.2853 0.3004 0.6270 -0.0057 -0.0293 0.0223  412 PHE C CZ  
8995  N N   . ASP C 413 ? 0.2988 0.5130 0.9100 -0.0263 -0.0982 -0.0413 413 ASP C N   
8996  C CA  . ASP C 413 ? 0.3921 0.6520 1.0365 -0.0227 -0.1231 -0.0577 413 ASP C CA  
8997  C C   . ASP C 413 ? 0.4610 0.7321 1.0658 0.0030  -0.1451 -0.0542 413 ASP C C   
8998  O O   . ASP C 413 ? 0.4961 0.7701 1.0933 0.0204  -0.1351 -0.0375 413 ASP C O   
8999  C CB  . ASP C 413 ? 0.3918 0.6814 1.0885 -0.0263 -0.1068 -0.0539 413 ASP C CB  
9000  C CG  . ASP C 413 ? 0.4446 0.7768 1.1692 -0.0274 -0.1293 -0.0727 413 ASP C CG  
9001  O OD1 . ASP C 413 ? 0.4528 0.7988 1.1487 -0.0146 -0.1577 -0.0822 413 ASP C OD1 
9002  O OD2 . ASP C 413 ? 0.4920 0.8450 1.2668 -0.0402 -0.1177 -0.0773 413 ASP C OD2 
9003  N N   . LEU C 414 ? 0.4539 0.7278 1.0289 0.0068  -0.1719 -0.0694 414 LEU C N   
9004  C CA  . LEU C 414 ? 0.4239 0.7025 0.9530 0.0325  -0.1904 -0.0639 414 LEU C CA  
9005  C C   . LEU C 414 ? 0.4765 0.7980 1.0162 0.0419  -0.2121 -0.0751 414 LEU C C   
9006  O O   . LEU C 414 ? 0.4974 0.8224 0.9946 0.0618  -0.2297 -0.0733 414 LEU C O   
9007  C CB  . LEU C 414 ? 0.3902 0.6358 0.8633 0.0356  -0.2022 -0.0677 414 LEU C CB  
9008  C CG  . LEU C 414 ? 0.2777 0.4706 0.7094 0.0286  -0.1768 -0.0537 414 LEU C CG  
9009  C CD1 . LEU C 414 ? 0.2897 0.4537 0.6664 0.0305  -0.1868 -0.0595 414 LEU C CD1 
9010  C CD2 . LEU C 414 ? 0.2691 0.4463 0.6762 0.0441  -0.1582 -0.0310 414 LEU C CD2 
9011  N N   . ASN C 415 ? 0.5002 0.8545 1.0958 0.0284  -0.2096 -0.0850 415 ASN C N   
9012  C CA  . ASN C 415 ? 0.5693 0.9703 1.1819 0.0368  -0.2307 -0.0953 415 ASN C CA  
9013  C C   . ASN C 415 ? 0.5637 0.9867 1.1786 0.0618  -0.2260 -0.0755 415 ASN C C   
9014  O O   . ASN C 415 ? 0.5346 0.9503 1.1714 0.0618  -0.2015 -0.0611 415 ASN C O   
9015  C CB  . ASN C 415 ? 0.6204 1.0485 1.2955 0.0123  -0.2286 -0.1134 415 ASN C CB  
9016  C CG  . ASN C 415 ? 0.6505 1.0525 1.3249 -0.0119 -0.2296 -0.1327 415 ASN C CG  
9017  O OD1 . ASN C 415 ? 0.6560 1.0435 1.2874 -0.0086 -0.2476 -0.1436 415 ASN C OD1 
9018  N ND2 . ASN C 415 ? 0.6695 1.0630 1.3897 -0.0352 -0.2078 -0.1358 415 ASN C ND2 
9019  N N   . ASN C 416 ? 0.6017 1.0503 1.1938 0.0837  -0.2476 -0.0742 416 ASN C N   
9020  C CA  . ASN C 416 ? 0.6446 1.1023 1.2230 0.1126  -0.2425 -0.0518 416 ASN C CA  
9021  C C   . ASN C 416 ? 0.6256 1.1338 1.2557 0.1196  -0.2423 -0.0491 416 ASN C C   
9022  O O   . ASN C 416 ? 0.6529 1.2032 1.3167 0.1116  -0.2607 -0.0653 416 ASN C O   
9023  C CB  . ASN C 416 ? 0.7563 1.2071 1.2748 0.1375  -0.2613 -0.0442 416 ASN C CB  
9024  C CG  . ASN C 416 ? 0.8642 1.2761 1.3322 0.1305  -0.2684 -0.0524 416 ASN C CG  
9025  O OD1 . ASN C 416 ? 0.9259 1.3485 1.3920 0.1187  -0.2871 -0.0732 416 ASN C OD1 
9026  N ND2 . ASN C 416 ? 0.8739 1.2394 1.3013 0.1372  -0.2524 -0.0372 416 ASN C ND2 
9027  N N   . PRO C 417 ? 0.5922 1.0959 1.2291 0.1348  -0.2205 -0.0294 417 PRO C N   
9028  C CA  . PRO C 417 ? 0.6280 1.1785 1.3061 0.1493  -0.2188 -0.0223 417 PRO C CA  
9029  C C   . PRO C 417 ? 0.7002 1.2707 1.3482 0.1798  -0.2401 -0.0104 417 PRO C C   
9030  O O   . PRO C 417 ? 0.7260 1.3287 1.3806 0.1781  -0.2671 -0.0229 417 PRO C O   
9031  C CB  . PRO C 417 ? 0.5951 1.1210 1.2771 0.1568  -0.1861 -0.0056 417 PRO C CB  
9032  C CG  . PRO C 417 ? 0.5575 1.0238 1.1816 0.1593  -0.1775 0.0027  417 PRO C CG  
9033  C CD  . PRO C 417 ? 0.5454 0.9983 1.1456 0.1427  -0.1978 -0.0126 417 PRO C CD  
9034  N N   . SER D 10  ? 0.9434 1.0772 1.4690 0.1339  0.1571  0.0269  10  SER D N   
9035  C CA  . SER D 10  ? 0.9707 1.0718 1.4656 0.1356  0.1875  0.0036  10  SER D CA  
9036  C C   . SER D 10  ? 0.9535 1.0372 1.3803 0.1301  0.1864  -0.0124 10  SER D C   
9037  O O   . SER D 10  ? 1.0194 1.0731 1.4089 0.1280  0.2062  -0.0316 10  SER D O   
9038  C CB  . SER D 10  ? 0.9266 1.0096 1.4568 0.1439  0.1950  0.0064  10  SER D CB  
9039  O OG  . SER D 10  ? 0.9480 0.9971 1.4505 0.1443  0.2254  -0.0167 10  SER D OG  
9040  N N   . LYS D 11  ? 0.8526 0.9546 1.2641 0.1266  0.1632  -0.0035 11  LYS D N   
9041  C CA  . LYS D 11  ? 0.7716 0.8612 1.1270 0.1219  0.1593  -0.0140 11  LYS D CA  
9042  C C   . LYS D 11  ? 0.5284 0.5911 0.8694 0.1254  0.1607  -0.0197 11  LYS D C   
9043  O O   . LYS D 11  ? 0.5613 0.5964 0.8928 0.1259  0.1805  -0.0341 11  LYS D O   
9044  C CB  . LYS D 11  ? 0.7164 0.7953 1.0233 0.1128  0.1770  -0.0320 11  LYS D CB  
9045  C CG  . LYS D 11  ? 0.6654 0.7592 0.9435 0.1065  0.1632  -0.0291 11  LYS D CG  
9046  C CD  . LYS D 11  ? 0.6697 0.7716 0.9327 0.0983  0.1725  -0.0340 11  LYS D CD  
9047  C CE  . LYS D 11  ? 0.7473 0.8254 0.9831 0.0932  0.1972  -0.0500 11  LYS D CE  
9048  N NZ  . LYS D 11  ? 0.7864 0.8752 1.0155 0.0855  0.2056  -0.0508 11  LYS D NZ  
9049  N N   . PRO D 12  ? 0.4398 0.5108 0.7820 0.1275  0.1389  -0.0068 12  PRO D N   
9050  C CA  . PRO D 12  ? 0.4347 0.4845 0.7645 0.1282  0.1316  -0.0058 12  PRO D CA  
9051  C C   . PRO D 12  ? 0.4429 0.4642 0.7097 0.1187  0.1412  -0.0258 12  PRO D C   
9052  O O   . PRO D 12  ? 0.4016 0.4250 0.6282 0.1099  0.1443  -0.0348 12  PRO D O   
9053  C CB  . PRO D 12  ? 0.3987 0.4684 0.7231 0.1235  0.0985  0.0157  12  PRO D CB  
9054  C CG  . PRO D 12  ? 0.3843 0.4734 0.6852 0.1159  0.0912  0.0158  12  PRO D CG  
9055  C CD  . PRO D 12  ? 0.3822 0.4790 0.7127 0.1202  0.1117  0.0082  12  PRO D CD  
9056  N N   . ASN D 13  ? 0.4697 0.4639 0.7304 0.1193  0.1445  -0.0311 13  ASN D N   
9057  C CA  . ASN D 13  ? 0.5070 0.4721 0.7105 0.1078  0.1496  -0.0477 13  ASN D CA  
9058  C C   . ASN D 13  ? 0.4540 0.4205 0.6307 0.0998  0.1242  -0.0364 13  ASN D C   
9059  O O   . ASN D 13  ? 0.4561 0.4041 0.5888 0.0883  0.1224  -0.0453 13  ASN D O   
9060  C CB  . ASN D 13  ? 0.6026 0.5300 0.8122 0.1110  0.1737  -0.0650 13  ASN D CB  
9061  C CG  . ASN D 13  ? 0.6913 0.6106 0.9027 0.1127  0.2037  -0.0819 13  ASN D CG  
9062  O OD1 . ASN D 13  ? 0.7024 0.6277 0.8780 0.1039  0.2087  -0.0893 13  ASN D OD1 
9063  N ND2 . ASN D 13  ? 0.7211 0.6320 0.9695 0.1194  0.2161  -0.0825 13  ASN D ND2 
9064  N N   . LEU D 14  ? 0.3842 0.3739 0.5871 0.1043  0.1043  -0.0153 14  LEU D N   
9065  C CA  . LEU D 14  ? 0.3212 0.3148 0.5045 0.0978  0.0836  -0.0024 14  LEU D CA  
9066  C C   . LEU D 14  ? 0.3036 0.3272 0.5002 0.0995  0.0653  0.0176  14  LEU D C   
9067  O O   . LEU D 14  ? 0.3012 0.3371 0.5374 0.1068  0.0618  0.0284  14  LEU D O   
9068  C CB  . LEU D 14  ? 0.3423 0.3127 0.5404 0.0991  0.0819  0.0009  14  LEU D CB  
9069  C CG  . LEU D 14  ? 0.3400 0.3078 0.5178 0.0904  0.0650  0.0123  14  LEU D CG  
9070  C CD1 . LEU D 14  ? 0.3483 0.3023 0.4811 0.0778  0.0661  0.0001  14  LEU D CD1 
9071  C CD2 . LEU D 14  ? 0.3701 0.3173 0.5771 0.0942  0.0636  0.0186  14  LEU D CD2 
9072  N N   . LEU D 15  ? 0.3431 0.3773 0.5063 0.0917  0.0540  0.0227  15  LEU D N   
9073  C CA  . LEU D 15  ? 0.2973 0.3541 0.4595 0.0901  0.0384  0.0388  15  LEU D CA  
9074  C C   . LEU D 15  ? 0.3461 0.4013 0.4918 0.0846  0.0276  0.0510  15  LEU D C   
9075  O O   . LEU D 15  ? 0.3913 0.4346 0.5185 0.0801  0.0315  0.0453  15  LEU D O   
9076  C CB  . LEU D 15  ? 0.2751 0.3443 0.4117 0.0860  0.0398  0.0318  15  LEU D CB  
9077  C CG  . LEU D 15  ? 0.2760 0.3457 0.4231 0.0891  0.0532  0.0185  15  LEU D CG  
9078  C CD1 . LEU D 15  ? 0.2819 0.3601 0.4001 0.0834  0.0536  0.0124  15  LEU D CD1 
9079  C CD2 . LEU D 15  ? 0.2559 0.3378 0.4478 0.0958  0.0507  0.0273  15  LEU D CD2 
9080  N N   . VAL D 16  ? 0.3372 0.4046 0.4882 0.0831  0.0136  0.0692  16  VAL D N   
9081  C CA  . VAL D 16  ? 0.3507 0.4165 0.4878 0.0774  0.0058  0.0828  16  VAL D CA  
9082  C C   . VAL D 16  ? 0.3690 0.4496 0.4780 0.0706  -0.0023 0.0927  16  VAL D C   
9083  O O   . VAL D 16  ? 0.3620 0.4526 0.4748 0.0693  -0.0124 0.1003  16  VAL D O   
9084  C CB  . VAL D 16  ? 0.3836 0.4414 0.5536 0.0802  -0.0029 0.0987  16  VAL D CB  
9085  C CG1 . VAL D 16  ? 0.3506 0.4062 0.5057 0.0728  -0.0098 0.1140  16  VAL D CG1 
9086  C CG2 . VAL D 16  ? 0.3690 0.4062 0.5650 0.0870  0.0086  0.0857  16  VAL D CG2 
9087  N N   . LEU D 17  ? 0.3775 0.4582 0.4586 0.0654  0.0029  0.0923  17  LEU D N   
9088  C CA  . LEU D 17  ? 0.3950 0.4842 0.4443 0.0585  0.0012  0.0991  17  LEU D CA  
9089  C C   . LEU D 17  ? 0.3680 0.4560 0.4079 0.0526  -0.0002 0.1153  17  LEU D C   
9090  O O   . LEU D 17  ? 0.3815 0.4674 0.4205 0.0519  0.0087  0.1141  17  LEU D O   
9091  C CB  . LEU D 17  ? 0.4119 0.5034 0.4389 0.0585  0.0141  0.0839  17  LEU D CB  
9092  C CG  . LEU D 17  ? 0.4593 0.5543 0.4518 0.0520  0.0177  0.0874  17  LEU D CG  
9093  C CD1 . LEU D 17  ? 0.4566 0.5534 0.4346 0.0472  0.0067  0.0889  17  LEU D CD1 
9094  C CD2 . LEU D 17  ? 0.4798 0.5750 0.4607 0.0540  0.0331  0.0746  17  LEU D CD2 
9095  N N   . PRO D 18  ? 0.3710 0.4612 0.4047 0.0467  -0.0127 0.1328  18  PRO D N   
9096  C CA  . PRO D 18  ? 0.3950 0.4840 0.4155 0.0391  -0.0130 0.1502  18  PRO D CA  
9097  C C   . PRO D 18  ? 0.4390 0.5315 0.4201 0.0334  0.0026  0.1458  18  PRO D C   
9098  O O   . PRO D 18  ? 0.4511 0.5446 0.4049 0.0311  0.0059  0.1358  18  PRO D O   
9099  C CB  . PRO D 18  ? 0.3975 0.4875 0.4176 0.0325  -0.0328 0.1706  18  PRO D CB  
9100  C CG  . PRO D 18  ? 0.3599 0.4518 0.4133 0.0403  -0.0430 0.1651  18  PRO D CG  
9101  C CD  . PRO D 18  ? 0.3577 0.4517 0.4009 0.0453  -0.0292 0.1410  18  PRO D CD  
9102  N N   . VAL D 19  ? 0.4080 0.5013 0.3896 0.0310  0.0134  0.1528  19  VAL D N   
9103  C CA  . VAL D 19  ? 0.4133 0.5106 0.3675 0.0275  0.0334  0.1497  19  VAL D CA  
9104  C C   . VAL D 19  ? 0.4551 0.5532 0.3966 0.0181  0.0373  0.1703  19  VAL D C   
9105  O O   . VAL D 19  ? 0.4668 0.5631 0.4305 0.0160  0.0250  0.1861  19  VAL D O   
9106  C CB  . VAL D 19  ? 0.4739 0.5757 0.4500 0.0348  0.0476  0.1375  19  VAL D CB  
9107  C CG1 . VAL D 19  ? 0.4275 0.5274 0.4114 0.0423  0.0446  0.1185  19  VAL D CG1 
9108  C CG2 . VAL D 19  ? 0.4871 0.5891 0.4966 0.0346  0.0431  0.1476  19  VAL D CG2 
9109  N N   . GLN D 20  ? 0.4744 0.5732 0.3797 0.0120  0.0559  0.1702  20  GLN D N   
9110  C CA  . GLN D 20  ? 0.5060 0.6052 0.3925 0.0012  0.0634  0.1903  20  GLN D CA  
9111  C C   . GLN D 20  ? 0.5128 0.6187 0.3970 0.0016  0.0943  0.1888  20  GLN D C   
9112  O O   . GLN D 20  ? 0.5374 0.6427 0.4096 0.0067  0.1128  0.1715  20  GLN D O   
9113  C CB  . GLN D 20  ? 0.5654 0.6551 0.3991 -0.0121 0.0557  0.1975  20  GLN D CB  
9114  C CG  . GLN D 20  ? 0.6748 0.7632 0.4871 -0.0256 0.0584  0.2217  20  GLN D CG  
9115  C CD  . GLN D 20  ? 0.8143 0.8916 0.5742 -0.0418 0.0422  0.2329  20  GLN D CD  
9116  O OE1 . GLN D 20  ? 0.8959 0.9637 0.5973 -0.0538 0.0585  0.2297  20  GLN D OE1 
9117  N NE2 . GLN D 20  ? 0.8431 0.9201 0.6238 -0.0432 0.0099  0.2467  20  GLN D NE2 
9118  N N   . GLU D 21  ? 0.5161 0.6284 0.4152 -0.0037 0.1006  0.2082  21  GLU D N   
9119  C CA  . GLU D 21  ? 0.5508 0.6727 0.4553 -0.0036 0.1319  0.2106  21  GLU D CA  
9120  C C   . GLU D 21  ? 0.6147 0.7282 0.4605 -0.0139 0.1546  0.2116  21  GLU D C   
9121  O O   . GLU D 21  ? 0.6533 0.7574 0.4601 -0.0269 0.1430  0.2246  21  GLU D O   
9122  C CB  . GLU D 21  ? 0.5735 0.7063 0.5193 -0.0071 0.1302  0.2325  21  GLU D CB  
9123  C CG  . GLU D 21  ? 0.6208 0.7701 0.6005 -0.0031 0.1580  0.2353  21  GLU D CG  
9124  C CD  . GLU D 21  ? 0.7052 0.8592 0.6650 -0.0127 0.1863  0.2508  21  GLU D CD  
9125  O OE1 . GLU D 21  ? 0.7607 0.9012 0.6714 -0.0244 0.1828  0.2564  21  GLU D OE1 
9126  O OE2 . GLU D 21  ? 0.6906 0.8566 0.6863 -0.0095 0.2056  0.2506  21  GLU D OE2 
9127  N N   . ASP D 22  ? 0.6330 0.7478 0.4718 -0.0087 0.1870  0.1978  22  ASP D N   
9128  C CA  . ASP D 22  ? 0.6900 0.7898 0.4731 -0.0198 0.2127  0.1909  22  ASP D CA  
9129  C C   . ASP D 22  ? 0.6997 0.8085 0.5071 -0.0242 0.2345  0.2009  22  ASP D C   
9130  O O   . ASP D 22  ? 0.6086 0.7327 0.4692 -0.0131 0.2494  0.1973  22  ASP D O   
9131  C CB  . ASP D 22  ? 0.6854 0.7732 0.4488 -0.0139 0.2318  0.1612  22  ASP D CB  
9132  C CG  . ASP D 22  ? 0.7806 0.8526 0.4897 -0.0286 0.2558  0.1485  22  ASP D CG  
9133  O OD1 . ASP D 22  ? 0.8571 0.9141 0.5037 -0.0464 0.2449  0.1531  22  ASP D OD1 
9134  O OD2 . ASP D 22  ? 0.7874 0.8652 0.5184 -0.0225 0.2833  0.1357  22  ASP D OD2 
9135  N N   . ALA D 23  ? 0.7191 0.8187 0.4886 -0.0412 0.2348  0.2148  23  ALA D N   
9136  C CA  . ALA D 23  ? 0.7608 0.8706 0.5541 -0.0470 0.2521  0.2286  23  ALA D CA  
9137  C C   . ALA D 23  ? 0.7929 0.9087 0.5981 -0.0430 0.2892  0.2113  23  ALA D C   
9138  O O   . ALA D 23  ? 0.7544 0.8897 0.6191 -0.0350 0.3008  0.2189  23  ALA D O   
9139  C CB  . ALA D 23  ? 0.8224 0.9151 0.5607 -0.0678 0.2468  0.2443  23  ALA D CB  
9140  N N   . SER D 24  ? 0.8359 0.9374 0.5897 -0.0478 0.3047  0.1890  24  SER D N   
9141  C CA  . SER D 24  ? 0.8573 0.9649 0.6210 -0.0424 0.3392  0.1721  24  SER D CA  
9142  C C   . SER D 24  ? 0.8125 0.9347 0.6524 -0.0198 0.3467  0.1650  24  SER D C   
9143  O O   . SER D 24  ? 0.8117 0.9486 0.6975 -0.0137 0.3677  0.1700  24  SER D O   
9144  C CB  . SER D 24  ? 0.9084 0.9988 0.6062 -0.0479 0.3468  0.1494  24  SER D CB  
9145  O OG  . SER D 24  ? 0.9433 1.0339 0.6542 -0.0376 0.3795  0.1311  24  SER D OG  
9146  N N   . THR D 25  ? 0.7586 0.8774 0.6126 -0.0085 0.3278  0.1560  25  THR D N   
9147  C CA  . THR D 25  ? 0.6781 0.8078 0.5952 0.0106  0.3310  0.1486  25  THR D CA  
9148  C C   . THR D 25  ? 0.6106 0.7611 0.5920 0.0181  0.3090  0.1690  25  THR D C   
9149  O O   . THR D 25  ? 0.5644 0.7289 0.6058 0.0302  0.3113  0.1709  25  THR D O   
9150  C CB  . THR D 25  ? 0.6335 0.7475 0.5280 0.0174  0.3234  0.1261  25  THR D CB  
9151  O OG1 . THR D 25  ? 0.6055 0.7157 0.4799 0.0141  0.2936  0.1322  25  THR D OG1 
9152  C CG2 . THR D 25  ? 0.6948 0.7875 0.5260 0.0094  0.3417  0.1051  25  THR D CG2 
9153  N N   . GLY D 26  ? 0.6056 0.7577 0.5749 0.0101  0.2854  0.1857  26  GLY D N   
9154  C CA  . GLY D 26  ? 0.5524 0.7229 0.5774 0.0146  0.2619  0.2045  26  GLY D CA  
9155  C C   . GLY D 26  ? 0.5245 0.6952 0.5621 0.0243  0.2425  0.1957  26  GLY D C   
9156  O O   . GLY D 26  ? 0.4729 0.6576 0.5556 0.0268  0.2232  0.2080  26  GLY D O   
9157  N N   . LEU D 27  ? 0.5582 0.7119 0.5529 0.0274  0.2473  0.1742  27  LEU D N   
9158  C CA  . LEU D 27  ? 0.5280 0.6796 0.5268 0.0362  0.2317  0.1628  27  LEU D CA  
9159  C C   . LEU D 27  ? 0.4999 0.6397 0.4598 0.0294  0.2033  0.1626  27  LEU D C   
9160  O O   . LEU D 27  ? 0.5070 0.6400 0.4316 0.0185  0.2002  0.1729  27  LEU D O   
9161  C CB  . LEU D 27  ? 0.5509 0.6876 0.5309 0.0426  0.2483  0.1371  27  LEU D CB  
9162  C CG  . LEU D 27  ? 0.5739 0.7174 0.5970 0.0497  0.2699  0.1338  27  LEU D CG  
9163  C CD1 . LEU D 27  ? 0.6167 0.7417 0.6171 0.0545  0.2858  0.1090  27  LEU D CD1 
9164  C CD2 . LEU D 27  ? 0.5060 0.6699 0.5971 0.0578  0.2561  0.1468  27  LEU D CD2 
9165  N N   . HIS D 28  ? 0.4916 0.6278 0.4620 0.0350  0.1797  0.1509  28  HIS D N   
9166  C CA  . HIS D 28  ? 0.4826 0.6081 0.4299 0.0304  0.1504  0.1486  28  HIS D CA  
9167  C C   . HIS D 28  ? 0.5308 0.6433 0.4457 0.0331  0.1476  0.1279  28  HIS D C   
9168  O O   . HIS D 28  ? 0.5539 0.6665 0.4796 0.0411  0.1596  0.1143  28  HIS D O   
9169  C CB  . HIS D 28  ? 0.4058 0.5368 0.3951 0.0330  0.1254  0.1536  28  HIS D CB  
9170  C CG  . HIS D 28  ? 0.3931 0.5325 0.4103 0.0272  0.1221  0.1747  28  HIS D CG  
9171  N ND1 . HIS D 28  ? 0.3803 0.5134 0.3977 0.0209  0.1014  0.1864  28  HIS D ND1 
9172  C CD2 . HIS D 28  ? 0.4153 0.5689 0.4648 0.0262  0.1371  0.1877  28  HIS D CD2 
9173  C CE1 . HIS D 28  ? 0.4115 0.5525 0.4564 0.0155  0.1030  0.2046  28  HIS D CE1 
9174  N NE2 . HIS D 28  ? 0.4068 0.5617 0.4720 0.0181  0.1242  0.2063  28  HIS D NE2 
9175  N N   . TRP D 29  ? 0.5642 0.6659 0.4432 0.0255  0.1301  0.1277  29  TRP D N   
9176  C CA  . TRP D 29  ? 0.5358 0.6248 0.3819 0.0246  0.1243  0.1106  29  TRP D CA  
9177  C C   . TRP D 29  ? 0.5509 0.6384 0.3991 0.0213  0.0922  0.1154  29  TRP D C   
9178  O O   . TRP D 29  ? 0.5487 0.6407 0.4132 0.0183  0.0774  0.1321  29  TRP D O   
9179  C CB  . TRP D 29  ? 0.5520 0.6255 0.3384 0.0141  0.1427  0.1056  29  TRP D CB  
9180  C CG  . TRP D 29  ? 0.5902 0.6591 0.3410 -0.0011 0.1336  0.1242  29  TRP D CG  
9181  C CD1 . TRP D 29  ? 0.5800 0.6549 0.3323 -0.0061 0.1460  0.1420  29  TRP D CD1 
9182  C CD2 . TRP D 29  ? 0.6702 0.7285 0.3816 -0.0145 0.1082  0.1298  29  TRP D CD2 
9183  N NE1 . TRP D 29  ? 0.5980 0.6653 0.3116 -0.0218 0.1300  0.1582  29  TRP D NE1 
9184  C CE2 . TRP D 29  ? 0.6753 0.7327 0.3641 -0.0274 0.1054  0.1518  29  TRP D CE2 
9185  C CE3 . TRP D 29  ? 0.7206 0.7716 0.4178 -0.0178 0.0857  0.1207  29  TRP D CE3 
9186  C CZ2 . TRP D 29  ? 0.7253 0.7739 0.3763 -0.0438 0.0794  0.1661  29  TRP D CZ2 
9187  C CZ3 . TRP D 29  ? 0.7533 0.7972 0.4166 -0.0340 0.0598  0.1349  29  TRP D CZ3 
9188  C CH2 . TRP D 29  ? 0.7479 0.7904 0.3880 -0.0469 0.0560  0.1578  29  TRP D CH2 
9189  N N   . ALA D 30  ? 0.5761 0.6574 0.4128 0.0222  0.0825  0.1014  30  ALA D N   
9190  C CA  . ALA D 30  ? 0.5462 0.6281 0.3911 0.0199  0.0546  0.1061  30  ALA D CA  
9191  C C   . ALA D 30  ? 0.5438 0.6151 0.3485 0.0107  0.0466  0.0981  30  ALA D C   
9192  O O   . ALA D 30  ? 0.5398 0.6021 0.3210 0.0107  0.0618  0.0815  30  ALA D O   
9193  C CB  . ALA D 30  ? 0.4753 0.5644 0.3664 0.0317  0.0473  0.0983  30  ALA D CB  
9194  N N   . ASN D 31  ? 0.5854 0.6569 0.3848 0.0020  0.0216  0.1113  31  ASN D N   
9195  C CA  . ASN D 31  ? 0.6497 0.7142 0.4233 -0.0075 0.0057  0.1062  31  ASN D CA  
9196  C C   . ASN D 31  ? 0.6341 0.7077 0.4516 0.0036  -0.0028 0.0963  31  ASN D C   
9197  O O   . ASN D 31  ? 0.6241 0.7086 0.4873 0.0115  -0.0139 0.1050  31  ASN D O   
9198  C CB  . ASN D 31  ? 0.6981 0.7617 0.4544 -0.0228 -0.0212 0.1288  31  ASN D CB  
9199  C CG  . ASN D 31  ? 0.7802 0.8281 0.4695 -0.0407 -0.0140 0.1344  31  ASN D CG  
9200  O OD1 . ASN D 31  ? 0.8215 0.8705 0.5035 -0.0469 -0.0169 0.1540  31  ASN D OD1 
9201  N ND2 . ASN D 31  ? 0.8183 0.8488 0.4559 -0.0500 -0.0031 0.1167  31  ASN D ND2 
9202  N N   . ILE D 32  ? 0.6633 0.7302 0.4667 0.0042  0.0056  0.0774  32  ILE D N   
9203  C CA  . ILE D 32  ? 0.6338 0.7080 0.4723 0.0122  -0.0007 0.0678  32  ILE D CA  
9204  C C   . ILE D 32  ? 0.6626 0.7350 0.4888 0.0002  -0.0228 0.0700  32  ILE D C   
9205  O O   . ILE D 32  ? 0.7624 0.8197 0.5386 -0.0143 -0.0252 0.0660  32  ILE D O   
9206  C CB  . ILE D 32  ? 0.7724 0.8414 0.6109 0.0208  0.0214  0.0477  32  ILE D CB  
9207  C CG1 . ILE D 32  ? 0.7631 0.8359 0.6179 0.0307  0.0402  0.0486  32  ILE D CG1 
9208  C CG2 . ILE D 32  ? 0.7285 0.8051 0.6016 0.0278  0.0161  0.0396  32  ILE D CG2 
9209  C CD1 . ILE D 32  ? 0.7293 0.8143 0.6299 0.0400  0.0339  0.0550  32  ILE D CD1 
9210  N N   . HIS D 33  ? 0.5664 0.6529 0.4382 0.0049  -0.0385 0.0765  33  HIS D N   
9211  C CA  . HIS D 33  ? 0.5377 0.6269 0.4097 -0.0065 -0.0612 0.0815  33  HIS D CA  
9212  C C   . HIS D 33  ? 0.5314 0.6181 0.4067 -0.0042 -0.0532 0.0627  33  HIS D C   
9213  O O   . HIS D 33  ? 0.5020 0.5964 0.4126 0.0097  -0.0402 0.0542  33  HIS D O   
9214  C CB  . HIS D 33  ? 0.5143 0.6217 0.4413 -0.0027 -0.0812 0.1011  33  HIS D CB  
9215  C CG  . HIS D 33  ? 0.5530 0.6613 0.4766 -0.0083 -0.0951 0.1236  33  HIS D CG  
9216  N ND1 . HIS D 33  ? 0.5522 0.6577 0.4770 -0.0002 -0.0809 0.1263  33  HIS D ND1 
9217  C CD2 . HIS D 33  ? 0.5991 0.7107 0.5193 -0.0228 -0.1238 0.1468  33  HIS D CD2 
9218  C CE1 . HIS D 33  ? 0.5700 0.6762 0.4913 -0.0088 -0.0987 0.1496  33  HIS D CE1 
9219  N NE2 . HIS D 33  ? 0.6063 0.7163 0.5245 -0.0226 -0.1255 0.1631  33  HIS D NE2 
9220  N N   . LYS D 34  ? 0.5763 0.6488 0.4096 -0.0197 -0.0609 0.0562  34  LYS D N   
9221  C CA  . LYS D 34  ? 0.5352 0.6008 0.3656 -0.0204 -0.0545 0.0387  34  LYS D CA  
9222  C C   . LYS D 34  ? 0.5425 0.6032 0.3557 -0.0402 -0.0803 0.0430  34  LYS D C   
9223  O O   . LYS D 34  ? 0.5616 0.6167 0.3442 -0.0569 -0.1007 0.0561  34  LYS D O   
9224  C CB  . LYS D 34  ? 0.5589 0.6021 0.3464 -0.0187 -0.0286 0.0192  34  LYS D CB  
9225  C CG  . LYS D 34  ? 0.5677 0.6144 0.3678 -0.0025 -0.0044 0.0169  34  LYS D CG  
9226  C CD  . LYS D 34  ? 0.5924 0.6447 0.4266 0.0120  0.0110  0.0061  34  LYS D CD  
9227  C CE  . LYS D 34  ? 0.6700 0.7031 0.4794 0.0083  0.0221  -0.0112 34  LYS D CE  
9228  N NZ  . LYS D 34  ? 0.6948 0.7297 0.5298 0.0215  0.0398  -0.0196 34  LYS D NZ  
9229  N N   . ARG D 35  ? 0.5377 0.5991 0.3677 -0.0404 -0.0800 0.0327  35  ARG D N   
9230  C CA  . ARG D 35  ? 0.5759 0.6280 0.3859 -0.0608 -0.1017 0.0320  35  ARG D CA  
9231  C C   . ARG D 35  ? 0.5890 0.6639 0.4401 -0.0706 -0.1347 0.0553  35  ARG D C   
9232  O O   . ARG D 35  ? 0.5678 0.6644 0.4612 -0.0622 -0.1422 0.0738  35  ARG D O   
9233  C CB  . ARG D 35  ? 0.6645 0.6837 0.3949 -0.0801 -0.1036 0.0235  35  ARG D CB  
9234  C CG  . ARG D 35  ? 0.7022 0.6979 0.3982 -0.0705 -0.0689 0.0003  35  ARG D CG  
9235  C CD  . ARG D 35  ? 0.7886 0.7527 0.4084 -0.0859 -0.0624 -0.0075 35  ARG D CD  
9236  N NE  . ARG D 35  ? 0.8287 0.7812 0.4377 -0.0699 -0.0250 -0.0228 35  ARG D NE  
9237  C CZ  . ARG D 35  ? 0.9222 0.8461 0.4712 -0.0770 -0.0051 -0.0343 35  ARG D CZ  
9238  N NH1 . ARG D 35  ? 1.0103 0.9105 0.4935 -0.1021 -0.0196 -0.0337 35  ARG D NH1 
9239  N NH2 . ARG D 35  ? 0.9005 0.8195 0.4557 -0.0599 0.0296  -0.0453 35  ARG D NH2 
9240  N N   . THR D 36  ? 0.6595 0.7283 0.5012 -0.0890 -0.1546 0.0547  36  THR D N   
9241  C CA  . THR D 36  ? 0.6862 0.7749 0.5631 -0.1038 -0.1909 0.0791  36  THR D CA  
9242  C C   . THR D 36  ? 0.7578 0.8196 0.5653 -0.1353 -0.2175 0.0796  36  THR D C   
9243  O O   . THR D 36  ? 0.8156 0.8543 0.5876 -0.1476 -0.2158 0.0617  36  THR D O   
9244  C CB  . THR D 36  ? 0.5518 0.6637 0.4962 -0.0981 -0.1925 0.0814  36  THR D CB  
9245  O OG1 . THR D 36  ? 0.5088 0.6387 0.5040 -0.0710 -0.1638 0.0768  36  THR D OG1 
9246  C CG2 . THR D 36  ? 0.5364 0.6743 0.5315 -0.1107 -0.2284 0.1103  36  THR D CG2 
9247  N N   . PRO D 37  ? 0.7635 0.8251 0.5479 -0.1503 -0.2428 0.1003  37  PRO D N   
9248  C CA  . PRO D 37  ? 0.7353 0.8210 0.5604 -0.1393 -0.2499 0.1249  37  PRO D CA  
9249  C C   . PRO D 37  ? 0.7354 0.8140 0.5447 -0.1181 -0.2149 0.1127  37  PRO D C   
9250  O O   . PRO D 37  ? 0.8196 0.8701 0.5664 -0.1196 -0.1919 0.0899  37  PRO D O   
9251  C CB  . PRO D 37  ? 0.7919 0.8662 0.5682 -0.1696 -0.2881 0.1463  37  PRO D CB  
9252  C CG  . PRO D 37  ? 0.8452 0.8773 0.5271 -0.1914 -0.2832 0.1218  37  PRO D CG  
9253  C CD  . PRO D 37  ? 0.8173 0.8469 0.5199 -0.1838 -0.2671 0.0993  37  PRO D CD  
9254  N N   . LEU D 38  ? 0.6463 0.7494 0.5148 -0.0988 -0.2104 0.1278  38  LEU D N   
9255  C CA  . LEU D 38  ? 0.6023 0.7018 0.4667 -0.0786 -0.1790 0.1179  38  LEU D CA  
9256  C C   . LEU D 38  ? 0.6425 0.7202 0.4361 -0.0917 -0.1796 0.1211  38  LEU D C   
9257  O O   . LEU D 38  ? 0.6736 0.7498 0.4465 -0.1118 -0.2100 0.1430  38  LEU D O   
9258  C CB  . LEU D 38  ? 0.5621 0.6886 0.5047 -0.0584 -0.1776 0.1342  38  LEU D CB  
9259  C CG  . LEU D 38  ? 0.5215 0.6503 0.4875 -0.0334 -0.1436 0.1198  38  LEU D CG  
9260  C CD1 . LEU D 38  ? 0.4929 0.6209 0.4696 -0.0236 -0.1218 0.0965  38  LEU D CD1 
9261  C CD2 . LEU D 38  ? 0.4782 0.6264 0.5117 -0.0184 -0.1461 0.1376  38  LEU D CD2 
9262  N N   . MET D 39  ? 0.6259 0.6867 0.3822 -0.0824 -0.1470 0.1013  39  MET D N   
9263  C CA  . MET D 39  ? 0.6834 0.7260 0.3786 -0.0930 -0.1419 0.1054  39  MET D CA  
9264  C C   . MET D 39  ? 0.6924 0.7340 0.3920 -0.0729 -0.1065 0.0947  39  MET D C   
9265  O O   . MET D 39  ? 0.6686 0.7208 0.4119 -0.0528 -0.0877 0.0828  39  MET D O   
9266  C CB  . MET D 39  ? 0.7657 0.7752 0.3752 -0.1177 -0.1437 0.0918  39  MET D CB  
9267  C CG  . MET D 39  ? 0.7821 0.7745 0.3762 -0.1136 -0.1218 0.0618  39  MET D CG  
9268  S SD  . MET D 39  ? 1.1889 1.1682 0.7691 -0.0925 -0.0715 0.0373  39  MET D SD  
9269  C CE  . MET D 39  ? 0.8843 0.8297 0.3682 -0.1145 -0.0617 0.0347  39  MET D CE  
9270  N N   . GLN D 40  ? 0.7456 0.7754 0.4008 -0.0803 -0.0990 0.1011  40  GLN D N   
9271  C CA  . GLN D 40  ? 0.6922 0.7242 0.3570 -0.0636 -0.0687 0.0962  40  GLN D CA  
9272  C C   . GLN D 40  ? 0.6981 0.7065 0.3094 -0.0649 -0.0358 0.0732  40  GLN D C   
9273  O O   . GLN D 40  ? 0.7607 0.7451 0.3034 -0.0844 -0.0348 0.0689  40  GLN D O   
9274  C CB  . GLN D 40  ? 0.7362 0.7736 0.3978 -0.0689 -0.0786 0.1213  40  GLN D CB  
9275  C CG  . GLN D 40  ? 0.7756 0.8358 0.5021 -0.0627 -0.1053 0.1448  40  GLN D CG  
9276  C CD  . GLN D 40  ? 0.8496 0.9122 0.5734 -0.0684 -0.1152 0.1710  40  GLN D CD  
9277  O OE1 . GLN D 40  ? 0.8518 0.9241 0.6167 -0.0529 -0.1041 0.1761  40  GLN D OE1 
9278  N NE2 . GLN D 40  ? 0.9160 0.9679 0.5886 -0.0927 -0.1374 0.1883  40  GLN D NE2 
9279  N N   . VAL D 41  ? 0.6525 0.6668 0.2964 -0.0447 -0.0086 0.0591  41  VAL D N   
9280  C CA  . VAL D 41  ? 0.7121 0.7084 0.3243 -0.0410 0.0259  0.0396  41  VAL D CA  
9281  C C   . VAL D 41  ? 0.6590 0.6669 0.2969 -0.0273 0.0476  0.0462  41  VAL D C   
9282  O O   . VAL D 41  ? 0.6233 0.6499 0.3179 -0.0109 0.0487  0.0483  41  VAL D O   
9283  C CB  . VAL D 41  ? 0.7817 0.7750 0.4169 -0.0294 0.0383  0.0187  41  VAL D CB  
9284  C CG1 . VAL D 41  ? 0.8856 0.8554 0.4852 -0.0280 0.0728  -0.0009 41  VAL D CG1 
9285  C CG2 . VAL D 41  ? 0.7944 0.7840 0.4258 -0.0402 0.0128  0.0153  41  VAL D CG2 
9286  N N   . PRO D 42  ? 0.6900 0.6856 0.2851 -0.0352 0.0663  0.0488  42  PRO D N   
9287  C CA  . PRO D 42  ? 0.6475 0.6566 0.2738 -0.0226 0.0874  0.0567  42  PRO D CA  
9288  C C   . PRO D 42  ? 0.6255 0.6351 0.2798 -0.0059 0.1176  0.0397  42  PRO D C   
9289  O O   . PRO D 42  ? 0.6716 0.6607 0.2921 -0.0083 0.1399  0.0219  42  PRO D O   
9290  C CB  . PRO D 42  ? 0.7016 0.6968 0.2707 -0.0385 0.0988  0.0656  42  PRO D CB  
9291  C CG  . PRO D 42  ? 0.7744 0.7408 0.2739 -0.0565 0.0979  0.0513  42  PRO D CG  
9292  C CD  . PRO D 42  ? 0.7624 0.7324 0.2796 -0.0580 0.0667  0.0479  42  PRO D CD  
9293  N N   . LEU D 43  ? 0.5681 0.5991 0.2836 0.0096  0.1165  0.0457  43  LEU D N   
9294  C CA  . LEU D 43  ? 0.5502 0.5865 0.3038 0.0249  0.1371  0.0352  43  LEU D CA  
9295  C C   . LEU D 43  ? 0.5181 0.5727 0.3150 0.0339  0.1475  0.0489  43  LEU D C   
9296  O O   . LEU D 43  ? 0.5133 0.5799 0.3276 0.0322  0.1310  0.0646  43  LEU D O   
9297  C CB  . LEU D 43  ? 0.5309 0.5735 0.3174 0.0324  0.1203  0.0276  43  LEU D CB  
9298  C CG  . LEU D 43  ? 0.5540 0.5820 0.3124 0.0249  0.1085  0.0143  43  LEU D CG  
9299  C CD1 . LEU D 43  ? 0.4240 0.4627 0.2211 0.0323  0.0936  0.0111  43  LEU D CD1 
9300  C CD2 . LEU D 43  ? 0.6046 0.6095 0.3299 0.0232  0.1334  -0.0036 43  LEU D CD2 
9301  N N   . LEU D 44  ? 0.5080 0.5641 0.3255 0.0430  0.1742  0.0440  44  LEU D N   
9302  C CA  . LEU D 44  ? 0.5050 0.5804 0.3702 0.0505  0.1826  0.0583  44  LEU D CA  
9303  C C   . LEU D 44  ? 0.4764 0.5666 0.3900 0.0574  0.1609  0.0630  44  LEU D C   
9304  O O   . LEU D 44  ? 0.4548 0.5419 0.3769 0.0618  0.1531  0.0521  44  LEU D O   
9305  C CB  . LEU D 44  ? 0.5448 0.6191 0.4257 0.0584  0.2175  0.0538  44  LEU D CB  
9306  C CG  . LEU D 44  ? 0.5355 0.6310 0.4724 0.0640  0.2252  0.0703  44  LEU D CG  
9307  C CD1 . LEU D 44  ? 0.5284 0.6272 0.4512 0.0553  0.2351  0.0832  44  LEU D CD1 
9308  C CD2 . LEU D 44  ? 0.5872 0.6824 0.5629 0.0721  0.2401  0.0626  44  LEU D CD2 
9309  N N   . LEU D 45  ? 0.4561 0.5599 0.3974 0.0564  0.1514  0.0793  45  LEU D N   
9310  C CA  . LEU D 45  ? 0.4083 0.5221 0.3898 0.0602  0.1335  0.0837  45  LEU D CA  
9311  C C   . LEU D 45  ? 0.3772 0.5016 0.3996 0.0668  0.1454  0.0873  45  LEU D C   
9312  O O   . LEU D 45  ? 0.3554 0.4906 0.4010 0.0669  0.1581  0.1005  45  LEU D O   
9313  C CB  . LEU D 45  ? 0.4046 0.5236 0.3970 0.0546  0.1179  0.0990  45  LEU D CB  
9314  C CG  . LEU D 45  ? 0.3632 0.4874 0.3915 0.0556  0.1017  0.1028  45  LEU D CG  
9315  C CD1 . LEU D 45  ? 0.3642 0.4803 0.3853 0.0579  0.0878  0.0885  45  LEU D CD1 
9316  C CD2 . LEU D 45  ? 0.3451 0.4700 0.3837 0.0496  0.0895  0.1168  45  LEU D CD2 
9317  N N   . ASP D 46  ? 0.3927 0.5151 0.4271 0.0715  0.1398  0.0781  46  ASP D N   
9318  C CA  . ASP D 46  ? 0.4102 0.5423 0.4856 0.0771  0.1477  0.0838  46  ASP D CA  
9319  C C   . ASP D 46  ? 0.3760 0.5114 0.4709 0.0740  0.1230  0.0869  46  ASP D C   
9320  O O   . ASP D 46  ? 0.3109 0.4387 0.3963 0.0749  0.1142  0.0763  46  ASP D O   
9321  C CB  . ASP D 46  ? 0.4385 0.5614 0.5083 0.0844  0.1662  0.0709  46  ASP D CB  
9322  C CG  . ASP D 46  ? 0.4288 0.5625 0.5494 0.0916  0.1757  0.0801  46  ASP D CG  
9323  O OD1 . ASP D 46  ? 0.4287 0.5792 0.5884 0.0896  0.1679  0.0979  46  ASP D OD1 
9324  O OD2 . ASP D 46  ? 0.4087 0.5326 0.5319 0.0980  0.1887  0.0704  46  ASP D OD2 
9325  N N   . LEU D 47  ? 0.3687 0.5135 0.4877 0.0686  0.1123  0.1016  47  LEU D N   
9326  C CA  . LEU D 47  ? 0.3527 0.4953 0.4805 0.0620  0.0887  0.1037  47  LEU D CA  
9327  C C   . LEU D 47  ? 0.3472 0.4904 0.4900 0.0632  0.0833  0.1021  47  LEU D C   
9328  O O   . LEU D 47  ? 0.3496 0.4830 0.4767 0.0587  0.0684  0.0942  47  LEU D O   
9329  C CB  . LEU D 47  ? 0.3322 0.4840 0.4880 0.0542  0.0796  0.1216  47  LEU D CB  
9330  C CG  . LEU D 47  ? 0.3061 0.4510 0.4661 0.0440  0.0550  0.1232  47  LEU D CG  
9331  C CD1 . LEU D 47  ? 0.2921 0.4180 0.4167 0.0413  0.0452  0.1081  47  LEU D CD1 
9332  C CD2 . LEU D 47  ? 0.3052 0.4592 0.4971 0.0343  0.0446  0.1427  47  LEU D CD2 
9333  N N   . ASN D 48  ? 0.3422 0.4964 0.5174 0.0691  0.0966  0.1110  48  ASN D N   
9334  C CA  . ASN D 48  ? 0.2872 0.4434 0.4848 0.0698  0.0896  0.1150  48  ASN D CA  
9335  C C   . ASN D 48  ? 0.3093 0.4556 0.4925 0.0788  0.1032  0.1002  48  ASN D C   
9336  O O   . ASN D 48  ? 0.3308 0.4770 0.5327 0.0802  0.0986  0.1038  48  ASN D O   
9337  C CB  . ASN D 48  ? 0.2931 0.4686 0.5476 0.0710  0.0932  0.1374  48  ASN D CB  
9338  C CG  . ASN D 48  ? 0.2868 0.4711 0.5589 0.0587  0.0733  0.1539  48  ASN D CG  
9339  O OD1 . ASN D 48  ? 0.3087 0.4830 0.5604 0.0471  0.0495  0.1516  48  ASN D OD1 
9340  N ND2 . ASN D 48  ? 0.2846 0.4860 0.5945 0.0598  0.0838  0.1705  48  ASN D ND2 
9341  N N   . GLY D 49  ? 0.3353 0.4716 0.4843 0.0830  0.1176  0.0849  49  GLY D N   
9342  C CA  . GLY D 49  ? 0.3458 0.4692 0.4766 0.0892  0.1302  0.0697  49  GLY D CA  
9343  C C   . GLY D 49  ? 0.3342 0.4489 0.4496 0.0852  0.1129  0.0615  49  GLY D C   
9344  O O   . GLY D 49  ? 0.3190 0.4315 0.4152 0.0781  0.0962  0.0586  49  GLY D O   
9345  N N   . LYS D 50  ? 0.3482 0.4564 0.4734 0.0901  0.1195  0.0578  50  LYS D N   
9346  C CA  . LYS D 50  ? 0.3254 0.4267 0.4418 0.0857  0.1047  0.0536  50  LYS D CA  
9347  C C   . LYS D 50  ? 0.3424 0.4314 0.4181 0.0834  0.1043  0.0355  50  LYS D C   
9348  O O   . LYS D 50  ? 0.3357 0.4212 0.3995 0.0780  0.0917  0.0316  50  LYS D O   
9349  C CB  . LYS D 50  ? 0.3128 0.4110 0.4590 0.0913  0.1110  0.0588  50  LYS D CB  
9350  C CG  . LYS D 50  ? 0.3219 0.4350 0.5176 0.0920  0.1055  0.0815  50  LYS D CG  
9351  C CD  . LYS D 50  ? 0.3760 0.4842 0.6031 0.0981  0.1102  0.0872  50  LYS D CD  
9352  C CE  . LYS D 50  ? 0.4518 0.5767 0.7393 0.1008  0.1071  0.1126  50  LYS D CE  
9353  N NZ  . LYS D 50  ? 0.5215 0.6398 0.8458 0.1092  0.1149  0.1185  50  LYS D NZ  
9354  N N   . HIS D 51  ? 0.3439 0.4263 0.3983 0.0863  0.1180  0.0255  51  HIS D N   
9355  C CA  . HIS D 51  ? 0.3397 0.4119 0.3587 0.0821  0.1139  0.0113  51  HIS D CA  
9356  C C   . HIS D 51  ? 0.3661 0.4335 0.3575 0.0808  0.1226  0.0059  51  HIS D C   
9357  O O   . HIS D 51  ? 0.4087 0.4791 0.4052 0.0838  0.1361  0.0113  51  HIS D O   
9358  C CB  . HIS D 51  ? 0.3662 0.4245 0.3801 0.0829  0.1180  0.0011  51  HIS D CB  
9359  C CG  . HIS D 51  ? 0.3617 0.4068 0.3773 0.0891  0.1398  -0.0048 51  HIS D CG  
9360  N ND1 . HIS D 51  ? 0.3771 0.4205 0.4275 0.0964  0.1496  0.0013  51  HIS D ND1 
9361  C CD2 . HIS D 51  ? 0.3669 0.3970 0.3524 0.0883  0.1548  -0.0167 51  HIS D CD2 
9362  C CE1 . HIS D 51  ? 0.3923 0.4199 0.4377 0.1019  0.1731  -0.0082 51  HIS D CE1 
9363  N NE2 . HIS D 51  ? 0.4064 0.4243 0.4078 0.0961  0.1771  -0.0202 51  HIS D NE2 
9364  N N   . LEU D 52  ? 0.3537 0.4145 0.3167 0.0749  0.1138  -0.0028 52  LEU D N   
9365  C CA  . LEU D 52  ? 0.4065 0.4590 0.3361 0.0701  0.1183  -0.0076 52  LEU D CA  
9366  C C   . LEU D 52  ? 0.4808 0.5127 0.3870 0.0689  0.1327  -0.0213 52  LEU D C   
9367  O O   . LEU D 52  ? 0.5108 0.5340 0.4156 0.0672  0.1278  -0.0295 52  LEU D O   
9368  C CB  . LEU D 52  ? 0.4093 0.4652 0.3241 0.0628  0.0986  -0.0074 52  LEU D CB  
9369  C CG  . LEU D 52  ? 0.4600 0.5096 0.3402 0.0544  0.0952  -0.0069 52  LEU D CG  
9370  C CD1 . LEU D 52  ? 0.4436 0.5057 0.3341 0.0516  0.0753  0.0024  52  LEU D CD1 
9371  C CD2 . LEU D 52  ? 0.5091 0.5404 0.3554 0.0461  0.0950  -0.0193 52  LEU D CD2 
9372  N N   . TRP D 53  ? 0.5468 0.5680 0.4309 0.0682  0.1512  -0.0245 53  TRP D N   
9373  C CA  . TRP D 53  ? 0.5954 0.5898 0.4474 0.0649  0.1670  -0.0410 53  TRP D CA  
9374  C C   . TRP D 53  ? 0.6158 0.5964 0.4144 0.0532  0.1706  -0.0454 53  TRP D C   
9375  O O   . TRP D 53  ? 0.5758 0.5676 0.3709 0.0520  0.1719  -0.0342 53  TRP D O   
9376  C CB  . TRP D 53  ? 0.5692 0.5563 0.4481 0.0765  0.1949  -0.0440 53  TRP D CB  
9377  C CG  . TRP D 53  ? 0.5359 0.5360 0.4372 0.0804  0.2079  -0.0332 53  TRP D CG  
9378  C CD1 . TRP D 53  ? 0.4929 0.5168 0.4422 0.0881  0.2054  -0.0160 53  TRP D CD1 
9379  C CD2 . TRP D 53  ? 0.5454 0.5343 0.4222 0.0755  0.2257  -0.0384 53  TRP D CD2 
9380  N NE1 . TRP D 53  ? 0.5007 0.5296 0.4601 0.0888  0.2204  -0.0096 53  TRP D NE1 
9381  C CE2 . TRP D 53  ? 0.5401 0.5483 0.4554 0.0817  0.2344  -0.0234 53  TRP D CE2 
9382  C CE3 . TRP D 53  ? 0.5563 0.5200 0.3799 0.0652  0.2344  -0.0538 53  TRP D CE3 
9383  C CZ2 . TRP D 53  ? 0.5561 0.5605 0.4608 0.0793  0.2539  -0.0234 53  TRP D CZ2 
9384  C CZ3 . TRP D 53  ? 0.5717 0.5308 0.3814 0.0625  0.2532  -0.0542 53  TRP D CZ3 
9385  C CH2 . TRP D 53  ? 0.5544 0.5343 0.4053 0.0700  0.2640  -0.0393 53  TRP D CH2 
9386  N N   . VAL D 54  ? 0.6580 0.6127 0.4132 0.0425  0.1701  -0.0606 54  VAL D N   
9387  C CA  . VAL D 54  ? 0.7144 0.6515 0.4089 0.0266  0.1690  -0.0648 54  VAL D CA  
9388  C C   . VAL D 54  ? 0.7793 0.6819 0.4355 0.0191  0.1846  -0.0854 54  VAL D C   
9389  O O   . VAL D 54  ? 0.7924 0.6827 0.4628 0.0229  0.1869  -0.0966 54  VAL D O   
9390  C CB  . VAL D 54  ? 0.6826 0.6295 0.3644 0.0134  0.1326  -0.0564 54  VAL D CB  
9391  C CG1 . VAL D 54  ? 0.6860 0.6228 0.3681 0.0081  0.1179  -0.0667 54  VAL D CG1 
9392  C CG2 . VAL D 54  ? 0.7407 0.6738 0.3634 -0.0045 0.1265  -0.0539 54  VAL D CG2 
9393  N N   . THR D 55  ? 0.8552 0.7437 0.4689 0.0080  0.1915  -0.0889 55  THR D N   
9394  C CA  . THR D 55  ? 0.9143 0.7687 0.4898 -0.0017 0.2002  -0.1079 55  THR D CA  
9395  C C   . THR D 55  ? 0.9455 0.7837 0.4788 -0.0205 0.1721  -0.1133 55  THR D C   
9396  O O   . THR D 55  ? 0.9663 0.8113 0.4693 -0.0349 0.1482  -0.1020 55  THR D O   
9397  C CB  . THR D 55  ? 0.8917 0.7324 0.4279 -0.0099 0.2170  -0.1105 55  THR D CB  
9398  O OG1 . THR D 55  ? 0.8656 0.7223 0.4446 0.0062  0.2432  -0.1046 55  THR D OG1 
9399  C CG2 . THR D 55  ? 0.9704 0.7707 0.4638 -0.0208 0.2269  -0.1318 55  THR D CG2 
9400  N N   . CYS D 56  ? 0.9600 0.7767 0.4941 -0.0214 0.1734  -0.1287 56  CYS D N   
9401  C CA  . CYS D 56  ? 0.9919 0.7922 0.4927 -0.0401 0.1467  -0.1348 56  CYS D CA  
9402  C C   . CYS D 56  ? 1.1204 0.8835 0.5709 -0.0549 0.1543  -0.1507 56  CYS D C   
9403  O O   . CYS D 56  ? 1.1331 0.8737 0.5907 -0.0477 0.1780  -0.1660 56  CYS D O   
9404  C CB  . CYS D 56  ? 0.9104 0.7119 0.4472 -0.0326 0.1423  -0.1399 56  CYS D CB  
9405  S SG  . CYS D 56  ? 0.7794 0.6320 0.3839 -0.0161 0.1275  -0.1159 56  CYS D SG  
9406  N N   . SER D 57  ? 1.2203 0.9768 0.6201 -0.0763 0.1335  -0.1451 57  SER D N   
9407  C CA  . SER D 57  ? 1.3596 1.0807 0.7026 -0.0933 0.1401  -0.1577 57  SER D CA  
9408  C C   . SER D 57  ? 1.3977 1.0907 0.6913 -0.1208 0.1122  -0.1646 57  SER D C   
9409  O O   . SER D 57  ? 1.3545 1.0431 0.6598 -0.1263 0.0938  -0.1689 57  SER D O   
9410  C CB  . SER D 57  ? 1.4359 1.1662 0.7521 -0.0987 0.1432  -0.1453 57  SER D CB  
9411  O OG  . SER D 57  ? 1.4673 1.2092 0.7590 -0.1180 0.1049  -0.1277 57  SER D OG  
9412  N N   . GLN D 58  ? 1.4786 1.1498 0.7165 -0.1378 0.1147  -0.1670 58  GLN D N   
9413  C CA  . GLN D 58  ? 1.5501 1.1946 0.7266 -0.1690 0.0884  -0.1681 58  GLN D CA  
9414  C C   . GLN D 58  ? 1.4988 1.1576 0.6860 -0.1840 0.0434  -0.1550 58  GLN D C   
9415  O O   . GLN D 58  ? 1.4534 1.1050 0.6603 -0.1831 0.0376  -0.1645 58  GLN D O   
9416  C CB  . GLN D 58  ? 1.4776 1.1229 0.6121 -0.1809 0.0875  -0.1561 58  GLN D CB  
9417  C CG  . GLN D 58  ? 1.5616 1.1774 0.6275 -0.2152 0.0618  -0.1550 58  GLN D CG  
9418  C CD  . GLN D 58  ? 1.6508 1.2166 0.6696 -0.2266 0.0820  -0.1817 58  GLN D CD  
9419  O OE1 . GLN D 58  ? 1.6503 1.1975 0.6632 -0.2379 0.0659  -0.1908 58  GLN D OE1 
9420  N NE2 . GLN D 58  ? 1.7371 1.2796 0.7212 -0.2249 0.1174  -0.1941 58  GLN D NE2 
9421  N N   . HIS D 59  ? 1.5010 1.1794 0.6771 -0.1991 0.0108  -0.1321 59  HIS D N   
9422  C CA  . HIS D 59  ? 1.4654 1.1628 0.6622 -0.2126 -0.0328 -0.1156 59  HIS D CA  
9423  C C   . HIS D 59  ? 1.3563 1.0992 0.6131 -0.1929 -0.0396 -0.0974 59  HIS D C   
9424  O O   . HIS D 59  ? 1.3421 1.1114 0.6096 -0.1986 -0.0649 -0.0725 59  HIS D O   
9425  C CB  . HIS D 59  ? 1.5235 1.2145 0.6798 -0.2433 -0.0694 -0.0984 59  HIS D CB  
9426  C CG  . HIS D 59  ? 1.6223 1.2654 0.7084 -0.2646 -0.0596 -0.1158 59  HIS D CG  
9427  N ND1 . HIS D 59  ? 1.6788 1.3031 0.7169 -0.2688 -0.0374 -0.1200 59  HIS D ND1 
9428  C CD2 . HIS D 59  ? 1.6807 1.2886 0.7359 -0.2824 -0.0659 -0.1317 59  HIS D CD2 
9429  C CE1 . HIS D 59  ? 1.7723 1.3510 0.7499 -0.2896 -0.0314 -0.1377 59  HIS D CE1 
9430  N NE2 . HIS D 59  ? 1.7754 1.3430 0.7618 -0.2984 -0.0493 -0.1448 59  HIS D NE2 
9431  N N   . TYR D 60  ? 1.2690 1.0189 0.5650 -0.1699 -0.0157 -0.1095 60  TYR D N   
9432  C CA  . TYR D 60  ? 1.1605 0.9489 0.5117 -0.1537 -0.0231 -0.0954 60  TYR D CA  
9433  C C   . TYR D 60  ? 1.1927 0.9949 0.5603 -0.1717 -0.0672 -0.0818 60  TYR D C   
9434  O O   . TYR D 60  ? 1.2442 1.0301 0.6127 -0.1798 -0.0739 -0.0942 60  TYR D O   
9435  C CB  . TYR D 60  ? 1.0527 0.8401 0.4392 -0.1289 0.0105  -0.1121 60  TYR D CB  
9436  C CG  . TYR D 60  ? 0.9034 0.7379 0.3741 -0.1055 0.0058  -0.0953 60  TYR D CG  
9437  C CD1 . TYR D 60  ? 0.8316 0.6914 0.3494 -0.1084 -0.0242 -0.0824 60  TYR D CD1 
9438  C CD2 . TYR D 60  ? 0.8315 0.6851 0.3399 -0.0802 0.0327  -0.0922 60  TYR D CD2 
9439  C CE1 . TYR D 60  ? 0.7280 0.6276 0.3211 -0.0872 -0.0246 -0.0690 60  TYR D CE1 
9440  C CE2 . TYR D 60  ? 0.7394 0.6323 0.3219 -0.0606 0.0278  -0.0781 60  TYR D CE2 
9441  C CZ  . TYR D 60  ? 0.6895 0.6034 0.3103 -0.0644 0.0007  -0.0678 60  TYR D CZ  
9442  O OH  . TYR D 60  ? 0.6669 0.6149 0.3535 -0.0467 -0.0007 -0.0562 60  TYR D OH  
9443  N N   . SER D 61  ? 1.1452 0.9792 0.5334 -0.1778 -0.0981 -0.0542 61  SER D N   
9444  C CA  . SER D 61  ? 1.1084 0.9622 0.5293 -0.1930 -0.1405 -0.0364 61  SER D CA  
9445  C C   . SER D 61  ? 0.9540 0.8593 0.4725 -0.1679 -0.1446 -0.0165 61  SER D C   
9446  O O   . SER D 61  ? 0.9127 0.8431 0.4574 -0.1559 -0.1444 0.0009  61  SER D O   
9447  C CB  . SER D 61  ? 1.1710 1.0223 0.5659 -0.2167 -0.1716 -0.0166 61  SER D CB  
9448  O OG  . SER D 61  ? 1.1570 1.0299 0.5927 -0.2312 -0.2128 0.0038  61  SER D OG  
9449  N N   . SER D 62  ? 0.8577 0.7750 0.4262 -0.1612 -0.1466 -0.0206 62  SER D N   
9450  C CA  . SER D 62  ? 0.7519 0.7130 0.4092 -0.1398 -0.1477 -0.0054 62  SER D CA  
9451  C C   . SER D 62  ? 0.7943 0.7614 0.4872 -0.1460 -0.1600 -0.0070 62  SER D C   
9452  O O   . SER D 62  ? 0.8405 0.7805 0.5092 -0.1490 -0.1462 -0.0281 62  SER D O   
9453  C CB  . SER D 62  ? 0.6637 0.6336 0.3487 -0.1100 -0.1105 -0.0154 62  SER D CB  
9454  O OG  . SER D 62  ? 0.6232 0.6301 0.3851 -0.0934 -0.1122 -0.0028 62  SER D OG  
9455  N N   . SER D 63  ? 0.7763 0.7798 0.5325 -0.1469 -0.1843 0.0165  63  SER D N   
9456  C CA  . SER D 63  ? 0.7680 0.7843 0.5692 -0.1530 -0.1967 0.0198  63  SER D CA  
9457  C C   . SER D 63  ? 0.7086 0.7469 0.5697 -0.1265 -0.1687 0.0152  63  SER D C   
9458  O O   . SER D 63  ? 0.7097 0.7608 0.6126 -0.1285 -0.1727 0.0179  63  SER D O   
9459  C CB  . SER D 63  ? 0.7888 0.8347 0.6344 -0.1687 -0.2367 0.0496  63  SER D CB  
9460  O OG  . SER D 63  ? 0.7438 0.8278 0.6540 -0.1489 -0.2338 0.0696  63  SER D OG  
9461  N N   . THR D 64  ? 0.6678 0.7095 0.5310 -0.1035 -0.1408 0.0090  64  THR D N   
9462  C CA  . THR D 64  ? 0.6075 0.6665 0.5186 -0.0812 -0.1155 0.0047  64  THR D CA  
9463  C C   . THR D 64  ? 0.6043 0.6364 0.4794 -0.0709 -0.0865 -0.0173 64  THR D C   
9464  O O   . THR D 64  ? 0.5929 0.6342 0.4962 -0.0536 -0.0653 -0.0213 64  THR D O   
9465  C CB  . THR D 64  ? 0.5377 0.6274 0.4964 -0.0621 -0.1081 0.0188  64  THR D CB  
9466  O OG1 . THR D 64  ? 0.5334 0.6164 0.4602 -0.0620 -0.1116 0.0233  64  THR D OG1 
9467  C CG2 . THR D 64  ? 0.5308 0.6520 0.5507 -0.0659 -0.1282 0.0400  64  THR D CG2 
9468  N N   . TYR D 65  ? 0.6185 0.6157 0.4318 -0.0828 -0.0854 -0.0313 65  TYR D N   
9469  C CA  . TYR D 65  ? 0.6123 0.5846 0.3993 -0.0716 -0.0562 -0.0506 65  TYR D CA  
9470  C C   . TYR D 65  ? 0.6113 0.5727 0.4136 -0.0725 -0.0499 -0.0605 65  TYR D C   
9471  O O   . TYR D 65  ? 0.6252 0.5794 0.4254 -0.0904 -0.0690 -0.0601 65  TYR D O   
9472  C CB  . TYR D 65  ? 0.6500 0.5854 0.3662 -0.0828 -0.0509 -0.0642 65  TYR D CB  
9473  C CG  . TYR D 65  ? 0.6690 0.5750 0.3640 -0.0725 -0.0194 -0.0850 65  TYR D CG  
9474  C CD1 . TYR D 65  ? 0.6506 0.5630 0.3569 -0.0518 0.0065  -0.0862 65  TYR D CD1 
9475  C CD2 . TYR D 65  ? 0.7252 0.5974 0.3958 -0.0833 -0.0163 -0.1019 65  TYR D CD2 
9476  C CE1 . TYR D 65  ? 0.6661 0.5545 0.3643 -0.0413 0.0348  -0.1019 65  TYR D CE1 
9477  C CE2 . TYR D 65  ? 0.7457 0.5909 0.4063 -0.0721 0.0134  -0.1193 65  TYR D CE2 
9478  C CZ  . TYR D 65  ? 0.7152 0.5699 0.3923 -0.0506 0.0388  -0.1184 65  TYR D CZ  
9479  O OH  . TYR D 65  ? 0.7468 0.5760 0.4225 -0.0395 0.0674  -0.1331 65  TYR D OH  
9480  N N   . GLN D 66  ? 0.5856 0.5471 0.4060 -0.0540 -0.0250 -0.0667 66  GLN D N   
9481  C CA  . GLN D 66  ? 0.6048 0.5513 0.4362 -0.0523 -0.0143 -0.0759 66  GLN D CA  
9482  C C   . GLN D 66  ? 0.5734 0.5027 0.3978 -0.0361 0.0135  -0.0864 66  GLN D C   
9483  O O   . GLN D 66  ? 0.5536 0.4979 0.3888 -0.0212 0.0255  -0.0812 66  GLN D O   
9484  C CB  . GLN D 66  ? 0.6354 0.6120 0.5211 -0.0472 -0.0177 -0.0632 66  GLN D CB  
9485  C CG  . GLN D 66  ? 0.7507 0.7446 0.6589 -0.0624 -0.0415 -0.0521 66  GLN D CG  
9486  C CD  . GLN D 66  ? 0.7972 0.8206 0.7589 -0.0547 -0.0365 -0.0407 66  GLN D CD  
9487  O OE1 . GLN D 66  ? 0.7905 0.8071 0.7615 -0.0495 -0.0228 -0.0446 66  GLN D OE1 
9488  N NE2 . GLN D 66  ? 0.8314 0.8867 0.8288 -0.0538 -0.0459 -0.0259 66  GLN D NE2 
9489  N N   . ALA D 67  ? 0.6183 0.5170 0.4312 -0.0392 0.0228  -0.0994 67  ALA D N   
9490  C CA  . ALA D 67  ? 0.6254 0.5108 0.4481 -0.0230 0.0478  -0.1053 67  ALA D CA  
9491  C C   . ALA D 67  ? 0.6030 0.4967 0.4671 -0.0184 0.0485  -0.0980 67  ALA D C   
9492  O O   . ALA D 67  ? 0.6499 0.5226 0.5122 -0.0287 0.0439  -0.1041 67  ALA D O   
9493  C CB  . ALA D 67  ? 0.6803 0.5200 0.4614 -0.0275 0.0631  -0.1258 67  ALA D CB  
9494  N N   . PRO D 68  ? 0.5251 0.4464 0.4229 -0.0048 0.0539  -0.0847 68  PRO D N   
9495  C CA  . PRO D 68  ? 0.5014 0.4317 0.4329 -0.0027 0.0537  -0.0750 68  PRO D CA  
9496  C C   . PRO D 68  ? 0.5194 0.4184 0.4537 -0.0015 0.0637  -0.0818 68  PRO D C   
9497  O O   . PRO D 68  ? 0.5346 0.4110 0.4561 0.0061  0.0787  -0.0916 68  PRO D O   
9498  C CB  . PRO D 68  ? 0.4580 0.4133 0.4098 0.0108  0.0604  -0.0630 68  PRO D CB  
9499  C CG  . PRO D 68  ? 0.4328 0.4032 0.3711 0.0126  0.0570  -0.0630 68  PRO D CG  
9500  C CD  . PRO D 68  ? 0.4788 0.4234 0.3811 0.0061  0.0579  -0.0770 68  PRO D CD  
9501  N N   . PHE D 69  ? 0.5337 0.4306 0.4869 -0.0087 0.0572  -0.0762 69  PHE D N   
9502  C CA  . PHE D 69  ? 0.5659 0.4309 0.5260 -0.0080 0.0654  -0.0811 69  PHE D CA  
9503  C C   . PHE D 69  ? 0.5533 0.4258 0.5426 0.0067  0.0759  -0.0681 69  PHE D C   
9504  O O   . PHE D 69  ? 0.5195 0.4224 0.5220 0.0111  0.0725  -0.0541 69  PHE D O   
9505  C CB  . PHE D 69  ? 0.5892 0.4468 0.5587 -0.0236 0.0527  -0.0784 69  PHE D CB  
9506  C CG  . PHE D 69  ? 0.5869 0.4787 0.5833 -0.0270 0.0443  -0.0596 69  PHE D CG  
9507  C CD1 . PHE D 69  ? 0.5793 0.4768 0.6002 -0.0214 0.0492  -0.0450 69  PHE D CD1 
9508  C CD2 . PHE D 69  ? 0.5947 0.5120 0.5925 -0.0368 0.0322  -0.0557 69  PHE D CD2 
9509  C CE1 . PHE D 69  ? 0.5631 0.4885 0.6003 -0.0267 0.0445  -0.0292 69  PHE D CE1 
9510  C CE2 . PHE D 69  ? 0.5761 0.5229 0.5988 -0.0395 0.0300  -0.0401 69  PHE D CE2 
9511  C CZ  . PHE D 69  ? 0.5553 0.5045 0.5931 -0.0350 0.0374  -0.0282 69  PHE D CZ  
9512  N N   . CYS D 70  ? 0.5555 0.3989 0.5554 0.0137  0.0884  -0.0723 70  CYS D N   
9513  C CA  . CYS D 70  ? 0.5237 0.3748 0.5574 0.0268  0.0954  -0.0564 70  CYS D CA  
9514  C C   . CYS D 70  ? 0.5151 0.3848 0.5697 0.0197  0.0818  -0.0364 70  CYS D C   
9515  O O   . CYS D 70  ? 0.5284 0.3904 0.5817 0.0073  0.0735  -0.0366 70  CYS D O   
9516  C CB  . CYS D 70  ? 0.5582 0.3742 0.6093 0.0362  0.1118  -0.0626 70  CYS D CB  
9517  S SG  . CYS D 70  ? 0.6718 0.5017 0.7690 0.0557  0.1222  -0.0425 70  CYS D SG  
9518  N N   . HIS D 71  ? 0.4957 0.3890 0.5666 0.0260  0.0796  -0.0189 71  HIS D N   
9519  C CA  . HIS D 71  ? 0.4880 0.4000 0.5698 0.0182  0.0683  0.0012  71  HIS D CA  
9520  C C   . HIS D 71  ? 0.4878 0.4238 0.5503 0.0077  0.0613  0.0004  71  HIS D C   
9521  O O   . HIS D 71  ? 0.4835 0.4311 0.5491 -0.0014 0.0555  0.0139  71  HIS D O   
9522  C CB  . HIS D 71  ? 0.4979 0.3907 0.5988 0.0115  0.0642  0.0109  71  HIS D CB  
9523  C CG  . HIS D 71  ? 0.5038 0.3700 0.6315 0.0225  0.0727  0.0120  71  HIS D CG  
9524  N ND1 . HIS D 71  ? 0.4985 0.3713 0.6524 0.0340  0.0749  0.0270  71  HIS D ND1 
9525  C CD2 . HIS D 71  ? 0.5249 0.3565 0.6607 0.0237  0.0802  0.0006  71  HIS D CD2 
9526  C CE1 . HIS D 71  ? 0.5052 0.3509 0.6879 0.0439  0.0853  0.0255  71  HIS D CE1 
9527  N NE2 . HIS D 71  ? 0.5267 0.3448 0.6965 0.0380  0.0899  0.0081  71  HIS D NE2 
9528  N N   . SER D 72  ? 0.4823 0.4255 0.5264 0.0087  0.0629  -0.0140 72  SER D N   
9529  C CA  . SER D 72  ? 0.4732 0.4406 0.5082 0.0016  0.0580  -0.0137 72  SER D CA  
9530  C C   . SER D 72  ? 0.4409 0.4301 0.4740 0.0057  0.0593  -0.0044 72  SER D C   
9531  O O   . SER D 72  ? 0.4365 0.4242 0.4730 0.0138  0.0613  0.0012  72  SER D O   
9532  C CB  . SER D 72  ? 0.4770 0.4453 0.4964 0.0009  0.0563  -0.0285 72  SER D CB  
9533  O OG  . SER D 72  ? 0.4671 0.4347 0.4764 0.0120  0.0622  -0.0341 72  SER D OG  
9534  N N   . THR D 73  ? 0.4216 0.4300 0.4508 -0.0002 0.0587  -0.0029 73  THR D N   
9535  C CA  . THR D 73  ? 0.3881 0.4120 0.4099 0.0026  0.0615  0.0017  73  THR D CA  
9536  C C   . THR D 73  ? 0.3956 0.4225 0.4114 0.0135  0.0626  -0.0056 73  THR D C   
9537  O O   . THR D 73  ? 0.4163 0.4476 0.4281 0.0175  0.0632  -0.0003 73  THR D O   
9538  C CB  . THR D 73  ? 0.3582 0.3992 0.3801 -0.0042 0.0655  0.0014  73  THR D CB  
9539  O OG1 . THR D 73  ? 0.3731 0.4195 0.4034 -0.0046 0.0627  -0.0071 73  THR D OG1 
9540  C CG2 . THR D 73  ? 0.3704 0.4104 0.3955 -0.0158 0.0676  0.0111  73  THR D CG2 
9541  N N   . GLN D 74  ? 0.3887 0.4117 0.4015 0.0163  0.0617  -0.0165 74  GLN D N   
9542  C CA  . GLN D 74  ? 0.3436 0.3678 0.3480 0.0251  0.0635  -0.0222 74  GLN D CA  
9543  C C   . GLN D 74  ? 0.3876 0.4003 0.3954 0.0333  0.0686  -0.0197 74  GLN D C   
9544  O O   . GLN D 74  ? 0.3901 0.4098 0.3977 0.0399  0.0708  -0.0168 74  GLN D O   
9545  C CB  . GLN D 74  ? 0.3703 0.3888 0.3643 0.0226  0.0602  -0.0331 74  GLN D CB  
9546  C CG  . GLN D 74  ? 0.3911 0.4265 0.3905 0.0160  0.0533  -0.0323 74  GLN D CG  
9547  C CD  . GLN D 74  ? 0.4470 0.4788 0.4545 0.0049  0.0474  -0.0327 74  GLN D CD  
9548  O OE1 . GLN D 74  ? 0.4894 0.5085 0.5004 0.0015  0.0494  -0.0311 74  GLN D OE1 
9549  N NE2 . GLN D 74  ? 0.5008 0.5450 0.5157 -0.0016 0.0387  -0.0324 74  GLN D NE2 
9550  N N   . CYS D 75  ? 0.3757 0.3702 0.3911 0.0329  0.0709  -0.0200 75  CYS D N   
9551  C CA  . CYS D 75  ? 0.3709 0.3545 0.4000 0.0420  0.0778  -0.0159 75  CYS D CA  
9552  C C   . CYS D 75  ? 0.3795 0.3750 0.4244 0.0424  0.0725  0.0021  75  CYS D C   
9553  O O   . CYS D 75  ? 0.4068 0.4060 0.4645 0.0500  0.0751  0.0090  75  CYS D O   
9554  C CB  . CYS D 75  ? 0.3923 0.3504 0.4294 0.0415  0.0826  -0.0209 75  CYS D CB  
9555  S SG  . CYS D 75  ? 0.5839 0.5217 0.5924 0.0371  0.0869  -0.0436 75  CYS D SG  
9556  N N   . SER D 76  ? 0.3981 0.3993 0.4404 0.0325  0.0648  0.0106  76  SER D N   
9557  C CA  . SER D 76  ? 0.4053 0.4147 0.4514 0.0280  0.0572  0.0277  76  SER D CA  
9558  C C   . SER D 76  ? 0.3967 0.4203 0.4317 0.0298  0.0560  0.0274  76  SER D C   
9559  O O   . SER D 76  ? 0.4079 0.4349 0.4524 0.0310  0.0505  0.0397  76  SER D O   
9560  C CB  . SER D 76  ? 0.4111 0.4216 0.4467 0.0144  0.0522  0.0346  76  SER D CB  
9561  O OG  . SER D 76  ? 0.4216 0.4359 0.4516 0.0065  0.0437  0.0512  76  SER D OG  
9562  N N   . ARG D 77  ? 0.3691 0.4004 0.3877 0.0294  0.0597  0.0150  77  ARG D N   
9563  C CA  . ARG D 77  ? 0.3807 0.4223 0.3898 0.0313  0.0594  0.0134  77  ARG D CA  
9564  C C   . ARG D 77  ? 0.3897 0.4321 0.4101 0.0415  0.0615  0.0141  77  ARG D C   
9565  O O   . ARG D 77  ? 0.4014 0.4499 0.4237 0.0416  0.0575  0.0215  77  ARG D O   
9566  C CB  . ARG D 77  ? 0.3833 0.4323 0.3819 0.0309  0.0635  0.0014  77  ARG D CB  
9567  C CG  . ARG D 77  ? 0.4332 0.4893 0.4232 0.0317  0.0635  0.0008  77  ARG D CG  
9568  C CD  . ARG D 77  ? 0.4624 0.5263 0.4506 0.0331  0.0678  -0.0087 77  ARG D CD  
9569  N NE  . ARG D 77  ? 0.4693 0.5357 0.4514 0.0343  0.0688  -0.0094 77  ARG D NE  
9570  C CZ  . ARG D 77  ? 0.4587 0.5312 0.4456 0.0385  0.0715  -0.0149 77  ARG D CZ  
9571  N NH1 . ARG D 77  ? 0.4456 0.5248 0.4435 0.0410  0.0711  -0.0184 77  ARG D NH1 
9572  N NH2 . ARG D 77  ? 0.4552 0.5257 0.4370 0.0390  0.0728  -0.0157 77  ARG D NH2 
9573  N N   . ALA D 78  ? 0.3745 0.4091 0.4012 0.0484  0.0688  0.0064  78  ALA D N   
9574  C CA  . ALA D 78  ? 0.3713 0.4045 0.4081 0.0582  0.0764  0.0058  78  ALA D CA  
9575  C C   . ALA D 78  ? 0.3951 0.4261 0.4613 0.0625  0.0767  0.0203  78  ALA D C   
9576  O O   . ALA D 78  ? 0.3885 0.4209 0.4715 0.0711  0.0852  0.0229  78  ALA D O   
9577  C CB  . ALA D 78  ? 0.3583 0.3785 0.3844 0.0617  0.0864  -0.0092 78  ALA D CB  
9578  N N   . ASN D 79  ? 0.4162 0.4442 0.4912 0.0561  0.0679  0.0312  79  ASN D N   
9579  C CA  . ASN D 79  ? 0.4281 0.4555 0.5359 0.0583  0.0634  0.0498  79  ASN D CA  
9580  C C   . ASN D 79  ? 0.4775 0.4919 0.6135 0.0706  0.0783  0.0468  79  ASN D C   
9581  O O   . ASN D 79  ? 0.4723 0.4905 0.6444 0.0787  0.0821  0.0594  79  ASN D O   
9582  C CB  . ASN D 79  ? 0.4427 0.4850 0.5609 0.0576  0.0556  0.0630  79  ASN D CB  
9583  C CG  . ASN D 79  ? 0.5445 0.5900 0.6964 0.0550  0.0434  0.0875  79  ASN D CG  
9584  O OD1 . ASN D 79  ? 0.5692 0.6069 0.7265 0.0490  0.0356  0.0970  79  ASN D OD1 
9585  N ND2 . ASN D 79  ? 0.6021 0.6595 0.7819 0.0591  0.0410  0.1004  79  ASN D ND2 
9586  N N   . THR D 80  ? 0.5070 0.5046 0.6282 0.0714  0.0875  0.0301  80  THR D N   
9587  C CA  . THR D 80  ? 0.4950 0.4723 0.6373 0.0812  0.1036  0.0240  80  THR D CA  
9588  C C   . THR D 80  ? 0.5711 0.5296 0.7132 0.0754  0.1002  0.0217  80  THR D C   
9589  O O   . THR D 80  ? 0.6013 0.5561 0.7130 0.0660  0.0952  0.0104  80  THR D O   
9590  C CB  . THR D 80  ? 0.4946 0.4607 0.6134 0.0867  0.1218  0.0020  80  THR D CB  
9591  O OG1 . THR D 80  ? 0.6263 0.5644 0.7557 0.0930  0.1385  -0.0083 80  THR D OG1 
9592  C CG2 . THR D 80  ? 0.4282 0.3949 0.5033 0.0765  0.1146  -0.0128 80  THR D CG2 
9593  N N   . HIS D 81  ? 0.6122 0.5592 0.7928 0.0809  0.1025  0.0341  81  HIS D N   
9594  C CA  . HIS D 81  ? 0.6681 0.5950 0.8506 0.0748  0.0989  0.0333  81  HIS D CA  
9595  C C   . HIS D 81  ? 0.6832 0.5796 0.8892 0.0862  0.1191  0.0227  81  HIS D C   
9596  O O   . HIS D 81  ? 0.6787 0.5546 0.9023 0.0845  0.1179  0.0263  81  HIS D O   
9597  C CB  . HIS D 81  ? 0.7212 0.6592 0.9238 0.0662  0.0786  0.0608  81  HIS D CB  
9598  C CG  . HIS D 81  ? 0.7504 0.7108 0.9200 0.0530  0.0631  0.0660  81  HIS D CG  
9599  N ND1 . HIS D 81  ? 0.7546 0.7150 0.8934 0.0399  0.0569  0.0602  81  HIS D ND1 
9600  C CD2 . HIS D 81  ? 0.7362 0.7176 0.8995 0.0509  0.0550  0.0751  81  HIS D CD2 
9601  C CE1 . HIS D 81  ? 0.7158 0.6950 0.8311 0.0315  0.0484  0.0645  81  HIS D CE1 
9602  N NE2 . HIS D 81  ? 0.7102 0.7006 0.8371 0.0373  0.0461  0.0728  81  HIS D NE2 
9603  N N   . GLN D 82  ? 0.6753 0.5670 0.8798 0.0974  0.1396  0.0089  82  GLN D N   
9604  C CA  . GLN D 82  ? 0.6376 0.4960 0.8525 0.1082  0.1660  -0.0081 82  GLN D CA  
9605  C C   . GLN D 82  ? 0.6029 0.4381 0.7599 0.0995  0.1736  -0.0385 82  GLN D C   
9606  O O   . GLN D 82  ? 0.5883 0.4361 0.7080 0.0952  0.1728  -0.0483 82  GLN D O   
9607  C CB  . GLN D 82  ? 0.6603 0.5260 0.9051 0.1240  0.1874  -0.0052 82  GLN D CB  
9608  C CG  . GLN D 82  ? 0.7714 0.6017 1.0008 0.1319  0.2203  -0.0325 82  GLN D CG  
9609  C CD  . GLN D 82  ? 0.8490 0.6939 1.0937 0.1384  0.2355  -0.0284 82  GLN D CD  
9610  O OE1 . GLN D 82  ? 0.8753 0.7517 1.1581 0.1429  0.2273  -0.0051 82  GLN D OE1 
9611  N NE2 . GLN D 82  ? 0.8879 0.7083 1.1010 0.1372  0.2571  -0.0509 82  GLN D NE2 
9612  N N   . CYS D 83  ? 0.6035 0.4035 0.7536 0.0954  0.1791  -0.0520 83  CYS D N   
9613  C CA  . CYS D 83  ? 0.6079 0.3831 0.7019 0.0827  0.1808  -0.0788 83  CYS D CA  
9614  C C   . CYS D 83  ? 0.6455 0.3941 0.7095 0.0880  0.2086  -0.1036 83  CYS D C   
9615  O O   . CYS D 83  ? 0.6685 0.4037 0.7623 0.1036  0.2346  -0.1049 83  CYS D O   
9616  C CB  . CYS D 83  ? 0.6213 0.3650 0.7184 0.0741  0.1755  -0.0840 83  CYS D CB  
9617  S SG  . CYS D 83  ? 0.8551 0.6276 0.9717 0.0622  0.1436  -0.0576 83  CYS D SG  
9618  N N   . PHE D 84  ? 0.6555 0.3954 0.6606 0.0739  0.2036  -0.1223 84  PHE D N   
9619  C CA  . PHE D 84  ? 0.7017 0.4179 0.6653 0.0745  0.2273  -0.1446 84  PHE D CA  
9620  C C   . PHE D 84  ? 0.7813 0.4468 0.7061 0.0628  0.2352  -0.1700 84  PHE D C   
9621  O O   . PHE D 84  ? 0.8033 0.4579 0.7080 0.0468  0.2146  -0.1746 84  PHE D O   
9622  C CB  . PHE D 84  ? 0.7045 0.4473 0.6262 0.0648  0.2130  -0.1444 84  PHE D CB  
9623  C CG  . PHE D 84  ? 0.7413 0.4683 0.6181 0.0625  0.2320  -0.1607 84  PHE D CG  
9624  C CD1 . PHE D 84  ? 0.6534 0.4052 0.5518 0.0744  0.2441  -0.1490 84  PHE D CD1 
9625  C CD2 . PHE D 84  ? 0.7722 0.4677 0.5871 0.0442  0.2284  -0.1815 84  PHE D CD2 
9626  C CE1 . PHE D 84  ? 0.6912 0.4356 0.5512 0.0692  0.2553  -0.1584 84  PHE D CE1 
9627  C CE2 . PHE D 84  ? 0.7857 0.4741 0.5599 0.0387  0.2381  -0.1900 84  PHE D CE2 
9628  C CZ  . PHE D 84  ? 0.7735 0.4858 0.5704 0.0517  0.2531  -0.1788 84  PHE D CZ  
9629  N N   . THR D 85  ? 0.8581 0.5063 0.7758 0.0669  0.2555  -0.1792 85  THR D N   
9630  C CA  . THR D 85  ? 0.9671 0.5695 0.8438 0.0545  0.2621  -0.2024 85  THR D CA  
9631  C C   . THR D 85  ? 1.0121 0.6069 0.8332 0.0467  0.2732  -0.2164 85  THR D C   
9632  O O   . THR D 85  ? 0.9865 0.5944 0.8242 0.0587  0.2929  -0.2110 85  THR D O   
9633  C CB  . THR D 85  ? 0.9972 0.5767 0.9195 0.0664  0.2800  -0.2018 85  THR D CB  
9634  O OG1 . THR D 85  ? 0.9812 0.5664 0.9534 0.0711  0.2663  -0.1861 85  THR D OG1 
9635  C CG2 . THR D 85  ? 1.0642 0.5945 0.9406 0.0531  0.2876  -0.2273 85  THR D CG2 
9636  N N   . CYS D 86  ? 1.0842 0.6563 0.8398 0.0248  0.2595  -0.2332 86  CYS D N   
9637  C CA  . CYS D 86  ? 1.1733 0.7401 0.8734 0.0151  0.2660  -0.2429 86  CYS D CA  
9638  C C   . CYS D 86  ? 1.3040 0.8338 0.9870 0.0159  0.2936  -0.2595 86  CYS D C   
9639  O O   . CYS D 86  ? 1.3607 0.8504 1.0241 0.0063  0.2949  -0.2758 86  CYS D O   
9640  C CB  . CYS D 86  ? 1.1887 0.7463 0.8241 -0.0108 0.2390  -0.2515 86  CYS D CB  
9641  S SG  . CYS D 86  ? 1.3091 0.8712 0.8884 -0.0192 0.2466  -0.2545 86  CYS D SG  
9642  N N   . THR D 87  ? 1.3569 0.9000 1.0461 0.0262  0.3159  -0.2552 87  THR D N   
9643  C CA  . THR D 87  ? 1.4661 0.9786 1.1488 0.0307  0.3488  -0.2686 87  THR D CA  
9644  C C   . THR D 87  ? 1.5530 1.0437 1.1641 0.0153  0.3603  -0.2838 87  THR D C   
9645  O O   . THR D 87  ? 1.6437 1.1118 1.2513 0.0204  0.3923  -0.2938 87  THR D O   
9646  C CB  . THR D 87  ? 1.4476 0.9880 1.2008 0.0550  0.3717  -0.2513 87  THR D CB  
9647  O OG1 . THR D 87  ? 1.5436 1.0548 1.2910 0.0590  0.4067  -0.2642 87  THR D OG1 
9648  C CG2 . THR D 87  ? 1.3913 0.9745 1.1462 0.0579  0.3649  -0.2349 87  THR D CG2 
9649  N N   . ASP D 88  ? 1.5148 1.0108 1.0697 -0.0041 0.3355  -0.2847 88  ASP D N   
9650  C CA  . ASP D 88  ? 1.5568 1.0248 1.0375 -0.0227 0.3434  -0.2996 88  ASP D CA  
9651  C C   . ASP D 88  ? 1.7283 1.1541 1.1488 -0.0483 0.3243  -0.3180 88  ASP D C   
9652  O O   . ASP D 88  ? 1.8068 1.1910 1.2179 -0.0502 0.3415  -0.3359 88  ASP D O   
9653  C CB  . ASP D 88  ? 1.4989 1.0002 0.9578 -0.0274 0.3327  -0.2857 88  ASP D CB  
9654  C CG  . ASP D 88  ? 1.4637 0.9945 0.9202 -0.0361 0.2936  -0.2721 88  ASP D CG  
9655  O OD1 . ASP D 88  ? 1.5031 1.0234 0.9603 -0.0441 0.2727  -0.2761 88  ASP D OD1 
9656  O OD2 . ASP D 88  ? 1.3991 0.9639 0.8568 -0.0345 0.2847  -0.2568 88  ASP D OD2 
9657  N N   . SER D 89  ? 1.6874 1.1236 1.0702 -0.0682 0.2882  -0.3126 89  SER D N   
9658  C CA  . SER D 89  ? 1.7256 1.1265 1.0535 -0.0956 0.2640  -0.3261 89  SER D CA  
9659  C C   . SER D 89  ? 1.6880 1.0706 1.0477 -0.0938 0.2563  -0.3329 89  SER D C   
9660  O O   . SER D 89  ? 1.6221 1.0269 1.0494 -0.0724 0.2615  -0.3228 89  SER D O   
9661  C CB  . SER D 89  ? 1.7098 1.1356 1.0070 -0.1154 0.2237  -0.3123 89  SER D CB  
9662  O OG  . SER D 89  ? 1.7438 1.1488 1.0157 -0.1382 0.1929  -0.3180 89  SER D OG  
9663  N N   . THR D 90  ? 1.7288 1.0699 1.0392 -0.1176 0.2427  -0.3490 90  THR D N   
9664  C CA  . THR D 90  ? 1.7069 1.0298 1.0418 -0.1212 0.2286  -0.3544 90  THR D CA  
9665  C C   . THR D 90  ? 1.6974 1.0367 1.0159 -0.1444 0.1821  -0.3438 90  THR D C   
9666  O O   . THR D 90  ? 1.6995 1.0246 1.0295 -0.1548 0.1622  -0.3466 90  THR D O   
9667  C CB  . THR D 90  ? 1.7720 1.0356 1.0704 -0.1324 0.2439  -0.3795 90  THR D CB  
9668  O OG1 . THR D 90  ? 1.8107 1.0563 1.1001 -0.1192 0.2860  -0.3906 90  THR D OG1 
9669  C CG2 . THR D 90  ? 1.7330 0.9810 1.0827 -0.1231 0.2439  -0.3832 90  THR D CG2 
9670  N N   . THR D 91  ? 1.6908 1.0601 0.9847 -0.1532 0.1644  -0.3303 91  THR D N   
9671  C CA  . THR D 91  ? 1.6524 1.0509 0.9486 -0.1697 0.1215  -0.3138 91  THR D CA  
9672  C C   . THR D 91  ? 1.5477 0.9988 0.8830 -0.1517 0.1203  -0.2932 91  THR D C   
9673  O O   . THR D 91  ? 1.5265 0.9902 0.8680 -0.1340 0.1469  -0.2911 91  THR D O   
9674  C CB  . THR D 91  ? 1.8074 1.1908 1.0340 -0.2035 0.0919  -0.3140 91  THR D CB  
9675  O OG1 . THR D 91  ? 1.7820 1.1952 1.0220 -0.2199 0.0480  -0.2955 91  THR D OG1 
9676  C CG2 . THR D 91  ? 1.8162 1.2044 1.0007 -0.2047 0.1047  -0.3114 91  THR D CG2 
9677  N N   . THR D 92  ? 1.4645 0.9459 0.8263 -0.1576 0.0893  -0.2779 92  THR D N   
9678  C CA  . THR D 92  ? 1.3462 0.8749 0.7479 -0.1407 0.0879  -0.2597 92  THR D CA  
9679  C C   . THR D 92  ? 1.3107 0.8679 0.6845 -0.1500 0.0698  -0.2448 92  THR D C   
9680  O O   . THR D 92  ? 1.3531 0.9006 0.6813 -0.1754 0.0446  -0.2427 92  THR D O   
9681  C CB  . THR D 92  ? 1.2993 0.8476 0.7466 -0.1418 0.0664  -0.2499 92  THR D CB  
9682  O OG1 . THR D 92  ? 1.3158 0.8679 0.7416 -0.1713 0.0246  -0.2425 92  THR D OG1 
9683  C CG2 . THR D 92  ? 1.3151 0.8366 0.7953 -0.1322 0.0831  -0.2610 92  THR D CG2 
9684  N N   . ARG D 93  ? 1.2344 0.8265 0.6393 -0.1290 0.0829  -0.2330 93  ARG D N   
9685  C CA  . ARG D 93  ? 1.1835 0.8069 0.5744 -0.1325 0.0689  -0.2162 93  ARG D CA  
9686  C C   . ARG D 93  ? 1.0938 0.7545 0.5382 -0.1064 0.0831  -0.2047 93  ARG D C   
9687  O O   . ARG D 93  ? 1.0616 0.7196 0.5470 -0.0866 0.1065  -0.2102 93  ARG D O   
9688  C CB  . ARG D 93  ? 1.2345 0.8429 0.5806 -0.1356 0.0859  -0.2205 93  ARG D CB  
9689  C CG  . ARG D 93  ? 1.2592 0.8638 0.6312 -0.1094 0.1288  -0.2285 93  ARG D CG  
9690  C CD  . ARG D 93  ? 1.3516 0.9449 0.6858 -0.1109 0.1490  -0.2318 93  ARG D CD  
9691  N NE  . ARG D 93  ? 1.3833 0.9786 0.7569 -0.0847 0.1885  -0.2363 93  ARG D NE  
9692  C CZ  . ARG D 93  ? 1.3448 0.9763 0.7619 -0.0641 0.2006  -0.2220 93  ARG D CZ  
9693  N NH1 . ARG D 93  ? 1.2995 0.9657 0.7230 -0.0656 0.1789  -0.2041 93  ARG D NH1 
9694  N NH2 . ARG D 93  ? 1.3374 0.9705 0.7944 -0.0426 0.2335  -0.2242 93  ARG D NH2 
9695  N N   . PRO D 94  ? 1.0514 0.7466 0.4977 -0.1066 0.0684  -0.1869 94  PRO D N   
9696  C CA  . PRO D 94  ? 0.9475 0.6868 0.4583 -0.0789 0.0805  -0.1701 94  PRO D CA  
9697  C C   . PRO D 94  ? 0.9204 0.6462 0.4382 -0.0579 0.1229  -0.1808 94  PRO D C   
9698  O O   . PRO D 94  ? 0.9441 0.6560 0.4332 -0.0600 0.1370  -0.1856 94  PRO D O   
9699  C CB  . PRO D 94  ? 0.9222 0.6922 0.4244 -0.0849 0.0600  -0.1505 94  PRO D CB  
9700  C CG  . PRO D 94  ? 0.9695 0.7296 0.4354 -0.1138 0.0240  -0.1476 94  PRO D CG  
9701  C CD  . PRO D 94  ? 1.0660 0.7714 0.4764 -0.1295 0.0349  -0.1736 94  PRO D CD  
9702  N N   . GLY D 95  ? 0.8525 0.5965 0.4331 -0.0358 0.1358  -0.1752 95  GLY D N   
9703  C CA  . GLY D 95  ? 0.8476 0.5887 0.4555 -0.0147 0.1703  -0.1781 95  GLY D CA  
9704  C C   . GLY D 95  ? 0.8998 0.6058 0.5128 -0.0127 0.1864  -0.1938 95  GLY D C   
9705  O O   . GLY D 95  ? 0.9304 0.6366 0.5829 0.0054  0.2105  -0.1928 95  GLY D O   
9706  N N   . CYS D 96  ? 0.9419 0.6180 0.5176 -0.0327 0.1707  -0.2067 96  CYS D N   
9707  C CA  . CYS D 96  ? 1.0014 0.6385 0.5742 -0.0342 0.1841  -0.2232 96  CYS D CA  
9708  C C   . CYS D 96  ? 1.0177 0.6378 0.5923 -0.0469 0.1637  -0.2290 96  CYS D C   
9709  O O   . CYS D 96  ? 1.0667 0.6681 0.5968 -0.0715 0.1407  -0.2361 96  CYS D O   
9710  C CB  . CYS D 96  ? 1.0873 0.6922 0.5999 -0.0500 0.1903  -0.2374 96  CYS D CB  
9711  S SG  . CYS D 96  ? 1.8340 1.3841 1.3312 -0.0564 0.2051  -0.2605 96  CYS D SG  
9712  N N   . HIS D 97  ? 0.9628 0.5904 0.5922 -0.0316 0.1706  -0.2236 97  HIS D N   
9713  C CA  . HIS D 97  ? 0.9355 0.5513 0.5812 -0.0416 0.1522  -0.2244 97  HIS D CA  
9714  C C   . HIS D 97  ? 0.9733 0.5750 0.6703 -0.0223 0.1751  -0.2251 97  HIS D C   
9715  O O   . HIS D 97  ? 0.9478 0.5589 0.6756 -0.0009 0.2003  -0.2203 97  HIS D O   
9716  C CB  . HIS D 97  ? 0.8289 0.4965 0.5099 -0.0455 0.1180  -0.1993 97  HIS D CB  
9717  C CG  . HIS D 97  ? 0.8149 0.5064 0.4642 -0.0586 0.0964  -0.1919 97  HIS D CG  
9718  N ND1 . HIS D 97  ? 0.7964 0.5203 0.4534 -0.0462 0.1020  -0.1800 97  HIS D ND1 
9719  C CD2 . HIS D 97  ? 0.8346 0.5232 0.4497 -0.0834 0.0670  -0.1917 97  HIS D CD2 
9720  C CE1 . HIS D 97  ? 0.8078 0.5466 0.4368 -0.0618 0.0781  -0.1731 97  HIS D CE1 
9721  N NE2 . HIS D 97  ? 0.8317 0.5508 0.4361 -0.0846 0.0558  -0.1791 97  HIS D NE2 
9722  N N   . ASN D 98  ? 1.0413 0.6261 0.7554 -0.0303 0.1630  -0.2262 98  ASN D N   
9723  C CA  . ASN D 98  ? 1.1005 0.6811 0.8737 -0.0122 0.1778  -0.2188 98  ASN D CA  
9724  C C   . ASN D 98  ? 0.9815 0.6101 0.8056 -0.0110 0.1507  -0.1905 98  ASN D C   
9725  O O   . ASN D 98  ? 0.9175 0.5708 0.7284 -0.0265 0.1233  -0.1827 98  ASN D O   
9726  C CB  . ASN D 98  ? 1.2898 0.8102 1.0484 -0.0196 0.1903  -0.2406 98  ASN D CB  
9727  C CG  . ASN D 98  ? 1.4363 0.9387 1.1762 -0.0110 0.2164  -0.2527 98  ASN D CG  
9728  O OD1 . ASN D 98  ? 1.3663 0.8933 1.1198 0.0049  0.2333  -0.2451 98  ASN D OD1 
9729  N ND2 . ASN D 98  ? 1.6434 1.1017 1.3541 -0.0224 0.2206  -0.2712 98  ASN D ND2 
9730  N N   . ASN D 99  ? 0.9426 0.5860 0.8248 0.0071  0.1591  -0.1737 99  ASN D N   
9731  C CA  . ASN D 99  ? 0.8722 0.5581 0.7985 0.0082  0.1377  -0.1465 99  ASN D CA  
9732  C C   . ASN D 99  ? 0.7182 0.4539 0.6421 0.0079  0.1226  -0.1319 99  ASN D C   
9733  O O   . ASN D 99  ? 0.6518 0.4160 0.5880 -0.0005 0.1018  -0.1176 99  ASN D O   
9734  C CB  . ASN D 99  ? 0.9633 0.6360 0.8910 -0.0097 0.1182  -0.1456 99  ASN D CB  
9735  C CG  . ASN D 99  ? 1.0725 0.6931 1.0088 -0.0090 0.1326  -0.1584 99  ASN D CG  
9736  O OD1 . ASN D 99  ? 1.0912 0.7047 1.0690 0.0084  0.1491  -0.1504 99  ASN D OD1 
9737  N ND2 . ASN D 99  ? 1.1250 0.7071 1.0238 -0.0286 0.1259  -0.1779 99  ASN D ND2 
9738  N N   . THR D 100 ? 0.6578 0.4013 0.5663 0.0173  0.1357  -0.1364 100 THR D N   
9739  C CA  . THR D 100 ? 0.6091 0.3964 0.5213 0.0209  0.1259  -0.1222 100 THR D CA  
9740  C C   . THR D 100 ? 0.5548 0.3604 0.5085 0.0401  0.1388  -0.1072 100 THR D C   
9741  O O   . THR D 100 ? 0.5649 0.3553 0.5512 0.0486  0.1490  -0.1030 100 THR D O   
9742  C CB  . THR D 100 ? 0.6563 0.4402 0.5215 0.0144  0.1273  -0.1348 100 THR D CB  
9743  O OG1 . THR D 100 ? 0.7191 0.4652 0.5611 0.0195  0.1538  -0.1535 100 THR D OG1 
9744  C CG2 . THR D 100 ? 0.6584 0.4351 0.4907 -0.0079 0.1043  -0.1415 100 THR D CG2 
9745  N N   . CYS D 101 ? 0.5470 0.3840 0.5023 0.0461  0.1371  -0.0977 101 CYS D N   
9746  C CA  . CYS D 101 ? 0.5609 0.4168 0.5559 0.0616  0.1456  -0.0816 101 CYS D CA  
9747  C C   . CYS D 101 ? 0.5746 0.4297 0.5622 0.0715  0.1653  -0.0871 101 CYS D C   
9748  O O   . CYS D 101 ? 0.6068 0.4642 0.5566 0.0656  0.1647  -0.0963 101 CYS D O   
9749  C CB  . CYS D 101 ? 0.5567 0.4514 0.5661 0.0597  0.1266  -0.0623 101 CYS D CB  
9750  S SG  . CYS D 101 ? 0.9175 0.8191 0.9397 0.0488  0.1075  -0.0515 101 CYS D SG  
9751  N N   . GLY D 102 ? 0.5643 0.4186 0.5927 0.0862  0.1817  -0.0784 102 GLY D N   
9752  C CA  . GLY D 102 ? 0.5957 0.4499 0.6286 0.0975  0.2052  -0.0813 102 GLY D CA  
9753  C C   . GLY D 102 ? 0.5801 0.4739 0.6405 0.1031  0.1960  -0.0596 102 GLY D C   
9754  O O   . GLY D 102 ? 0.5295 0.4429 0.6269 0.1048  0.1805  -0.0394 102 GLY D O   
9755  N N   . LEU D 103 ? 0.6002 0.5027 0.6416 0.1049  0.2063  -0.0632 103 LEU D N   
9756  C CA  . LEU D 103 ? 0.5817 0.5187 0.6423 0.1079  0.1971  -0.0450 103 LEU D CA  
9757  C C   . LEU D 103 ? 0.5711 0.5112 0.6436 0.1149  0.2171  -0.0431 103 LEU D C   
9758  O O   . LEU D 103 ? 0.6333 0.5576 0.6676 0.1099  0.2287  -0.0582 103 LEU D O   
9759  C CB  . LEU D 103 ? 0.5999 0.5509 0.6198 0.0957  0.1768  -0.0477 103 LEU D CB  
9760  C CG  . LEU D 103 ? 0.5907 0.5734 0.6224 0.0943  0.1594  -0.0311 103 LEU D CG  
9761  C CD1 . LEU D 103 ? 0.5855 0.5811 0.6549 0.0954  0.1455  -0.0139 103 LEU D CD1 
9762  C CD2 . LEU D 103 ? 0.5933 0.5816 0.5879 0.0831  0.1423  -0.0372 103 LEU D CD2 
9763  N N   . LEU D 104 ? 0.4994 0.4604 0.6232 0.1225  0.2161  -0.0224 104 LEU D N   
9764  C CA  . LEU D 104 ? 0.5338 0.4998 0.6713 0.1258  0.2310  -0.0182 104 LEU D CA  
9765  C C   . LEU D 104 ? 0.4936 0.4816 0.6137 0.1215  0.2247  -0.0126 104 LEU D C   
9766  O O   . LEU D 104 ? 0.4724 0.4848 0.6122 0.1214  0.2080  0.0035  104 LEU D O   
9767  C CB  . LEU D 104 ? 0.5964 0.5736 0.8003 0.1343  0.2328  0.0031  104 LEU D CB  
9768  C CG  . LEU D 104 ? 0.6924 0.6629 0.9131 0.1390  0.2566  0.0025  104 LEU D CG  
9769  C CD1 . LEU D 104 ? 0.7728 0.7072 0.9669 0.1395  0.2775  -0.0203 104 LEU D CD1 
9770  C CD2 . LEU D 104 ? 0.7038 0.6912 0.9951 0.1458  0.2550  0.0285  104 LEU D CD2 
9771  N N   . SER D 105 ? 0.5111 0.4891 0.5940 0.1174  0.2382  -0.0252 105 SER D N   
9772  C CA  . SER D 105 ? 0.4702 0.4653 0.5340 0.1126  0.2345  -0.0202 105 SER D CA  
9773  C C   . SER D 105 ? 0.4939 0.4973 0.5840 0.1168  0.2512  -0.0106 105 SER D C   
9774  O O   . SER D 105 ? 0.5513 0.5385 0.6502 0.1209  0.2716  -0.0167 105 SER D O   
9775  C CB  . SER D 105 ? 0.4721 0.4510 0.4710 0.1024  0.2353  -0.0383 105 SER D CB  
9776  O OG  . SER D 105 ? 0.4818 0.4533 0.4559 0.0974  0.2200  -0.0464 105 SER D OG  
9777  N N   . SER D 106 ? 0.4318 0.4587 0.5337 0.1154  0.2441  0.0040  106 SER D N   
9778  C CA  . SER D 106 ? 0.4423 0.4784 0.5723 0.1187  0.2596  0.0151  106 SER D CA  
9779  C C   . SER D 106 ? 0.4588 0.4979 0.5506 0.1116  0.2650  0.0121  106 SER D C   
9780  O O   . SER D 106 ? 0.4816 0.5311 0.5524 0.1059  0.2487  0.0152  106 SER D O   
9781  C CB  . SER D 106 ? 0.4685 0.5310 0.6578 0.1225  0.2463  0.0404  106 SER D CB  
9782  O OG  . SER D 106 ? 0.5167 0.5760 0.7486 0.1288  0.2458  0.0472  106 SER D OG  
9783  N N   . ASN D 107 ? 0.4795 0.5147 0.4978 0.0845  0.1732  -0.1214 107 ASN D N   
9784  C CA  . ASN D 107 ? 0.4778 0.5411 0.4765 0.0779  0.1819  -0.1150 107 ASN D CA  
9785  C C   . ASN D 107 ? 0.4746 0.5419 0.4921 0.0828  0.1830  -0.1005 107 ASN D C   
9786  O O   . ASN D 107 ? 0.5030 0.5730 0.5460 0.0895  0.1898  -0.1104 107 ASN D O   
9787  C CB  . ASN D 107 ? 0.5004 0.5871 0.4927 0.0744  0.1970  -0.1389 107 ASN D CB  
9788  C CG  . ASN D 107 ? 0.5548 0.6744 0.5246 0.0653  0.2058  -0.1311 107 ASN D CG  
9789  O OD1 . ASN D 107 ? 0.5474 0.6745 0.5199 0.0650  0.2048  -0.1113 107 ASN D OD1 
9790  N ND2 . ASN D 107 ? 0.6142 0.7548 0.5618 0.0565  0.2139  -0.1466 107 ASN D ND2 
9791  N N   . PRO D 108 ? 0.4710 0.5382 0.4787 0.0794  0.1758  -0.0774 108 PRO D N   
9792  C CA  . PRO D 108 ? 0.4499 0.5163 0.4786 0.0841  0.1747  -0.0644 108 PRO D CA  
9793  C C   . PRO D 108 ? 0.5259 0.6196 0.5603 0.0829  0.1879  -0.0656 108 PRO D C   
9794  O O   . PRO D 108 ? 0.5464 0.6409 0.6036 0.0877  0.1890  -0.0601 108 PRO D O   
9795  C CB  . PRO D 108 ? 0.4060 0.4647 0.4223 0.0800  0.1637  -0.0423 108 PRO D CB  
9796  C CG  . PRO D 108 ? 0.4130 0.4822 0.4008 0.0718  0.1642  -0.0412 108 PRO D CG  
9797  C CD  . PRO D 108 ? 0.4347 0.5019 0.4164 0.0718  0.1680  -0.0628 108 PRO D CD  
9798  N N   . VAL D 109 ? 0.5593 0.6767 0.5728 0.0753  0.1975  -0.0725 109 VAL D N   
9799  C CA  . VAL D 109 ? 0.5494 0.6978 0.5645 0.0717  0.2111  -0.0738 109 VAL D CA  
9800  C C   . VAL D 109 ? 0.5755 0.7332 0.6104 0.0777  0.2241  -0.0998 109 VAL D C   
9801  O O   . VAL D 109 ? 0.5952 0.7630 0.6536 0.0823  0.2311  -0.1005 109 VAL D O   
9802  C CB  . VAL D 109 ? 0.5436 0.7178 0.5263 0.0589  0.2154  -0.0685 109 VAL D CB  
9803  C CG1 . VAL D 109 ? 0.5764 0.7866 0.5596 0.0537  0.2310  -0.0728 109 VAL D CG1 
9804  C CG2 . VAL D 109 ? 0.5024 0.6699 0.4723 0.0537  0.2030  -0.0409 109 VAL D CG2 
9805  N N   . THR D 110 ? 0.5605 0.7134 0.5892 0.0780  0.2269  -0.1218 110 THR D N   
9806  C CA  . THR D 110 ? 0.5509 0.7113 0.5974 0.0831  0.2366  -0.1475 110 THR D CA  
9807  C C   . THR D 110 ? 0.5396 0.6718 0.6220 0.0957  0.2295  -0.1534 110 THR D C   
9808  O O   . THR D 110 ? 0.5581 0.6905 0.6609 0.1015  0.2319  -0.1694 110 THR D O   
9809  C CB  . THR D 110 ? 0.5981 0.7618 0.6224 0.0772  0.2378  -0.1662 110 THR D CB  
9810  O OG1 . THR D 110 ? 0.5953 0.7296 0.6219 0.0805  0.2282  -0.1720 110 THR D OG1 
9811  C CG2 . THR D 110 ? 0.6374 0.8260 0.6236 0.0632  0.2408  -0.1568 110 THR D CG2 
9812  N N   . GLN D 111 ? 0.5613 0.6677 0.6486 0.0988  0.2174  -0.1380 111 GLN D N   
9813  C CA  . GLN D 111 ? 0.5938 0.6729 0.7135 0.1089  0.2080  -0.1388 111 GLN D CA  
9814  C C   . GLN D 111 ? 0.8004 0.8632 0.9268 0.1116  0.2053  -0.1599 111 GLN D C   
9815  O O   . GLN D 111 ? 0.8148 0.8562 0.9698 0.1191  0.1963  -0.1612 111 GLN D O   
9816  C CB  . GLN D 111 ? 0.6519 0.7400 0.8052 0.1163  0.2117  -0.1386 111 GLN D CB  
9817  C CG  . GLN D 111 ? 0.7254 0.8241 0.8815 0.1151  0.2124  -0.1168 111 GLN D CG  
9818  C CD  . GLN D 111 ? 0.8336 0.9079 0.9903 0.1156  0.1946  -0.0941 111 GLN D CD  
9819  O OE1 . GLN D 111 ? 0.8953 0.9667 1.0254 0.1085  0.1878  -0.0786 111 GLN D OE1 
9820  N NE2 . GLN D 111 ? 0.8482 0.9067 1.0369 0.1234  0.1869  -0.0922 111 GLN D NE2 
9821  N N   . GLU D 112 ? 0.7768 0.8495 0.8760 0.1041  0.2103  -0.1736 112 GLU D N   
9822  C CA  . GLU D 112 ? 0.7394 0.7944 0.8400 0.1043  0.2053  -0.1909 112 GLU D CA  
9823  C C   . GLU D 112 ? 0.6800 0.7069 0.7769 0.1042  0.1930  -0.1814 112 GLU D C   
9824  O O   . GLU D 112 ? 0.6207 0.6467 0.6947 0.0989  0.1847  -0.1589 112 GLU D O   
9825  C CB  . GLU D 112 ? 0.7490 0.8238 0.8188 0.0945  0.2132  -0.2067 112 GLU D CB  
9826  C CG  . GLU D 112 ? 0.7859 0.8829 0.8625 0.0945  0.2243  -0.2229 112 GLU D CG  
9827  C CD  . GLU D 112 ? 0.8212 0.9422 0.8624 0.0823  0.2318  -0.2331 112 GLU D CD  
9828  O OE1 . GLU D 112 ? 0.8157 0.9460 0.8251 0.0733  0.2301  -0.2200 112 GLU D OE1 
9829  O OE2 . GLU D 112 ? 0.8766 1.0072 0.9229 0.0810  0.2388  -0.2538 112 GLU D OE2 
9830  N N   . SER D 113 ? 0.6781 0.6819 0.7939 0.1080  0.1854  -0.1922 113 SER D N   
9831  C CA  . SER D 113 ? 0.6724 0.6520 0.7782 0.1048  0.1711  -0.1821 113 SER D CA  
9832  C C   . SER D 113 ? 0.6780 0.6479 0.7825 0.1020  0.1718  -0.2053 113 SER D C   
9833  O O   . SER D 113 ? 0.7168 0.6908 0.8363 0.1041  0.1766  -0.2238 113 SER D O   
9834  C CB  . SER D 113 ? 0.6532 0.6091 0.7874 0.1114  0.1570  -0.1643 113 SER D CB  
9835  O OG  . SER D 113 ? 0.6787 0.6225 0.8537 0.1198  0.1571  -0.1779 113 SER D OG  
9836  N N   . GLY D 114 ? 0.6452 0.6022 0.7279 0.0950  0.1607  -0.1971 114 GLY D N   
9837  C CA  . GLY D 114 ? 0.6466 0.5947 0.7264 0.0909  0.1605  -0.2183 114 GLY D CA  
9838  C C   . GLY D 114 ? 0.6430 0.5668 0.7178 0.0871  0.1435  -0.2036 114 GLY D C   
9839  O O   . GLY D 114 ? 0.6072 0.5295 0.6668 0.0845  0.1346  -0.1786 114 GLY D O   
9840  N N   . LEU D 115 ? 0.6661 0.5714 0.7562 0.0865  0.1393  -0.2195 115 LEU D N   
9841  C CA  . LEU D 115 ? 0.6673 0.5507 0.7543 0.0818  0.1231  -0.2054 115 LEU D CA  
9842  C C   . LEU D 115 ? 0.6835 0.5759 0.7315 0.0703  0.1221  -0.2079 115 LEU D C   
9843  O O   . LEU D 115 ? 0.7260 0.6245 0.7664 0.0657  0.1291  -0.2321 115 LEU D O   
9844  C CB  . LEU D 115 ? 0.6714 0.5283 0.7968 0.0860  0.1162  -0.2169 115 LEU D CB  
9845  C CG  . LEU D 115 ? 0.6674 0.5032 0.7924 0.0811  0.0978  -0.1941 115 LEU D CG  
9846  C CD1 . LEU D 115 ? 0.6164 0.4473 0.7563 0.0860  0.0891  -0.1669 115 LEU D CD1 
9847  C CD2 . LEU D 115 ? 0.7247 0.5358 0.8776 0.0803  0.0900  -0.2067 115 LEU D CD2 
9848  N N   . GLY D 116 ? 0.6268 0.5217 0.6512 0.0654  0.1135  -0.1833 116 GLY D N   
9849  C CA  . GLY D 116 ? 0.5864 0.4895 0.5768 0.0548  0.1099  -0.1801 116 GLY D CA  
9850  C C   . GLY D 116 ? 0.5571 0.4392 0.5502 0.0505  0.0949  -0.1688 116 GLY D C   
9851  O O   . GLY D 116 ? 0.5706 0.4323 0.5911 0.0548  0.0868  -0.1627 116 GLY D O   
9852  N N   . GLU D 117 ? 0.5455 0.4348 0.5107 0.0410  0.0907  -0.1650 117 GLU D N   
9853  C CA  . GLU D 117 ? 0.5373 0.4113 0.5011 0.0350  0.0771  -0.1541 117 GLU D CA  
9854  C C   . GLU D 117 ? 0.5191 0.4024 0.4633 0.0320  0.0712  -0.1288 117 GLU D C   
9855  O O   . GLU D 117 ? 0.5193 0.4230 0.4404 0.0296  0.0763  -0.1245 117 GLU D O   
9856  C CB  . GLU D 117 ? 0.5663 0.4410 0.5170 0.0258  0.0766  -0.1720 117 GLU D CB  
9857  C CG  . GLU D 117 ? 0.6102 0.4675 0.5647 0.0190  0.0631  -0.1652 117 GLU D CG  
9858  C CD  . GLU D 117 ? 0.6841 0.5462 0.6219 0.0088  0.0630  -0.1825 117 GLU D CD  
9859  O OE1 . GLU D 117 ? 0.7150 0.6001 0.6233 0.0032  0.0674  -0.1825 117 GLU D OE1 
9860  O OE2 . GLU D 117 ? 0.7092 0.5527 0.6649 0.0061  0.0584  -0.1963 117 GLU D OE2 
9861  N N   . LEU D 118 ? 0.5167 0.3864 0.4713 0.0316  0.0603  -0.1121 118 LEU D N   
9862  C CA  . LEU D 118 ? 0.5017 0.3805 0.4401 0.0284  0.0551  -0.0913 118 LEU D CA  
9863  C C   . LEU D 118 ? 0.5177 0.4081 0.4311 0.0195  0.0531  -0.0918 118 LEU D C   
9864  O O   . LEU D 118 ? 0.5344 0.4178 0.4463 0.0131  0.0488  -0.1014 118 LEU D O   
9865  C CB  . LEU D 118 ? 0.5074 0.3720 0.4606 0.0274  0.0440  -0.0755 118 LEU D CB  
9866  C CG  . LEU D 118 ? 0.5017 0.3764 0.4422 0.0246  0.0397  -0.0559 118 LEU D CG  
9867  C CD1 . LEU D 118 ? 0.4809 0.3676 0.4193 0.0313  0.0468  -0.0495 118 LEU D CD1 
9868  C CD2 . LEU D 118 ? 0.4951 0.3583 0.4486 0.0210  0.0289  -0.0428 118 LEU D CD2 
9869  N N   . ALA D 119 ? 0.5105 0.4187 0.4068 0.0189  0.0555  -0.0805 119 ALA D N   
9870  C CA  . ALA D 119 ? 0.5072 0.4297 0.3817 0.0111  0.0535  -0.0786 119 ALA D CA  
9871  C C   . ALA D 119 ? 0.4918 0.4216 0.3615 0.0102  0.0482  -0.0588 119 ALA D C   
9872  O O   . ALA D 119 ? 0.4787 0.4064 0.3579 0.0158  0.0487  -0.0484 119 ALA D O   
9873  C CB  . ALA D 119 ? 0.5113 0.4529 0.3705 0.0103  0.0624  -0.0866 119 ALA D CB  
9874  N N   . GLN D 120 ? 0.4976 0.4371 0.3537 0.0029  0.0434  -0.0548 120 GLN D N   
9875  C CA  . GLN D 120 ? 0.4902 0.4387 0.3438 0.0019  0.0390  -0.0383 120 GLN D CA  
9876  C C   . GLN D 120 ? 0.4969 0.4655 0.3342 -0.0033 0.0387  -0.0352 120 GLN D C   
9877  O O   . GLN D 120 ? 0.5315 0.5036 0.3581 -0.0104 0.0366  -0.0441 120 GLN D O   
9878  C CB  . GLN D 120 ? 0.5290 0.4671 0.3895 -0.0030 0.0303  -0.0340 120 GLN D CB  
9879  C CG  . GLN D 120 ? 0.5456 0.4940 0.4057 -0.0050 0.0262  -0.0199 120 GLN D CG  
9880  C CD  . GLN D 120 ? 0.5878 0.5294 0.4522 -0.0123 0.0180  -0.0168 120 GLN D CD  
9881  O OE1 . GLN D 120 ? 0.6014 0.5308 0.4768 -0.0121 0.0153  -0.0143 120 GLN D OE1 
9882  N NE2 . GLN D 120 ? 0.5969 0.5481 0.4532 -0.0197 0.0134  -0.0154 120 GLN D NE2 
9883  N N   . ASP D 121 ? 0.4951 0.4773 0.3317 -0.0001 0.0403  -0.0225 121 ASP D N   
9884  C CA  . ASP D 121 ? 0.4828 0.4851 0.3077 -0.0050 0.0384  -0.0157 121 ASP D CA  
9885  C C   . ASP D 121 ? 0.4699 0.4814 0.3041 -0.0002 0.0379  0.0006  121 ASP D C   
9886  O O   . ASP D 121 ? 0.4915 0.4941 0.3387 0.0060  0.0395  0.0042  121 ASP D O   
9887  C CB  . ASP D 121 ? 0.5060 0.5200 0.3172 -0.0076 0.0441  -0.0234 121 ASP D CB  
9888  C CG  . ASP D 121 ? 0.5064 0.5394 0.3010 -0.0176 0.0394  -0.0217 121 ASP D CG  
9889  O OD1 . ASP D 121 ? 0.4976 0.5388 0.2941 -0.0203 0.0324  -0.0095 121 ASP D OD1 
9890  O OD2 . ASP D 121 ? 0.5157 0.5580 0.2958 -0.0232 0.0431  -0.0329 121 ASP D OD2 
9891  N N   . VAL D 122 ? 0.5126 0.5423 0.3418 -0.0037 0.0350  0.0103  122 VAL D N   
9892  C CA  . VAL D 122 ? 0.5398 0.5790 0.3816 0.0009  0.0341  0.0257  122 VAL D CA  
9893  C C   . VAL D 122 ? 0.5833 0.6256 0.4288 0.0063  0.0403  0.0305  122 VAL D C   
9894  O O   . VAL D 122 ? 0.6391 0.6902 0.4722 0.0030  0.0435  0.0281  122 VAL D O   
9895  C CB  . VAL D 122 ? 0.5608 0.6196 0.3997 -0.0049 0.0275  0.0367  122 VAL D CB  
9896  C CG1 . VAL D 122 ? 0.5554 0.6234 0.4126 0.0007  0.0266  0.0528  122 VAL D CG1 
9897  C CG2 . VAL D 122 ? 0.5786 0.6369 0.4171 -0.0102 0.0210  0.0341  122 VAL D CG2 
9898  N N   . LEU D 123 ? 0.5342 0.5710 0.3968 0.0136  0.0422  0.0368  123 LEU D N   
9899  C CA  . LEU D 123 ? 0.4943 0.5363 0.3649 0.0180  0.0463  0.0455  123 LEU D CA  
9900  C C   . LEU D 123 ? 0.4723 0.5218 0.3614 0.0208  0.0422  0.0596  123 LEU D C   
9901  O O   . LEU D 123 ? 0.4736 0.5183 0.3736 0.0227  0.0398  0.0582  123 LEU D O   
9902  C CB  . LEU D 123 ? 0.4684 0.4958 0.3459 0.0242  0.0525  0.0386  123 LEU D CB  
9903  C CG  . LEU D 123 ? 0.4014 0.4314 0.2900 0.0291  0.0570  0.0466  123 LEU D CG  
9904  C CD1 . LEU D 123 ? 0.3841 0.4059 0.2694 0.0317  0.0638  0.0368  123 LEU D CD1 
9905  C CD2 . LEU D 123 ? 0.3883 0.4125 0.2976 0.0345  0.0556  0.0519  123 LEU D CD2 
9906  N N   . ALA D 124 ? 0.4531 0.5154 0.3473 0.0205  0.0413  0.0730  124 ALA D N   
9907  C CA  . ALA D 124 ? 0.4072 0.4758 0.3247 0.0240  0.0372  0.0872  124 ALA D CA  
9908  C C   . ALA D 124 ? 0.4154 0.4816 0.3469 0.0289  0.0411  0.0945  124 ALA D C   
9909  O O   . ALA D 124 ? 0.4206 0.4886 0.3402 0.0271  0.0457  0.0939  124 ALA D O   
9910  C CB  . ALA D 124 ? 0.4024 0.4902 0.3179 0.0179  0.0296  0.1010  124 ALA D CB  
9911  N N   . ILE D 125 ? 0.3995 0.4624 0.3575 0.0346  0.0398  0.1004  125 ILE D N   
9912  C CA  . ILE D 125 ? 0.3757 0.4349 0.3514 0.0391  0.0428  0.1073  125 ILE D CA  
9913  C C   . ILE D 125 ? 0.3857 0.4482 0.3934 0.0431  0.0378  0.1186  125 ILE D C   
9914  O O   . ILE D 125 ? 0.4129 0.4763 0.4311 0.0447  0.0349  0.1149  125 ILE D O   
9915  C CB  . ILE D 125 ? 0.3466 0.3894 0.3234 0.0438  0.0497  0.0933  125 ILE D CB  
9916  C CG1 . ILE D 125 ? 0.3381 0.3780 0.3317 0.0472  0.0526  0.1005  125 ILE D CG1 
9917  C CG2 . ILE D 125 ? 0.3605 0.3955 0.3485 0.0470  0.0494  0.0830  125 ILE D CG2 
9918  C CD1 . ILE D 125 ? 0.3259 0.3525 0.3212 0.0508  0.0584  0.0887  125 ILE D CD1 
9919  N N   . HIS D 126 ? 0.3595 0.4249 0.3851 0.0444  0.0367  0.1326  126 HIS D N   
9920  C CA  . HIS D 126 ? 0.3650 0.4321 0.4261 0.0487  0.0316  0.1435  126 HIS D CA  
9921  C C   . HIS D 126 ? 0.3593 0.4132 0.4415 0.0557  0.0357  0.1286  126 HIS D C   
9922  O O   . HIS D 126 ? 0.3950 0.4377 0.4714 0.0575  0.0420  0.1169  126 HIS D O   
9923  C CB  . HIS D 126 ? 0.4046 0.4756 0.4832 0.0481  0.0292  0.1623  126 HIS D CB  
9924  C CG  . HIS D 126 ? 0.4550 0.5451 0.5252 0.0405  0.0219  0.1834  126 HIS D CG  
9925  N ND1 . HIS D 126 ? 0.5046 0.6064 0.5919 0.0393  0.0125  0.1976  126 HIS D ND1 
9926  C CD2 . HIS D 126 ? 0.4439 0.5457 0.4931 0.0329  0.0225  0.1939  126 HIS D CD2 
9927  C CE1 . HIS D 126 ? 0.5178 0.6379 0.5923 0.0305  0.0067  0.2168  126 HIS D CE1 
9928  N NE2 . HIS D 126 ? 0.4812 0.6024 0.5318 0.0262  0.0130  0.2144  126 HIS D NE2 
9929  N N   . SER D 127 ? 0.3277 0.3848 0.4351 0.0591  0.0322  0.1286  127 SER D N   
9930  C CA  . SER D 127 ? 0.3588 0.4068 0.4944 0.0656  0.0360  0.1163  127 SER D CA  
9931  C C   . SER D 127 ? 0.3676 0.4142 0.5406 0.0694  0.0324  0.1304  127 SER D C   
9932  O O   . SER D 127 ? 0.3623 0.4138 0.5337 0.0662  0.0280  0.1496  127 SER D O   
9933  C CB  . SER D 127 ? 0.3745 0.4283 0.5207 0.0674  0.0356  0.1059  127 SER D CB  
9934  O OG  . SER D 127 ? 0.3802 0.4468 0.5414 0.0670  0.0277  0.1210  127 SER D OG  
9935  N N   . THR D 128 ? 0.3600 0.4007 0.5676 0.0755  0.0344  0.1210  128 THR D N   
9936  C CA  . THR D 128 ? 0.3734 0.4116 0.6233 0.0796  0.0299  0.1341  128 THR D CA  
9937  C C   . THR D 128 ? 0.4239 0.4686 0.7118 0.0848  0.0259  0.1341  128 THR D C   
9938  O O   . THR D 128 ? 0.4667 0.5160 0.7508 0.0861  0.0295  0.1181  128 THR D O   
9939  C CB  . THR D 128 ? 0.3588 0.3828 0.6252 0.0826  0.0357  0.1227  128 THR D CB  
9940  O OG1 . THR D 128 ? 0.3680 0.3885 0.6418 0.0858  0.0424  0.0975  128 THR D OG1 
9941  C CG2 . THR D 128 ? 0.3212 0.3401 0.5530 0.0779  0.0398  0.1223  128 THR D CG2 
9942  N N   . HIS D 129 ? 0.4265 0.4728 0.7527 0.0875  0.0182  0.1535  129 HIS D N   
9943  C CA  . HIS D 129 ? 0.4260 0.4785 0.7955 0.0933  0.0134  0.1558  129 HIS D CA  
9944  C C   . HIS D 129 ? 0.4565 0.4987 0.8788 0.0993  0.0109  0.1609  129 HIS D C   
9945  O O   . HIS D 129 ? 0.4758 0.5190 0.9161 0.0977  0.0018  0.1871  129 HIS D O   
9946  C CB  . HIS D 129 ? 0.4501 0.5191 0.8150 0.0893  0.0026  0.1804  129 HIS D CB  
9947  C CG  . HIS D 129 ? 0.4883 0.5666 0.8961 0.0951  -0.0030 0.1837  129 HIS D CG  
9948  N ND1 . HIS D 129 ? 0.5145 0.5980 0.9654 0.0972  -0.0146 0.2091  129 HIS D ND1 
9949  C CD2 . HIS D 129 ? 0.4874 0.5725 0.9031 0.0988  0.0011  0.1656  129 HIS D CD2 
9950  C CE1 . HIS D 129 ? 0.5082 0.5998 0.9899 0.1016  -0.0170 0.2043  129 HIS D CE1 
9951  N NE2 . HIS D 129 ? 0.4932 0.5873 0.9575 0.1040  -0.0074 0.1790  129 HIS D NE2 
9952  N N   . GLY D 130 ? 0.4659 0.4994 0.9144 0.1055  0.0187  0.1360  130 GLY D N   
9953  C CA  . GLY D 130 ? 0.4652 0.4858 0.9487 0.1053  0.0178  0.1324  130 GLY D CA  
9954  C C   . GLY D 130 ? 0.4785 0.4893 0.9443 0.1012  0.0183  0.1418  130 GLY D C   
9955  O O   . GLY D 130 ? 0.4606 0.4673 0.8968 0.1016  0.0262  0.1300  130 GLY D O   
9956  N N   . SER D 131 ? 0.5007 0.5094 0.9839 0.0962  0.0099  0.1636  131 SER D N   
9957  C CA  . SER D 131 ? 0.5031 0.5053 0.9731 0.0910  0.0096  0.1755  131 SER D CA  
9958  C C   . SER D 131 ? 0.4588 0.4730 0.8947 0.0859  0.0046  0.2029  131 SER D C   
9959  O O   . SER D 131 ? 0.3843 0.3968 0.8063 0.0807  0.0045  0.2147  131 SER D O   
9960  C CB  . SER D 131 ? 0.5168 0.5124 1.0261 0.0870  0.0039  0.1834  131 SER D CB  
9961  O OG  . SER D 131 ? 0.5274 0.5346 1.0517 0.0823  -0.0073 0.2113  131 SER D OG  
9962  N N   . LYS D 132 ? 0.4667 0.4947 0.8886 0.0866  0.0006  0.2120  132 LYS D N   
9963  C CA  . LYS D 132 ? 0.4500 0.4931 0.8349 0.0792  -0.0044 0.2347  132 LYS D CA  
9964  C C   . LYS D 132 ? 0.4028 0.4498 0.7332 0.0761  0.0041  0.2150  132 LYS D C   
9965  O O   . LYS D 132 ? 0.4096 0.4497 0.7349 0.0806  0.0117  0.1892  132 LYS D O   
9966  C CB  . LYS D 132 ? 0.4869 0.5467 0.8862 0.0760  -0.0161 0.2560  132 LYS D CB  
9967  C CG  . LYS D 132 ? 0.5630 0.6241 1.0035 0.0715  -0.0247 0.2703  132 LYS D CG  
9968  C CD  . LYS D 132 ? 0.6532 0.7369 1.0819 0.0614  -0.0360 0.2997  132 LYS D CD  
9969  C CE  . LYS D 132 ? 0.7134 0.8026 1.1877 0.0574  -0.0465 0.3161  132 LYS D CE  
9970  N NZ  . LYS D 132 ? 0.7201 0.8291 1.1953 0.0529  -0.0563 0.3326  132 LYS D NZ  
9971  N N   . LEU D 133 ? 0.4138 0.4730 0.7045 0.0676  0.0024  0.2277  133 LEU D N   
9972  C CA  . LEU D 133 ? 0.4120 0.4768 0.6561 0.0642  0.0078  0.2129  133 LEU D CA  
9973  C C   . LEU D 133 ? 0.4210 0.4951 0.6724 0.0659  0.0029  0.2119  133 LEU D C   
9974  O O   . LEU D 133 ? 0.4623 0.5474 0.7384 0.0650  -0.0074 0.2332  133 LEU D O   
9975  C CB  . LEU D 133 ? 0.4341 0.5118 0.6383 0.0543  0.0070  0.2262  133 LEU D CB  
9976  C CG  . LEU D 133 ? 0.4282 0.5004 0.6144 0.0514  0.0140  0.2240  133 LEU D CG  
9977  C CD1 . LEU D 133 ? 0.4564 0.5467 0.6064 0.0412  0.0130  0.2367  133 LEU D CD1 
9978  C CD2 . LEU D 133 ? 0.3614 0.4189 0.5295 0.0557  0.0246  0.1954  133 LEU D CD2 
9979  N N   . GLY D 134 ? 0.4112 0.4823 0.6415 0.0675  0.0095  0.1889  134 GLY D N   
9980  C CA  . GLY D 134 ? 0.3733 0.4542 0.6088 0.0685  0.0058  0.1861  134 GLY D CA  
9981  C C   . GLY D 134 ? 0.3911 0.4833 0.5816 0.0602  0.0044  0.1878  134 GLY D C   
9982  O O   . GLY D 134 ? 0.3763 0.4707 0.5364 0.0538  0.0056  0.1933  134 GLY D O   
9983  N N   . PRO D 135 ? 0.4197 0.5201 0.6071 0.0598  0.0023  0.1820  135 PRO D N   
9984  C CA  . PRO D 135 ? 0.4474 0.5589 0.5955 0.0514  0.0000  0.1824  135 PRO D CA  
9985  C C   . PRO D 135 ? 0.4603 0.5613 0.5682 0.0485  0.0092  0.1631  135 PRO D C   
9986  O O   . PRO D 135 ? 0.4316 0.5182 0.5429 0.0535  0.0170  0.1469  135 PRO D O   
9987  C CB  . PRO D 135 ? 0.4620 0.5818 0.6248 0.0533  -0.0032 0.1773  135 PRO D CB  
9988  C CG  . PRO D 135 ? 0.4524 0.5621 0.6518 0.0631  0.0024  0.1637  135 PRO D CG  
9989  C CD  . PRO D 135 ? 0.4426 0.5433 0.6666 0.0672  0.0022  0.1734  135 PRO D CD  
9990  N N   . MET D 136 ? 0.4903 0.5991 0.5620 0.0402  0.0078  0.1649  136 MET D N   
9991  C CA  . MET D 136 ? 0.4991 0.5984 0.5360 0.0374  0.0154  0.1468  136 MET D CA  
9992  C C   . MET D 136 ? 0.4490 0.5417 0.4836 0.0395  0.0184  0.1288  136 MET D C   
9993  O O   . MET D 136 ? 0.4796 0.5819 0.5229 0.0384  0.0134  0.1310  136 MET D O   
9994  C CB  . MET D 136 ? 0.5843 0.6955 0.5871 0.0276  0.0128  0.1510  136 MET D CB  
9995  C CG  . MET D 136 ? 0.6483 0.7730 0.6505 0.0226  0.0087  0.1714  136 MET D CG  
9996  S SD  . MET D 136 ? 0.6003 0.7152 0.5925 0.0239  0.0180  0.1673  136 MET D SD  
9997  C CE  . MET D 136 ? 0.5030 0.6168 0.4520 0.0177  0.0243  0.1475  136 MET D CE  
9998  N N   . VAL D 137 ? 0.3717 0.4499 0.3946 0.0415  0.0260  0.1123  137 VAL D N   
9999  C CA  . VAL D 137 ? 0.3492 0.4223 0.3644 0.0410  0.0287  0.0963  137 VAL D CA  
10000 C C   . VAL D 137 ? 0.3763 0.4421 0.3580 0.0358  0.0315  0.0865  137 VAL D C   
10001 O O   . VAL D 137 ? 0.4315 0.4928 0.4006 0.0352  0.0343  0.0875  137 VAL D O   
10002 C CB  . VAL D 137 ? 0.3454 0.4094 0.3808 0.0472  0.0344  0.0853  137 VAL D CB  
10003 C CG1 . VAL D 137 ? 0.3551 0.4272 0.4260 0.0521  0.0321  0.0902  137 VAL D CG1 
10004 C CG2 . VAL D 137 ? 0.3470 0.3992 0.3824 0.0502  0.0395  0.0836  137 VAL D CG2 
10005 N N   . LYS D 138 ? 0.4036 0.4689 0.3731 0.0318  0.0305  0.0775  138 LYS D N   
10006 C CA  . LYS D 138 ? 0.4032 0.4617 0.3450 0.0264  0.0314  0.0689  138 LYS D CA  
10007 C C   . LYS D 138 ? 0.4135 0.4587 0.3505 0.0267  0.0352  0.0558  138 LYS D C   
10008 O O   . LYS D 138 ? 0.4005 0.4465 0.3491 0.0276  0.0357  0.0519  138 LYS D O   
10009 C CB  . LYS D 138 ? 0.4432 0.5122 0.3727 0.0191  0.0252  0.0709  138 LYS D CB  
10010 C CG  . LYS D 138 ? 0.4768 0.5617 0.4071 0.0163  0.0199  0.0852  138 LYS D CG  
10011 C CD  . LYS D 138 ? 0.5357 0.6324 0.4546 0.0082  0.0130  0.0866  138 LYS D CD  
10012 C CE  . LYS D 138 ? 0.5891 0.7049 0.5093 0.0041  0.0062  0.1031  138 LYS D CE  
10013 N NZ  . LYS D 138 ? 0.6310 0.7596 0.5388 -0.0050 -0.0011 0.1041  138 LYS D NZ  
10014 N N   . VAL D 139 ? 0.4462 0.4809 0.3666 0.0254  0.0379  0.0495  139 VAL D N   
10015 C CA  . VAL D 139 ? 0.4409 0.4638 0.3526 0.0230  0.0386  0.0392  139 VAL D CA  
10016 C C   . VAL D 139 ? 0.4738 0.4963 0.3675 0.0161  0.0349  0.0350  139 VAL D C   
10017 O O   . VAL D 139 ? 0.4926 0.5115 0.3741 0.0150  0.0367  0.0313  139 VAL D O   
10018 C CB  . VAL D 139 ? 0.4201 0.4303 0.3311 0.0268  0.0436  0.0344  139 VAL D CB  
10019 C CG1 . VAL D 139 ? 0.4259 0.4247 0.3320 0.0239  0.0426  0.0267  139 VAL D CG1 
10020 C CG2 . VAL D 139 ? 0.3642 0.3753 0.2928 0.0328  0.0470  0.0383  139 VAL D CG2 
10021 N N   . PRO D 140 ? 0.4610 0.4880 0.3538 0.0108  0.0303  0.0344  140 PRO D N   
10022 C CA  . PRO D 140 ? 0.4737 0.5025 0.3514 0.0034  0.0257  0.0312  140 PRO D CA  
10023 C C   . PRO D 140 ? 0.4980 0.5107 0.3645 0.0005  0.0264  0.0204  140 PRO D C   
10024 O O   . PRO D 140 ? 0.5227 0.5357 0.3765 -0.0043 0.0248  0.0151  140 PRO D O   
10025 C CB  . PRO D 140 ? 0.4476 0.4852 0.3316 -0.0012 0.0209  0.0338  140 PRO D CB  
10026 C CG  . PRO D 140 ? 0.4215 0.4660 0.3246 0.0048  0.0236  0.0388  140 PRO D CG  
10027 C CD  . PRO D 140 ? 0.4093 0.4423 0.3157 0.0109  0.0293  0.0360  140 PRO D CD  
10028 N N   . GLN D 141 ? 0.5353 0.5353 0.4080 0.0031  0.0284  0.0172  141 GLN D N   
10029 C CA  . GLN D 141 ? 0.5810 0.5649 0.4490 0.0016  0.0284  0.0083  141 GLN D CA  
10030 C C   . GLN D 141 ? 0.5338 0.5091 0.4070 0.0089  0.0343  0.0061  141 GLN D C   
10031 O O   . GLN D 141 ? 0.5189 0.4825 0.3989 0.0100  0.0339  0.0044  141 GLN D O   
10032 C CB  . GLN D 141 ? 0.6827 0.6580 0.5553 -0.0033 0.0236  0.0081  141 GLN D CB  
10033 C CG  . GLN D 141 ? 0.8005 0.7808 0.6694 -0.0121 0.0171  0.0092  141 GLN D CG  
10034 C CD  . GLN D 141 ? 0.9212 0.9171 0.7963 -0.0133 0.0163  0.0169  141 GLN D CD  
10035 O OE1 . GLN D 141 ? 0.9601 0.9611 0.8437 -0.0077 0.0205  0.0202  141 GLN D OE1 
10036 N NE2 . GLN D 141 ? 0.9856 0.9895 0.8585 -0.0209 0.0111  0.0186  141 GLN D NE2 
10037 N N   . PHE D 142 ? 0.5008 0.4829 0.3714 0.0130  0.0391  0.0070  142 PHE D N   
10038 C CA  . PHE D 142 ? 0.4631 0.4389 0.3397 0.0195  0.0450  0.0054  142 PHE D CA  
10039 C C   . PHE D 142 ? 0.4333 0.3965 0.3083 0.0197  0.0468  -0.0060 142 PHE D C   
10040 O O   . PHE D 142 ? 0.4807 0.4457 0.3458 0.0162  0.0475  -0.0141 142 PHE D O   
10041 C CB  . PHE D 142 ? 0.4908 0.4791 0.3662 0.0227  0.0495  0.0111  142 PHE D CB  
10042 C CG  . PHE D 142 ? 0.5176 0.5017 0.4005 0.0289  0.0556  0.0106  142 PHE D CG  
10043 C CD1 . PHE D 142 ? 0.5133 0.4945 0.4097 0.0334  0.0564  0.0162  142 PHE D CD1 
10044 C CD2 . PHE D 142 ? 0.5353 0.5199 0.4123 0.0297  0.0610  0.0033  142 PHE D CD2 
10045 C CE1 . PHE D 142 ? 0.5337 0.5116 0.4378 0.0385  0.0616  0.0161  142 PHE D CE1 
10046 C CE2 . PHE D 142 ? 0.5322 0.5144 0.4177 0.0352  0.0669  0.0031  142 PHE D CE2 
10047 C CZ  . PHE D 142 ? 0.5177 0.4962 0.4167 0.0396  0.0667  0.0103  142 PHE D CZ  
10048 N N   . LEU D 143 ? 0.4251 0.3766 0.3114 0.0236  0.0477  -0.0070 143 LEU D N   
10049 C CA  . LEU D 143 ? 0.4281 0.3667 0.3197 0.0252  0.0491  -0.0171 143 LEU D CA  
10050 C C   . LEU D 143 ? 0.4279 0.3694 0.3226 0.0313  0.0575  -0.0219 143 LEU D C   
10051 O O   . LEU D 143 ? 0.4429 0.3888 0.3433 0.0359  0.0608  -0.0151 143 LEU D O   
10052 C CB  . LEU D 143 ? 0.4376 0.3634 0.3427 0.0254  0.0440  -0.0134 143 LEU D CB  
10053 C CG  . LEU D 143 ? 0.4609 0.3843 0.3643 0.0179  0.0356  -0.0086 143 LEU D CG  
10054 C CD1 . LEU D 143 ? 0.4660 0.3811 0.3818 0.0167  0.0304  -0.0018 143 LEU D CD1 
10055 C CD2 . LEU D 143 ? 0.4834 0.4003 0.3817 0.0127  0.0325  -0.0176 143 LEU D CD2 
10056 N N   . PHE D 144 ? 0.4544 0.3937 0.3463 0.0309  0.0613  -0.0351 144 PHE D N   
10057 C CA  . PHE D 144 ? 0.4320 0.3779 0.3256 0.0355  0.0705  -0.0418 144 PHE D CA  
10058 C C   . PHE D 144 ? 0.4795 0.4172 0.3776 0.0353  0.0735  -0.0598 144 PHE D C   
10059 O O   . PHE D 144 ? 0.5462 0.4721 0.4464 0.0316  0.0675  -0.0655 144 PHE D O   
10060 C CB  . PHE D 144 ? 0.4374 0.4037 0.3147 0.0326  0.0748  -0.0376 144 PHE D CB  
10061 C CG  . PHE D 144 ? 0.4550 0.4294 0.3151 0.0247  0.0732  -0.0450 144 PHE D CG  
10062 C CD1 . PHE D 144 ? 0.4495 0.4251 0.3023 0.0192  0.0651  -0.0380 144 PHE D CD1 
10063 C CD2 . PHE D 144 ? 0.4655 0.4484 0.3167 0.0220  0.0801  -0.0599 144 PHE D CD2 
10064 C CE1 . PHE D 144 ? 0.4546 0.4387 0.2917 0.0110  0.0629  -0.0446 144 PHE D CE1 
10065 C CE2 . PHE D 144 ? 0.4712 0.4633 0.3052 0.0132  0.0783  -0.0678 144 PHE D CE2 
10066 C CZ  . PHE D 144 ? 0.4594 0.4516 0.2863 0.0077  0.0692  -0.0595 144 PHE D CZ  
10067 N N   . SER D 145 ? 0.4670 0.4120 0.3676 0.0389  0.0830  -0.0697 145 SER D N   
10068 C CA  . SER D 145 ? 0.4653 0.4035 0.3738 0.0395  0.0873  -0.0901 145 SER D CA  
10069 C C   . SER D 145 ? 0.5213 0.4777 0.4108 0.0339  0.0951  -0.1039 145 SER D C   
10070 O O   . SER D 145 ? 0.5565 0.5327 0.4342 0.0330  0.1014  -0.0989 145 SER D O   
10071 C CB  . SER D 145 ? 0.4454 0.3775 0.3773 0.0483  0.0929  -0.0946 145 SER D CB  
10072 O OG  . SER D 145 ? 0.4683 0.3952 0.4113 0.0498  0.0983  -0.1163 145 SER D OG  
10073 N N   . CYS D 146 ? 0.5418 0.4927 0.4285 0.0290  0.0940  -0.1209 146 CYS D N   
10074 C CA  . CYS D 146 ? 0.5535 0.5219 0.4249 0.0233  0.1029  -0.1395 146 CYS D CA  
10075 C C   . CYS D 146 ? 0.5804 0.5465 0.4709 0.0300  0.1134  -0.1586 146 CYS D C   
10076 O O   . CYS D 146 ? 0.6158 0.5637 0.5261 0.0326  0.1123  -0.1741 146 CYS D O   
10077 C CB  . CYS D 146 ? 0.5612 0.5255 0.4222 0.0144  0.0977  -0.1524 146 CYS D CB  
10078 S SG  . CYS D 146 ? 0.6653 0.6450 0.4981 0.0039  0.0890  -0.1352 146 CYS D SG  
10079 N N   . ALA D 147 ? 0.5808 0.5661 0.4680 0.0325  0.1235  -0.1573 147 ALA D N   
10080 C CA  . ALA D 147 ? 0.5858 0.5713 0.4947 0.0400  0.1343  -0.1735 147 ALA D CA  
10081 C C   . ALA D 147 ? 0.6795 0.6831 0.5784 0.0343  0.1462  -0.2012 147 ALA D C   
10082 O O   . ALA D 147 ? 0.7030 0.7262 0.5727 0.0235  0.1470  -0.2027 147 ALA D O   
10083 C CB  . ALA D 147 ? 0.5637 0.5609 0.4769 0.0455  0.1393  -0.1577 147 ALA D CB  
10084 N N   . PRO D 148 ? 0.7332 0.7317 0.6578 0.0411  0.1554  -0.2239 148 PRO D N   
10085 C CA  . PRO D 148 ? 0.7420 0.7609 0.6596 0.0360  0.1693  -0.2540 148 PRO D CA  
10086 C C   . PRO D 148 ? 0.7562 0.8123 0.6481 0.0295  0.1797  -0.2492 148 PRO D C   
10087 O O   . PRO D 148 ? 0.7633 0.8276 0.6589 0.0342  0.1825  -0.2315 148 PRO D O   
10088 C CB  . PRO D 148 ? 0.7329 0.7372 0.6912 0.0476  0.1745  -0.2710 148 PRO D CB  
10089 C CG  . PRO D 148 ? 0.7068 0.6914 0.6895 0.0583  0.1678  -0.2502 148 PRO D CG  
10090 C CD  . PRO D 148 ? 0.7185 0.6919 0.6821 0.0533  0.1524  -0.2238 148 PRO D CD  
10091 N N   . SER D 149 ? 0.7508 0.8273 0.6190 0.0181  0.1816  -0.2595 149 SER D N   
10092 C CA  . SER D 149 ? 0.7691 0.8807 0.6107 0.0089  0.1870  -0.2497 149 SER D CA  
10093 C C   . SER D 149 ? 0.7638 0.8895 0.6199 0.0152  0.1975  -0.2483 149 SER D C   
10094 O O   . SER D 149 ? 0.7764 0.9253 0.6170 0.0108  0.2004  -0.2303 149 SER D O   
10095 C CB  . SER D 149 ? 0.8189 0.9477 0.6405 -0.0037 0.1877  -0.2660 149 SER D CB  
10096 O OG  . SER D 149 ? 0.8705 1.0301 0.6825 -0.0091 0.1969  -0.2669 149 SER D OG  
10097 N N   . PHE D 150 ? 0.7384 0.8509 0.6260 0.0248  0.2026  -0.2664 150 PHE D N   
10098 C CA  . PHE D 150 ? 0.7204 0.8475 0.6235 0.0304  0.2128  -0.2674 150 PHE D CA  
10099 C C   . PHE D 150 ? 0.6652 0.7908 0.5756 0.0374  0.2122  -0.2430 150 PHE D C   
10100 O O   . PHE D 150 ? 0.6733 0.8184 0.5862 0.0382  0.2199  -0.2364 150 PHE D O   
10101 C CB  . PHE D 150 ? 0.7670 0.8781 0.7065 0.0400  0.2166  -0.2909 150 PHE D CB  
10102 C CG  . PHE D 150 ? 0.7725 0.8515 0.7476 0.0540  0.2103  -0.2853 150 PHE D CG  
10103 C CD1 . PHE D 150 ? 0.7215 0.8008 0.7150 0.0632  0.2126  -0.2704 150 PHE D CD1 
10104 C CD2 . PHE D 150 ? 0.7843 0.8333 0.7755 0.0571  0.2012  -0.2939 150 PHE D CD2 
10105 C CE1 . PHE D 150 ? 0.6717 0.7232 0.6981 0.0747  0.2054  -0.2638 150 PHE D CE1 
10106 C CE2 . PHE D 150 ? 0.7436 0.7641 0.7680 0.0686  0.1939  -0.2862 150 PHE D CE2 
10107 C CZ  . PHE D 150 ? 0.6936 0.7159 0.7352 0.0773  0.1957  -0.2707 150 PHE D CZ  
10108 N N   . LEU D 151 ? 0.6162 0.7197 0.5305 0.0416  0.2034  -0.2299 151 LEU D N   
10109 C CA  . LEU D 151 ? 0.5996 0.6969 0.5292 0.0498  0.2031  -0.2104 151 LEU D CA  
10110 C C   . LEU D 151 ? 0.6077 0.7314 0.5154 0.0431  0.2061  -0.1882 151 LEU D C   
10111 O O   . LEU D 151 ? 0.5855 0.7132 0.5083 0.0487  0.2091  -0.1758 151 LEU D O   
10112 C CB  . LEU D 151 ? 0.5537 0.6180 0.4920 0.0545  0.1875  -0.1952 151 LEU D CB  
10113 C CG  . LEU D 151 ? 0.4881 0.5379 0.4503 0.0645  0.1820  -0.1748 151 LEU D CG  
10114 C CD1 . LEU D 151 ? 0.5465 0.5929 0.5443 0.0748  0.1905  -0.1901 151 LEU D CD1 
10115 C CD2 . LEU D 151 ? 0.4703 0.4914 0.4372 0.0669  0.1653  -0.1567 151 LEU D CD2 
10116 N N   . ALA D 152 ? 0.6384 0.7796 0.5130 0.0306  0.2031  -0.1807 152 ALA D N   
10117 C CA  . ALA D 152 ? 0.6332 0.7973 0.4889 0.0234  0.2024  -0.1550 152 ALA D CA  
10118 C C   . ALA D 152 ? 0.6849 0.8804 0.5277 0.0149  0.2106  -0.1569 152 ALA D C   
10119 O O   . ALA D 152 ? 0.7042 0.9208 0.5316 0.0069  0.2097  -0.1355 152 ALA D O   
10120 C CB  . ALA D 152 ? 0.6102 0.7711 0.4424 0.0153  0.1889  -0.1370 152 ALA D CB  
10121 N N   . GLN D 153 ? 0.7045 0.9024 0.5562 0.0164  0.2177  -0.1815 153 GLN D N   
10122 C CA  . GLN D 153 ? 0.7433 0.9714 0.5805 0.0064  0.2251  -0.1870 153 GLN D CA  
10123 C C   . GLN D 153 ? 0.7320 0.9771 0.5810 0.0089  0.2339  -0.1774 153 GLN D C   
10124 O O   . GLN D 153 ? 0.7647 1.0378 0.6004 -0.0007 0.2399  -0.1765 153 GLN D O   
10125 C CB  . GLN D 153 ? 0.7992 1.0253 0.6432 0.0065  0.2303  -0.2188 153 GLN D CB  
10126 C CG  . GLN D 153 ? 0.8552 1.0792 0.6777 -0.0031 0.2233  -0.2286 153 GLN D CG  
10127 C CD  . GLN D 153 ? 0.9655 1.1848 0.8000 -0.0023 0.2285  -0.2612 153 GLN D CD  
10128 O OE1 . GLN D 153 ? 0.9744 1.1928 0.8340 0.0057  0.2373  -0.2764 153 GLN D OE1 
10129 N NE2 . GLN D 153 ? 1.0294 1.2451 0.8487 -0.0104 0.2225  -0.2722 153 GLN D NE2 
10130 N N   . LYS D 154 ? 0.7263 0.9559 0.6005 0.0209  0.2345  -0.1697 154 LYS D N   
10131 C CA  . LYS D 154 ? 0.7389 0.9843 0.6274 0.0236  0.2430  -0.1618 154 LYS D CA  
10132 C C   . LYS D 154 ? 0.6820 0.9207 0.5807 0.0282  0.2391  -0.1369 154 LYS D C   
10133 O O   . LYS D 154 ? 0.6535 0.8676 0.5641 0.0360  0.2325  -0.1347 154 LYS D O   
10134 C CB  . LYS D 154 ? 0.8004 1.0380 0.7199 0.0349  0.2509  -0.1850 154 LYS D CB  
10135 C CG  . LYS D 154 ? 0.8718 1.1197 0.7865 0.0304  0.2571  -0.2121 154 LYS D CG  
10136 C CD  . LYS D 154 ? 0.9116 1.1522 0.8617 0.0422  0.2644  -0.2333 154 LYS D CD  
10137 C CE  . LYS D 154 ? 0.9139 1.1300 0.8970 0.0569  0.2599  -0.2247 154 LYS D CE  
10138 N NZ  . LYS D 154 ? 0.9548 1.1614 0.9742 0.0679  0.2642  -0.2451 154 LYS D NZ  
10139 N N   . GLY D 155 ? 0.6812 0.9422 0.5751 0.0219  0.2426  -0.1178 155 GLY D N   
10140 C CA  . GLY D 155 ? 0.6521 0.9094 0.5632 0.0269  0.2411  -0.0971 155 GLY D CA  
10141 C C   . GLY D 155 ? 0.6234 0.8794 0.5196 0.0211  0.2304  -0.0708 155 GLY D C   
10142 O O   . GLY D 155 ? 0.6198 0.8722 0.5275 0.0230  0.2254  -0.0483 155 GLY D O   
10143 N N   . LEU D 156 ? 0.5961 0.8481 0.4694 0.0150  0.2230  -0.0719 156 LEU D N   
10144 C CA  . LEU D 156 ? 0.5653 0.8080 0.4280 0.0115  0.2091  -0.0469 156 LEU D CA  
10145 C C   . LEU D 156 ? 0.5948 0.8667 0.4351 -0.0037 0.2078  -0.0283 156 LEU D C   
10146 O O   . LEU D 156 ? 0.6564 0.9464 0.4857 -0.0116 0.2139  -0.0385 156 LEU D O   
10147 C CB  . LEU D 156 ? 0.5512 0.7704 0.4051 0.0135  0.1995  -0.0563 156 LEU D CB  
10148 C CG  . LEU D 156 ? 0.5153 0.7038 0.3895 0.0260  0.1990  -0.0771 156 LEU D CG  
10149 C CD1 . LEU D 156 ? 0.5008 0.6686 0.3639 0.0253  0.1875  -0.0792 156 LEU D CD1 
10150 C CD2 . LEU D 156 ? 0.4800 0.6472 0.3832 0.0375  0.1953  -0.0666 156 LEU D CD2 
10151 N N   . PRO D 157 ? 0.5663 0.8381 0.4034 -0.0073 0.1969  0.0004  157 PRO D N   
10152 C CA  . PRO D 157 ? 0.5803 0.8723 0.3996 -0.0221 0.1904  0.0201  157 PRO D CA  
10153 C C   . PRO D 157 ? 0.6236 0.9229 0.4180 -0.0308 0.1880  0.0061  157 PRO D C   
10154 O O   . PRO D 157 ? 0.6119 0.8952 0.4034 -0.0251 0.1876  -0.0122 157 PRO D O   
10155 C CB  . PRO D 157 ? 0.5564 0.8381 0.3825 -0.0209 0.1773  0.0496  157 PRO D CB  
10156 C CG  . PRO D 157 ? 0.5216 0.7736 0.3760 -0.0060 0.1766  0.0478  157 PRO D CG  
10157 C CD  . PRO D 157 ? 0.5287 0.7674 0.3866 0.0027  0.1846  0.0167  157 PRO D CD  
10158 N N   . ASN D 158 ? 0.6990 1.0230 0.4770 -0.0446 0.1858  0.0143  158 ASN D N   
10159 C CA  . ASN D 158 ? 0.8029 1.1367 0.5586 -0.0529 0.1842  -0.0015 158 ASN D CA  
10160 C C   . ASN D 158 ? 0.7918 1.1130 0.5384 -0.0542 0.1706  0.0082  158 ASN D C   
10161 O O   . ASN D 158 ? 0.7878 1.1033 0.5413 -0.0538 0.1603  0.0346  158 ASN D O   
10162 C CB  . ASN D 158 ? 0.9154 1.2829 0.6557 -0.0683 0.1851  0.0041  158 ASN D CB  
10163 C CG  . ASN D 158 ? 0.9887 1.3697 0.7268 -0.0782 0.1724  0.0393  158 ASN D CG  
10164 O OD1 . ASN D 158 ? 1.0143 1.3832 0.7540 -0.0774 0.1597  0.0572  158 ASN D OD1 
10165 N ND2 . ASN D 158 ? 1.0195 1.4267 0.7562 -0.0877 0.1753  0.0497  158 ASN D ND2 
10166 N N   . ASN D 159 ? 0.7944 1.1098 0.5290 -0.0547 0.1709  -0.0144 159 ASN D N   
10167 C CA  . ASN D 159 ? 0.7934 1.0980 0.5184 -0.0564 0.1590  -0.0099 159 ASN D CA  
10168 C C   . ASN D 159 ? 0.7234 0.9995 0.4629 -0.0435 0.1559  -0.0074 159 ASN D C   
10169 O O   . ASN D 159 ? 0.7128 0.9781 0.4461 -0.0437 0.1469  -0.0058 159 ASN D O   
10170 C CB  . ASN D 159 ? 0.8719 1.1945 0.5877 -0.0684 0.1458  0.0196  159 ASN D CB  
10171 C CG  . ASN D 159 ? 0.9782 1.3252 0.6725 -0.0829 0.1433  0.0118  159 ASN D CG  
10172 O OD1 . ASN D 159 ? 1.0303 1.4042 0.7181 -0.0934 0.1450  0.0186  159 ASN D OD1 
10173 N ND2 . ASN D 159 ? 1.0032 1.3424 0.6867 -0.0845 0.1384  -0.0015 159 ASN D ND2 
10174 N N   . VAL D 160 ? 0.6715 0.9369 0.4308 -0.0327 0.1635  -0.0086 160 VAL D N   
10175 C CA  . VAL D 160 ? 0.6442 0.8787 0.4217 -0.0192 0.1595  -0.0090 160 VAL D CA  
10176 C C   . VAL D 160 ? 0.7155 0.9318 0.4947 -0.0132 0.1638  -0.0400 160 VAL D C   
10177 O O   . VAL D 160 ? 0.7600 0.9859 0.5397 -0.0128 0.1765  -0.0628 160 VAL D O   
10178 C CB  . VAL D 160 ? 0.5681 0.7906 0.3716 -0.0092 0.1621  0.0010  160 VAL D CB  
10179 C CG1 . VAL D 160 ? 0.4584 0.6444 0.2835 0.0050  0.1589  -0.0094 160 VAL D CG1 
10180 C CG2 . VAL D 160 ? 0.5183 0.7467 0.3271 -0.0128 0.1529  0.0339  160 VAL D CG2 
10181 N N   . GLN D 161 ? 0.7343 0.9243 0.5172 -0.0085 0.1532  -0.0408 161 GLN D N   
10182 C CA  . GLN D 161 ? 0.7202 0.8958 0.5008 -0.0066 0.1547  -0.0675 161 GLN D CA  
10183 C C   . GLN D 161 ? 0.6254 0.7639 0.4315 0.0072  0.1507  -0.0739 161 GLN D C   
10184 O O   . GLN D 161 ? 0.6054 0.7267 0.4132 0.0090  0.1481  -0.0905 161 GLN D O   
10185 C CB  . GLN D 161 ? 0.7625 0.9443 0.5214 -0.0167 0.1452  -0.0641 161 GLN D CB  
10186 C CG  . GLN D 161 ? 0.8372 1.0580 0.5681 -0.0325 0.1499  -0.0651 161 GLN D CG  
10187 C CD  . GLN D 161 ? 0.8948 1.1233 0.6089 -0.0425 0.1364  -0.0489 161 GLN D CD  
10188 O OE1 . GLN D 161 ? 0.9177 1.1249 0.6376 -0.0382 0.1265  -0.0444 161 GLN D OE1 
10189 N NE2 . GLN D 161 ? 0.9142 1.1677 0.6151 -0.0544 0.1327  -0.0365 161 GLN D NE2 
10190 N N   . GLY D 162 ? 0.5386 0.6660 0.3648 0.0159  0.1501  -0.0604 162 GLY D N   
10191 C CA  . GLY D 162 ? 0.4856 0.5819 0.3348 0.0272  0.1454  -0.0632 162 GLY D CA  
10192 C C   . GLY D 162 ? 0.4500 0.5394 0.3152 0.0331  0.1418  -0.0425 162 GLY D C   
10193 O O   . GLY D 162 ? 0.4629 0.5709 0.3261 0.0300  0.1458  -0.0301 162 GLY D O   
10194 N N   . ALA D 163 ? 0.4196 0.4835 0.3006 0.0405  0.1341  -0.0388 163 ALA D N   
10195 C CA  . ALA D 163 ? 0.3952 0.4513 0.2922 0.0457  0.1304  -0.0220 163 ALA D CA  
10196 C C   . ALA D 163 ? 0.4462 0.4825 0.3478 0.0479  0.1190  -0.0134 163 ALA D C   
10197 O O   . ALA D 163 ? 0.4599 0.4829 0.3592 0.0481  0.1144  -0.0223 163 ALA D O   
10198 C CB  . ALA D 163 ? 0.3846 0.4343 0.3027 0.0533  0.1364  -0.0291 163 ALA D CB  
10199 N N   . LEU D 164 ? 0.4588 0.4945 0.3678 0.0489  0.1147  0.0036  164 LEU D N   
10200 C CA  . LEU D 164 ? 0.4876 0.5065 0.4047 0.0516  0.1058  0.0101  164 LEU D CA  
10201 C C   . LEU D 164 ? 0.4560 0.4646 0.3931 0.0576  0.1061  0.0123  164 LEU D C   
10202 O O   . LEU D 164 ? 0.4776 0.4943 0.4230 0.0587  0.1103  0.0192  164 LEU D O   
10203 C CB  . LEU D 164 ? 0.5424 0.5685 0.4554 0.0478  0.1001  0.0255  164 LEU D CB  
10204 C CG  . LEU D 164 ? 0.5924 0.6307 0.5131 0.0472  0.1029  0.0396  164 LEU D CG  
10205 C CD1 . LEU D 164 ? 0.6050 0.6323 0.5439 0.0510  0.0978  0.0489  164 LEU D CD1 
10206 C CD2 . LEU D 164 ? 0.6207 0.6785 0.5285 0.0399  0.1020  0.0502  164 LEU D CD2 
10207 N N   . GLY D 165 ? 0.4352 0.4274 0.3797 0.0605  0.1011  0.0071  165 GLY D N   
10208 C CA  . GLY D 165 ? 0.4052 0.3887 0.3675 0.0650  0.1002  0.0086  165 GLY D CA  
10209 C C   . GLY D 165 ? 0.3754 0.3522 0.3429 0.0643  0.0930  0.0175  165 GLY D C   
10210 O O   . GLY D 165 ? 0.3745 0.3466 0.3348 0.0617  0.0874  0.0176  165 GLY D O   
10211 N N   . LEU D 166 ? 0.3645 0.3422 0.3452 0.0661  0.0936  0.0237  166 LEU D N   
10212 C CA  . LEU D 166 ? 0.3378 0.3110 0.3249 0.0649  0.0880  0.0295  166 LEU D CA  
10213 C C   . LEU D 166 ? 0.3785 0.3447 0.3779 0.0661  0.0851  0.0279  166 LEU D C   
10214 O O   . LEU D 166 ? 0.3833 0.3489 0.3911 0.0650  0.0825  0.0316  166 LEU D O   
10215 C CB  . LEU D 166 ? 0.3680 0.3489 0.3616 0.0645  0.0899  0.0387  166 LEU D CB  
10216 C CG  . LEU D 166 ? 0.4237 0.4141 0.4081 0.0622  0.0911  0.0448  166 LEU D CG  
10217 C CD1 . LEU D 166 ? 0.4125 0.4091 0.4095 0.0617  0.0919  0.0560  166 LEU D CD1 
10218 C CD2 . LEU D 166 ? 0.4305 0.4179 0.4069 0.0601  0.0856  0.0438  166 LEU D CD2 
10219 N N   . GLY D 167 ? 0.3639 0.3254 0.3656 0.0681  0.0854  0.0220  167 GLY D N   
10220 C CA  . GLY D 167 ? 0.3960 0.3523 0.4116 0.0691  0.0818  0.0224  167 GLY D CA  
10221 C C   . GLY D 167 ? 0.4207 0.3705 0.4340 0.0648  0.0730  0.0239  167 GLY D C   
10222 O O   . GLY D 167 ? 0.4101 0.3585 0.4115 0.0616  0.0704  0.0229  167 GLY D O   
10223 N N   . GLN D 168 ? 0.4346 0.3825 0.4598 0.0638  0.0683  0.0267  168 GLN D N   
10224 C CA  . GLN D 168 ? 0.4450 0.3901 0.4676 0.0578  0.0595  0.0295  168 GLN D CA  
10225 C C   . GLN D 168 ? 0.4685 0.4053 0.4909 0.0574  0.0549  0.0281  168 GLN D C   
10226 O O   . GLN D 168 ? 0.5146 0.4474 0.5507 0.0585  0.0508  0.0306  168 GLN D O   
10227 C CB  . GLN D 168 ? 0.3804 0.3294 0.4152 0.0552  0.0552  0.0344  168 GLN D CB  
10228 C CG  . GLN D 168 ? 0.3281 0.2840 0.3626 0.0533  0.0581  0.0345  168 GLN D CG  
10229 C CD  . GLN D 168 ? 0.3504 0.3086 0.3725 0.0482  0.0564  0.0320  168 GLN D CD  
10230 O OE1 . GLN D 168 ? 0.4242 0.3845 0.4420 0.0416  0.0501  0.0328  168 GLN D OE1 
10231 N NE2 . GLN D 168 ? 0.3327 0.2920 0.3500 0.0506  0.0617  0.0297  168 GLN D NE2 
10232 N N   . ALA D 169 ? 0.4584 0.3926 0.4672 0.0557  0.0550  0.0247  169 ALA D N   
10233 C CA  . ALA D 169 ? 0.4097 0.3347 0.4187 0.0552  0.0511  0.0221  169 ALA D CA  
10234 C C   . ALA D 169 ? 0.4003 0.3260 0.3928 0.0495  0.0483  0.0217  169 ALA D C   
10235 O O   . ALA D 169 ? 0.4462 0.3792 0.4288 0.0489  0.0521  0.0211  169 ALA D O   
10236 C CB  . ALA D 169 ? 0.4092 0.3313 0.4225 0.0618  0.0583  0.0136  169 ALA D CB  
10237 N N   . PRO D 170 ? 0.4005 0.3189 0.3927 0.0451  0.0411  0.0229  170 PRO D N   
10238 C CA  . PRO D 170 ? 0.3891 0.3103 0.3674 0.0379  0.0371  0.0245  170 PRO D CA  
10239 C C   . PRO D 170 ? 0.4026 0.3267 0.3669 0.0388  0.0422  0.0185  170 PRO D C   
10240 O O   . PRO D 170 ? 0.4282 0.3601 0.3832 0.0345  0.0414  0.0203  170 PRO D O   
10241 C CB  . PRO D 170 ? 0.4012 0.3125 0.3861 0.0332  0.0281  0.0281  170 PRO D CB  
10242 C CG  . PRO D 170 ? 0.4302 0.3316 0.4324 0.0400  0.0291  0.0249  170 PRO D CG  
10243 C CD  . PRO D 170 ? 0.4125 0.3209 0.4208 0.0455  0.0349  0.0253  170 PRO D CD  
10244 N N   . ILE D 171 ? 0.4231 0.3435 0.3865 0.0437  0.0474  0.0112  171 ILE D N   
10245 C CA  . ILE D 171 ? 0.3784 0.3050 0.3278 0.0434  0.0515  0.0074  171 ILE D CA  
10246 C C   . ILE D 171 ? 0.3858 0.3201 0.3346 0.0487  0.0599  0.0058  171 ILE D C   
10247 O O   . ILE D 171 ? 0.4246 0.3636 0.3642 0.0491  0.0640  0.0014  171 ILE D O   
10248 C CB  . ILE D 171 ? 0.4201 0.3402 0.3634 0.0411  0.0501  -0.0002 171 ILE D CB  
10249 C CG1 . ILE D 171 ? 0.4391 0.3518 0.3919 0.0460  0.0540  -0.0094 171 ILE D CG1 
10250 C CG2 . ILE D 171 ? 0.4206 0.3346 0.3634 0.0341  0.0411  0.0033  171 ILE D CG2 
10251 C CD1 . ILE D 171 ? 0.4339 0.3448 0.3777 0.0439  0.0558  -0.0204 171 ILE D CD1 
10252 N N   . SER D 172 ? 0.4022 0.3395 0.3603 0.0516  0.0619  0.0103  172 SER D N   
10253 C CA  . SER D 172 ? 0.4208 0.3668 0.3795 0.0554  0.0689  0.0117  172 SER D CA  
10254 C C   . SER D 172 ? 0.4233 0.3774 0.3728 0.0529  0.0688  0.0156  172 SER D C   
10255 O O   . SER D 172 ? 0.4416 0.3955 0.3875 0.0491  0.0639  0.0169  172 SER D O   
10256 C CB  . SER D 172 ? 0.3991 0.3463 0.3710 0.0577  0.0698  0.0163  172 SER D CB  
10257 O OG  . SER D 172 ? 0.4080 0.3567 0.3808 0.0541  0.0652  0.0204  172 SER D OG  
10258 N N   . LEU D 173 ? 0.4176 0.3806 0.3652 0.0546  0.0738  0.0184  173 LEU D N   
10259 C CA  . LEU D 173 ? 0.4057 0.3770 0.3482 0.0526  0.0726  0.0240  173 LEU D CA  
10260 C C   . LEU D 173 ? 0.4167 0.3882 0.3691 0.0524  0.0696  0.0282  173 LEU D C   
10261 O O   . LEU D 173 ? 0.4398 0.4143 0.3899 0.0499  0.0663  0.0292  173 LEU D O   
10262 C CB  . LEU D 173 ? 0.4147 0.3966 0.3563 0.0536  0.0775  0.0295  173 LEU D CB  
10263 C CG  . LEU D 173 ? 0.4038 0.3945 0.3468 0.0520  0.0750  0.0388  173 LEU D CG  
10264 C CD1 . LEU D 173 ? 0.3965 0.3905 0.3268 0.0479  0.0710  0.0372  173 LEU D CD1 
10265 C CD2 . LEU D 173 ? 0.4238 0.4256 0.3689 0.0520  0.0787  0.0477  173 LEU D CD2 
10266 N N   . GLN D 174 ? 0.3835 0.3532 0.3482 0.0546  0.0712  0.0297  174 GLN D N   
10267 C CA  . GLN D 174 ? 0.3798 0.3512 0.3546 0.0538  0.0692  0.0309  174 GLN D CA  
10268 C C   . GLN D 174 ? 0.4419 0.4109 0.4126 0.0495  0.0647  0.0260  174 GLN D C   
10269 O O   . GLN D 174 ? 0.4446 0.4186 0.4178 0.0473  0.0633  0.0249  174 GLN D O   
10270 C CB  . GLN D 174 ? 0.3786 0.3493 0.3677 0.0560  0.0716  0.0326  174 GLN D CB  
10271 C CG  . GLN D 174 ? 0.3498 0.3155 0.3421 0.0547  0.0700  0.0289  174 GLN D CG  
10272 C CD  . GLN D 174 ? 0.3376 0.2993 0.3272 0.0569  0.0716  0.0285  174 GLN D CD  
10273 O OE1 . GLN D 174 ? 0.3978 0.3613 0.3816 0.0590  0.0750  0.0290  174 GLN D OE1 
10274 N NE2 . GLN D 174 ? 0.3366 0.2946 0.3317 0.0561  0.0691  0.0273  174 GLN D NE2 
10275 N N   . ASN D 175 ? 0.4369 0.3996 0.4031 0.0479  0.0625  0.0236  175 ASN D N   
10276 C CA  . ASN D 175 ? 0.4394 0.4015 0.4021 0.0422  0.0573  0.0218  175 ASN D CA  
10277 C C   . ASN D 175 ? 0.4215 0.3870 0.3749 0.0390  0.0552  0.0210  175 ASN D C   
10278 O O   . ASN D 175 ? 0.3966 0.3681 0.3492 0.0342  0.0529  0.0199  175 ASN D O   
10279 C CB  A ASN D 175 ? 0.4917 0.4457 0.4545 0.0410  0.0537  0.0221  175 ASN D CB  
10280 C CB  B ASN D 175 ? 0.4917 0.4455 0.4545 0.0411  0.0539  0.0221  175 ASN D CB  
10281 C CG  A ASN D 175 ? 0.5543 0.5069 0.5285 0.0433  0.0546  0.0238  175 ASN D CG  
10282 C CG  B ASN D 175 ? 0.5118 0.4659 0.4706 0.0336  0.0470  0.0234  175 ASN D CG  
10283 O OD1 A ASN D 175 ? 0.6172 0.5709 0.5975 0.0483  0.0597  0.0241  175 ASN D OD1 
10284 O OD1 B ASN D 175 ? 0.5173 0.4753 0.4799 0.0293  0.0440  0.0253  175 ASN D OD1 
10285 N ND2 A ASN D 175 ? 0.5506 0.5024 0.5281 0.0387  0.0490  0.0261  175 ASN D ND2 
10286 N ND2 B ASN D 175 ? 0.5518 0.5028 0.5025 0.0308  0.0441  0.0228  175 ASN D ND2 
10287 N N   . GLN D 176 ? 0.3968 0.3609 0.3432 0.0409  0.0564  0.0212  176 GLN D N   
10288 C CA  . GLN D 176 ? 0.3668 0.3351 0.3049 0.0374  0.0538  0.0209  176 GLN D CA  
10289 C C   . GLN D 176 ? 0.3729 0.3519 0.3166 0.0382  0.0550  0.0233  176 GLN D C   
10290 O O   . GLN D 176 ? 0.3640 0.3492 0.3063 0.0344  0.0524  0.0226  176 GLN D O   
10291 C CB  . GLN D 176 ? 0.3552 0.3201 0.2833 0.0378  0.0541  0.0191  176 GLN D CB  
10292 C CG  . GLN D 176 ? 0.3480 0.3017 0.2734 0.0361  0.0516  0.0146  176 GLN D CG  
10293 C CD  . GLN D 176 ? 0.3821 0.3336 0.2978 0.0349  0.0519  0.0094  176 GLN D CD  
10294 O OE1 . GLN D 176 ? 0.4005 0.3545 0.3083 0.0302  0.0483  0.0088  176 GLN D OE1 
10295 N NE2 . GLN D 176 ? 0.4101 0.3584 0.3266 0.0387  0.0565  0.0046  176 GLN D NE2 
10296 N N   . LEU D 177 ? 0.3393 0.3210 0.2921 0.0429  0.0585  0.0267  177 LEU D N   
10297 C CA  . LEU D 177 ? 0.3082 0.2985 0.2724 0.0444  0.0590  0.0297  177 LEU D CA  
10298 C C   . LEU D 177 ? 0.3413 0.3350 0.3165 0.0431  0.0594  0.0244  177 LEU D C   
10299 O O   . LEU D 177 ? 0.3508 0.3528 0.3316 0.0416  0.0586  0.0227  177 LEU D O   
10300 C CB  . LEU D 177 ? 0.3065 0.2982 0.2806 0.0491  0.0618  0.0362  177 LEU D CB  
10301 C CG  . LEU D 177 ? 0.3342 0.3285 0.2969 0.0489  0.0620  0.0419  177 LEU D CG  
10302 C CD1 . LEU D 177 ? 0.3433 0.3403 0.3159 0.0520  0.0648  0.0498  177 LEU D CD1 
10303 C CD2 . LEU D 177 ? 0.3281 0.3311 0.2863 0.0463  0.0582  0.0459  177 LEU D CD2 
10304 N N   . PHE D 178 ? 0.3480 0.3373 0.3263 0.0428  0.0608  0.0211  178 PHE D N   
10305 C CA  . PHE D 178 ? 0.3237 0.3183 0.3097 0.0396  0.0615  0.0144  178 PHE D CA  
10306 C C   . PHE D 178 ? 0.3512 0.3531 0.3286 0.0332  0.0589  0.0110  178 PHE D C   
10307 O O   . PHE D 178 ? 0.3594 0.3719 0.3450 0.0314  0.0605  0.0057  178 PHE D O   
10308 C CB  . PHE D 178 ? 0.3871 0.3771 0.3719 0.0376  0.0612  0.0126  178 PHE D CB  
10309 C CG  . PHE D 178 ? 0.4299 0.4144 0.4250 0.0428  0.0640  0.0152  178 PHE D CG  
10310 C CD1 . PHE D 178 ? 0.4172 0.4027 0.4259 0.0477  0.0667  0.0179  178 PHE D CD1 
10311 C CD2 . PHE D 178 ? 0.4482 0.4273 0.4414 0.0422  0.0632  0.0163  178 PHE D CD2 
10312 C CE1 . PHE D 178 ? 0.3908 0.3722 0.4096 0.0513  0.0689  0.0216  178 PHE D CE1 
10313 C CE2 . PHE D 178 ? 0.4433 0.4190 0.4469 0.0463  0.0659  0.0190  178 PHE D CE2 
10314 C CZ  . PHE D 178 ? 0.3777 0.3546 0.3933 0.0505  0.0689  0.0216  178 PHE D CZ  
10315 N N   . SER D 179 ? 0.3456 0.3424 0.3083 0.0293  0.0551  0.0137  179 SER D N   
10316 C CA  . SER D 179 ? 0.3530 0.3568 0.3077 0.0215  0.0518  0.0120  179 SER D CA  
10317 C C   . SER D 179 ? 0.3899 0.4009 0.3439 0.0212  0.0513  0.0127  179 SER D C   
10318 O O   . SER D 179 ? 0.4165 0.4390 0.3705 0.0157  0.0509  0.0097  179 SER D O   
10319 C CB  . SER D 179 ? 0.4016 0.3965 0.3450 0.0169  0.0466  0.0159  179 SER D CB  
10320 O OG  . SER D 179 ? 0.5196 0.5055 0.4562 0.0191  0.0447  0.0187  179 SER D OG  
10321 N N   . HIS D 180 ? 0.3568 0.3634 0.3101 0.0262  0.0512  0.0168  180 HIS D N   
10322 C CA  . HIS D 180 ? 0.3385 0.3536 0.2918 0.0251  0.0496  0.0185  180 HIS D CA  
10323 C C   . HIS D 180 ? 0.3685 0.3958 0.3403 0.0279  0.0528  0.0158  180 HIS D C   
10324 O O   . HIS D 180 ? 0.3992 0.4382 0.3746 0.0247  0.0522  0.0139  180 HIS D O   
10325 C CB  . HIS D 180 ? 0.3398 0.3505 0.2870 0.0282  0.0480  0.0241  180 HIS D CB  
10326 C CG  . HIS D 180 ? 0.3730 0.3925 0.3170 0.0249  0.0445  0.0266  180 HIS D CG  
10327 N ND1 . HIS D 180 ? 0.3925 0.4224 0.3485 0.0281  0.0443  0.0312  180 HIS D ND1 
10328 C CD2 . HIS D 180 ? 0.3929 0.4130 0.3251 0.0183  0.0403  0.0258  180 HIS D CD2 
10329 C CE1 . HIS D 180 ? 0.3760 0.4134 0.3265 0.0236  0.0402  0.0332  180 HIS D CE1 
10330 N NE2 . HIS D 180 ? 0.4136 0.4450 0.3492 0.0174  0.0379  0.0294  180 HIS D NE2 
10331 N N   . PHE D 181 ? 0.3470 0.3721 0.3331 0.0338  0.0563  0.0152  181 PHE D N   
10332 C CA  . PHE D 181 ? 0.3074 0.3420 0.3167 0.0379  0.0591  0.0125  181 PHE D CA  
10333 C C   . PHE D 181 ? 0.3293 0.3696 0.3504 0.0364  0.0637  0.0010  181 PHE D C   
10334 O O   . PHE D 181 ? 0.3525 0.4002 0.3960 0.0400  0.0669  -0.0043 181 PHE D O   
10335 C CB  . PHE D 181 ? 0.2934 0.3228 0.3159 0.0450  0.0591  0.0206  181 PHE D CB  
10336 C CG  . PHE D 181 ? 0.3434 0.3735 0.3572 0.0454  0.0548  0.0315  181 PHE D CG  
10337 C CD1 . PHE D 181 ? 0.3902 0.4312 0.4127 0.0453  0.0519  0.0354  181 PHE D CD1 
10338 C CD2 . PHE D 181 ? 0.3484 0.3702 0.3456 0.0451  0.0538  0.0370  181 PHE D CD2 
10339 C CE1 . PHE D 181 ? 0.4226 0.4666 0.4353 0.0440  0.0470  0.0458  181 PHE D CE1 
10340 C CE2 . PHE D 181 ? 0.3858 0.4110 0.3728 0.0438  0.0503  0.0453  181 PHE D CE2 
10341 C CZ  . PHE D 181 ? 0.4029 0.4395 0.3969 0.0427  0.0464  0.0502  181 PHE D CZ  
10342 N N   . GLY D 182 ? 0.3295 0.3670 0.3372 0.0310  0.0639  -0.0032 182 GLY D N   
10343 C CA  . GLY D 182 ? 0.3295 0.3748 0.3455 0.0277  0.0681  -0.0146 182 GLY D CA  
10344 C C   . GLY D 182 ? 0.3733 0.4127 0.4081 0.0338  0.0714  -0.0180 182 GLY D C   
10345 O O   . GLY D 182 ? 0.3823 0.4300 0.4345 0.0338  0.0759  -0.0296 182 GLY D O   
10346 N N   . LEU D 183 ? 0.3951 0.4207 0.4273 0.0385  0.0695  -0.0087 183 LEU D N   
10347 C CA  . LEU D 183 ? 0.3979 0.4168 0.4481 0.0438  0.0718  -0.0090 183 LEU D CA  
10348 C C   . LEU D 183 ? 0.3833 0.4013 0.4314 0.0395  0.0733  -0.0166 183 LEU D C   
10349 O O   . LEU D 183 ? 0.3907 0.4104 0.4204 0.0330  0.0712  -0.0170 183 LEU D O   
10350 C CB  . LEU D 183 ? 0.4026 0.4108 0.4492 0.0489  0.0695  0.0048  183 LEU D CB  
10351 C CG  . LEU D 183 ? 0.3459 0.3562 0.3916 0.0517  0.0668  0.0145  183 LEU D CG  
10352 C CD1 . LEU D 183 ? 0.2974 0.3003 0.3338 0.0540  0.0653  0.0261  183 LEU D CD1 
10353 C CD2 . LEU D 183 ? 0.3330 0.3491 0.4064 0.0562  0.0675  0.0147  183 LEU D CD2 
10354 N N   . LYS D 184 ? 0.3705 0.3863 0.4390 0.0423  0.0762  -0.0219 184 LYS D N   
10355 C CA  . LYS D 184 ? 0.3742 0.3876 0.4411 0.0387  0.0766  -0.0264 184 LYS D CA  
10356 C C   . LYS D 184 ? 0.3747 0.3770 0.4279 0.0406  0.0733  -0.0132 184 LYS D C   
10357 O O   . LYS D 184 ? 0.3516 0.3470 0.4069 0.0464  0.0727  -0.0027 184 LYS D O   
10358 C CB  . LYS D 184 ? 0.4392 0.4506 0.5334 0.0417  0.0799  -0.0343 184 LYS D CB  
10359 C CG  . LYS D 184 ? 0.5065 0.5138 0.5994 0.0383  0.0793  -0.0361 184 LYS D CG  
10360 C CD  . LYS D 184 ? 0.5518 0.5589 0.6699 0.0381  0.0824  -0.0481 184 LYS D CD  
10361 C CE  . LYS D 184 ? 0.5675 0.5707 0.6795 0.0340  0.0803  -0.0458 184 LYS D CE  
10362 N NZ  . LYS D 184 ? 0.5838 0.5809 0.7211 0.0355  0.0818  -0.0506 184 LYS D NZ  
10363 N N   . ARG D 185 ? 0.3544 0.3568 0.3946 0.0351  0.0711  -0.0136 185 ARG D N   
10364 C CA  . ARG D 185 ? 0.3316 0.3249 0.3617 0.0371  0.0685  -0.0030 185 ARG D CA  
10365 C C   . ARG D 185 ? 0.3641 0.3507 0.4083 0.0414  0.0702  0.0006  185 ARG D C   
10366 O O   . ARG D 185 ? 0.3584 0.3450 0.4048 0.0384  0.0693  -0.0011 185 ARG D O   
10367 C CB  . ARG D 185 ? 0.3287 0.3251 0.3438 0.0298  0.0643  -0.0029 185 ARG D CB  
10368 C CG  . ARG D 185 ? 0.3258 0.3294 0.3274 0.0242  0.0620  -0.0044 185 ARG D CG  
10369 C CD  . ARG D 185 ? 0.3904 0.3961 0.3791 0.0165  0.0563  -0.0003 185 ARG D CD  
10370 N NE  . ARG D 185 ? 0.4810 0.4745 0.4650 0.0206  0.0530  0.0093  185 ARG D NE  
10371 C CZ  . ARG D 185 ? 0.4903 0.4785 0.4655 0.0218  0.0510  0.0136  185 ARG D CZ  
10372 N NH1 . ARG D 185 ? 0.4799 0.4744 0.4490 0.0187  0.0511  0.0111  185 ARG D NH1 
10373 N NH2 . ARG D 185 ? 0.5254 0.5028 0.4995 0.0257  0.0491  0.0194  185 ARG D NH2 
10374 N N   . GLN D 186 ? 0.3708 0.3532 0.4248 0.0477  0.0721  0.0070  186 GLN D N   
10375 C CA  . GLN D 186 ? 0.3746 0.3522 0.4442 0.0511  0.0737  0.0122  186 GLN D CA  
10376 C C   . GLN D 186 ? 0.3400 0.3154 0.4107 0.0563  0.0743  0.0241  186 GLN D C   
10377 O O   . GLN D 186 ? 0.3355 0.3136 0.4058 0.0577  0.0737  0.0259  186 GLN D O   
10378 C CB  . GLN D 186 ? 0.3767 0.3558 0.4687 0.0502  0.0753  0.0031  186 GLN D CB  
10379 C CG  . GLN D 186 ? 0.3921 0.3658 0.5045 0.0527  0.0762  0.0080  186 GLN D CG  
10380 C CD  . GLN D 186 ? 0.4615 0.4356 0.5986 0.0518  0.0776  -0.0033 186 GLN D CD  
10381 O OE1 . GLN D 186 ? 0.5276 0.5048 0.6663 0.0466  0.0781  -0.0155 186 GLN D OE1 
10382 N NE2 . GLN D 186 ? 0.4249 0.3969 0.5826 0.0564  0.0779  -0.0001 186 GLN D NE2 
10383 N N   . PHE D 187 ? 0.3274 0.3001 0.3982 0.0580  0.0754  0.0326  187 PHE D N   
10384 C CA  . PHE D 187 ? 0.3566 0.3309 0.4296 0.0610  0.0763  0.0446  187 PHE D CA  
10385 C C   . PHE D 187 ? 0.3651 0.3383 0.4539 0.0617  0.0779  0.0520  187 PHE D C   
10386 O O   . PHE D 187 ? 0.3706 0.3418 0.4630 0.0604  0.0787  0.0485  187 PHE D O   
10387 C CB  . PHE D 187 ? 0.3312 0.3076 0.3816 0.0612  0.0769  0.0482  187 PHE D CB  
10388 C CG  . PHE D 187 ? 0.3692 0.3438 0.4116 0.0611  0.0789  0.0468  187 PHE D CG  
10389 C CD1 . PHE D 187 ? 0.3439 0.3151 0.3783 0.0593  0.0770  0.0389  187 PHE D CD1 
10390 C CD2 . PHE D 187 ? 0.3829 0.3609 0.4272 0.0623  0.0823  0.0541  187 PHE D CD2 
10391 C CE1 . PHE D 187 ? 0.3543 0.3239 0.3861 0.0599  0.0780  0.0385  187 PHE D CE1 
10392 C CE2 . PHE D 187 ? 0.3828 0.3603 0.4234 0.0630  0.0847  0.0517  187 PHE D CE2 
10393 C CZ  . PHE D 187 ? 0.3714 0.3440 0.4072 0.0623  0.0822  0.0440  187 PHE D CZ  
10394 N N   . SER D 188 ? 0.3611 0.3369 0.4608 0.0629  0.0774  0.0636  188 SER D N   
10395 C CA  . SER D 188 ? 0.3922 0.3679 0.5105 0.0626  0.0780  0.0732  188 SER D CA  
10396 C C   . SER D 188 ? 0.4126 0.3966 0.5229 0.0619  0.0791  0.0884  188 SER D C   
10397 O O   . SER D 188 ? 0.3977 0.3872 0.5006 0.0618  0.0772  0.0949  188 SER D O   
10398 C CB  . SER D 188 ? 0.4100 0.3813 0.5577 0.0634  0.0754  0.0735  188 SER D CB  
10399 O OG  . SER D 188 ? 0.4089 0.3754 0.5627 0.0629  0.0756  0.0567  188 SER D OG  
10400 N N   . VAL D 189 ? 0.4058 0.3931 0.5181 0.0605  0.0821  0.0943  189 VAL D N   
10401 C CA  . VAL D 189 ? 0.3364 0.3353 0.4394 0.0583  0.0845  0.1074  189 VAL D CA  
10402 C C   . VAL D 189 ? 0.3337 0.3360 0.4593 0.0556  0.0833  0.1230  189 VAL D C   
10403 O O   . VAL D 189 ? 0.3266 0.3236 0.4692 0.0553  0.0838  0.1215  189 VAL D O   
10404 C CB  . VAL D 189 ? 0.3387 0.3420 0.4248 0.0584  0.0901  0.1011  189 VAL D CB  
10405 C CG1 . VAL D 189 ? 0.3709 0.3896 0.4435 0.0554  0.0938  0.1110  189 VAL D CG1 
10406 C CG2 . VAL D 189 ? 0.3342 0.3312 0.4036 0.0607  0.0897  0.0862  189 VAL D CG2 
10407 N N   . CYS D 190 ? 0.3537 0.3651 0.4811 0.0529  0.0806  0.1391  190 CYS D N   
10408 C CA  . CYS D 190 ? 0.3577 0.3752 0.5052 0.0488  0.0787  0.1582  190 CYS D CA  
10409 C C   . CYS D 190 ? 0.4026 0.4403 0.5312 0.0431  0.0810  0.1726  190 CYS D C   
10410 O O   . CYS D 190 ? 0.4196 0.4654 0.5459 0.0404  0.0764  0.1852  190 CYS D O   
10411 C CB  . CYS D 190 ? 0.3501 0.3604 0.5266 0.0497  0.0709  0.1676  190 CYS D CB  
10412 S SG  . CYS D 190 ? 0.4536 0.4601 0.6688 0.0462  0.0674  0.1840  190 CYS D SG  
10413 N N   . LEU D 191 ? 0.4126 0.4601 0.5285 0.0409  0.0883  0.1702  191 LEU D N   
10414 C CA  . LEU D 191 ? 0.3729 0.4430 0.4693 0.0344  0.0926  0.1805  191 LEU D CA  
10415 C C   . LEU D 191 ? 0.3627 0.4451 0.4761 0.0271  0.0895  0.2052  191 LEU D C   
10416 O O   . LEU D 191 ? 0.3791 0.4548 0.5167 0.0267  0.0884  0.2109  191 LEU D O   
10417 C CB  . LEU D 191 ? 0.3802 0.4577 0.4609 0.0351  0.1025  0.1674  191 LEU D CB  
10418 C CG  . LEU D 191 ? 0.3836 0.4493 0.4498 0.0419  0.1052  0.1444  191 LEU D CG  
10419 C CD1 . LEU D 191 ? 0.4118 0.4870 0.4683 0.0425  0.1147  0.1340  191 LEU D CD1 
10420 C CD2 . LEU D 191 ? 0.3776 0.4445 0.4236 0.0418  0.1026  0.1401  191 LEU D CD2 
10421 N N   . SER D 192 ? 0.3856 0.4871 0.4863 0.0200  0.0875  0.2206  192 SER D N   
10422 C CA  . SER D 192 ? 0.4380 0.5551 0.5526 0.0109  0.0836  0.2477  192 SER D CA  
10423 C C   . SER D 192 ? 0.4750 0.6176 0.5712 0.0032  0.0932  0.2508  192 SER D C   
10424 O O   . SER D 192 ? 0.4942 0.6510 0.5606 0.0017  0.1002  0.2390  192 SER D O   
10425 C CB  . SER D 192 ? 0.4550 0.5815 0.5687 0.0060  0.0743  0.2659  192 SER D CB  
10426 O OG  . SER D 192 ? 0.5163 0.6608 0.6430 -0.0045 0.0696  0.2953  192 SER D OG  
10427 N N   . ARG D 193 ? 0.4412 0.5904 0.5564 -0.0020 0.0939  0.2657  193 ARG D N   
10428 C CA  . ARG D 193 ? 0.4570 0.6338 0.5576 -0.0103 0.1036  0.2700  193 ARG D CA  
10429 C C   . ARG D 193 ? 0.4689 0.6774 0.5473 -0.0227 0.1029  0.2857  193 ARG D C   
10430 O O   . ARG D 193 ? 0.4736 0.7057 0.5338 -0.0290 0.1112  0.2803  193 ARG D O   
10431 C CB  . ARG D 193 ? 0.4939 0.6703 0.6217 -0.0135 0.1038  0.2824  193 ARG D CB  
10432 C CG  . ARG D 193 ? 0.5812 0.7630 0.7311 -0.0220 0.0922  0.3093  193 ARG D CG  
10433 C CD  . ARG D 193 ? 0.6615 0.8455 0.8324 -0.0253 0.0941  0.3149  193 ARG D CD  
10434 N NE  . ARG D 193 ? 0.7352 0.8918 0.9269 -0.0159 0.0971  0.3028  193 ARG D NE  
10435 C CZ  . ARG D 193 ? 0.7824 0.9364 0.9887 -0.0155 0.1017  0.2980  193 ARG D CZ  
10436 N NH1 . ARG D 193 ? 0.8143 0.9922 1.0192 -0.0242 0.1054  0.3078  193 ARG D NH1 
10437 N NH2 . ARG D 193 ? 0.7736 0.9015 0.9941 -0.0062 0.1004  0.2790  193 ARG D NH2 
10438 N N   . TYR D 194 ? 0.4916 0.6991 0.5732 -0.0257 0.0901  0.2990  194 TYR D N   
10439 C CA  . TYR D 194 ? 0.5438 0.7788 0.6068 -0.0377 0.0845  0.3098  194 TYR D CA  
10440 C C   . TYR D 194 ? 0.5197 0.7617 0.5515 -0.0377 0.0866  0.2969  194 TYR D C   
10441 O O   . TYR D 194 ? 0.5507 0.7740 0.5857 -0.0298 0.0833  0.2922  194 TYR D O   
10442 C CB  . TYR D 194 ? 0.6341 0.8676 0.7251 -0.0423 0.0676  0.3350  194 TYR D CB  
10443 C CG  . TYR D 194 ? 0.7104 0.9295 0.8383 -0.0400 0.0644  0.3449  194 TYR D CG  
10444 C CD1 . TYR D 194 ? 0.7890 1.0250 0.9192 -0.0479 0.0677  0.3522  194 TYR D CD1 
10445 C CD2 . TYR D 194 ? 0.7134 0.9021 0.8737 -0.0303 0.0585  0.3448  194 TYR D CD2 
10446 C CE1 . TYR D 194 ? 0.8131 1.0360 0.9773 -0.0463 0.0645  0.3604  194 TYR D CE1 
10447 C CE2 . TYR D 194 ? 0.7476 0.9225 0.9423 -0.0287 0.0555  0.3508  194 TYR D CE2 
10448 C CZ  . TYR D 194 ? 0.7886 0.9805 0.9850 -0.0369 0.0582  0.3592  194 TYR D CZ  
10449 O OH  . TYR D 194 ? 0.7850 0.9638 1.0154 -0.0360 0.0549  0.3648  194 TYR D OH  
10450 N N   . SER D 195 ? 0.5424 0.8114 0.5442 -0.0470 0.0922  0.2901  195 SER D N   
10451 C CA  . SER D 195 ? 0.5661 0.8432 0.5377 -0.0486 0.0936  0.2764  195 SER D CA  
10452 C C   . SER D 195 ? 0.6228 0.9031 0.5995 -0.0537 0.0777  0.2947  195 SER D C   
10453 O O   . SER D 195 ? 0.6845 0.9646 0.6443 -0.0532 0.0752  0.2869  195 SER D O   
10454 C CB  . SER D 195 ? 0.6101 0.9153 0.5511 -0.0579 0.1041  0.2620  195 SER D CB  
10455 O OG  . SER D 195 ? 0.6577 0.9873 0.6004 -0.0707 0.0990  0.2800  195 SER D OG  
10456 N N   . THR D 196 ? 0.6258 0.9089 0.6290 -0.0583 0.0662  0.3192  196 THR D N   
10457 C CA  . THR D 196 ? 0.6444 0.9354 0.6575 -0.0642 0.0504  0.3390  196 THR D CA  
10458 C C   . THR D 196 ? 0.6174 0.8804 0.6596 -0.0532 0.0416  0.3442  196 THR D C   
10459 O O   . THR D 196 ? 0.6450 0.9112 0.7039 -0.0559 0.0281  0.3606  196 THR D O   
10460 C CB  . THR D 196 ? 0.6663 0.9764 0.6982 -0.0750 0.0410  0.3642  196 THR D CB  
10461 O OG1 . THR D 196 ? 0.6759 0.9656 0.7455 -0.0684 0.0378  0.3742  196 THR D OG1 
10462 C CG2 . THR D 196 ? 0.6718 1.0116 0.6765 -0.0865 0.0502  0.3592  196 THR D CG2 
10463 N N   . SER D 197 ? 0.5868 0.8232 0.6390 -0.0410 0.0490  0.3309  197 SER D N   
10464 C CA  . SER D 197 ? 0.5885 0.7982 0.6663 -0.0302 0.0423  0.3318  197 SER D CA  
10465 C C   . SER D 197 ? 0.5456 0.7345 0.6122 -0.0189 0.0539  0.3093  197 SER D C   
10466 O O   . SER D 197 ? 0.5626 0.7512 0.6177 -0.0172 0.0663  0.2967  197 SER D O   
10467 C CB  . SER D 197 ? 0.6381 0.8333 0.7609 -0.0273 0.0340  0.3470  197 SER D CB  
10468 O OG  . SER D 197 ? 0.6718 0.8590 0.8006 -0.0249 0.0432  0.3408  197 SER D OG  
10469 N N   . ASN D 198 ? 0.5121 0.6852 0.5833 -0.0113 0.0499  0.3044  198 ASN D N   
10470 C CA  . ASN D 198 ? 0.4880 0.6405 0.5476 -0.0004 0.0572  0.2723  198 ASN D CA  
10471 C C   . ASN D 198 ? 0.4536 0.5779 0.5424 0.0102  0.0584  0.2612  198 ASN D C   
10472 O O   . ASN D 198 ? 0.4302 0.5452 0.5536 0.0116  0.0512  0.2761  198 ASN D O   
10473 C CB  . ASN D 198 ? 0.4914 0.6396 0.5422 0.0027  0.0515  0.2651  198 ASN D CB  
10474 C CG  . ASN D 198 ? 0.5342 0.7083 0.5494 -0.0072 0.0522  0.2669  198 ASN D CG  
10475 O OD1 . ASN D 198 ? 0.5918 0.7860 0.5841 -0.0153 0.0597  0.2664  198 ASN D OD1 
10476 N ND2 . ASN D 198 ? 0.5248 0.7000 0.5359 -0.0072 0.0447  0.2678  198 ASN D ND2 
10477 N N   . GLY D 199 ? 0.4124 0.5241 0.4878 0.0171  0.0672  0.2348  199 GLY D N   
10478 C CA  . GLY D 199 ? 0.4130 0.4989 0.5092 0.0267  0.0679  0.2197  199 GLY D CA  
10479 C C   . GLY D 199 ? 0.4426 0.5168 0.5282 0.0331  0.0669  0.2011  199 GLY D C   
10480 O O   . GLY D 199 ? 0.4859 0.5704 0.5547 0.0301  0.0638  0.2039  199 GLY D O   
10481 N N   . ALA D 200 ? 0.4072 0.4617 0.5017 0.0407  0.0690  0.1826  200 ALA D N   
10482 C CA  . ALA D 200 ? 0.4144 0.4597 0.4996 0.0454  0.0678  0.1666  200 ALA D CA  
10483 C C   . ALA D 200 ? 0.3828 0.4131 0.4640 0.0508  0.0729  0.1445  200 ALA D C   
10484 O O   . ALA D 200 ? 0.4172 0.4408 0.5104 0.0522  0.0758  0.1414  200 ALA D O   
10485 C CB  . ALA D 200 ? 0.4241 0.4636 0.5352 0.0480  0.0597  0.1739  200 ALA D CB  
10486 N N   . ILE D 201 ? 0.3772 0.4034 0.4416 0.0529  0.0731  0.1306  201 ILE D N   
10487 C CA  . ILE D 201 ? 0.3248 0.3373 0.3889 0.0572  0.0750  0.1123  201 ILE D CA  
10488 C C   . ILE D 201 ? 0.3475 0.3544 0.4224 0.0596  0.0703  0.1077  201 ILE D C   
10489 O O   . ILE D 201 ? 0.3391 0.3528 0.4084 0.0584  0.0665  0.1131  201 ILE D O   
10490 C CB  . ILE D 201 ? 0.3479 0.3608 0.3855 0.0569  0.0792  0.0998  201 ILE D CB  
10491 C CG1 . ILE D 201 ? 0.3974 0.4202 0.4258 0.0543  0.0848  0.1045  201 ILE D CG1 
10492 C CG2 . ILE D 201 ? 0.3112 0.3115 0.3504 0.0599  0.0803  0.0845  201 ILE D CG2 
10493 C CD1 . ILE D 201 ? 0.4262 0.4486 0.4350 0.0549  0.0894  0.0914  201 ILE D CD1 
10494 N N   . LEU D 202 ? 0.3379 0.3344 0.4297 0.0625  0.0705  0.0978  202 LEU D N   
10495 C CA  . LEU D 202 ? 0.3439 0.3371 0.4488 0.0647  0.0675  0.0908  202 LEU D CA  
10496 C C   . LEU D 202 ? 0.3626 0.3505 0.4539 0.0648  0.0699  0.0728  202 LEU D C   
10497 O O   . LEU D 202 ? 0.3693 0.3521 0.4593 0.0643  0.0726  0.0655  202 LEU D O   
10498 C CB  . LEU D 202 ? 0.3276 0.3155 0.4678 0.0669  0.0658  0.0931  202 LEU D CB  
10499 C CG  . LEU D 202 ? 0.3338 0.3263 0.4967 0.0672  0.0607  0.1121  202 LEU D CG  
10500 C CD1 . LEU D 202 ? 0.3218 0.3204 0.4770 0.0634  0.0610  0.1282  202 LEU D CD1 
10501 C CD2 . LEU D 202 ? 0.3521 0.3365 0.5541 0.0703  0.0588  0.1096  202 LEU D CD2 
10502 N N   . PHE D 203 ? 0.3586 0.3492 0.4414 0.0645  0.0682  0.0668  203 PHE D N   
10503 C CA  . PHE D 203 ? 0.3848 0.3727 0.4532 0.0629  0.0695  0.0522  203 PHE D CA  
10504 C C   . PHE D 203 ? 0.3841 0.3732 0.4695 0.0635  0.0693  0.0421  203 PHE D C   
10505 O O   . PHE D 203 ? 0.3827 0.3770 0.4786 0.0649  0.0672  0.0447  203 PHE D O   
10506 C CB  . PHE D 203 ? 0.3744 0.3655 0.4173 0.0607  0.0683  0.0520  203 PHE D CB  
10507 C CG  . PHE D 203 ? 0.4083 0.4004 0.4348 0.0598  0.0695  0.0588  203 PHE D CG  
10508 C CD1 . PHE D 203 ? 0.3925 0.3924 0.4182 0.0593  0.0683  0.0712  203 PHE D CD1 
10509 C CD2 . PHE D 203 ? 0.4051 0.3923 0.4183 0.0591  0.0720  0.0527  203 PHE D CD2 
10510 C CE1 . PHE D 203 ? 0.3897 0.3940 0.3994 0.0574  0.0706  0.0753  203 PHE D CE1 
10511 C CE2 . PHE D 203 ? 0.4213 0.4110 0.4222 0.0587  0.0745  0.0562  203 PHE D CE2 
10512 C CZ  . PHE D 203 ? 0.4106 0.4096 0.4084 0.0575  0.0744  0.0665  203 PHE D CZ  
10513 N N   . GLY D 204 ? 0.3474 0.3337 0.4367 0.0618  0.0715  0.0302  204 GLY D N   
10514 C CA  . GLY D 204 ? 0.3357 0.3259 0.4414 0.0614  0.0727  0.0178  204 GLY D CA  
10515 C C   . GLY D 204 ? 0.3495 0.3356 0.4803 0.0625  0.0747  0.0119  204 GLY D C   
10516 O O   . GLY D 204 ? 0.3836 0.3637 0.5193 0.0632  0.0745  0.0191  204 GLY D O   
10517 N N   . ASP D 205 ? 0.3703 0.3610 0.5187 0.0621  0.0768  -0.0020 205 ASP D N   
10518 C CA  . ASP D 205 ? 0.3906 0.3784 0.5637 0.0619  0.0793  -0.0132 205 ASP D CA  
10519 C C   . ASP D 205 ? 0.4121 0.3926 0.6191 0.0674  0.0777  -0.0041 205 ASP D C   
10520 O O   . ASP D 205 ? 0.4036 0.3858 0.6278 0.0719  0.0757  0.0027  205 ASP D O   
10521 C CB  . ASP D 205 ? 0.4137 0.4116 0.5952 0.0591  0.0832  -0.0338 205 ASP D CB  
10522 C CG  . ASP D 205 ? 0.4955 0.4923 0.6988 0.0570  0.0864  -0.0499 205 ASP D CG  
10523 O OD1 . ASP D 205 ? 0.6040 0.5919 0.8116 0.0567  0.0851  -0.0446 205 ASP D OD1 
10524 O OD2 . ASP D 205 ? 0.4726 0.4784 0.6891 0.0551  0.0907  -0.0688 205 ASP D OD2 
10525 N N   . ILE D 206 ? 0.4302 0.4030 0.6473 0.0667  0.0775  -0.0013 206 ILE D N   
10526 C CA  . ILE D 206 ? 0.4602 0.4256 0.7132 0.0707  0.0754  0.0072  206 ILE D CA  
10527 C C   . ILE D 206 ? 0.4744 0.4357 0.7529 0.0690  0.0781  -0.0111 206 ILE D C   
10528 O O   . ILE D 206 ? 0.4692 0.4220 0.7714 0.0695  0.0766  -0.0059 206 ILE D O   
10529 C CB  . ILE D 206 ? 0.5008 0.4611 0.7494 0.0707  0.0723  0.0285  206 ILE D CB  
10530 C CG1 . ILE D 206 ? 0.4528 0.4111 0.6830 0.0661  0.0743  0.0249  206 ILE D CG1 
10531 C CG2 . ILE D 206 ? 0.5492 0.5150 0.7764 0.0718  0.0698  0.0456  206 ILE D CG2 
10532 C CD1 . ILE D 206 ? 0.4357 0.3915 0.6655 0.0660  0.0725  0.0443  206 ILE D CD1 
10533 N N   . ASN D 207 ? 0.5190 0.4879 0.7923 0.0658  0.0823  -0.0330 207 ASN D N   
10534 C CA  . ASN D 207 ? 0.5295 0.4974 0.8211 0.0621  0.0856  -0.0533 207 ASN D CA  
10535 C C   . ASN D 207 ? 0.5478 0.5181 0.8747 0.0650  0.0891  -0.0718 207 ASN D C   
10536 O O   . ASN D 207 ? 0.5564 0.5281 0.8978 0.0609  0.0928  -0.0930 207 ASN D O   
10537 C CB  . ASN D 207 ? 0.5579 0.5358 0.8168 0.0535  0.0882  -0.0674 207 ASN D CB  
10538 C CG  . ASN D 207 ? 0.5430 0.5185 0.7708 0.0506  0.0849  -0.0517 207 ASN D CG  
10539 O OD1 . ASN D 207 ? 0.5158 0.4913 0.7233 0.0533  0.0828  -0.0363 207 ASN D OD1 
10540 N ND2 . ASN D 207 ? 0.5293 0.5038 0.7546 0.0449  0.0846  -0.0569 207 ASN D ND2 
10541 N N   . ASP D 208 ? 0.5808 0.5533 0.9235 0.0715  0.0882  -0.0660 208 ASP D N   
10542 C CA  . ASP D 208 ? 0.6097 0.5854 0.9913 0.0746  0.0924  -0.0870 208 ASP D CA  
10543 C C   . ASP D 208 ? 0.5748 0.5437 0.9885 0.0807  0.0857  -0.0702 208 ASP D C   
10544 O O   . ASP D 208 ? 0.5240 0.4998 0.9389 0.0849  0.0844  -0.0633 208 ASP D O   
10545 C CB  . ASP D 208 ? 0.6333 0.6272 0.9966 0.0715  0.0983  -0.1055 208 ASP D CB  
10546 C CG  . ASP D 208 ? 0.6422 0.6437 1.0337 0.0699  0.1021  -0.1295 208 ASP D CG  
10547 O OD1 . ASP D 208 ? 0.6165 0.6084 1.0400 0.0701  0.0991  -0.1322 208 ASP D OD1 
10548 O OD2 . ASP D 208 ? 0.6707 0.6893 1.0495 0.0665  0.1077  -0.1455 208 ASP D OD2 
10549 N N   . PRO D 209 ? 0.5823 0.5390 1.0228 0.0798  0.0809  -0.0633 209 PRO D N   
10550 C CA  . PRO D 209 ? 0.5708 0.5209 1.0448 0.0828  0.0732  -0.0458 209 PRO D CA  
10551 C C   . PRO D 209 ? 0.5394 0.4962 1.0396 0.0853  0.0731  -0.0559 209 PRO D C   
10552 O O   . PRO D 209 ? 0.5427 0.4993 1.0580 0.0893  0.0668  -0.0362 209 PRO D O   
10553 C CB  . PRO D 209 ? 0.5943 0.5335 1.0920 0.0785  0.0710  -0.0483 209 PRO D CB  
10554 C CG  . PRO D 209 ? 0.5990 0.5411 1.0807 0.0733  0.0784  -0.0743 209 PRO D CG  
10555 C CD  . PRO D 209 ? 0.5790 0.5289 1.0196 0.0743  0.0826  -0.0731 209 PRO D CD  
10556 N N   . ASN D 210 ? 0.4978 0.4625 1.0023 0.0824  0.0801  -0.0855 210 ASN D N   
10557 C CA  . ASN D 210 ? 0.4778 0.4505 1.0085 0.0845  0.0814  -0.0977 210 ASN D CA  
10558 C C   . ASN D 210 ? 0.4413 0.4247 0.9569 0.0892  0.0813  -0.0888 210 ASN D C   
10559 O O   . ASN D 210 ? 0.4566 0.4430 0.9968 0.0932  0.0781  -0.0836 210 ASN D O   
10560 C CB  . ASN D 210 ? 0.5117 0.4946 1.0436 0.0790  0.0902  -0.1324 210 ASN D CB  
10561 C CG  . ASN D 210 ? 0.5720 0.5465 1.1289 0.0742  0.0902  -0.1450 210 ASN D CG  
10562 O OD1 . ASN D 210 ? 0.6156 0.5777 1.2052 0.0760  0.0835  -0.1312 210 ASN D OD1 
10563 N ND2 . ASN D 210 ? 0.5632 0.5456 1.1046 0.0669  0.0972  -0.1702 210 ASN D ND2 
10564 N N   . ASN D 211 ? 0.4442 0.4339 0.9202 0.0885  0.0847  -0.0870 211 ASN D N   
10565 C CA  . ASN D 211 ? 0.4547 0.4561 0.9130 0.0920  0.0853  -0.0794 211 ASN D CA  
10566 C C   . ASN D 211 ? 0.4041 0.4002 0.8455 0.0956  0.0791  -0.0493 211 ASN D C   
10567 O O   . ASN D 211 ? 0.3962 0.4018 0.8152 0.0974  0.0805  -0.0430 211 ASN D O   
10568 C CB  . ASN D 211 ? 0.4996 0.5166 0.9289 0.0870  0.0947  -0.1028 211 ASN D CB  
10569 C CG  . ASN D 211 ? 0.5574 0.5839 1.0051 0.0827  0.1007  -0.1318 211 ASN D CG  
10570 O OD1 . ASN D 211 ? 0.5711 0.5989 1.0512 0.0861  0.0989  -0.1341 211 ASN D OD1 
10571 N ND2 . ASN D 211 ? 0.5710 0.6043 1.0005 0.0746  0.1073  -0.1534 211 ASN D ND2 
10572 N N   . ASN D 212 ? 0.4127 0.3951 0.8647 0.0957  0.0727  -0.0308 212 ASN D N   
10573 C CA  . ASN D 212 ? 0.4214 0.4003 0.8556 0.0976  0.0673  -0.0023 212 ASN D CA  
10574 C C   . ASN D 212 ? 0.4136 0.3832 0.8725 0.0975  0.0577  0.0225  212 ASN D C   
10575 O O   . ASN D 212 ? 0.4166 0.3763 0.8804 0.0942  0.0565  0.0261  212 ASN D O   
10576 C CB  . ASN D 212 ? 0.4592 0.4347 0.8575 0.0935  0.0717  -0.0056 212 ASN D CB  
10577 C CG  . ASN D 212 ? 0.4775 0.4549 0.8351 0.0904  0.0670  0.0181  212 ASN D CG  
10578 O OD1 . ASN D 212 ? 0.4822 0.4605 0.8473 0.0926  0.0603  0.0410  212 ASN D OD1 
10579 N ND2 . ASN D 212 ? 0.4545 0.4335 0.7702 0.0848  0.0704  0.0122  212 ASN D ND2 
10580 N N   . ASN D 213 ? 0.3914 0.3662 0.8668 0.1000  0.0506  0.0401  213 ASN D N   
10581 C CA  . ASN D 213 ? 0.3781 0.3481 0.8780 0.0983  0.0407  0.0657  213 ASN D CA  
10582 C C   . ASN D 213 ? 0.3587 0.3287 0.8346 0.0959  0.0361  0.0933  213 ASN D C   
10583 O O   . ASN D 213 ? 0.3614 0.3280 0.8530 0.0920  0.0293  0.1129  213 ASN D O   
10584 C CB  . ASN D 213 ? 0.3332 0.3107 0.8604 0.1007  0.0340  0.0759  213 ASN D CB  
10585 C CG  . ASN D 213 ? 0.3843 0.3591 0.9491 0.1019  0.0364  0.0540  213 ASN D CG  
10586 O OD1 . ASN D 213 ? 0.3922 0.3574 0.9753 0.0993  0.0384  0.0419  213 ASN D OD1 
10587 N ND2 . ASN D 213 ? 0.3803 0.3646 0.9595 0.1056  0.0358  0.0497  213 ASN D ND2 
10588 N N   . TYR D 214 ? 0.3434 0.3192 0.7824 0.0975  0.0398  0.0955  214 TYR D N   
10589 C CA  . TYR D 214 ? 0.3625 0.3408 0.7740 0.0940  0.0364  0.1200  214 TYR D CA  
10590 C C   . TYR D 214 ? 0.3838 0.3515 0.7939 0.0907  0.0388  0.1202  214 TYR D C   
10591 O O   . TYR D 214 ? 0.3674 0.3362 0.7736 0.0867  0.0340  0.1435  214 TYR D O   
10592 C CB  . TYR D 214 ? 0.3420 0.3302 0.6992 0.0900  0.0400  0.1149  214 TYR D CB  
10593 C CG  . TYR D 214 ? 0.3327 0.3275 0.6587 0.0841  0.0363  0.1376  214 TYR D CG  
10594 C CD1 . TYR D 214 ? 0.3238 0.3297 0.6539 0.0823  0.0278  0.1620  214 TYR D CD1 
10595 C CD2 . TYR D 214 ? 0.3474 0.3391 0.6420 0.0797  0.0412  0.1347  214 TYR D CD2 
10596 C CE1 . TYR D 214 ? 0.3243 0.3394 0.6253 0.0754  0.0251  0.1816  214 TYR D CE1 
10597 C CE2 . TYR D 214 ? 0.3432 0.3431 0.6113 0.0741  0.0391  0.1533  214 TYR D CE2 
10598 C CZ  . TYR D 214 ? 0.3348 0.3469 0.6051 0.0715  0.0314  0.1760  214 TYR D CZ  
10599 O OH  . TYR D 214 ? 0.3536 0.3772 0.5964 0.0646  0.0302  0.1926  214 TYR D OH  
10600 N N   . ILE D 215 ? 0.3998 0.3592 0.8132 0.0914  0.0460  0.0947  215 ILE D N   
10601 C CA  . ILE D 215 ? 0.4307 0.3812 0.8408 0.0877  0.0484  0.0931  215 ILE D CA  
10602 C C   . ILE D 215 ? 0.4599 0.4028 0.9086 0.0843  0.0445  0.0901  215 ILE D C   
10603 O O   . ILE D 215 ? 0.4477 0.3831 0.9007 0.0808  0.0463  0.0848  215 ILE D O   
10604 C CB  . ILE D 215 ? 0.3872 0.3370 0.7667 0.0849  0.0570  0.0664  215 ILE D CB  
10605 C CG1 . ILE D 215 ? 0.4092 0.3568 0.8129 0.0877  0.0619  0.0380  215 ILE D CG1 
10606 C CG2 . ILE D 215 ? 0.3347 0.2943 0.6634 0.0821  0.0593  0.0673  215 ILE D CG2 
10607 C CD1 . ILE D 215 ? 0.4260 0.3772 0.7973 0.0832  0.0692  0.0142  215 ILE D CD1 
10608 N N   . HIS D 216 ? 0.4841 0.4292 0.9631 0.0852  0.0392  0.0925  216 HIS D N   
10609 C CA  . HIS D 216 ? 0.5157 0.4536 1.0355 0.0824  0.0360  0.0874  216 HIS D CA  
10610 C C   . HIS D 216 ? 0.4627 0.3973 0.9941 0.0768  0.0301  0.1101  216 HIS D C   
10611 O O   . HIS D 216 ? 0.3924 0.3190 0.9451 0.0737  0.0305  0.1013  216 HIS D O   
10612 C CB  . HIS D 216 ? 0.5708 0.5124 1.1231 0.0848  0.0313  0.0879  216 HIS D CB  
10613 C CG  . HIS D 216 ? 0.6212 0.5554 1.2179 0.0828  0.0294  0.0775  216 HIS D CG  
10614 N ND1 . HIS D 216 ? 0.6424 0.5728 1.2510 0.0837  0.0364  0.0454  216 HIS D ND1 
10615 C CD2 . HIS D 216 ? 0.6419 0.5732 1.2752 0.0793  0.0213  0.0944  216 HIS D CD2 
10616 C CE1 . HIS D 216 ? 0.6641 0.5887 1.3156 0.0814  0.0329  0.0421  216 HIS D CE1 
10617 N NE2 . HIS D 216 ? 0.6594 0.5838 1.3276 0.0789  0.0236  0.0719  216 HIS D NE2 
10618 N N   . ASN D 217 ? 0.4603 0.4030 0.9776 0.0746  0.0247  0.1390  217 ASN D N   
10619 C CA  . ASN D 217 ? 0.4779 0.4216 1.0034 0.0681  0.0195  0.1616  217 ASN D CA  
10620 C C   . ASN D 217 ? 0.4877 0.4260 0.9916 0.0658  0.0256  0.1560  217 ASN D C   
10621 O O   . ASN D 217 ? 0.5146 0.4530 1.0282 0.0602  0.0226  0.1700  217 ASN D O   
10622 C CB  . ASN D 217 ? 0.5375 0.4958 1.0494 0.0649  0.0127  0.1930  217 ASN D CB  
10623 C CG  . ASN D 217 ? 0.6514 0.6156 1.1713 0.0568  0.0072  0.2178  217 ASN D CG  
10624 O OD1 . ASN D 217 ? 0.6782 0.6403 1.2367 0.0533  0.0010  0.2242  217 ASN D OD1 
10625 N ND2 . ASN D 217 ? 0.6888 0.6621 1.1727 0.0534  0.0094  0.2322  217 ASN D ND2 
10626 N N   . SER D 218 ? 0.4506 0.3854 0.9268 0.0697  0.0339  0.1359  218 SER D N   
10627 C CA  . SER D 218 ? 0.4123 0.3428 0.8681 0.0678  0.0396  0.1310  218 SER D CA  
10628 C C   . SER D 218 ? 0.3908 0.3110 0.8614 0.0673  0.0440  0.1034  218 SER D C   
10629 O O   . SER D 218 ? 0.4138 0.3303 0.8696 0.0656  0.0486  0.0963  218 SER D O   
10630 C CB  . SER D 218 ? 0.4064 0.3418 0.8198 0.0714  0.0456  0.1302  218 SER D CB  
10631 O OG  . SER D 218 ? 0.3867 0.3204 0.7901 0.0756  0.0512  0.1037  218 SER D OG  
10632 N N   . LEU D 219 ? 0.3424 0.2590 0.8436 0.0681  0.0424  0.0882  219 LEU D N   
10633 C CA  . LEU D 219 ? 0.3805 0.2905 0.8915 0.0673  0.0476  0.0580  219 LEU D CA  
10634 C C   . LEU D 219 ? 0.3877 0.2906 0.9108 0.0618  0.0477  0.0549  219 LEU D C   
10635 O O   . LEU D 219 ? 0.4045 0.3047 0.9170 0.0605  0.0534  0.0335  219 LEU D O   
10636 C CB  . LEU D 219 ? 0.4092 0.3185 0.9550 0.0687  0.0460  0.0430  219 LEU D CB  
10637 C CG  . LEU D 219 ? 0.4030 0.3193 0.9351 0.0738  0.0494  0.0319  219 LEU D CG  
10638 C CD1 . LEU D 219 ? 0.4271 0.3438 0.9965 0.0751  0.0480  0.0186  219 LEU D CD1 
10639 C CD2 . LEU D 219 ? 0.4239 0.3423 0.9253 0.0739  0.0580  0.0090  219 LEU D CD2 
10640 N N   . ASP D 220 ? 0.4130 0.3146 0.9581 0.0579  0.0412  0.0762  220 ASP D N   
10641 C CA  . ASP D 220 ? 0.4536 0.3492 1.0126 0.0525  0.0409  0.0733  220 ASP D CA  
10642 C C   . ASP D 220 ? 0.4008 0.2973 0.9247 0.0512  0.0457  0.0771  220 ASP D C   
10643 O O   . ASP D 220 ? 0.4144 0.3058 0.9389 0.0479  0.0487  0.0632  220 ASP D O   
10644 C CB  . ASP D 220 ? 0.5370 0.4332 1.1291 0.0481  0.0325  0.0966  220 ASP D CB  
10645 C CG  . ASP D 220 ? 0.5854 0.4916 1.1685 0.0483  0.0272  0.1277  220 ASP D CG  
10646 O OD1 . ASP D 220 ? 0.5852 0.4971 1.1346 0.0519  0.0304  0.1319  220 ASP D OD1 
10647 O OD2 . ASP D 220 ? 0.6079 0.5175 1.2189 0.0443  0.0195  0.1481  220 ASP D OD2 
10648 N N   . VAL D 221 ? 0.3781 0.2818 0.8729 0.0535  0.0464  0.0960  221 VAL D N   
10649 C CA  . VAL D 221 ? 0.4014 0.3075 0.8621 0.0535  0.0516  0.1005  221 VAL D CA  
10650 C C   . VAL D 221 ? 0.4141 0.3196 0.8508 0.0554  0.0585  0.0732  221 VAL D C   
10651 O O   . VAL D 221 ? 0.4249 0.3325 0.8452 0.0507  0.0612  0.0652  221 VAL D O   
10652 C CB  . VAL D 221 ? 0.3266 0.2427 0.7612 0.0559  0.0513  0.1233  221 VAL D CB  
10653 C CG1 . VAL D 221 ? 0.3176 0.2437 0.7099 0.0530  0.0567  0.1233  221 VAL D CG1 
10654 C CG2 . VAL D 221 ? 0.3447 0.2678 0.7973 0.0513  0.0439  0.1509  221 VAL D CG2 
10655 N N   . LEU D 222 ? 0.3889 0.2961 0.8207 0.0601  0.0603  0.0592  222 LEU D N   
10656 C CA  . LEU D 222 ? 0.3728 0.2856 0.7767 0.0596  0.0657  0.0342  222 LEU D CA  
10657 C C   . LEU D 222 ? 0.3951 0.3029 0.8155 0.0554  0.0679  0.0096  222 LEU D C   
10658 O O   . LEU D 222 ? 0.4425 0.3566 0.8370 0.0509  0.0712  -0.0062 222 LEU D O   
10659 C CB  . LEU D 222 ? 0.3844 0.3009 0.7882 0.0650  0.0666  0.0265  222 LEU D CB  
10660 C CG  . LEU D 222 ? 0.3958 0.3197 0.7786 0.0683  0.0645  0.0473  222 LEU D CG  
10661 C CD1 . LEU D 222 ? 0.3691 0.2970 0.7561 0.0732  0.0652  0.0377  222 LEU D CD1 
10662 C CD2 . LEU D 222 ? 0.3972 0.3295 0.7333 0.0651  0.0673  0.0504  222 LEU D CD2 
10663 N N   . HIS D 223 ? 0.3780 0.2755 0.8422 0.0558  0.0653  0.0064  223 HIS D N   
10664 C CA  . HIS D 223 ? 0.4640 0.3576 0.9468 0.0505  0.0669  -0.0182 223 HIS D CA  
10665 C C   . HIS D 223 ? 0.4511 0.3440 0.9219 0.0439  0.0669  -0.0158 223 HIS D C   
10666 O O   . HIS D 223 ? 0.4508 0.3460 0.9182 0.0378  0.0692  -0.0381 223 HIS D O   
10667 C CB  . HIS D 223 ? 0.5706 0.4598 1.0948 0.0485  0.0617  -0.0183 223 HIS D CB  
10668 C CG  . HIS D 223 ? 0.7090 0.5955 1.2544 0.0429  0.0636  -0.0456 223 HIS D CG  
10669 N ND1 . HIS D 223 ? 0.7867 0.6667 1.3550 0.0373  0.0601  -0.0425 223 HIS D ND1 
10670 C CD2 . HIS D 223 ? 0.7696 0.6614 1.3161 0.0410  0.0689  -0.0774 223 HIS D CD2 
10671 C CE1 . HIS D 223 ? 0.8313 0.7115 1.4140 0.0324  0.0629  -0.0718 223 HIS D CE1 
10672 N NE2 . HIS D 223 ? 0.8264 0.7146 1.3957 0.0342  0.0685  -0.0937 223 HIS D NE2 
10673 N N   . ASP D 224 ? 0.4520 0.3454 0.9146 0.0435  0.0638  0.0116  224 ASP D N   
10674 C CA  . ASP D 224 ? 0.4774 0.3725 0.9323 0.0369  0.0630  0.0178  224 ASP D CA  
10675 C C   . ASP D 224 ? 0.4653 0.3737 0.8739 0.0357  0.0655  0.0240  224 ASP D C   
10676 O O   . ASP D 224 ? 0.4396 0.3518 0.8405 0.0315  0.0650  0.0340  224 ASP D O   
10677 C CB  . ASP D 224 ? 0.5231 0.4114 1.0070 0.0360  0.0581  0.0437  224 ASP D CB  
10678 C CG  . ASP D 224 ? 0.5514 0.4303 1.0808 0.0343  0.0537  0.0367  224 ASP D CG  
10679 O OD1 . ASP D 224 ? 0.5496 0.4248 1.0923 0.0322  0.0555  0.0089  224 ASP D OD1 
10680 O OD2 . ASP D 224 ? 0.5608 0.4415 1.1092 0.0338  0.0481  0.0581  224 ASP D OD2 
10681 N N   . LEU D 225 ? 0.4399 0.3552 0.8200 0.0396  0.0682  0.0185  225 LEU D N   
10682 C CA  . LEU D 225 ? 0.3997 0.3258 0.7395 0.0389  0.0702  0.0228  225 LEU D CA  
10683 C C   . LEU D 225 ? 0.3727 0.3033 0.7030 0.0320  0.0704  0.0088  225 LEU D C   
10684 O O   . LEU D 225 ? 0.3765 0.3057 0.7178 0.0278  0.0704  -0.0122 225 LEU D O   
10685 C CB  . LEU D 225 ? 0.3851 0.3169 0.6988 0.0429  0.0723  0.0164  225 LEU D CB  
10686 C CG  . LEU D 225 ? 0.3505 0.2829 0.6594 0.0492  0.0719  0.0322  225 LEU D CG  
10687 C CD1 . LEU D 225 ? 0.3705 0.3100 0.6483 0.0510  0.0740  0.0241  225 LEU D CD1 
10688 C CD2 . LEU D 225 ? 0.3111 0.2469 0.6128 0.0497  0.0712  0.0562  225 LEU D CD2 
10689 N N   . VAL D 226 ? 0.3770 0.3145 0.6878 0.0305  0.0704  0.0202  226 VAL D N   
10690 C CA  . VAL D 226 ? 0.3743 0.3187 0.6729 0.0241  0.0695  0.0111  226 VAL D CA  
10691 C C   . VAL D 226 ? 0.3751 0.3287 0.6384 0.0261  0.0705  0.0125  226 VAL D C   
10692 O O   . VAL D 226 ? 0.3820 0.3369 0.6326 0.0318  0.0723  0.0261  226 VAL D O   
10693 C CB  . VAL D 226 ? 0.4820 0.4270 0.7955 0.0205  0.0680  0.0238  226 VAL D CB  
10694 C CG1 . VAL D 226 ? 0.5113 0.4668 0.8079 0.0158  0.0668  0.0219  226 VAL D CG1 
10695 C CG2 . VAL D 226 ? 0.4669 0.4028 0.8156 0.0160  0.0658  0.0172  226 VAL D CG2 
10696 N N   . TYR D 227 ? 0.3904 0.3510 0.6390 0.0206  0.0689  -0.0015 227 TYR D N   
10697 C CA  . TYR D 227 ? 0.3600 0.3284 0.5786 0.0215  0.0685  -0.0003 227 TYR D CA  
10698 C C   . TYR D 227 ? 0.3654 0.3422 0.5750 0.0167  0.0651  0.0034  227 TYR D C   
10699 O O   . TYR D 227 ? 0.4103 0.3900 0.6325 0.0099  0.0625  -0.0015 227 TYR D O   
10700 C CB  . TYR D 227 ? 0.3891 0.3615 0.5957 0.0184  0.0684  -0.0173 227 TYR D CB  
10701 C CG  . TYR D 227 ? 0.4453 0.4117 0.6563 0.0247  0.0716  -0.0188 227 TYR D CG  
10702 C CD1 . TYR D 227 ? 0.4826 0.4498 0.6739 0.0303  0.0727  -0.0104 227 TYR D CD1 
10703 C CD2 . TYR D 227 ? 0.4453 0.4051 0.6829 0.0254  0.0731  -0.0276 227 TYR D CD2 
10704 C CE1 . TYR D 227 ? 0.4925 0.4558 0.6882 0.0357  0.0748  -0.0102 227 TYR D CE1 
10705 C CE2 . TYR D 227 ? 0.4642 0.4195 0.7092 0.0317  0.0752  -0.0269 227 TYR D CE2 
10706 C CZ  . TYR D 227 ? 0.4996 0.4574 0.7226 0.0366  0.0759  -0.0176 227 TYR D CZ  
10707 O OH  . TYR D 227 ? 0.5498 0.5048 0.7800 0.0423  0.0772  -0.0158 227 TYR D OH  
10708 N N   . THR D 228 ? 0.3466 0.3276 0.5368 0.0203  0.0648  0.0119  228 THR D N   
10709 C CA  . THR D 228 ? 0.3552 0.3447 0.5390 0.0168  0.0609  0.0165  228 THR D CA  
10710 C C   . THR D 228 ? 0.3602 0.3532 0.5210 0.0184  0.0589  0.0179  228 THR D C   
10711 O O   . THR D 228 ? 0.3550 0.3430 0.5056 0.0245  0.0621  0.0196  228 THR D O   
10712 C CB  . THR D 228 ? 0.4405 0.4307 0.6369 0.0209  0.0630  0.0308  228 THR D CB  
10713 O OG1 . THR D 228 ? 0.4050 0.4043 0.6028 0.0170  0.0586  0.0343  228 THR D OG1 
10714 C CG2 . THR D 228 ? 0.4543 0.4420 0.6418 0.0299  0.0681  0.0409  228 THR D CG2 
10715 N N   . PRO D 229 ? 0.3603 0.3622 0.5142 0.0124  0.0527  0.0182  229 PRO D N   
10716 C CA  . PRO D 229 ? 0.3355 0.3399 0.4703 0.0128  0.0497  0.0201  229 PRO D CA  
10717 C C   . PRO D 229 ? 0.3297 0.3286 0.4610 0.0226  0.0528  0.0304  229 PRO D C   
10718 O O   . PRO D 229 ? 0.3582 0.3569 0.5008 0.0274  0.0552  0.0383  229 PRO D O   
10719 C CB  . PRO D 229 ? 0.3421 0.3582 0.4755 0.0036  0.0411  0.0218  229 PRO D CB  
10720 C CG  . PRO D 229 ? 0.3535 0.3745 0.4988 -0.0043 0.0400  0.0136  229 PRO D CG  
10721 C CD  . PRO D 229 ? 0.3634 0.3746 0.5261 0.0033  0.0469  0.0164  229 PRO D CD  
10722 N N   . LEU D 230 ? 0.3190 0.3146 0.4346 0.0249  0.0531  0.0291  230 LEU D N   
10723 C CA  . LEU D 230 ? 0.3240 0.3144 0.4342 0.0333  0.0559  0.0359  230 LEU D CA  
10724 C C   . LEU D 230 ? 0.3319 0.3250 0.4359 0.0313  0.0493  0.0401  230 LEU D C   
10725 O O   . LEU D 230 ? 0.3704 0.3677 0.4640 0.0239  0.0435  0.0373  230 LEU D O   
10726 C CB  . LEU D 230 ? 0.2956 0.2799 0.3946 0.0371  0.0604  0.0323  230 LEU D CB  
10727 C CG  . LEU D 230 ? 0.2798 0.2593 0.3698 0.0441  0.0633  0.0365  230 LEU D CG  
10728 C CD1 . LEU D 230 ? 0.2627 0.2425 0.3629 0.0502  0.0689  0.0424  230 LEU D CD1 
10729 C CD2 . LEU D 230 ? 0.2933 0.2692 0.3733 0.0454  0.0663  0.0324  230 LEU D CD2 
10730 N N   . THR D 231 ? 0.3669 0.3589 0.4794 0.0373  0.0499  0.0471  231 THR D N   
10731 C CA  . THR D 231 ? 0.3643 0.3565 0.4764 0.0371  0.0432  0.0524  231 THR D CA  
10732 C C   . THR D 231 ? 0.3522 0.3364 0.4621 0.0463  0.0482  0.0528  231 THR D C   
10733 O O   . THR D 231 ? 0.3356 0.3179 0.4476 0.0529  0.0570  0.0510  231 THR D O   
10734 C CB  . THR D 231 ? 0.3258 0.3257 0.4564 0.0352  0.0374  0.0598  231 THR D CB  
10735 O OG1 . THR D 231 ? 0.3513 0.3525 0.4970 0.0413  0.0446  0.0608  231 THR D OG1 
10736 C CG2 . THR D 231 ? 0.3097 0.3195 0.4385 0.0231  0.0293  0.0594  231 THR D CG2 
10737 N N   . ILE D 232 ? 0.4150 0.3957 0.5207 0.0455  0.0422  0.0553  232 ILE D N   
10738 C CA  . ILE D 232 ? 0.4363 0.4084 0.5383 0.0525  0.0459  0.0533  232 ILE D CA  
10739 C C   . ILE D 232 ? 0.3905 0.3602 0.5102 0.0563  0.0410  0.0584  232 ILE D C   
10740 O O   . ILE D 232 ? 0.4033 0.3751 0.5288 0.0506  0.0304  0.0658  232 ILE D O   
10741 C CB  . ILE D 232 ? 0.3424 0.3098 0.4246 0.0483  0.0432  0.0504  232 ILE D CB  
10742 C CG1 . ILE D 232 ? 0.3280 0.2987 0.3970 0.0444  0.0467  0.0451  232 ILE D CG1 
10743 C CG2 . ILE D 232 ? 0.3432 0.3018 0.4213 0.0549  0.0472  0.0470  232 ILE D CG2 
10744 C CD1 . ILE D 232 ? 0.3018 0.2708 0.3701 0.0507  0.0566  0.0413  232 ILE D CD1 
10745 N N   . SER D 233 ? 0.4087 0.3753 0.5383 0.0655  0.0486  0.0544  233 SER D N   
10746 C CA  . SER D 233 ? 0.4556 0.4192 0.6070 0.0707  0.0454  0.0567  233 SER D CA  
10747 C C   . SER D 233 ? 0.5151 0.4678 0.6622 0.0702  0.0396  0.0562  233 SER D C   
10748 O O   . SER D 233 ? 0.5063 0.4547 0.6315 0.0665  0.0399  0.0530  233 SER D O   
10749 C CB  . SER D 233 ? 0.4418 0.4086 0.6066 0.0802  0.0572  0.0498  233 SER D CB  
10750 O OG  . SER D 233 ? 0.4404 0.4024 0.5902 0.0838  0.0657  0.0401  233 SER D OG  
10751 N N   . LYS D 234 ? 0.5427 0.4908 0.7130 0.0739  0.0341  0.0596  234 LYS D N   
10752 C CA  . LYS D 234 ? 0.5598 0.4962 0.7296 0.0727  0.0273  0.0604  234 LYS D CA  
10753 C C   . LYS D 234 ? 0.5305 0.4594 0.6870 0.0776  0.0371  0.0470  234 LYS D C   
10754 O O   . LYS D 234 ? 0.5141 0.4340 0.6612 0.0746  0.0328  0.0461  234 LYS D O   
10755 C CB  . LYS D 234 ? 0.5918 0.5233 0.7956 0.0770  0.0195  0.0663  234 LYS D CB  
10756 C CG  . LYS D 234 ? 0.6553 0.5929 0.8714 0.0690  0.0044  0.0838  234 LYS D CG  
10757 C CD  . LYS D 234 ? 0.7208 0.6536 0.9758 0.0744  -0.0037 0.0910  234 LYS D CD  
10758 C CE  . LYS D 234 ? 0.7650 0.7104 1.0395 0.0701  -0.0141 0.1065  234 LYS D CE  
10759 N NZ  . LYS D 234 ? 0.7861 0.7290 1.1054 0.0788  -0.0186 0.1112  234 LYS D NZ  
10760 N N   . GLN D 235 ? 0.5274 0.4619 0.6816 0.0837  0.0501  0.0373  235 GLN D N   
10761 C CA  . GLN D 235 ? 0.5424 0.4728 0.6830 0.0871  0.0593  0.0247  235 GLN D CA  
10762 C C   . GLN D 235 ? 0.5107 0.4458 0.6220 0.0825  0.0639  0.0236  235 GLN D C   
10763 O O   . GLN D 235 ? 0.5113 0.4470 0.6088 0.0843  0.0718  0.0148  235 GLN D O   
10764 C CB  . GLN D 235 ? 0.5904 0.5260 0.7476 0.0960  0.0710  0.0137  235 GLN D CB  
10765 C CG  . GLN D 235 ? 0.6411 0.5690 0.8308 0.1018  0.0665  0.0116  235 GLN D CG  
10766 C CD  . GLN D 235 ? 0.8969 0.8090 1.0861 0.1003  0.0596  0.0083  235 GLN D CD  
10767 O OE1 . GLN D 235 ? 0.8919 0.8005 1.0597 0.0986  0.0644  -0.0010 235 GLN D OE1 
10768 N NE2 . GLN D 235 ? 0.8878 0.7909 1.1017 0.1000  0.0472  0.0175  235 GLN D NE2 
10769 N N   . GLY D 236 ? 0.4636 0.4033 0.5671 0.0764  0.0586  0.0324  236 GLY D N   
10770 C CA  . GLY D 236 ? 0.4474 0.3903 0.5279 0.0720  0.0612  0.0318  236 GLY D CA  
10771 C C   . GLY D 236 ? 0.4418 0.3938 0.5195 0.0741  0.0704  0.0306  236 GLY D C   
10772 O O   . GLY D 236 ? 0.4341 0.3880 0.4956 0.0724  0.0740  0.0290  236 GLY D O   
10773 N N   . GLU D 237 ? 0.4301 0.3883 0.5254 0.0775  0.0736  0.0324  237 GLU D N   
10774 C CA  . GLU D 237 ? 0.3798 0.3479 0.4764 0.0788  0.0819  0.0332  237 GLU D CA  
10775 C C   . GLU D 237 ? 0.3555 0.3271 0.4532 0.0735  0.0779  0.0398  237 GLU D C   
10776 O O   . GLU D 237 ? 0.3601 0.3308 0.4643 0.0696  0.0696  0.0438  237 GLU D O   
10777 C CB  . GLU D 237 ? 0.3816 0.3568 0.4984 0.0846  0.0881  0.0313  237 GLU D CB  
10778 C CG  . GLU D 237 ? 0.4539 0.4269 0.5740 0.0902  0.0936  0.0214  237 GLU D CG  
10779 C CD  . GLU D 237 ? 0.5060 0.4832 0.6541 0.0963  0.0959  0.0190  237 GLU D CD  
10780 O OE1 . GLU D 237 ? 0.4899 0.4621 0.6551 0.0963  0.0864  0.0248  237 GLU D OE1 
10781 O OE2 . GLU D 237 ? 0.5282 0.5158 0.6822 0.1005  0.1072  0.0115  237 GLU D OE2 
10782 N N   . TYR D 238 ? 0.3618 0.3387 0.4548 0.0728  0.0837  0.0411  238 TYR D N   
10783 C CA  . TYR D 238 ? 0.3215 0.3008 0.4177 0.0681  0.0810  0.0452  238 TYR D CA  
10784 C C   . TYR D 238 ? 0.3275 0.3143 0.4424 0.0684  0.0828  0.0495  238 TYR D C   
10785 O O   . TYR D 238 ? 0.3427 0.3365 0.4638 0.0718  0.0905  0.0508  238 TYR D O   
10786 C CB  . TYR D 238 ? 0.2921 0.2718 0.3781 0.0669  0.0849  0.0458  238 TYR D CB  
10787 C CG  . TYR D 238 ? 0.2860 0.2597 0.3550 0.0659  0.0825  0.0421  238 TYR D CG  
10788 C CD1 . TYR D 238 ? 0.2997 0.2696 0.3640 0.0613  0.0759  0.0399  238 TYR D CD1 
10789 C CD2 . TYR D 238 ? 0.3272 0.3015 0.3846 0.0685  0.0871  0.0406  238 TYR D CD2 
10790 C CE1 . TYR D 238 ? 0.3274 0.2937 0.3772 0.0600  0.0740  0.0368  238 TYR D CE1 
10791 C CE2 . TYR D 238 ? 0.3410 0.3108 0.3837 0.0671  0.0844  0.0376  238 TYR D CE2 
10792 C CZ  . TYR D 238 ? 0.3560 0.3215 0.3958 0.0631  0.0779  0.0361  238 TYR D CZ  
10793 O OH  . TYR D 238 ? 0.3763 0.3392 0.4030 0.0614  0.0756  0.0335  238 TYR D OH  
10794 N N   . PHE D 239 ? 0.3240 0.3113 0.4469 0.0637  0.0756  0.0516  239 PHE D N   
10795 C CA  . PHE D 239 ? 0.3343 0.3291 0.4760 0.0624  0.0751  0.0559  239 PHE D CA  
10796 C C   . PHE D 239 ? 0.3151 0.3110 0.4594 0.0553  0.0711  0.0564  239 PHE D C   
10797 O O   . PHE D 239 ? 0.3421 0.3344 0.4764 0.0501  0.0656  0.0526  239 PHE D O   
10798 C CB  . PHE D 239 ? 0.3631 0.3600 0.5172 0.0630  0.0688  0.0583  239 PHE D CB  
10799 C CG  . PHE D 239 ? 0.3972 0.3955 0.5607 0.0711  0.0743  0.0570  239 PHE D CG  
10800 C CD1 . PHE D 239 ? 0.3896 0.3803 0.5438 0.0747  0.0746  0.0523  239 PHE D CD1 
10801 C CD2 . PHE D 239 ? 0.4340 0.4421 0.6170 0.0748  0.0798  0.0591  239 PHE D CD2 
10802 C CE1 . PHE D 239 ? 0.4027 0.3948 0.5672 0.0821  0.0806  0.0480  239 PHE D CE1 
10803 C CE2 . PHE D 239 ? 0.4666 0.4779 0.6602 0.0824  0.0863  0.0550  239 PHE D CE2 
10804 C CZ  . PHE D 239 ? 0.4413 0.4441 0.6258 0.0862  0.0868  0.0486  239 PHE D CZ  
10805 N N   . ILE D 240 ? 0.3375 0.3394 0.4965 0.0544  0.0740  0.0601  240 ILE D N   
10806 C CA  . ILE D 240 ? 0.3225 0.3263 0.4899 0.0471  0.0694  0.0598  240 ILE D CA  
10807 C C   . ILE D 240 ? 0.3496 0.3625 0.5363 0.0455  0.0671  0.0649  240 ILE D C   
10808 O O   . ILE D 240 ? 0.3777 0.3959 0.5735 0.0511  0.0708  0.0689  240 ILE D O   
10809 C CB  . ILE D 240 ? 0.2971 0.2982 0.4675 0.0459  0.0741  0.0600  240 ILE D CB  
10810 C CG1 . ILE D 240 ? 0.2845 0.2911 0.4624 0.0507  0.0824  0.0675  240 ILE D CG1 
10811 C CG2 . ILE D 240 ? 0.2865 0.2797 0.4414 0.0465  0.0746  0.0549  240 ILE D CG2 
10812 C CD1 . ILE D 240 ? 0.2694 0.2754 0.4556 0.0484  0.0854  0.0721  240 ILE D CD1 
10813 N N   . GLN D 241 ? 0.3618 0.3779 0.5562 0.0376  0.0612  0.0639  241 GLN D N   
10814 C CA  . GLN D 241 ? 0.3764 0.4025 0.5897 0.0351  0.0578  0.0694  241 GLN D CA  
10815 C C   . GLN D 241 ? 0.3860 0.4154 0.6146 0.0333  0.0625  0.0724  241 GLN D C   
10816 O O   . GLN D 241 ? 0.4051 0.4296 0.6336 0.0281  0.0621  0.0683  241 GLN D O   
10817 C CB  . GLN D 241 ? 0.4321 0.4627 0.6444 0.0257  0.0467  0.0674  241 GLN D CB  
10818 C CG  . GLN D 241 ? 0.4832 0.5256 0.7163 0.0213  0.0417  0.0735  241 GLN D CG  
10819 C CD  . GLN D 241 ? 0.4904 0.5390 0.7386 0.0293  0.0433  0.0820  241 GLN D CD  
10820 O OE1 . GLN D 241 ? 0.5183 0.5626 0.7605 0.0363  0.0448  0.0824  241 GLN D OE1 
10821 N NE2 . GLN D 241 ? 0.4733 0.5325 0.7432 0.0281  0.0430  0.0878  241 GLN D NE2 
10822 N N   . VAL D 242 ? 0.3672 0.4051 0.6106 0.0378  0.0677  0.0794  242 VAL D N   
10823 C CA  . VAL D 242 ? 0.3251 0.3691 0.5857 0.0348  0.0715  0.0847  242 VAL D CA  
10824 C C   . VAL D 242 ? 0.3766 0.4320 0.6567 0.0304  0.0656  0.0887  242 VAL D C   
10825 O O   . VAL D 242 ? 0.4020 0.4662 0.6914 0.0354  0.0663  0.0926  242 VAL D O   
10826 C CB  . VAL D 242 ? 0.2681 0.3175 0.5311 0.0413  0.0827  0.0905  242 VAL D CB  
10827 C CG1 . VAL D 242 ? 0.2577 0.3165 0.5407 0.0369  0.0860  0.0985  242 VAL D CG1 
10828 C CG2 . VAL D 242 ? 0.2991 0.3386 0.5433 0.0438  0.0868  0.0879  242 VAL D CG2 
10829 N N   . ASN D 243 ? 0.3373 0.3930 0.6251 0.0209  0.0593  0.0870  243 ASN D N   
10830 C CA  . ASN D 243 ? 0.3210 0.3889 0.6271 0.0153  0.0526  0.0912  243 ASN D CA  
10831 C C   . ASN D 243 ? 0.3350 0.4141 0.6635 0.0167  0.0587  0.1000  243 ASN D C   
10832 O O   . ASN D 243 ? 0.3382 0.4306 0.6839 0.0168  0.0560  0.1058  243 ASN D O   
10833 C CB  . ASN D 243 ? 0.3430 0.4094 0.6492 0.0032  0.0437  0.0845  243 ASN D CB  
10834 C CG  . ASN D 243 ? 0.4080 0.4739 0.6974 -0.0013 0.0348  0.0783  243 ASN D CG  
10835 O OD1 . ASN D 243 ? 0.4118 0.4762 0.6901 0.0049  0.0344  0.0801  243 ASN D OD1 
10836 N ND2 . ASN D 243 ? 0.4488 0.5174 0.7371 -0.0133 0.0271  0.0709  243 ASN D ND2 
10837 N N   . ALA D 244 ? 0.3232 0.3983 0.6528 0.0173  0.0665  0.1023  244 ALA D N   
10838 C CA  . ALA D 244 ? 0.2809 0.3681 0.6308 0.0167  0.0728  0.1118  244 ALA D CA  
10839 C C   . ALA D 244 ? 0.2716 0.3551 0.6170 0.0186  0.0819  0.1164  244 ALA D C   
10840 O O   . ALA D 244 ? 0.2973 0.3668 0.6288 0.0184  0.0813  0.1122  244 ALA D O   
10841 C CB  . ALA D 244 ? 0.2745 0.3661 0.6438 0.0061  0.0656  0.1137  244 ALA D CB  
10842 N N   . ILE D 245 ? 0.2830 0.3813 0.6413 0.0199  0.0900  0.1258  245 ILE D N   
10843 C CA  . ILE D 245 ? 0.2943 0.3943 0.6534 0.0180  0.0972  0.1345  245 ILE D CA  
10844 C C   . ILE D 245 ? 0.2742 0.3801 0.6577 0.0085  0.0948  0.1435  245 ILE D C   
10845 O O   . ILE D 245 ? 0.2913 0.4123 0.6924 0.0066  0.0950  0.1473  245 ILE D O   
10846 C CB  . ILE D 245 ? 0.2701 0.3864 0.6245 0.0243  0.1093  0.1391  245 ILE D CB  
10847 C CG1 . ILE D 245 ? 0.2667 0.3771 0.5997 0.0335  0.1114  0.1289  245 ILE D CG1 
10848 C CG2 . ILE D 245 ? 0.2768 0.3964 0.6286 0.0204  0.1154  0.1500  245 ILE D CG2 
10849 C CD1 . ILE D 245 ? 0.2754 0.4040 0.6077 0.0400  0.1233  0.1288  245 ILE D CD1 
10850 N N   . ARG D 246 ? 0.2796 0.3728 0.6666 0.0026  0.0916  0.1465  246 ARG D N   
10851 C CA  . ARG D 246 ? 0.3349 0.4304 0.7470 -0.0073 0.0886  0.1558  246 ARG D CA  
10852 C C   . ARG D 246 ? 0.3126 0.4183 0.7307 -0.0096 0.0964  0.1725  246 ARG D C   
10853 O O   . ARG D 246 ? 0.3644 0.4636 0.7690 -0.0069 0.0992  0.1758  246 ARG D O   
10854 C CB  . ARG D 246 ? 0.3729 0.4470 0.7902 -0.0133 0.0795  0.1480  246 ARG D CB  
10855 C CG  . ARG D 246 ? 0.3895 0.4615 0.8356 -0.0241 0.0750  0.1553  246 ARG D CG  
10856 C CD  . ARG D 246 ? 0.4369 0.4860 0.8881 -0.0271 0.0698  0.1498  246 ARG D CD  
10857 N NE  . ARG D 246 ? 0.4501 0.4857 0.8957 -0.0285 0.0627  0.1296  246 ARG D NE  
10858 C CZ  . ARG D 246 ? 0.5009 0.5192 0.9398 -0.0263 0.0607  0.1188  246 ARG D CZ  
10859 N NH1 . ARG D 246 ? 0.5133 0.5243 0.9508 -0.0219 0.0642  0.1277  246 ARG D NH1 
10860 N NH2 . ARG D 246 ? 0.5322 0.5425 0.9656 -0.0290 0.0552  0.0993  246 ARG D NH2 
10861 N N   . VAL D 247 ? 0.2999 0.4236 0.7379 -0.0153 0.0996  0.1842  247 VAL D N   
10862 C CA  . VAL D 247 ? 0.3046 0.4380 0.7513 -0.0211 0.1047  0.2024  247 VAL D CA  
10863 C C   . VAL D 247 ? 0.3230 0.4551 0.7998 -0.0324 0.0982  0.2111  247 VAL D C   
10864 O O   . VAL D 247 ? 0.3257 0.4726 0.8182 -0.0359 0.0985  0.2128  247 VAL D O   
10865 C CB  . VAL D 247 ? 0.3176 0.4795 0.7592 -0.0186 0.1172  0.2104  247 VAL D CB  
10866 C CG1 . VAL D 247 ? 0.3160 0.4901 0.7645 -0.0270 0.1215  0.2310  247 VAL D CG1 
10867 C CG2 . VAL D 247 ? 0.3146 0.4768 0.7286 -0.0076 0.1233  0.1991  247 VAL D CG2 
10868 N N   . ASN D 248 ? 0.3605 0.4742 0.8476 -0.0381 0.0916  0.2161  248 ASN D N   
10869 C CA  . ASN D 248 ? 0.3977 0.5039 0.9152 -0.0489 0.0835  0.2202  248 ASN D CA  
10870 C C   . ASN D 248 ? 0.3808 0.4822 0.9026 -0.0497 0.0770  0.2028  248 ASN D C   
10871 O O   . ASN D 248 ? 0.3771 0.4620 0.8854 -0.0454 0.0723  0.1855  248 ASN D O   
10872 C CB  . ASN D 248 ? 0.4456 0.5740 0.9836 -0.0578 0.0877  0.2414  248 ASN D CB  
10873 C CG  . ASN D 248 ? 0.4991 0.6300 1.0329 -0.0597 0.0899  0.2596  248 ASN D CG  
10874 O OD1 . ASN D 248 ? 0.5509 0.6634 1.0798 -0.0575 0.0864  0.2596  248 ASN D OD1 
10875 N ND2 . ASN D 248 ? 0.4828 0.6374 1.0155 -0.0632 0.0943  0.2739  248 ASN D ND2 
10876 N N   . LYS D 249 ? 0.4213 0.5396 0.9608 -0.0556 0.0766  0.2074  249 LYS D N   
10877 C CA  . LYS D 249 ? 0.4562 0.5722 0.9992 -0.0576 0.0690  0.1921  249 LYS D CA  
10878 C C   . LYS D 249 ? 0.3846 0.5209 0.9179 -0.0507 0.0731  0.1888  249 LYS D C   
10879 O O   . LYS D 249 ? 0.3420 0.4832 0.8835 -0.0543 0.0664  0.1817  249 LYS D O   
10880 C CB  . LYS D 249 ? 0.5349 0.6506 1.1096 -0.0711 0.0614  0.1962  249 LYS D CB  
10881 C CG  . LYS D 249 ? 0.6196 0.7153 1.2109 -0.0778 0.0575  0.2017  249 LYS D CG  
10882 C CD  . LYS D 249 ? 0.6570 0.7282 1.2532 -0.0819 0.0476  0.1816  249 LYS D CD  
10883 C CE  . LYS D 249 ? 0.6835 0.7340 1.3034 -0.0880 0.0435  0.1867  249 LYS D CE  
10884 N NZ  . LYS D 249 ? 0.6827 0.7096 1.3026 -0.0886 0.0368  0.1630  249 LYS D NZ  
10885 N N   . HIS D 250 ? 0.3721 0.5196 0.8886 -0.0411 0.0834  0.1930  250 HIS D N   
10886 C CA  . HIS D 250 ? 0.3361 0.5000 0.8440 -0.0322 0.0883  0.1881  250 HIS D CA  
10887 C C   . HIS D 250 ? 0.3387 0.4879 0.8190 -0.0225 0.0871  0.1741  250 HIS D C   
10888 O O   . HIS D 250 ? 0.3558 0.4920 0.8187 -0.0190 0.0898  0.1728  250 HIS D O   
10889 C CB  . HIS D 250 ? 0.3108 0.4992 0.8195 -0.0278 0.1020  0.1990  250 HIS D CB  
10890 C CG  . HIS D 250 ? 0.3215 0.5341 0.8578 -0.0354 0.1054  0.2120  250 HIS D CG  
10891 N ND1 . HIS D 250 ? 0.3239 0.5408 0.8746 -0.0458 0.1067  0.2275  250 HIS D ND1 
10892 C CD2 . HIS D 250 ? 0.3163 0.5520 0.8697 -0.0340 0.1083  0.2128  250 HIS D CD2 
10893 C CE1 . HIS D 250 ? 0.3437 0.5827 0.9125 -0.0502 0.1090  0.2350  250 HIS D CE1 
10894 N NE2 . HIS D 250 ? 0.3203 0.5726 0.8938 -0.0433 0.1109  0.2266  250 HIS D NE2 
10895 N N   . LEU D 251 ? 0.3308 0.4833 0.8094 -0.0191 0.0821  0.1653  251 LEU D N   
10896 C CA  . LEU D 251 ? 0.2929 0.4346 0.7482 -0.0109 0.0798  0.1534  251 LEU D CA  
10897 C C   . LEU D 251 ? 0.2946 0.4521 0.7488 -0.0007 0.0866  0.1535  251 LEU D C   
10898 O O   . LEU D 251 ? 0.2690 0.4448 0.7443 -0.0013 0.0865  0.1581  251 LEU D O   
10899 C CB  . LEU D 251 ? 0.2765 0.4095 0.7314 -0.0167 0.0668  0.1436  251 LEU D CB  
10900 C CG  . LEU D 251 ? 0.3018 0.4165 0.7555 -0.0258 0.0598  0.1369  251 LEU D CG  
10901 C CD1 . LEU D 251 ? 0.3078 0.4198 0.7574 -0.0319 0.0482  0.1255  251 LEU D CD1 
10902 C CD2 . LEU D 251 ? 0.3191 0.4170 0.7520 -0.0200 0.0644  0.1326  251 LEU D CD2 
10903 N N   . VAL D 252 ? 0.3086 0.4605 0.7416 0.0085  0.0932  0.1489  252 VAL D N   
10904 C CA  . VAL D 252 ? 0.2945 0.4571 0.7267 0.0189  0.0983  0.1451  252 VAL D CA  
10905 C C   . VAL D 252 ? 0.2678 0.4148 0.6845 0.0222  0.0887  0.1354  252 VAL D C   
10906 O O   . VAL D 252 ? 0.2891 0.4200 0.6826 0.0244  0.0886  0.1296  252 VAL D O   
10907 C CB  . VAL D 252 ? 0.2982 0.4679 0.7186 0.0260  0.1124  0.1454  252 VAL D CB  
10908 C CG1 . VAL D 252 ? 0.2724 0.4532 0.6968 0.0368  0.1183  0.1389  252 VAL D CG1 
10909 C CG2 . VAL D 252 ? 0.2705 0.4578 0.7048 0.0198  0.1208  0.1571  252 VAL D CG2 
10910 N N   . ILE D 253 ? 0.2900 0.4437 0.7207 0.0217  0.0802  0.1353  253 ILE D N   
10911 C CA  . ILE D 253 ? 0.2943 0.4369 0.7129 0.0216  0.0689  0.1292  253 ILE D CA  
10912 C C   . ILE D 253 ? 0.2947 0.4423 0.7178 0.0316  0.0687  0.1280  253 ILE D C   
10913 O O   . ILE D 253 ? 0.2672 0.4287 0.7141 0.0322  0.0640  0.1331  253 ILE D O   
10914 C CB  . ILE D 253 ? 0.2930 0.4395 0.7238 0.0102  0.0555  0.1313  253 ILE D CB  
10915 C CG1 . ILE D 253 ? 0.2889 0.4292 0.7201 0.0000  0.0553  0.1310  253 ILE D CG1 
10916 C CG2 . ILE D 253 ? 0.2603 0.3982 0.6755 0.0074  0.0434  0.1258  253 ILE D CG2 
10917 C CD1 . ILE D 253 ? 0.2679 0.4183 0.7197 -0.0118 0.0457  0.1344  253 ILE D CD1 
10918 N N   . PRO D 254 ? 0.3574 0.4929 0.7598 0.0391  0.0727  0.1215  254 PRO D N   
10919 C CA  . PRO D 254 ? 0.3641 0.4997 0.7696 0.0488  0.0725  0.1188  254 PRO D CA  
10920 C C   . PRO D 254 ? 0.3928 0.5250 0.8001 0.0444  0.0566  0.1213  254 PRO D C   
10921 O O   . PRO D 254 ? 0.3940 0.5173 0.7840 0.0351  0.0485  0.1196  254 PRO D O   
10922 C CB  . PRO D 254 ? 0.3762 0.4973 0.7542 0.0542  0.0797  0.1110  254 PRO D CB  
10923 C CG  . PRO D 254 ? 0.3822 0.5006 0.7483 0.0491  0.0865  0.1116  254 PRO D CG  
10924 C CD  . PRO D 254 ? 0.3894 0.5098 0.7653 0.0383  0.0776  0.1164  254 PRO D CD  
10925 N N   . THR D 255 ? 0.4466 0.5869 0.8753 0.0500  0.0519  0.1253  255 THR D N   
10926 C CA  . THR D 255 ? 0.4957 0.6337 0.9249 0.0449  0.0354  0.1303  255 THR D CA  
10927 C C   . THR D 255 ? 0.5223 0.6485 0.9430 0.0529  0.0338  0.1274  255 THR D C   
10928 O O   . THR D 255 ? 0.5412 0.6631 0.9552 0.0477  0.0203  0.1317  255 THR D O   
10929 C CB  . THR D 255 ? 0.3077 0.4645 0.7723 0.0430  0.0264  0.1411  255 THR D CB  
10930 O OG1 . THR D 255 ? 0.3582 0.5233 0.8509 0.0561  0.0342  0.1416  255 THR D OG1 
10931 C CG2 . THR D 255 ? 0.2692 0.4383 0.7438 0.0339  0.0268  0.1444  255 THR D CG2 
10932 N N   . GLU D 272 ? 0.8601 0.9011 1.0921 0.0221  -0.0171 0.1190  272 GLU D N   
10933 C CA  . GLU D 272 ? 0.8431 0.8878 1.0624 0.0185  -0.0092 0.1089  272 GLU D CA  
10934 C C   . GLU D 272 ? 0.7326 0.7649 0.9337 0.0252  0.0048  0.0956  272 GLU D C   
10935 O O   . GLU D 272 ? 0.6271 0.6597 0.8095 0.0190  0.0078  0.0874  272 GLU D O   
10936 C CB  . GLU D 272 ? 0.9277 0.9846 1.1305 0.0019  -0.0186 0.1096  272 GLU D CB  
10937 C CG  . GLU D 272 ? 1.0088 1.0808 1.2261 -0.0056 -0.0243 0.1139  272 GLU D CG  
10938 C CD  . GLU D 272 ? 1.0747 1.1440 1.3018 0.0010  -0.0124 0.1057  272 GLU D CD  
10939 O OE1 . GLU D 272 ? 1.1129 1.1706 1.3294 0.0081  -0.0002 0.0954  272 GLU D OE1 
10940 O OE2 . GLU D 272 ? 1.0831 1.1632 1.3292 -0.0016 -0.0158 0.1108  272 GLU D OE2 
10941 N N   . ILE D 273 ? 0.7381 0.7607 0.9461 0.0374  0.0127  0.0933  273 ILE D N   
10942 C CA  . ILE D 273 ? 0.7479 0.7611 0.9416 0.0442  0.0257  0.0827  273 ILE D CA  
10943 C C   . ILE D 273 ? 0.7496 0.7687 0.9522 0.0459  0.0338  0.0802  273 ILE D C   
10944 O O   . ILE D 273 ? 0.7931 0.8212 1.0173 0.0463  0.0316  0.0859  273 ILE D O   
10945 C CB  . ILE D 273 ? 0.7349 0.7391 0.9343 0.0554  0.0318  0.0802  273 ILE D CB  
10946 C CG1 . ILE D 273 ? 0.7514 0.7502 0.9520 0.0537  0.0214  0.0858  273 ILE D CG1 
10947 C CG2 . ILE D 273 ? 0.7236 0.7203 0.9039 0.0598  0.0432  0.0704  273 ILE D CG2 
10948 C CD1 . ILE D 273 ? 0.7675 0.7556 0.9732 0.0637  0.0271  0.0806  273 ILE D CD1 
10949 N N   . GLY D 274 ? 0.6684 0.6835 0.8571 0.0460  0.0421  0.0731  274 GLY D N   
10950 C CA  . GLY D 274 ? 0.6195 0.6395 0.8185 0.0473  0.0495  0.0726  274 GLY D CA  
10951 C C   . GLY D 274 ? 0.5861 0.6103 0.8024 0.0568  0.0573  0.0749  274 GLY D C   
10952 O O   . GLY D 274 ? 0.6206 0.6413 0.8386 0.0635  0.0590  0.0736  274 GLY D O   
10953 N N   . GLY D 275 ? 0.4835 0.5164 0.7144 0.0569  0.0624  0.0775  275 GLY D N   
10954 C CA  . GLY D 275 ? 0.4320 0.4729 0.6804 0.0648  0.0708  0.0787  275 GLY D CA  
10955 C C   . GLY D 275 ? 0.4296 0.4705 0.6677 0.0690  0.0835  0.0748  275 GLY D C   
10956 O O   . GLY D 275 ? 0.4795 0.5285 0.7275 0.0753  0.0925  0.0733  275 GLY D O   
10957 N N   . ALA D 276 ? 0.3837 0.4172 0.6030 0.0652  0.0844  0.0731  276 ALA D N   
10958 C CA  . ALA D 276 ? 0.3405 0.3762 0.5507 0.0678  0.0950  0.0724  276 ALA D CA  
10959 C C   . ALA D 276 ? 0.3486 0.3746 0.5363 0.0704  0.0965  0.0666  276 ALA D C   
10960 O O   . ALA D 276 ? 0.3520 0.3682 0.5262 0.0669  0.0909  0.0650  276 ALA D O   
10961 C CB  . ALA D 276 ? 0.3267 0.3638 0.5390 0.0617  0.0956  0.0776  276 ALA D CB  
10962 N N   . LEU D 277 ? 0.3620 0.3922 0.5464 0.0762  0.1045  0.0624  277 LEU D N   
10963 C CA  . LEU D 277 ? 0.3621 0.3851 0.5255 0.0780  0.1066  0.0568  277 LEU D CA  
10964 C C   . LEU D 277 ? 0.3356 0.3613 0.4865 0.0748  0.1112  0.0608  277 LEU D C   
10965 O O   . LEU D 277 ? 0.3291 0.3662 0.4880 0.0730  0.1169  0.0667  277 LEU D O   
10966 C CB  . LEU D 277 ? 0.3811 0.4088 0.5463 0.0846  0.1139  0.0489  277 LEU D CB  
10967 C CG  . LEU D 277 ? 0.4176 0.4410 0.5610 0.0857  0.1177  0.0420  277 LEU D CG  
10968 C CD1 . LEU D 277 ? 0.4253 0.4326 0.5575 0.0852  0.1084  0.0390  277 LEU D CD1 
10969 C CD2 . LEU D 277 ? 0.4421 0.4750 0.5898 0.0909  0.1279  0.0325  277 LEU D CD2 
10970 N N   . ILE D 278 ? 0.3631 0.3792 0.4960 0.0735  0.1079  0.0587  278 ILE D N   
10971 C CA  . ILE D 278 ? 0.3854 0.4039 0.5059 0.0712  0.1115  0.0627  278 ILE D CA  
10972 C C   . ILE D 278 ? 0.3910 0.4106 0.4941 0.0738  0.1158  0.0564  278 ILE D C   
10973 O O   . ILE D 278 ? 0.3993 0.4090 0.4946 0.0757  0.1115  0.0494  278 ILE D O   
10974 C CB  . ILE D 278 ? 0.3899 0.3981 0.5061 0.0675  0.1044  0.0651  278 ILE D CB  
10975 C CG1 . ILE D 278 ? 0.3791 0.3851 0.5120 0.0640  0.0993  0.0676  278 ILE D CG1 
10976 C CG2 . ILE D 278 ? 0.3771 0.3892 0.4866 0.0654  0.1073  0.0720  278 ILE D CG2 
10977 C CD1 . ILE D 278 ? 0.3733 0.3694 0.5034 0.0605  0.0927  0.0651  278 ILE D CD1 
10978 N N   . THR D 279 ? 0.3772 0.4101 0.4743 0.0728  0.1239  0.0590  279 THR D N   
10979 C CA  . THR D 279 ? 0.4050 0.4427 0.4857 0.0741  0.1293  0.0513  279 THR D CA  
10980 C C   . THR D 279 ? 0.4524 0.5039 0.5202 0.0692  0.1341  0.0588  279 THR D C   
10981 O O   . THR D 279 ? 0.4705 0.5313 0.5465 0.0655  0.1357  0.0703  279 THR D O   
10982 C CB  . THR D 279 ? 0.3989 0.4450 0.4889 0.0787  0.1369  0.0411  279 THR D CB  
10983 O OG1 . THR D 279 ? 0.4672 0.5179 0.5416 0.0793  0.1425  0.0308  279 THR D OG1 
10984 C CG2 . THR D 279 ? 0.3469 0.4116 0.4503 0.0772  0.1450  0.0468  279 THR D CG2 
10985 N N   . THR D 280 ? 0.4822 0.5364 0.5307 0.0680  0.1358  0.0538  280 THR D N   
10986 C CA  . THR D 280 ? 0.4445 0.5155 0.4800 0.0617  0.1396  0.0627  280 THR D CA  
10987 C C   . THR D 280 ? 0.4501 0.5401 0.4736 0.0601  0.1501  0.0532  280 THR D C   
10988 O O   . THR D 280 ? 0.4786 0.5860 0.4878 0.0534  0.1534  0.0596  280 THR D O   
10989 C CB  . THR D 280 ? 0.4245 0.4886 0.4455 0.0589  0.1323  0.0677  280 THR D CB  
10990 O OG1 . THR D 280 ? 0.4208 0.4748 0.4296 0.0618  0.1306  0.0539  280 THR D OG1 
10991 C CG2 . THR D 280 ? 0.4233 0.4731 0.4571 0.0592  0.1233  0.0774  280 THR D CG2 
10992 N N   . THR D 281 ? 0.4472 0.5357 0.4782 0.0656  0.1554  0.0379  281 THR D N   
10993 C CA  . THR D 281 ? 0.4870 0.5911 0.5072 0.0647  0.1655  0.0236  281 THR D CA  
10994 C C   . THR D 281 ? 0.4973 0.6257 0.5272 0.0633  0.1778  0.0216  281 THR D C   
10995 O O   . THR D 281 ? 0.4930 0.6371 0.5173 0.0628  0.1882  0.0065  281 THR D O   
10996 C CB  . THR D 281 ? 0.4826 0.5699 0.5066 0.0716  0.1640  0.0058  281 THR D CB  
10997 O OG1 . THR D 281 ? 0.4740 0.5489 0.5223 0.0782  0.1607  0.0054  281 THR D OG1 
10998 C CG2 . THR D 281 ? 0.4893 0.5589 0.4990 0.0704  0.1534  0.0080  281 THR D CG2 
10999 N N   . HIS D 282 ? 0.5111 0.6440 0.5560 0.0620  0.1769  0.0363  282 HIS D N   
11000 C CA  . HIS D 282 ? 0.5073 0.6680 0.5576 0.0571  0.1875  0.0410  282 HIS D CA  
11001 C C   . HIS D 282 ? 0.4529 0.6158 0.5085 0.0509  0.1815  0.0649  282 HIS D C   
11002 O O   . HIS D 282 ? 0.4800 0.6212 0.5450 0.0535  0.1709  0.0726  282 HIS D O   
11003 C CB  . HIS D 282 ? 0.5528 0.7178 0.6270 0.0640  0.1951  0.0293  282 HIS D CB  
11004 C CG  . HIS D 282 ? 0.5948 0.7381 0.6916 0.0704  0.1858  0.0341  282 HIS D CG  
11005 N ND1 . HIS D 282 ? 0.5776 0.7191 0.6858 0.0671  0.1801  0.0516  282 HIS D ND1 
11006 C CD2 . HIS D 282 ? 0.6269 0.7508 0.7374 0.0787  0.1806  0.0240  282 HIS D CD2 
11007 C CE1 . HIS D 282 ? 0.5687 0.6920 0.6946 0.0728  0.1724  0.0507  282 HIS D CE1 
11008 N NE2 . HIS D 282 ? 0.6028 0.7158 0.7301 0.0796  0.1721  0.0354  282 HIS D NE2 
11009 N N   . PRO D 283 ? 0.4135 0.6034 0.4632 0.0417  0.1880  0.0764  283 PRO D N   
11010 C CA  . PRO D 283 ? 0.3938 0.5868 0.4501 0.0345  0.1817  0.1010  283 PRO D CA  
11011 C C   . PRO D 283 ? 0.4034 0.5909 0.4873 0.0364  0.1797  0.1094  283 PRO D C   
11012 O O   . PRO D 283 ? 0.4235 0.5939 0.5179 0.0359  0.1694  0.1221  283 PRO D O   
11013 C CB  . PRO D 283 ? 0.3957 0.6236 0.4369 0.0229  0.1903  0.1099  283 PRO D CB  
11014 C CG  . PRO D 283 ? 0.4131 0.6589 0.4477 0.0252  0.2041  0.0875  283 PRO D CG  
11015 C CD  . PRO D 283 ? 0.4189 0.6388 0.4528 0.0362  0.2010  0.0668  283 PRO D CD  
11016 N N   . TYR D 284 ? 0.4133 0.6158 0.5105 0.0383  0.1894  0.1020  284 TYR D N   
11017 C CA  . TYR D 284 ? 0.4112 0.6125 0.5343 0.0382  0.1875  0.1119  284 TYR D CA  
11018 C C   . TYR D 284 ? 0.3920 0.5701 0.5327 0.0481  0.1819  0.1009  284 TYR D C   
11019 O O   . TYR D 284 ? 0.4047 0.5730 0.5410 0.0556  0.1827  0.0839  284 TYR D O   
11020 C CB  . TYR D 284 ? 0.4848 0.7195 0.6151 0.0332  0.2009  0.1131  284 TYR D CB  
11021 C CG  . TYR D 284 ? 0.5539 0.8157 0.6641 0.0215  0.2063  0.1245  284 TYR D CG  
11022 C CD1 . TYR D 284 ? 0.5872 0.8478 0.6953 0.0125  0.1975  0.1486  284 TYR D CD1 
11023 C CD2 . TYR D 284 ? 0.5918 0.8801 0.6853 0.0190  0.2196  0.1107  284 TYR D CD2 
11024 C CE1 . TYR D 284 ? 0.6249 0.9115 0.7149 0.0007  0.2007  0.1619  284 TYR D CE1 
11025 C CE2 . TYR D 284 ? 0.6257 0.9418 0.6981 0.0064  0.2239  0.1216  284 TYR D CE2 
11026 C CZ  . TYR D 284 ? 0.6493 0.9642 0.7195 -0.0030 0.2135  0.1483  284 TYR D CZ  
11027 O OH  . TYR D 284 ? 0.7010 1.0357 0.7491 -0.0169 0.2115  0.1573  284 TYR D OH  
11028 N N   . THR D 285 ? 0.3757 0.5458 0.5372 0.0471  0.1756  0.1110  285 THR D N   
11029 C CA  . THR D 285 ? 0.4002 0.5524 0.5782 0.0545  0.1697  0.1023  285 THR D CA  
11030 C C   . THR D 285 ? 0.3811 0.5486 0.5762 0.0594  0.1787  0.0920  285 THR D C   
11031 O O   . THR D 285 ? 0.4100 0.6010 0.6161 0.0554  0.1873  0.0974  285 THR D O   
11032 C CB  . THR D 285 ? 0.4087 0.5478 0.6033 0.0509  0.1596  0.1146  285 THR D CB  
11033 O OG1 . THR D 285 ? 0.3984 0.5210 0.5814 0.0482  0.1510  0.1209  285 THR D OG1 
11034 C CG2 . THR D 285 ? 0.3885 0.5136 0.5989 0.0567  0.1532  0.1061  285 THR D CG2 
11035 N N   . VAL D 286 ? 0.3582 0.5126 0.5576 0.0680  0.1762  0.0779  286 VAL D N   
11036 C CA  . VAL D 286 ? 0.3373 0.5044 0.5553 0.0742  0.1843  0.0664  286 VAL D CA  
11037 C C   . VAL D 286 ? 0.3488 0.5070 0.5931 0.0777  0.1761  0.0689  286 VAL D C   
11038 O O   . VAL D 286 ? 0.3737 0.5097 0.6166 0.0793  0.1640  0.0696  286 VAL D O   
11039 C CB  . VAL D 286 ? 0.3535 0.5141 0.5617 0.0813  0.1874  0.0486  286 VAL D CB  
11040 C CG1 . VAL D 286 ? 0.3166 0.4880 0.5506 0.0894  0.1950  0.0352  286 VAL D CG1 
11041 C CG2 . VAL D 286 ? 0.3602 0.5330 0.5413 0.0764  0.1956  0.0455  286 VAL D CG2 
11042 N N   . LEU D 287 ? 0.3441 0.5217 0.6123 0.0781  0.1827  0.0705  287 LEU D N   
11043 C CA  . LEU D 287 ? 0.3302 0.5029 0.6251 0.0806  0.1747  0.0738  287 LEU D CA  
11044 C C   . LEU D 287 ? 0.3208 0.5036 0.6396 0.0897  0.1806  0.0617  287 LEU D C   
11045 O O   . LEU D 287 ? 0.3390 0.5434 0.6630 0.0919  0.1949  0.0532  287 LEU D O   
11046 C CB  . LEU D 287 ? 0.3696 0.5555 0.6790 0.0728  0.1746  0.0883  287 LEU D CB  
11047 C CG  . LEU D 287 ? 0.3930 0.5712 0.6853 0.0634  0.1697  0.1014  287 LEU D CG  
11048 C CD1 . LEU D 287 ? 0.2890 0.4818 0.5997 0.0554  0.1705  0.1155  287 LEU D CD1 
11049 C CD2 . LEU D 287 ? 0.3939 0.5433 0.6756 0.0633  0.1553  0.1016  287 LEU D CD2 
11050 N N   . SER D 288 ? 0.3153 0.4838 0.6506 0.0944  0.1695  0.0611  288 SER D N   
11051 C CA  . SER D 288 ? 0.3611 0.5378 0.7259 0.1034  0.1728  0.0521  288 SER D CA  
11052 C C   . SER D 288 ? 0.3614 0.5653 0.7508 0.1015  0.1818  0.0568  288 SER D C   
11053 O O   . SER D 288 ? 0.3486 0.5580 0.7357 0.0929  0.1794  0.0700  288 SER D O   
11054 C CB  . SER D 288 ? 0.3891 0.5471 0.7678 0.1064  0.1566  0.0557  288 SER D CB  
11055 O OG  . SER D 288 ? 0.4056 0.5634 0.7912 0.0991  0.1467  0.0698  288 SER D OG  
11056 N N   . HIS D 289 ? 0.2997 0.5183 0.7095 0.1080  0.1900  0.0447  289 HIS D N   
11057 C CA  . HIS D 289 ? 0.3070 0.5528 0.7309 0.1047  0.1993  0.0451  289 HIS D CA  
11058 C C   . HIS D 289 ? 0.3730 0.6243 0.8174 0.0993  0.1916  0.0620  289 HIS D C   
11059 O O   . HIS D 289 ? 0.3302 0.5998 0.7742 0.0914  0.1977  0.0708  289 HIS D O   
11060 C CB  . HIS D 289 ? 0.3204 0.5762 0.7639 0.1129  0.2043  0.0278  289 HIS D CB  
11061 C CG  . HIS D 289 ? 0.3624 0.6493 0.8212 0.1100  0.2150  0.0261  289 HIS D CG  
11062 N ND1 . HIS D 289 ? 0.3799 0.6911 0.8208 0.1036  0.2298  0.0217  289 HIS D ND1 
11063 C CD2 . HIS D 289 ? 0.3307 0.6301 0.8204 0.1114  0.2125  0.0297  289 HIS D CD2 
11064 C CE1 . HIS D 289 ? 0.4085 0.7463 0.8688 0.1014  0.2365  0.0215  289 HIS D CE1 
11065 N NE2 . HIS D 289 ? 0.4248 0.7554 0.9153 0.1065  0.2264  0.0261  289 HIS D NE2 
11066 N N   . SER D 290 ? 0.4014 0.6382 0.8640 0.1024  0.1773  0.0673  290 SER D N   
11067 C CA  . SER D 290 ? 0.4151 0.6585 0.8985 0.0966  0.1690  0.0821  290 SER D CA  
11068 C C   . SER D 290 ? 0.3525 0.5920 0.8197 0.0860  0.1659  0.0959  290 SER D C   
11069 O O   . SER D 290 ? 0.3585 0.6125 0.8370 0.0786  0.1672  0.1062  290 SER D O   
11070 C CB  . SER D 290 ? 0.4699 0.6991 0.9726 0.1003  0.1527  0.0859  290 SER D CB  
11071 O OG  . SER D 290 ? 0.4981 0.7409 1.0270 0.0961  0.1470  0.0958  290 SER D OG  
11072 N N   . ILE D 291 ? 0.3474 0.5634 0.7831 0.0840  0.1595  0.0947  291 ILE D N   
11073 C CA  . ILE D 291 ? 0.3335 0.5393 0.7478 0.0735  0.1541  0.1046  291 ILE D CA  
11074 C C   . ILE D 291 ? 0.3085 0.5314 0.7126 0.0686  0.1677  0.1078  291 ILE D C   
11075 O O   . ILE D 291 ? 0.2778 0.5067 0.6845 0.0594  0.1667  0.1199  291 ILE D O   
11076 C CB  . ILE D 291 ? 0.3263 0.5051 0.7117 0.0734  0.1453  0.1012  291 ILE D CB  
11077 C CG1 . ILE D 291 ? 0.3274 0.4921 0.7221 0.0763  0.1311  0.0998  291 ILE D CG1 
11078 C CG2 . ILE D 291 ? 0.3144 0.4838 0.6818 0.0635  0.1411  0.1101  291 ILE D CG2 
11079 C CD1 . ILE D 291 ? 0.3070 0.4480 0.6757 0.0759  0.1224  0.0962  291 ILE D CD1 
11080 N N   . PHE D 292 ? 0.3194 0.5512 0.7126 0.0741  0.1802  0.0972  292 PHE D N   
11081 C CA  . PHE D 292 ? 0.3558 0.6084 0.7370 0.0684  0.1937  0.1000  292 PHE D CA  
11082 C C   . PHE D 292 ? 0.3920 0.6733 0.7979 0.0629  0.2013  0.1090  292 PHE D C   
11083 O O   . PHE D 292 ? 0.3982 0.6899 0.7976 0.0526  0.2038  0.1221  292 PHE D O   
11084 C CB  . PHE D 292 ? 0.3946 0.6566 0.7638 0.0751  0.2067  0.0837  292 PHE D CB  
11085 C CG  . PHE D 292 ? 0.4397 0.7293 0.7964 0.0679  0.2213  0.0855  292 PHE D CG  
11086 C CD1 . PHE D 292 ? 0.4538 0.7399 0.7815 0.0596  0.2208  0.0947  292 PHE D CD1 
11087 C CD2 . PHE D 292 ? 0.4544 0.7710 0.8231 0.0673  0.2313  0.0771  292 PHE D CD2 
11088 C CE1 . PHE D 292 ? 0.4659 0.7794 0.7803 0.0509  0.2323  0.0986  292 PHE D CE1 
11089 C CE2 . PHE D 292 ? 0.4693 0.8126 0.8219 0.0580  0.2428  0.0780  292 PHE D CE2 
11090 C CZ  . PHE D 292 ? 0.4705 0.8121 0.7950 0.0493  0.2427  0.0895  292 PHE D CZ  
11091 N N   . GLU D 293 ? 0.3797 0.6716 0.8109 0.0686  0.2023  0.1016  293 GLU D N   
11092 C CA  . GLU D 293 ? 0.3664 0.6832 0.8158 0.0628  0.2070  0.1071  293 GLU D CA  
11093 C C   . GLU D 293 ? 0.2969 0.6102 0.7597 0.0535  0.1969  0.1258  293 GLU D C   
11094 O O   . GLU D 293 ? 0.3035 0.6327 0.7671 0.0436  0.2006  0.1367  293 GLU D O   
11095 C CB  . GLU D 293 ? 0.4200 0.7463 0.8947 0.0718  0.2085  0.0941  293 GLU D CB  
11096 C CG  . GLU D 293 ? 0.4880 0.8277 0.9548 0.0783  0.2217  0.0741  293 GLU D CG  
11097 C CD  . GLU D 293 ? 0.5736 0.9461 1.0338 0.0699  0.2362  0.0734  293 GLU D CD  
11098 O OE1 . GLU D 293 ? 0.6275 1.0215 1.1105 0.0678  0.2393  0.0749  293 GLU D OE1 
11099 O OE2 . GLU D 293 ? 0.5916 0.9700 1.0237 0.0646  0.2441  0.0718  293 GLU D OE2 
11100 N N   . VAL D 294 ? 0.2843 0.5775 0.7575 0.0557  0.1835  0.1292  294 VAL D N   
11101 C CA  . VAL D 294 ? 0.2781 0.5666 0.7654 0.0466  0.1724  0.1436  294 VAL D CA  
11102 C C   . VAL D 294 ? 0.2809 0.5563 0.7453 0.0364  0.1688  0.1535  294 VAL D C   
11103 O O   . VAL D 294 ? 0.3405 0.6228 0.8152 0.0261  0.1669  0.1665  294 VAL D O   
11104 C CB  . VAL D 294 ? 0.3569 0.6236 0.8502 0.0498  0.1558  0.1408  294 VAL D CB  
11105 C CG1 . VAL D 294 ? 0.3329 0.5914 0.8327 0.0386  0.1431  0.1520  294 VAL D CG1 
11106 C CG2 . VAL D 294 ? 0.3375 0.6178 0.8602 0.0587  0.1566  0.1350  294 VAL D CG2 
11107 N N   . PHE D 295 ? 0.2812 0.5368 0.7169 0.0395  0.1672  0.1475  295 PHE D N   
11108 C CA  . PHE D 295 ? 0.2842 0.5257 0.6998 0.0315  0.1633  0.1561  295 PHE D CA  
11109 C C   . PHE D 295 ? 0.2986 0.5633 0.7127 0.0236  0.1746  0.1677  295 PHE D C   
11110 O O   . PHE D 295 ? 0.2974 0.5590 0.7148 0.0135  0.1698  0.1820  295 PHE D O   
11111 C CB  . PHE D 295 ? 0.3303 0.5499 0.7170 0.0373  0.1606  0.1465  295 PHE D CB  
11112 C CG  . PHE D 295 ? 0.3459 0.5560 0.7133 0.0306  0.1593  0.1550  295 PHE D CG  
11113 C CD1 . PHE D 295 ? 0.3459 0.5366 0.7160 0.0240  0.1474  0.1623  295 PHE D CD1 
11114 C CD2 . PHE D 295 ? 0.3406 0.5626 0.6890 0.0304  0.1696  0.1558  295 PHE D CD2 
11115 C CE1 . PHE D 295 ? 0.3591 0.5410 0.7170 0.0182  0.1456  0.1713  295 PHE D CE1 
11116 C CE2 . PHE D 295 ? 0.3595 0.5742 0.6929 0.0237  0.1671  0.1665  295 PHE D CE2 
11117 C CZ  . PHE D 295 ? 0.3610 0.5547 0.7008 0.0182  0.1548  0.1747  295 PHE D CZ  
11118 N N   . THR D 296 ? 0.3014 0.5902 0.7113 0.0273  0.1893  0.1617  296 THR D N   
11119 C CA  . THR D 296 ? 0.3435 0.6560 0.7457 0.0181  0.1989  0.1720  296 THR D CA  
11120 C C   . THR D 296 ? 0.3590 0.6869 0.7832 0.0093  0.1971  0.1832  296 THR D C   
11121 O O   . THR D 296 ? 0.3608 0.6966 0.7803 -0.0022 0.1965  0.1983  296 THR D O   
11122 C CB  . THR D 296 ? 0.3930 0.7266 0.7787 0.0225  0.2131  0.1574  296 THR D CB  
11123 O OG1 . THR D 296 ? 0.4778 0.8217 0.8831 0.0311  0.2173  0.1428  296 THR D OG1 
11124 C CG2 . THR D 296 ? 0.3840 0.7029 0.7455 0.0292  0.2146  0.1477  296 THR D CG2 
11125 N N   . GLN D 297 ? 0.3434 0.6755 0.7920 0.0138  0.1949  0.1773  297 GLN D N   
11126 C CA  . GLN D 297 ? 0.3722 0.7188 0.8416 0.0051  0.1926  0.1882  297 GLN D CA  
11127 C C   . GLN D 297 ? 0.3153 0.6425 0.7941 -0.0041 0.1790  0.2034  297 GLN D C   
11128 O O   . GLN D 297 ? 0.5101 0.8444 0.9929 -0.0151 0.1773  0.2175  297 GLN D O   
11129 C CB  . GLN D 297 ? 0.4149 0.7730 0.9092 0.0118  0.1933  0.1787  297 GLN D CB  
11130 C CG  . GLN D 297 ? 0.4917 0.8682 1.0065 0.0022  0.1923  0.1897  297 GLN D CG  
11131 C CD  . GLN D 297 ? 0.5681 0.9714 1.0714 -0.0064 0.2042  0.1951  297 GLN D CD  
11132 O OE1 . GLN D 297 ? 0.6342 1.0577 1.1285 -0.0021 0.2173  0.1825  297 GLN D OE1 
11133 N NE2 . GLN D 297 ? 0.5477 0.9515 1.0523 -0.0195 0.1990  0.2133  297 GLN D NE2 
11134 N N   . VAL D 298 ? 0.3166 0.6194 0.7992 -0.0002 0.1693  0.1998  298 VAL D N   
11135 C CA  . VAL D 298 ? 0.3422 0.6248 0.8331 -0.0091 0.1568  0.2102  298 VAL D CA  
11136 C C   . VAL D 298 ? 0.3821 0.6581 0.8579 -0.0174 0.1567  0.2229  298 VAL D C   
11137 O O   . VAL D 298 ? 0.4052 0.6753 0.8921 -0.0278 0.1491  0.2356  298 VAL D O   
11138 C CB  . VAL D 298 ? 0.3391 0.5910 0.8190 -0.0026 0.1448  0.1973  298 VAL D CB  
11139 C CG1 . VAL D 298 ? 0.2925 0.5179 0.7671 -0.0101 0.1332  0.2019  298 VAL D CG1 
11140 C CG2 . VAL D 298 ? 0.3439 0.5993 0.8434 0.0012  0.1388  0.1900  298 VAL D CG2 
11141 N N   . PHE D 299 ? 0.4091 0.6862 0.8603 -0.0128 0.1641  0.2197  299 PHE D N   
11142 C CA  . PHE D 299 ? 0.4032 0.6756 0.8391 -0.0201 0.1630  0.2325  299 PHE D CA  
11143 C C   . PHE D 299 ? 0.3851 0.6805 0.8238 -0.0300 0.1663  0.2456  299 PHE D C   
11144 O O   . PHE D 299 ? 0.3977 0.6857 0.8430 -0.0397 0.1583  0.2610  299 PHE D O   
11145 C CB  . PHE D 299 ? 0.4350 0.7076 0.8427 -0.0137 0.1704  0.2257  299 PHE D CB  
11146 C CG  . PHE D 299 ? 0.5156 0.7783 0.9089 -0.0205 0.1658  0.2392  299 PHE D CG  
11147 C CD1 . PHE D 299 ? 0.5448 0.7753 0.9388 -0.0202 0.1531  0.2398  299 PHE D CD1 
11148 C CD2 . PHE D 299 ? 0.5665 0.8493 0.9423 -0.0268 0.1711  0.2484  299 PHE D CD2 
11149 C CE1 . PHE D 299 ? 0.5688 0.7904 0.9555 -0.0259 0.1484  0.2536  299 PHE D CE1 
11150 C CE2 . PHE D 299 ? 0.6074 0.8813 0.9718 -0.0331 0.1646  0.2625  299 PHE D CE2 
11151 C CZ  . PHE D 299 ? 0.5958 0.8390 0.9681 -0.0322 0.1534  0.2661  299 PHE D CZ  
11152 N N   . ALA D 300 ? 0.3855 0.7086 0.8212 -0.0275 0.1779  0.2386  300 ALA D N   
11153 C CA  . ALA D 300 ? 0.4217 0.7715 0.8595 -0.0375 0.1830  0.2490  300 ALA D CA  
11154 C C   . ALA D 300 ? 0.4347 0.7825 0.8996 -0.0458 0.1741  0.2608  300 ALA D C   
11155 O O   . ALA D 300 ? 0.4384 0.7983 0.9058 -0.0567 0.1730  0.2758  300 ALA D O   
11156 C CB  . ALA D 300 ? 0.4550 0.8342 0.8886 -0.0323 0.1977  0.2345  300 ALA D CB  
11157 N N   . ASN D 301 ? 0.4533 0.7872 0.9384 -0.0411 0.1674  0.2538  301 ASN D N   
11158 C CA  . ASN D 301 ? 0.4928 0.8216 1.0036 -0.0492 0.1573  0.2630  301 ASN D CA  
11159 C C   . ASN D 301 ? 0.5373 0.8403 1.0516 -0.0570 0.1447  0.2750  301 ASN D C   
11160 O O   . ASN D 301 ? 0.5817 0.8798 1.1155 -0.0656 0.1361  0.2842  301 ASN D O   
11161 C CB  . ASN D 301 ? 0.5062 0.8283 1.0360 -0.0431 0.1524  0.2514  301 ASN D CB  
11162 C CG  . ASN D 301 ? 0.5621 0.9103 1.0983 -0.0365 0.1624  0.2417  301 ASN D CG  
11163 O OD1 . ASN D 301 ? 0.5803 0.9541 1.1105 -0.0387 0.1733  0.2437  301 ASN D OD1 
11164 N ND2 . ASN D 301 ? 0.5764 0.9194 1.1260 -0.0287 0.1584  0.2307  301 ASN D ND2 
11165 N N   . ASN D 302 ? 0.5277 0.8127 1.0250 -0.0533 0.1432  0.2734  302 ASN D N   
11166 C CA  . ASN D 302 ? 0.5097 0.7694 1.0112 -0.0594 0.1316  0.2835  302 ASN D CA  
11167 C C   . ASN D 302 ? 0.5406 0.8092 1.0263 -0.0651 0.1334  0.2987  302 ASN D C   
11168 O O   . ASN D 302 ? 0.5895 0.8388 1.0723 -0.0669 0.1257  0.3058  302 ASN D O   
11169 C CB  . ASN D 302 ? 0.4604 0.6929 0.9572 -0.0524 0.1270  0.2717  302 ASN D CB  
11170 C CG  . ASN D 302 ? 0.4444 0.6645 0.9605 -0.0513 0.1202  0.2601  302 ASN D CG  
11171 O OD1 . ASN D 302 ? 0.4271 0.6276 0.9601 -0.0577 0.1091  0.2614  302 ASN D OD1 
11172 N ND2 . ASN D 302 ? 0.4325 0.6650 0.9472 -0.0436 0.1263  0.2480  302 ASN D ND2 
11173 N N   . MET D 303 ? 0.5296 0.8292 1.0063 -0.0683 0.1433  0.3034  303 MET D N   
11174 C CA  . MET D 303 ? 0.5045 0.8188 0.9642 -0.0754 0.1455  0.3177  303 MET D CA  
11175 C C   . MET D 303 ? 0.5118 0.8540 0.9796 -0.0854 0.1493  0.3289  303 MET D C   
11176 O O   . MET D 303 ? 0.5132 0.8671 0.9960 -0.0847 0.1533  0.3224  303 MET D O   
11177 C CB  . MET D 303 ? 0.4725 0.7997 0.9019 -0.0688 0.1571  0.3075  303 MET D CB  
11178 C CG  . MET D 303 ? 0.4573 0.7580 0.8755 -0.0605 0.1529  0.2999  303 MET D CG  
11179 S SD  . MET D 303 ? 0.7185 0.9995 1.1326 -0.0668 0.1399  0.3187  303 MET D SD  
11180 C CE  . MET D 303 ? 0.5127 0.8242 0.8932 -0.0715 0.1490  0.3246  303 MET D CE  
11181 N N   . PRO D 304 ? 0.5565 0.9101 1.0158 -0.0952 0.1471  0.3466  304 PRO D N   
11182 C CA  . PRO D 304 ? 0.5869 0.9716 1.0497 -0.1055 0.1526  0.3571  304 PRO D CA  
11183 C C   . PRO D 304 ? 0.5926 1.0094 1.0374 -0.1021 0.1706  0.3417  304 PRO D C   
11184 O O   . PRO D 304 ? 0.5802 1.0064 0.9986 -0.1005 0.1774  0.3371  304 PRO D O   
11185 C CB  . PRO D 304 ? 0.6209 1.0089 1.0745 -0.1157 0.1454  0.3787  304 PRO D CB  
11186 C CG  . PRO D 304 ? 0.6198 0.9888 1.0554 -0.1089 0.1421  0.3748  304 PRO D CG  
11187 C CD  . PRO D 304 ? 0.5838 0.9226 1.0322 -0.0977 0.1384  0.3589  304 PRO D CD  
11188 N N   . LYS D 305 ? 0.5919 1.0249 1.0520 -0.1006 0.1778  0.3326  305 LYS D N   
11189 C CA  . LYS D 305 ? 0.5855 1.0466 1.0341 -0.0952 0.1950  0.3140  305 LYS D CA  
11190 C C   . LYS D 305 ? 0.6149 1.1096 1.0426 -0.1051 0.2059  0.3190  305 LYS D C   
11191 O O   . LYS D 305 ? 0.6544 1.1700 1.0662 -0.1008 0.2206  0.3014  305 LYS D O   
11192 C CB  . LYS D 305 ? 0.5578 1.0300 1.0320 -0.0917 0.1992  0.3044  305 LYS D CB  
11193 C CG  . LYS D 305 ? 0.5169 0.9730 0.9984 -0.0765 0.1997  0.2844  305 LYS D CG  
11194 C CD  . LYS D 305 ? 0.5037 0.9727 0.9634 -0.0675 0.2135  0.2649  305 LYS D CD  
11195 C CE  . LYS D 305 ? 0.4752 0.9278 0.9424 -0.0518 0.2133  0.2457  305 LYS D CE  
11196 N NZ  . LYS D 305 ? 0.4741 0.9479 0.9307 -0.0434 0.2289  0.2241  305 LYS D NZ  
11197 N N   . GLN D 306 ? 0.6018 1.1025 1.0301 -0.1184 0.1988  0.3418  306 GLN D N   
11198 C CA  . GLN D 306 ? 0.6177 1.1524 1.0260 -0.1291 0.2087  0.3473  306 GLN D CA  
11199 C C   . GLN D 306 ? 0.6450 1.1745 1.0260 -0.1323 0.2043  0.3556  306 GLN D C   
11200 O O   . GLN D 306 ? 0.6757 1.2295 1.0415 -0.1440 0.2071  0.3675  306 GLN D O   
11201 C CB  . GLN D 306 ? 0.6216 1.1729 1.0460 -0.1432 0.2045  0.3686  306 GLN D CB  
11202 C CG  . GLN D 306 ? 0.6005 1.1634 1.0517 -0.1422 0.2097  0.3617  306 GLN D CG  
11203 C CD  . GLN D 306 ? 0.5945 1.1929 1.0387 -0.1401 0.2304  0.3410  306 GLN D CD  
11204 O OE1 . GLN D 306 ? 0.5720 1.1678 1.0210 -0.1274 0.2382  0.3181  306 GLN D OE1 
11205 N NE2 . GLN D 306 ? 0.6182 1.2504 1.0527 -0.1524 0.2394  0.3485  306 GLN D NE2 
11206 N N   . ALA D 307 ? 0.6196 1.1198 0.9938 -0.1221 0.1981  0.3485  307 ALA D N   
11207 C CA  . ALA D 307 ? 0.5932 1.0871 0.9418 -0.1236 0.1935  0.3546  307 ALA D CA  
11208 C C   . ALA D 307 ? 0.5732 1.0756 0.8962 -0.1152 0.2072  0.3302  307 ALA D C   
11209 O O   . ALA D 307 ? 0.5291 1.0303 0.8277 -0.1164 0.2056  0.3316  307 ALA D O   
11210 C CB  . ALA D 307 ? 0.5159 0.9705 0.8760 -0.1193 0.1759  0.3655  307 ALA D CB  
11211 N N   . GLN D 308 ? 0.5668 1.0779 0.8975 -0.1066 0.2198  0.3076  308 GLN D N   
11212 C CA  . GLN D 308 ? 0.5636 1.0807 0.8760 -0.0967 0.2329  0.2814  308 GLN D CA  
11213 C C   . GLN D 308 ? 0.5567 1.1077 0.8433 -0.1043 0.2473  0.2729  308 GLN D C   
11214 O O   . GLN D 308 ? 0.5642 1.1426 0.8516 -0.1158 0.2528  0.2812  308 GLN D O   
11215 C CB  . GLN D 308 ? 0.5665 1.0828 0.9005 -0.0845 0.2408  0.2601  308 GLN D CB  
11216 C CG  . GLN D 308 ? 0.5417 1.0260 0.9009 -0.0768 0.2274  0.2655  308 GLN D CG  
11217 C CD  . GLN D 308 ? 0.5276 1.0121 0.9064 -0.0643 0.2339  0.2448  308 GLN D CD  
11218 O OE1 . GLN D 308 ? 0.5439 1.0510 0.9192 -0.0600 0.2484  0.2251  308 GLN D OE1 
11219 N NE2 . GLN D 308 ? 0.5120 0.9709 0.9127 -0.0582 0.2227  0.2481  308 GLN D NE2 
11220 N N   . VAL D 309 ? 0.5708 1.1187 0.8348 -0.0977 0.2535  0.2553  309 VAL D N   
11221 C CA  . VAL D 309 ? 0.5875 1.1630 0.8248 -0.1030 0.2675  0.2422  309 VAL D CA  
11222 C C   . VAL D 309 ? 0.5659 1.1409 0.8034 -0.0890 0.2816  0.2086  309 VAL D C   
11223 O O   . VAL D 309 ? 0.5097 1.0585 0.7589 -0.0760 0.2760  0.2005  309 VAL D O   
11224 C CB  . VAL D 309 ? 0.6944 1.2638 0.9025 -0.1100 0.2577  0.2564  309 VAL D CB  
11225 C CG1 . VAL D 309 ? 0.7269 1.3189 0.9046 -0.1131 0.2707  0.2391  309 VAL D CG1 
11226 C CG2 . VAL D 309 ? 0.6966 1.2702 0.9084 -0.1239 0.2441  0.2890  309 VAL D CG2 
11227 N N   . LYS D 310 ? 0.5745 1.1773 0.8002 -0.0914 0.2991  0.1893  310 LYS D N   
11228 C CA  . LYS D 310 ? 0.6037 1.2051 0.8308 -0.0781 0.3126  0.1565  310 LYS D CA  
11229 C C   . LYS D 310 ? 0.6382 1.2119 0.8484 -0.0698 0.3043  0.1514  310 LYS D C   
11230 O O   . LYS D 310 ? 0.6759 1.2507 0.8565 -0.0765 0.3014  0.1570  310 LYS D O   
11231 C CB  . LYS D 310 ? 0.6291 1.2617 0.8407 -0.0829 0.3317  0.1387  310 LYS D CB  
11232 C CG  . LYS D 310 ? 0.6357 1.2666 0.8546 -0.0681 0.3471  0.1035  310 LYS D CG  
11233 C CD  . LYS D 310 ? 0.6912 1.3538 0.8978 -0.0722 0.3663  0.0874  310 LYS D CD  
11234 C CE  . LYS D 310 ? 0.7062 1.3648 0.9219 -0.0556 0.3810  0.0539  310 LYS D CE  
11235 N NZ  . LYS D 310 ? 0.7055 1.3435 0.8955 -0.0496 0.3762  0.0436  310 LYS D NZ  
11236 N N   . ALA D 311 ? 0.6450 1.1951 0.8740 -0.0554 0.2998  0.1414  311 ALA D N   
11237 C CA  . ALA D 311 ? 0.6775 1.2018 0.8913 -0.0468 0.2928  0.1353  311 ALA D CA  
11238 C C   . ALA D 311 ? 0.7256 1.2611 0.9181 -0.0449 0.3070  0.1098  311 ALA D C   
11239 O O   . ALA D 311 ? 0.7452 1.2969 0.9496 -0.0405 0.3227  0.0876  311 ALA D O   
11240 C CB  . ALA D 311 ? 0.6598 1.1591 0.8986 -0.0313 0.2861  0.1285  311 ALA D CB  
11241 N N   . VAL D 312 ? 0.7438 1.2698 0.9066 -0.0478 0.3014  0.1132  312 VAL D N   
11242 C CA  . VAL D 312 ? 0.7719 1.3063 0.9123 -0.0464 0.3131  0.0905  312 VAL D CA  
11243 C C   . VAL D 312 ? 0.7528 1.2594 0.8777 -0.0396 0.3026  0.0889  312 VAL D C   
11244 O O   . VAL D 312 ? 0.7150 1.2034 0.8394 -0.0407 0.2871  0.1102  312 VAL D O   
11245 C CB  . VAL D 312 ? 0.7848 1.3488 0.8988 -0.0620 0.3188  0.0977  312 VAL D CB  
11246 C CG1 . VAL D 312 ? 0.8256 1.3949 0.9129 -0.0602 0.3271  0.0758  312 VAL D CG1 
11247 C CG2 . VAL D 312 ? 0.7585 1.3514 0.8901 -0.0665 0.3322  0.0944  312 VAL D CG2 
11248 N N   . GLY D 313 ? 0.7874 1.2899 0.9022 -0.0316 0.3112  0.0633  313 GLY D N   
11249 C CA  . GLY D 313 ? 0.7851 1.2626 0.8863 -0.0243 0.3030  0.0578  313 GLY D CA  
11250 C C   . GLY D 313 ? 0.7623 1.2182 0.8925 -0.0082 0.3006  0.0464  313 GLY D C   
11251 O O   . GLY D 313 ? 0.8133 1.2764 0.9702 -0.0011 0.3102  0.0312  313 GLY D O   
11252 N N   . PRO D 314 ? 0.6612 1.0910 0.7880 -0.0018 0.2872  0.0545  314 PRO D N   
11253 C CA  . PRO D 314 ? 0.5866 0.9944 0.7394 0.0145  0.2824  0.0462  314 PRO D CA  
11254 C C   . PRO D 314 ? 0.5507 0.9508 0.7308 0.0167  0.2739  0.0661  314 PRO D C   
11255 O O   . PRO D 314 ? 0.5329 0.9133 0.7362 0.0296  0.2693  0.0612  314 PRO D O   
11256 C CB  . PRO D 314 ? 0.5895 0.9712 0.7240 0.0197  0.2725  0.0485  314 PRO D CB  
11257 C CG  . PRO D 314 ? 0.6108 0.9981 0.7205 0.0056  0.2657  0.0714  314 PRO D CG  
11258 C CD  . PRO D 314 ? 0.6425 1.0613 0.7413 -0.0080 0.2762  0.0699  314 PRO D CD  
11259 N N   . PHE D 315 ? 0.5306 0.9442 0.7085 0.0037  0.2712  0.0882  315 PHE D N   
11260 C CA  . PHE D 315 ? 0.4921 0.8960 0.6946 0.0038  0.2619  0.1087  315 PHE D CA  
11261 C C   . PHE D 315 ? 0.5165 0.9392 0.7458 0.0041  0.2691  0.1036  315 PHE D C   
11262 O O   . PHE D 315 ? 0.5438 0.9938 0.7709 -0.0005 0.2825  0.0893  315 PHE D O   
11263 C CB  . PHE D 315 ? 0.4872 0.8923 0.6785 -0.0100 0.2526  0.1370  315 PHE D CB  
11264 C CG  . PHE D 315 ? 0.5157 0.9020 0.6853 -0.0107 0.2433  0.1457  315 PHE D CG  
11265 C CD1 . PHE D 315 ? 0.4793 0.8340 0.6576 0.0001  0.2343  0.1473  315 PHE D CD1 
11266 C CD2 . PHE D 315 ? 0.5814 0.9813 0.7229 -0.0225 0.2430  0.1526  315 PHE D CD2 
11267 C CE1 . PHE D 315 ? 0.4942 0.8318 0.6545 -0.0002 0.2262  0.1548  315 PHE D CE1 
11268 C CE2 . PHE D 315 ? 0.5855 0.9682 0.7092 -0.0229 0.2332  0.1614  315 PHE D CE2 
11269 C CZ  . PHE D 315 ? 0.5403 0.8922 0.6740 -0.0115 0.2253  0.1621  315 PHE D CZ  
11270 N N   . GLY D 316 ? 0.5068 0.9140 0.7623 0.0088  0.2601  0.1152  316 GLY D N   
11271 C CA  . GLY D 316 ? 0.5030 0.9253 0.7871 0.0096  0.2643  0.1127  316 GLY D CA  
11272 C C   . GLY D 316 ? 0.4849 0.9159 0.7775 -0.0029 0.2589  0.1372  316 GLY D C   
11273 O O   . GLY D 316 ? 0.4984 0.9495 0.8095 -0.0061 0.2644  0.1364  316 GLY D O   
11274 N N   . LEU D 317 ? 0.4649 0.8795 0.7468 -0.0097 0.2474  0.1588  317 LEU D N   
11275 C CA  . LEU D 317 ? 0.4378 0.8566 0.7305 -0.0216 0.2402  0.1827  317 LEU D CA  
11276 C C   . LEU D 317 ? 0.4510 0.8699 0.7197 -0.0334 0.2344  0.2010  317 LEU D C   
11277 O O   . LEU D 317 ? 0.4073 0.8016 0.6685 -0.0311 0.2244  0.2088  317 LEU D O   
11278 C CB  . LEU D 317 ? 0.3827 0.7747 0.7015 -0.0166 0.2276  0.1925  317 LEU D CB  
11279 C CG  . LEU D 317 ? 0.3884 0.7810 0.7226 -0.0283 0.2189  0.2156  317 LEU D CG  
11280 C CD1 . LEU D 317 ? 0.4030 0.8274 0.7473 -0.0353 0.2279  0.2154  317 LEU D CD1 
11281 C CD2 . LEU D 317 ? 0.4354 0.8000 0.7948 -0.0235 0.2067  0.2208  317 LEU D CD2 
11282 N N   . CYS D 318 ? 0.4907 0.9704 0.7522 0.0775  0.2696  0.2069  318 CYS D N   
11283 C CA  . CYS D 318 ? 0.5118 0.9891 0.7475 0.0753  0.2723  0.2263  318 CYS D CA  
11284 C C   . CYS D 318 ? 0.5716 1.0596 0.8293 0.0612  0.2798  0.2557  318 CYS D C   
11285 O O   . CYS D 318 ? 0.6139 1.1246 0.8960 0.0567  0.2878  0.2574  318 CYS D O   
11286 C CB  . CYS D 318 ? 0.5288 1.0290 0.7244 0.0898  0.2798  0.2145  318 CYS D CB  
11287 S SG  . CYS D 318 ? 0.5613 1.0440 0.7310 0.1051  0.2713  0.1788  318 CYS D SG  
11288 N N   . TYR D 319 ? 0.5878 1.0602 0.8389 0.0550  0.2776  0.2789  319 TYR D N   
11289 C CA  . TYR D 319 ? 0.6167 1.0940 0.8913 0.0417  0.2849  0.3087  319 TYR D CA  
11290 C C   . TYR D 319 ? 0.6520 1.1420 0.8982 0.0466  0.2910  0.3327  319 TYR D C   
11291 O O   . TYR D 319 ? 0.6316 1.1205 0.8411 0.0581  0.2862  0.3272  319 TYR D O   
11292 C CB  . TYR D 319 ? 0.5890 1.0296 0.8981 0.0263  0.2757  0.3179  319 TYR D CB  
11293 C CG  . TYR D 319 ? 0.5813 1.0147 0.9258 0.0176  0.2695  0.2995  319 TYR D CG  
11294 C CD1 . TYR D 319 ? 0.5935 1.0419 0.9760 0.0043  0.2753  0.3052  319 TYR D CD1 
11295 C CD2 . TYR D 319 ? 0.5874 1.0006 0.9284 0.0221  0.2571  0.2772  319 TYR D CD2 
11296 C CE1 . TYR D 319 ? 0.5958 1.0430 1.0112 -0.0038 0.2678  0.2879  319 TYR D CE1 
11297 C CE2 . TYR D 319 ? 0.5849 0.9957 0.9580 0.0147  0.2500  0.2616  319 TYR D CE2 
11298 C CZ  . TYR D 319 ? 0.5956 1.0248 1.0054 0.0019  0.2547  0.2666  319 TYR D CZ  
11299 O OH  . TYR D 319 ? 0.5827 1.0152 1.0241 -0.0051 0.2461  0.2505  319 TYR D OH  
11300 N N   . ASP D 320 ? 0.7027 1.2079 0.9665 0.0381  0.3015  0.3590  320 ASP D N   
11301 C CA  . ASP D 320 ? 0.7296 1.2428 0.9744 0.0412  0.3057  0.3883  320 ASP D CA  
11302 C C   . ASP D 320 ? 0.6923 1.1634 0.9566 0.0332  0.2959  0.4049  320 ASP D C   
11303 O O   . ASP D 320 ? 0.6602 1.1059 0.9650 0.0189  0.2933  0.4054  320 ASP D O   
11304 C CB  . ASP D 320 ? 0.7621 1.3074 1.0195 0.0359  0.3215  0.4115  320 ASP D CB  
11305 C CG  . ASP D 320 ? 0.7941 1.3464 1.0379 0.0387  0.3252  0.4460  320 ASP D CG  
11306 O OD1 . ASP D 320 ? 0.8113 1.3936 1.0141 0.0523  0.3277  0.4472  320 ASP D OD1 
11307 O OD2 . ASP D 320 ? 0.8035 1.3321 1.0783 0.0279  0.3251  0.4711  320 ASP D OD2 
11308 N N   . SER D 321 ? 0.6939 1.1585 0.9312 0.0425  0.2902  0.4166  321 SER D N   
11309 C CA  . SER D 321 ? 0.6988 1.1215 0.9535 0.0376  0.2799  0.4269  321 SER D CA  
11310 C C   . SER D 321 ? 0.7669 1.1686 1.0601 0.0261  0.2834  0.4577  321 SER D C   
11311 O O   . SER D 321 ? 0.7923 1.1546 1.1159 0.0165  0.2762  0.4536  321 SER D O   
11312 C CB  . SER D 321 ? 0.6808 1.1050 0.8955 0.0524  0.2715  0.4275  321 SER D CB  
11313 O OG  . SER D 321 ? 0.6554 1.0945 0.8363 0.0624  0.2677  0.3966  321 SER D OG  
11314 N N   . ARG D 322 ? 0.7876 1.2132 1.0816 0.0268  0.2945  0.4873  322 ARG D N   
11315 C CA  . ARG D 322 ? 0.8045 1.2057 1.1389 0.0161  0.2981  0.5158  322 ARG D CA  
11316 C C   . ARG D 322 ? 0.8154 1.2066 1.1955 -0.0029 0.3044  0.5104  322 ARG D C   
11317 O O   . ARG D 322 ? 0.8204 1.1880 1.2409 -0.0153 0.3077  0.5277  322 ARG D O   
11318 C CB  . ARG D 322 ? 0.8396 1.2685 1.1629 0.0235  0.3078  0.5527  322 ARG D CB  
11319 C CG  . ARG D 322 ? 0.8465 1.2537 1.1701 0.0312  0.3006  0.5738  322 ARG D CG  
11320 C CD  . ARG D 322 ? 0.8946 1.3277 1.2182 0.0364  0.3111  0.6148  322 ARG D CD  
11321 N NE  . ARG D 322 ? 0.9176 1.3519 1.2801 0.0214  0.3253  0.6319  322 ARG D NE  
11322 C CZ  . ARG D 322 ? 0.9645 1.4168 1.3387 0.0217  0.3372  0.6700  322 ARG D CZ  
11323 N NH1 . ARG D 322 ? 0.9875 1.4395 1.3990 0.0063  0.3504  0.6833  322 ARG D NH1 
11324 N NH2 . ARG D 322 ? 0.9917 1.4645 1.3412 0.0372  0.3361  0.6955  322 ARG D NH2 
11325 N N   . LYS D 323 ? 0.8348 1.2455 1.2093 -0.0049 0.3057  0.4846  323 LYS D N   
11326 C CA  . LYS D 323 ? 0.8771 1.2855 1.2922 -0.0220 0.3094  0.4729  323 LYS D CA  
11327 C C   . LYS D 323 ? 0.8904 1.2591 1.3308 -0.0316 0.2959  0.4489  323 LYS D C   
11328 O O   . LYS D 323 ? 0.9393 1.2917 1.4237 -0.0492 0.2963  0.4466  323 LYS D O   
11329 C CB  . LYS D 323 ? 0.8570 1.3057 1.2574 -0.0179 0.3156  0.4536  323 LYS D CB  
11330 C CG  . LYS D 323 ? 0.8828 1.3770 1.2640 -0.0113 0.3310  0.4708  323 LYS D CG  
11331 C CD  . LYS D 323 ? 0.8931 1.4008 1.3172 -0.0282 0.3429  0.4802  323 LYS D CD  
11332 C CE  . LYS D 323 ? 0.9194 1.4776 1.3279 -0.0227 0.3593  0.4895  323 LYS D CE  
11333 N NZ  . LYS D 323 ? 0.9413 1.5216 1.2985 -0.0037 0.3612  0.4978  323 LYS D NZ  
11334 N N   . ILE D 324 ? 0.8428 1.1997 1.2551 -0.0207 0.2842  0.4289  324 ILE D N   
11335 C CA  . ILE D 324 ? 0.7928 1.1159 1.2230 -0.0277 0.2710  0.4045  324 ILE D CA  
11336 C C   . ILE D 324 ? 0.8769 1.1567 1.3133 -0.0278 0.2614  0.4089  324 ILE D C   
11337 O O   . ILE D 324 ? 0.8591 1.1123 1.3108 -0.0343 0.2509  0.3871  324 ILE D O   
11338 C CB  . ILE D 324 ? 0.6632 0.9991 1.0633 -0.0165 0.2641  0.3759  324 ILE D CB  
11339 C CG1 . ILE D 324 ? 0.6425 0.9704 1.0006 0.0000  0.2581  0.3766  324 ILE D CG1 
11340 C CG2 . ILE D 324 ? 0.6552 1.0352 1.0447 -0.0117 0.2738  0.3694  324 ILE D CG2 
11341 C CD1 . ILE D 324 ? 0.6025 0.9378 0.9328 0.0108  0.2514  0.3478  324 ILE D CD1 
11342 N N   . SER D 325 ? 0.9692 1.2435 1.3950 -0.0199 0.2644  0.4355  325 SER D N   
11343 C CA  . SER D 325 ? 0.9887 1.2219 1.4259 -0.0195 0.2556  0.4382  325 SER D CA  
11344 C C   . SER D 325 ? 1.0426 1.2443 1.5337 -0.0378 0.2569  0.4406  325 SER D C   
11345 O O   . SER D 325 ? 1.0770 1.2478 1.5859 -0.0378 0.2546  0.4513  325 SER D O   
11346 C CB  . SER D 325 ? 0.9765 1.2161 1.3881 -0.0039 0.2571  0.4654  325 SER D CB  
11347 O OG  . SER D 325 ? 0.9677 1.1713 1.4067 -0.0062 0.2540  0.4778  325 SER D OG  
11348 N N   . GLY D 326 ? 1.0464 1.2583 1.5639 -0.0530 0.2607  0.4287  326 GLY D N   
11349 C CA  . GLY D 326 ? 1.0399 1.2256 1.6077 -0.0729 0.2597  0.4196  326 GLY D CA  
11350 C C   . GLY D 326 ? 0.9788 1.1437 1.5537 -0.0790 0.2455  0.3834  326 GLY D C   
11351 O O   . GLY D 326 ? 0.9889 1.1394 1.6026 -0.0967 0.2425  0.3669  326 GLY D O   
11352 N N   . GLY D 327 ? 0.8956 1.0623 1.4335 -0.0652 0.2370  0.3699  327 GLY D N   
11353 C CA  . GLY D 327 ? 0.7995 0.9467 1.3418 -0.0696 0.2237  0.3379  327 GLY D CA  
11354 C C   . GLY D 327 ? 0.7180 0.8917 1.2440 -0.0677 0.2185  0.3144  327 GLY D C   
11355 O O   . GLY D 327 ? 0.7065 0.9064 1.2489 -0.0763 0.2221  0.3090  327 GLY D O   
11356 N N   . ALA D 328 ? 0.6819 0.8507 1.1774 -0.0557 0.2106  0.3015  328 ALA D N   
11357 C CA  . ALA D 328 ? 0.6547 0.8446 1.1366 -0.0519 0.2047  0.2781  328 ALA D CA  
11358 C C   . ALA D 328 ? 0.6536 0.8256 1.1581 -0.0631 0.1917  0.2499  328 ALA D C   
11359 O O   . ALA D 328 ? 0.6765 0.8146 1.1938 -0.0689 0.1862  0.2451  328 ALA D O   
11360 C CB  . ALA D 328 ? 0.6236 0.8219 1.0591 -0.0322 0.2046  0.2795  328 ALA D CB  
11361 N N   . PRO D 329 ? 0.6280 0.8254 1.1375 -0.0650 0.1865  0.2304  329 PRO D N   
11362 C CA  . PRO D 329 ? 0.6100 0.7992 1.1437 -0.0771 0.1735  0.2036  329 PRO D CA  
11363 C C   . PRO D 329 ? 0.5884 0.7581 1.1032 -0.0700 0.1635  0.1880  329 PRO D C   
11364 O O   . PRO D 329 ? 0.5488 0.7146 1.0297 -0.0542 0.1662  0.1959  329 PRO D O   
11365 C CB  . PRO D 329 ? 0.5811 0.8121 1.1245 -0.0780 0.1713  0.1924  329 PRO D CB  
11366 C CG  . PRO D 329 ? 0.5647 0.8184 1.0767 -0.0599 0.1811  0.2066  329 PRO D CG  
11367 C CD  . PRO D 329 ? 0.6027 0.8404 1.0989 -0.0557 0.1922  0.2318  329 PRO D CD  
11368 N N   . SER D 330 ? 0.6302 0.7892 1.1679 -0.0827 0.1519  0.1644  330 SER D N   
11369 C CA  . SER D 330 ? 0.6798 0.8243 1.1934 -0.0759 0.1377  0.1416  330 SER D CA  
11370 C C   . SER D 330 ? 0.6358 0.8054 1.1151 -0.0596 0.1310  0.1334  330 SER D C   
11371 O O   . SER D 330 ? 0.6673 0.8697 1.1618 -0.0622 0.1288  0.1278  330 SER D O   
11372 C CB  . SER D 330 ? 0.7397 0.8774 1.2834 -0.0934 0.1259  0.1146  330 SER D CB  
11373 O OG  . SER D 330 ? 0.7517 0.9239 1.2979 -0.0951 0.1149  0.0963  330 SER D OG  
11374 N N   . VAL D 331 ? 0.5559 0.7110 0.9920 -0.0425 0.1284  0.1334  331 VAL D N   
11375 C CA  . VAL D 331 ? 0.4744 0.6459 0.8823 -0.0280 0.1212  0.1225  331 VAL D CA  
11376 C C   . VAL D 331 ? 0.4342 0.5832 0.8160 -0.0230 0.1073  0.1037  331 VAL D C   
11377 O O   . VAL D 331 ? 0.4519 0.5763 0.8080 -0.0154 0.1075  0.1056  331 VAL D O   
11378 C CB  . VAL D 331 ? 0.4087 0.5904 0.7900 -0.0117 0.1321  0.1373  331 VAL D CB  
11379 C CG1 . VAL D 331 ? 0.3737 0.5644 0.7286 0.0038  0.1256  0.1250  331 VAL D CG1 
11380 C CG2 . VAL D 331 ? 0.3727 0.5835 0.7806 -0.0168 0.1468  0.1556  331 VAL D CG2 
11381 N N   . ASP D 332 ? 0.3578 0.5194 0.7462 -0.0270 0.0952  0.0862  332 ASP D N   
11382 C CA  . ASP D 332 ? 0.3279 0.4714 0.6951 -0.0249 0.0831  0.0691  332 ASP D CA  
11383 C C   . ASP D 332 ? 0.3129 0.4732 0.6602 -0.0135 0.0742  0.0617  332 ASP D C   
11384 O O   . ASP D 332 ? 0.3023 0.4936 0.6657 -0.0138 0.0714  0.0616  332 ASP D O   
11385 C CB  . ASP D 332 ? 0.4004 0.5395 0.7944 -0.0427 0.0760  0.0528  332 ASP D CB  
11386 C CG  . ASP D 332 ? 0.4820 0.6004 0.9031 -0.0543 0.0859  0.0615  332 ASP D CG  
11387 O OD1 . ASP D 332 ? 0.4921 0.5925 0.9002 -0.0463 0.0955  0.0792  332 ASP D OD1 
11388 O OD2 . ASP D 332 ? 0.5171 0.6387 0.9744 -0.0717 0.0844  0.0512  332 ASP D OD2 
11389 N N   . LEU D 333 ? 0.3020 0.4426 0.6171 -0.0036 0.0698  0.0567  333 LEU D N   
11390 C CA  . LEU D 333 ? 0.2671 0.4182 0.5643 0.0063  0.0611  0.0510  333 LEU D CA  
11391 C C   . LEU D 333 ? 0.2594 0.4175 0.5594 -0.0027 0.0484  0.0352  333 LEU D C   
11392 O O   . LEU D 333 ? 0.2705 0.4077 0.5623 -0.0082 0.0460  0.0256  333 LEU D O   
11393 C CB  . LEU D 333 ? 0.2463 0.3739 0.5105 0.0194  0.0633  0.0530  333 LEU D CB  
11394 C CG  . LEU D 333 ? 0.2418 0.3644 0.4999 0.0276  0.0756  0.0648  333 LEU D CG  
11395 C CD1 . LEU D 333 ? 0.2529 0.3549 0.4810 0.0386  0.0764  0.0628  333 LEU D CD1 
11396 C CD2 . LEU D 333 ? 0.2411 0.3913 0.5131 0.0342  0.0800  0.0716  333 LEU D CD2 
11397 N N   . ILE D 334 ? 0.2635 0.4545 0.5758 -0.0036 0.0402  0.0322  334 ILE D N   
11398 C CA  . ILE D 334 ? 0.2746 0.4802 0.5850 -0.0108 0.0271  0.0167  334 ILE D CA  
11399 C C   . ILE D 334 ? 0.3033 0.5067 0.5829 0.0035  0.0223  0.0210  334 ILE D C   
11400 O O   . ILE D 334 ? 0.2959 0.5136 0.5725 0.0166  0.0223  0.0332  334 ILE D O   
11401 C CB  . ILE D 334 ? 0.2763 0.5243 0.6153 -0.0199 0.0189  0.0108  334 ILE D CB  
11402 C CG1 . ILE D 334 ? 0.3036 0.5542 0.6783 -0.0333 0.0269  0.0118  334 ILE D CG1 
11403 C CG2 . ILE D 334 ? 0.2896 0.5532 0.6260 -0.0305 0.0056  -0.0099 334 ILE D CG2 
11404 C CD1 . ILE D 334 ? 0.3228 0.5428 0.7069 -0.0475 0.0312  0.0010  334 ILE D CD1 
11405 N N   . LEU D 335 ? 0.3401 0.5254 0.5997 0.0009  0.0191  0.0109  335 LEU D N   
11406 C CA  . LEU D 335 ? 0.3704 0.5443 0.6005 0.0129  0.0180  0.0167  335 LEU D CA  
11407 C C   . LEU D 335 ? 0.4333 0.6360 0.6539 0.0135  0.0063  0.0130  335 LEU D C   
11408 O O   . LEU D 335 ? 0.4656 0.7002 0.7012 0.0045  -0.0024 0.0033  335 LEU D O   
11409 C CB  . LEU D 335 ? 0.3579 0.4965 0.5718 0.0111  0.0234  0.0107  335 LEU D CB  
11410 C CG  . LEU D 335 ? 0.3254 0.4409 0.5468 0.0120  0.0342  0.0175  335 LEU D CG  
11411 C CD1 . LEU D 335 ? 0.3394 0.4256 0.5469 0.0110  0.0378  0.0124  335 LEU D CD1 
11412 C CD2 . LEU D 335 ? 0.2866 0.4014 0.5018 0.0256  0.0404  0.0323  335 LEU D CD2 
11413 N N   . ASP D 336 ? 0.4955 0.6883 0.6916 0.0239  0.0065  0.0215  336 ASP D N   
11414 C CA  . ASP D 336 ? 0.6325 0.8518 0.8150 0.0288  -0.0025 0.0264  336 ASP D CA  
11415 C C   . ASP D 336 ? 0.7301 0.9812 0.9155 0.0155  -0.0133 0.0076  336 ASP D C   
11416 O O   . ASP D 336 ? 0.7727 1.0096 0.9553 0.0046  -0.0118 -0.0108 336 ASP D O   
11417 C CB  . ASP D 336 ? 0.6998 0.8927 0.8560 0.0356  0.0024  0.0330  336 ASP D CB  
11418 C CG  . ASP D 336 ? 0.7733 0.9895 0.9141 0.0435  -0.0040 0.0462  336 ASP D CG  
11419 O OD1 . ASP D 336 ? 0.8066 1.0461 0.9562 0.0534  -0.0082 0.0618  336 ASP D OD1 
11420 O OD2 . ASP D 336 ? 0.8019 1.0140 0.9225 0.0409  -0.0039 0.0430  336 ASP D OD2 
11421 N N   . LYS D 337 ? 0.7780 1.0738 0.9714 0.0166  -0.0241 0.0107  337 LYS D N   
11422 C CA  . LYS D 337 ? 0.8018 1.1376 0.9957 0.0043  -0.0363 -0.0091 337 LYS D CA  
11423 C C   . LYS D 337 ? 0.8076 1.1391 1.0270 -0.0142 -0.0358 -0.0349 337 LYS D C   
11424 O O   . LYS D 337 ? 0.8378 1.1855 1.0567 -0.0270 -0.0420 -0.0594 337 LYS D O   
11425 C CB  . LYS D 337 ? 0.7986 1.1359 0.9609 0.0046  -0.0383 -0.0143 337 LYS D CB  
11426 C CG  . LYS D 337 ? 0.7909 1.1839 0.9396 0.0068  -0.0520 -0.0120 337 LYS D CG  
11427 C CD  . LYS D 337 ? 0.7722 1.1730 0.9075 0.0261  -0.0522 0.0224  337 LYS D CD  
11428 C CE  . LYS D 337 ? 0.7702 1.2348 0.9032 0.0306  -0.0675 0.0309  337 LYS D CE  
11429 N NZ  . LYS D 337 ? 0.7529 1.2482 0.9178 0.0284  -0.0754 0.0280  337 LYS D NZ  
11430 N N   . ASN D 338 ? 0.7827 1.0929 1.0253 -0.0152 -0.0274 -0.0288 338 ASN D N   
11431 C CA  . ASN D 338 ? 0.7777 1.0703 1.0474 -0.0307 -0.0220 -0.0451 338 ASN D CA  
11432 C C   . ASN D 338 ? 0.8000 1.0748 1.0664 -0.0432 -0.0215 -0.0705 338 ASN D C   
11433 O O   . ASN D 338 ? 0.8338 1.1150 1.1270 -0.0594 -0.0234 -0.0917 338 ASN D O   
11434 C CB  . ASN D 338 ? 0.7878 1.1207 1.0913 -0.0417 -0.0295 -0.0529 338 ASN D CB  
11435 C CG  . ASN D 338 ? 0.7972 1.1567 1.1081 -0.0287 -0.0312 -0.0299 338 ASN D CG  
11436 O OD1 . ASN D 338 ? 0.8335 1.1690 1.1380 -0.0150 -0.0213 -0.0094 338 ASN D OD1 
11437 N ND2 . ASN D 338 ? 0.7685 1.1803 1.0947 -0.0327 -0.0440 -0.0348 338 ASN D ND2 
11438 N N   . ASP D 339 ? 0.7795 1.0307 1.0169 -0.0357 -0.0177 -0.0689 339 ASP D N   
11439 C CA  . ASP D 339 ? 0.7684 1.0002 1.0022 -0.0442 -0.0151 -0.0915 339 ASP D CA  
11440 C C   . ASP D 339 ? 0.7073 0.8934 0.9574 -0.0460 -0.0030 -0.0887 339 ASP D C   
11441 O O   . ASP D 339 ? 0.7567 0.9241 1.0185 -0.0547 0.0003  -0.1077 339 ASP D O   
11442 C CB  . ASP D 339 ? 0.8032 1.0336 1.0009 -0.0353 -0.0153 -0.0895 339 ASP D CB  
11443 C CG  . ASP D 339 ? 0.8572 1.1364 1.0368 -0.0344 -0.0272 -0.0932 339 ASP D CG  
11444 O OD1 . ASP D 339 ? 0.8691 1.1785 1.0572 -0.0466 -0.0352 -0.1188 339 ASP D OD1 
11445 O OD2 . ASP D 339 ? 0.8869 1.1750 1.0441 -0.0216 -0.0283 -0.0708 339 ASP D OD2 
11446 N N   . ALA D 340 ? 0.5703 0.7401 0.8209 -0.0367 0.0038  -0.0646 340 ALA D N   
11447 C CA  . ALA D 340 ? 0.4841 0.6148 0.7415 -0.0347 0.0151  -0.0562 340 ALA D CA  
11448 C C   . ALA D 340 ? 0.4223 0.5522 0.6969 -0.0326 0.0210  -0.0375 340 ALA D C   
11449 O O   . ALA D 340 ? 0.4183 0.5751 0.6963 -0.0295 0.0171  -0.0293 340 ALA D O   
11450 C CB  . ALA D 340 ? 0.4888 0.5971 0.7163 -0.0224 0.0194  -0.0468 340 ALA D CB  
11451 N N   . VAL D 341 ? 0.3989 0.5006 0.6854 -0.0335 0.0307  -0.0301 341 VAL D N   
11452 C CA  . VAL D 341 ? 0.3565 0.4583 0.6596 -0.0323 0.0386  -0.0120 341 VAL D CA  
11453 C C   . VAL D 341 ? 0.3406 0.4133 0.6283 -0.0223 0.0479  0.0028  341 VAL D C   
11454 O O   . VAL D 341 ? 0.3669 0.4162 0.6534 -0.0236 0.0499  -0.0026 341 VAL D O   
11455 C CB  . VAL D 341 ? 0.3109 0.4153 0.6547 -0.0487 0.0414  -0.0178 341 VAL D CB  
11456 C CG1 . VAL D 341 ? 0.2989 0.4010 0.6580 -0.0470 0.0525  0.0046  341 VAL D CG1 
11457 C CG2 . VAL D 341 ? 0.3138 0.4543 0.6749 -0.0593 0.0313  -0.0332 341 VAL D CG2 
11458 N N   . TRP D 342 ? 0.3265 0.4029 0.6031 -0.0117 0.0533  0.0200  342 TRP D N   
11459 C CA  . TRP D 342 ? 0.3186 0.3742 0.5833 -0.0036 0.0621  0.0335  342 TRP D CA  
11460 C C   . TRP D 342 ? 0.3698 0.4302 0.6563 -0.0070 0.0717  0.0490  342 TRP D C   
11461 O O   . TRP D 342 ? 0.3592 0.4377 0.6451 -0.0016 0.0761  0.0593  342 TRP D O   
11462 C CB  . TRP D 342 ? 0.3089 0.3647 0.5439 0.0107  0.0628  0.0393  342 TRP D CB  
11463 C CG  . TRP D 342 ? 0.3429 0.3791 0.5605 0.0180  0.0682  0.0460  342 TRP D CG  
11464 C CD1 . TRP D 342 ? 0.3877 0.4116 0.6142 0.0158  0.0737  0.0542  342 TRP D CD1 
11465 C CD2 . TRP D 342 ? 0.3549 0.3838 0.5456 0.0283  0.0679  0.0450  342 TRP D CD2 
11466 N NE1 . TRP D 342 ? 0.3859 0.4000 0.5908 0.0248  0.0757  0.0585  342 TRP D NE1 
11467 C CE2 . TRP D 342 ? 0.3785 0.3951 0.5619 0.0315  0.0721  0.0511  342 TRP D CE2 
11468 C CE3 . TRP D 342 ? 0.3351 0.3671 0.5099 0.0349  0.0646  0.0404  342 TRP D CE3 
11469 C CZ2 . TRP D 342 ? 0.3626 0.3729 0.5230 0.0397  0.0723  0.0494  342 TRP D CZ2 
11470 C CZ3 . TRP D 342 ? 0.3505 0.3711 0.5047 0.0423  0.0663  0.0392  342 TRP D CZ3 
11471 C CH2 . TRP D 342 ? 0.3482 0.3595 0.4953 0.0440  0.0696  0.0420  342 TRP D CH2 
11472 N N   . ARG D 343 ? 0.4072 0.4518 0.7148 -0.0155 0.0760  0.0516  343 ARG D N   
11473 C CA  . ARG D 343 ? 0.4369 0.4852 0.7682 -0.0202 0.0865  0.0696  343 ARG D CA  
11474 C C   . ARG D 343 ? 0.4139 0.4592 0.7245 -0.0077 0.0952  0.0899  343 ARG D C   
11475 O O   . ARG D 343 ? 0.4172 0.4463 0.7072 0.0002  0.0942  0.0909  343 ARG D O   
11476 C CB  . ARG D 343 ? 0.5319 0.5620 0.8972 -0.0337 0.0889  0.0668  343 ARG D CB  
11477 C CG  . ARG D 343 ? 0.6409 0.6841 1.0311 -0.0483 0.0812  0.0452  343 ARG D CG  
11478 C CD  . ARG D 343 ? 0.7629 0.7914 1.1965 -0.0647 0.0855  0.0408  343 ARG D CD  
11479 N NE  . ARG D 343 ? 0.8463 0.8422 1.2808 -0.0633 0.0858  0.0337  343 ARG D NE  
11480 C CZ  . ARG D 343 ? 0.8793 0.8691 1.3119 -0.0672 0.0771  0.0062  343 ARG D CZ  
11481 N NH1 . ARG D 343 ? 0.8830 0.8991 1.3104 -0.0731 0.0668  -0.0150 343 ARG D NH1 
11482 N NH2 . ARG D 343 ? 0.8858 0.8464 1.3219 -0.0643 0.0790  0.0004  343 ARG D NH2 
11483 N N   . ILE D 344 ? 0.4421 0.5079 0.7584 -0.0060 0.1038  0.1048  344 ILE D N   
11484 C CA  . ILE D 344 ? 0.4532 0.5245 0.7490 0.0054  0.1128  0.1227  344 ILE D CA  
11485 C C   . ILE D 344 ? 0.5200 0.5932 0.8384 -0.0002 0.1248  0.1464  344 ILE D C   
11486 O O   . ILE D 344 ? 0.5505 0.6381 0.8984 -0.0102 0.1310  0.1534  344 ILE D O   
11487 C CB  . ILE D 344 ? 0.3989 0.4957 0.6797 0.0147  0.1154  0.1215  344 ILE D CB  
11488 C CG1 . ILE D 344 ? 0.4007 0.4936 0.6634 0.0203  0.1044  0.1017  344 ILE D CG1 
11489 C CG2 . ILE D 344 ? 0.3900 0.4952 0.6461 0.0267  0.1242  0.1341  344 ILE D CG2 
11490 C CD1 . ILE D 344 ? 0.4105 0.5244 0.6645 0.0302  0.1068  0.0996  344 ILE D CD1 
11491 N N   . SER D 345 ? 0.5723 0.6323 0.8784 0.0062  0.1282  0.1604  345 SER D N   
11492 C CA  . SER D 345 ? 0.6501 0.7103 0.9759 0.0028  0.1400  0.1881  345 SER D CA  
11493 C C   . SER D 345 ? 0.6115 0.7047 0.9273 0.0082  0.1517  0.2055  345 SER D C   
11494 O O   . SER D 345 ? 0.5854 0.6955 0.8690 0.0198  0.1506  0.1978  345 SER D O   
11495 C CB  . SER D 345 ? 0.7351 0.7759 1.0489 0.0108  0.1390  0.1998  345 SER D CB  
11496 O OG  . SER D 345 ? 0.8053 0.8560 1.1233 0.0143  0.1511  0.2327  345 SER D OG  
11497 N N   . SER D 346 ? 0.5993 0.7021 0.9449 -0.0007 0.1639  0.2279  346 SER D N   
11498 C CA  . SER D 346 ? 0.6104 0.7482 0.9487 0.0039  0.1773  0.2461  346 SER D CA  
11499 C C   . SER D 346 ? 0.5951 0.7430 0.8990 0.0182  0.1824  0.2648  346 SER D C   
11500 O O   . SER D 346 ? 0.5790 0.7596 0.8651 0.0257  0.1923  0.2748  346 SER D O   
11501 C CB  . SER D 346 ? 0.6765 0.8214 1.0544 -0.0098 0.1871  0.2636  346 SER D CB  
11502 O OG  . SER D 346 ? 0.7276 0.8540 1.1133 -0.0104 0.1896  0.2851  346 SER D OG  
11503 N N   . GLU D 347 ? 0.6037 0.7277 0.8970 0.0231  0.1753  0.2674  347 GLU D N   
11504 C CA  . GLU D 347 ? 0.6424 0.7811 0.9019 0.0372  0.1777  0.2838  347 GLU D CA  
11505 C C   . GLU D 347 ? 0.6341 0.7811 0.8539 0.0482  0.1680  0.2555  347 GLU D C   
11506 O O   . GLU D 347 ? 0.6607 0.8301 0.8469 0.0600  0.1694  0.2592  347 GLU D O   
11507 C CB  . GLU D 347 ? 0.6916 0.8038 0.9604 0.0390  0.1739  0.3001  347 GLU D CB  
11508 C CG  . GLU D 347 ? 0.7865 0.8784 1.1000 0.0277  0.1784  0.3165  347 GLU D CG  
11509 C CD  . GLU D 347 ? 0.8790 0.9518 1.2005 0.0343  0.1750  0.3339  347 GLU D CD  
11510 O OE1 . GLU D 347 ? 0.9164 0.9912 1.2108 0.0465  0.1693  0.3359  347 GLU D OE1 
11511 O OE2 . GLU D 347 ? 0.8907 0.9478 1.2475 0.0274  0.1781  0.3447  347 GLU D OE2 
11512 N N   . ASN D 348 ? 0.6034 0.7344 0.8288 0.0437  0.1585  0.2270  348 ASN D N   
11513 C CA  . ASN D 348 ? 0.6312 0.7665 0.8262 0.0523  0.1507  0.2006  348 ASN D CA  
11514 C C   . ASN D 348 ? 0.6610 0.8227 0.8525 0.0552  0.1577  0.1918  348 ASN D C   
11515 O O   . ASN D 348 ? 0.7247 0.9039 0.8873 0.0661  0.1596  0.1825  348 ASN D O   
11516 C CB  . ASN D 348 ? 0.6561 0.7606 0.8570 0.0478  0.1369  0.1776  348 ASN D CB  
11517 C CG  . ASN D 348 ? 0.6529 0.7564 0.8248 0.0561  0.1289  0.1530  348 ASN D CG  
11518 O OD1 . ASN D 348 ? 0.6363 0.7545 0.8002 0.0603  0.1316  0.1425  348 ASN D OD1 
11519 N ND2 . ASN D 348 ? 0.6480 0.7337 0.8071 0.0586  0.1197  0.1444  348 ASN D ND2 
11520 N N   . PHE D 349 ? 0.5711 0.7379 0.7933 0.0460  0.1619  0.1936  349 PHE D N   
11521 C CA  . PHE D 349 ? 0.4879 0.6793 0.7103 0.0504  0.1671  0.1829  349 PHE D CA  
11522 C C   . PHE D 349 ? 0.4711 0.6991 0.6946 0.0536  0.1840  0.2013  349 PHE D C   
11523 O O   . PHE D 349 ? 0.4693 0.7206 0.6928 0.0595  0.1901  0.1922  349 PHE D O   
11524 C CB  . PHE D 349 ? 0.3960 0.5827 0.6498 0.0408  0.1615  0.1722  349 PHE D CB  
11525 C CG  . PHE D 349 ? 0.3732 0.5635 0.6668 0.0253  0.1670  0.1884  349 PHE D CG  
11526 C CD1 . PHE D 349 ? 0.3944 0.6153 0.7056 0.0226  0.1819  0.2062  349 PHE D CD1 
11527 C CD2 . PHE D 349 ? 0.3836 0.5482 0.7000 0.0126  0.1576  0.1827  349 PHE D CD2 
11528 C CE1 . PHE D 349 ? 0.4365 0.6599 0.7892 0.0062  0.1874  0.2203  349 PHE D CE1 
11529 C CE2 . PHE D 349 ? 0.4056 0.5717 0.7635 -0.0036 0.1625  0.1936  349 PHE D CE2 
11530 C CZ  . PHE D 349 ? 0.4415 0.6361 0.8188 -0.0075 0.1774  0.2130  349 PHE D CZ  
11531 N N   . MET D 350 ? 0.4885 0.7226 0.7152 0.0503  0.1924  0.2282  350 MET D N   
11532 C CA  . MET D 350 ? 0.5008 0.7725 0.7205 0.0547  0.2089  0.2486  350 MET D CA  
11533 C C   . MET D 350 ? 0.5446 0.8320 0.7205 0.0687  0.2100  0.2488  350 MET D C   
11534 O O   . MET D 350 ? 0.5544 0.8259 0.7162 0.0707  0.2028  0.2553  350 MET D O   
11535 C CB  . MET D 350 ? 0.4987 0.7648 0.7425 0.0434  0.2124  0.2757  350 MET D CB  
11536 C CG  . MET D 350 ? 0.5206 0.7785 0.8077 0.0282  0.2122  0.2740  350 MET D CG  
11537 S SD  . MET D 350 ? 0.6633 0.9548 0.9549 0.0314  0.2174  0.2567  350 MET D SD  
11538 C CE  . MET D 350 ? 0.4678 0.7945 0.7315 0.0408  0.2302  0.2730  350 MET D CE  
11539 N N   . VAL D 351 ? 0.5910 0.9083 0.7450 0.0781  0.2160  0.2374  351 VAL D N   
11540 C CA  . VAL D 351 ? 0.6379 0.9753 0.7498 0.0906  0.2163  0.2308  351 VAL D CA  
11541 C C   . VAL D 351 ? 0.6597 1.0290 0.7586 0.0925  0.2243  0.2502  351 VAL D C   
11542 O O   . VAL D 351 ? 0.6697 1.0542 0.7845 0.0886  0.2326  0.2557  351 VAL D O   
11543 C CB  . VAL D 351 ? 0.6655 1.0107 0.7604 0.1010  0.2162  0.1959  351 VAL D CB  
11544 C CG1 . VAL D 351 ? 0.6970 1.0615 0.7498 0.1121  0.2148  0.1825  351 VAL D CG1 
11545 C CG2 . VAL D 351 ? 0.6670 0.9731 0.7759 0.0980  0.2030  0.1751  351 VAL D CG2 
11546 N N   . GLN D 352 ? 0.6884 1.0713 0.7574 0.0992  0.2215  0.2595  352 GLN D N   
11547 C CA  . GLN D 352 ? 0.7625 1.1786 0.8165 0.1024  0.2277  0.2798  352 GLN D CA  
11548 C C   . GLN D 352 ? 0.7952 1.2461 0.8140 0.1129  0.2311  0.2546  352 GLN D C   
11549 O O   . GLN D 352 ? 0.8239 1.2804 0.8133 0.1206  0.2240  0.2356  352 GLN D O   
11550 C CB  . GLN D 352 ? 0.8143 1.2272 0.8585 0.1048  0.2207  0.3049  352 GLN D CB  
11551 C CG  . GLN D 352 ? 0.8814 1.3292 0.9094 0.1099  0.2244  0.3305  352 GLN D CG  
11552 C CD  . GLN D 352 ? 0.9189 1.3589 0.9426 0.1140  0.2149  0.3530  352 GLN D CD  
11553 O OE1 . GLN D 352 ? 0.9078 1.3236 0.9290 0.1151  0.2051  0.3420  352 GLN D OE1 
11554 N NE2 . GLN D 352 ? 0.9547 1.4163 0.9787 0.1169  0.2180  0.3846  352 GLN D NE2 
11555 N N   . ALA D 353 ? 0.8055 1.2796 0.8289 0.1128  0.2420  0.2518  353 ALA D N   
11556 C CA  . ALA D 353 ? 0.7994 1.3070 0.7916 0.1225  0.2466  0.2270  353 ALA D CA  
11557 C C   . ALA D 353 ? 0.8464 1.3898 0.8112 0.1271  0.2478  0.2468  353 ALA D C   
11558 O O   . ALA D 353 ? 0.8950 1.4430 0.8370 0.1316  0.2382  0.2499  353 ALA D O   
11559 C CB  . ALA D 353 ? 0.7657 1.2855 0.7750 0.1217  0.2584  0.2152  353 ALA D CB  
11560 N N   . GLN D 354 ? 0.8232 1.3942 0.7927 0.1259  0.2596  0.2619  354 GLN D N   
11561 C CA  . GLN D 354 ? 0.8362 1.4464 0.7818 0.1308  0.2624  0.2823  354 GLN D CA  
11562 C C   . GLN D 354 ? 0.8162 1.4295 0.7909 0.1229  0.2727  0.3174  354 GLN D C   
11563 O O   . GLN D 354 ? 0.8303 1.4198 0.8393 0.1142  0.2771  0.3177  354 GLN D O   
11564 C CB  . GLN D 354 ? 0.8875 1.5385 0.8024 0.1392  0.2690  0.2555  354 GLN D CB  
11565 C CG  . GLN D 354 ? 0.9257 1.5863 0.8054 0.1474  0.2588  0.2237  354 GLN D CG  
11566 C CD  . GLN D 354 ? 0.9745 1.6699 0.8320 0.1540  0.2673  0.1927  354 GLN D CD  
11567 O OE1 . GLN D 354 ? 0.9881 1.7249 0.8318 0.1569  0.2756  0.2065  354 GLN D OE1 
11568 N NE2 . GLN D 354 ? 0.9945 1.6721 0.8521 0.1564  0.2667  0.1510  354 GLN D NE2 
11569 N N   . ASP D 355 ? 0.8063 1.4490 0.7700 0.1256  0.2759  0.3474  355 ASP D N   
11570 C CA  . ASP D 355 ? 0.8686 1.5243 0.8563 0.1190  0.2892  0.3769  355 ASP D CA  
11571 C C   . ASP D 355 ? 0.8338 1.4478 0.8688 0.1058  0.2898  0.3963  355 ASP D C   
11572 O O   . ASP D 355 ? 0.8269 1.4438 0.8889 0.0975  0.3010  0.4033  355 ASP D O   
11573 C CB  . ASP D 355 ? 0.9205 1.6034 0.9046 0.1200  0.3025  0.3547  355 ASP D CB  
11574 C CG  . ASP D 355 ? 0.9947 1.7227 0.9349 0.1319  0.3046  0.3351  355 ASP D CG  
11575 O OD1 . ASP D 355 ? 1.0184 1.7479 0.9300 0.1391  0.2925  0.3193  355 ASP D OD1 
11576 O OD2 . ASP D 355 ? 1.0261 1.7889 0.9617 0.1335  0.3184  0.3329  355 ASP D OD2 
11577 N N   . GLY D 356 ? 0.8269 1.4027 0.8741 0.1032  0.2779  0.4018  356 GLY D N   
11578 C CA  . GLY D 356 ? 0.8361 1.3732 0.9301 0.0897  0.2788  0.4168  356 GLY D CA  
11579 C C   . GLY D 356 ? 0.8151 1.3401 0.9300 0.0824  0.2823  0.3903  356 GLY D C   
11580 O O   . GLY D 356 ? 0.8180 1.3334 0.9702 0.0705  0.2889  0.4010  356 GLY D O   
11581 N N   . VAL D 357 ? 0.7847 1.3134 0.8770 0.0898  0.2782  0.3552  357 VAL D N   
11582 C CA  . VAL D 357 ? 0.7117 1.2287 0.8257 0.0851  0.2800  0.3301  357 VAL D CA  
11583 C C   . VAL D 357 ? 0.7012 1.1817 0.8171 0.0854  0.2669  0.3109  357 VAL D C   
11584 O O   . VAL D 357 ? 0.7150 1.1955 0.7995 0.0950  0.2597  0.2949  357 VAL D O   
11585 C CB  . VAL D 357 ? 0.6621 1.2128 0.7555 0.0942  0.2883  0.3038  357 VAL D CB  
11586 C CG1 . VAL D 357 ? 0.6209 1.1588 0.7404 0.0914  0.2888  0.2791  357 VAL D CG1 
11587 C CG2 . VAL D 357 ? 0.6531 1.2421 0.7445 0.0936  0.3022  0.3238  357 VAL D CG2 
11588 N N   . SER D 358 ? 0.6756 1.1263 0.8298 0.0740  0.2637  0.3128  358 SER D N   
11589 C CA  . SER D 358 ? 0.6575 1.0728 0.8193 0.0724  0.2520  0.2974  358 SER D CA  
11590 C C   . SER D 358 ? 0.5973 1.0065 0.7810 0.0698  0.2512  0.2727  358 SER D C   
11591 O O   . SER D 358 ? 0.5438 0.9586 0.7597 0.0605  0.2562  0.2779  358 SER D O   
11592 C CB  . SER D 358 ? 0.7031 1.0858 0.8919 0.0614  0.2464  0.3202  358 SER D CB  
11593 O OG  . SER D 358 ? 0.7430 1.1265 0.9684 0.0487  0.2534  0.3366  358 SER D OG  
11594 N N   . CYS D 359 ? 0.5978 0.9982 0.7648 0.0787  0.2448  0.2458  359 CYS D N   
11595 C CA  . CYS D 359 ? 0.4366 0.8347 0.6209 0.0806  0.2434  0.2217  359 CYS D CA  
11596 C C   . CYS D 359 ? 0.4047 0.7696 0.6081 0.0757  0.2320  0.2129  359 CYS D C   
11597 O O   . CYS D 359 ? 0.3966 0.7395 0.5880 0.0759  0.2249  0.2146  359 CYS D O   
11598 C CB  . CYS D 359 ? 0.4426 0.8574 0.5977 0.0959  0.2463  0.1948  359 CYS D CB  
11599 S SG  . CYS D 359 ? 0.7690 1.2282 0.9087 0.1013  0.2613  0.1975  359 CYS D SG  
11600 N N   . LEU D 360 ? 0.3884 0.7528 0.6219 0.0719  0.2300  0.2030  360 LEU D N   
11601 C CA  . LEU D 360 ? 0.3601 0.6989 0.6124 0.0681  0.2187  0.1920  360 LEU D CA  
11602 C C   . LEU D 360 ? 0.4563 0.7848 0.6817 0.0829  0.2141  0.1693  360 LEU D C   
11603 O O   . LEU D 360 ? 0.4518 0.7935 0.6683 0.0946  0.2174  0.1522  360 LEU D O   
11604 C CB  . LEU D 360 ? 0.3498 0.6993 0.6384 0.0623  0.2168  0.1866  360 LEU D CB  
11605 C CG  . LEU D 360 ? 0.3581 0.6889 0.6683 0.0583  0.2040  0.1749  360 LEU D CG  
11606 C CD1 . LEU D 360 ? 0.3457 0.6517 0.6690 0.0432  0.1982  0.1861  360 LEU D CD1 
11607 C CD2 . LEU D 360 ? 0.3657 0.7168 0.7087 0.0549  0.2015  0.1692  360 LEU D CD2 
11608 N N   . GLY D 361 ? 0.4639 0.7617 0.6748 0.0812  0.2030  0.1655  361 GLY D N   
11609 C CA  . GLY D 361 ? 0.4535 0.7364 0.6324 0.0926  0.1961  0.1433  361 GLY D CA  
11610 C C   . GLY D 361 ? 0.4381 0.7028 0.6231 0.0980  0.1867  0.1204  361 GLY D C   
11611 O O   . GLY D 361 ? 0.4477 0.6833 0.6189 0.0986  0.1748  0.1078  361 GLY D O   
11612 N N   . PHE D 362 ? 0.4407 0.7245 0.6476 0.1029  0.1925  0.1167  362 PHE D N   
11613 C CA  . PHE D 362 ? 0.4270 0.6971 0.6409 0.1112  0.1851  0.0984  362 PHE D CA  
11614 C C   . PHE D 362 ? 0.4369 0.7291 0.6505 0.1278  0.1975  0.0854  362 PHE D C   
11615 O O   . PHE D 362 ? 0.4784 0.7998 0.6971 0.1281  0.2082  0.0915  362 PHE D O   
11616 C CB  . PHE D 362 ? 0.3923 0.6628 0.6395 0.1027  0.1768  0.1051  362 PHE D CB  
11617 C CG  . PHE D 362 ? 0.3936 0.6404 0.6436 0.0872  0.1643  0.1116  362 PHE D CG  
11618 C CD1 . PHE D 362 ? 0.4095 0.6608 0.6671 0.0745  0.1685  0.1285  362 PHE D CD1 
11619 C CD2 . PHE D 362 ? 0.3946 0.6149 0.6412 0.0857  0.1495  0.1014  362 PHE D CD2 
11620 C CE1 . PHE D 362 ? 0.3858 0.6135 0.6497 0.0611  0.1582  0.1322  362 PHE D CE1 
11621 C CE2 . PHE D 362 ? 0.3956 0.5965 0.6452 0.0722  0.1392  0.1045  362 PHE D CE2 
11622 C CZ  . PHE D 362 ? 0.3978 0.6014 0.6572 0.0601  0.1436  0.1185  362 PHE D CZ  
11623 N N   . VAL D 363 ? 0.4038 0.6759 0.6090 0.1390  0.1934  0.0655  363 VAL D N   
11624 C CA  . VAL D 363 ? 0.3957 0.6794 0.5998 0.1532  0.2025  0.0483  363 VAL D CA  
11625 C C   . VAL D 363 ? 0.3457 0.6178 0.5737 0.1620  0.1967  0.0407  363 VAL D C   
11626 O O   . VAL D 363 ? 0.3999 0.6481 0.6349 0.1612  0.1858  0.0428  363 VAL D O   
11627 C CB  . VAL D 363 ? 0.4128 0.6855 0.5855 0.1597  0.2059  0.0283  363 VAL D CB  
11628 C CG1 . VAL D 363 ? 0.4855 0.7654 0.6588 0.1718  0.2140  0.0054  363 VAL D CG1 
11629 C CG2 . VAL D 363 ? 0.3728 0.6649 0.5211 0.1526  0.2111  0.0384  363 VAL D CG2 
11630 N N   . ASP D 364 ? 0.3615 0.6525 0.6021 0.1708  0.2040  0.0330  364 ASP D N   
11631 C CA  . ASP D 364 ? 0.3724 0.6576 0.6379 0.1805  0.1990  0.0291  364 ASP D CA  
11632 C C   . ASP D 364 ? 0.3892 0.6412 0.6458 0.1911  0.1967  0.0098  364 ASP D C   
11633 O O   . ASP D 364 ? 0.4261 0.6771 0.6694 0.1975  0.2056  -0.0102 364 ASP D O   
11634 C CB  . ASP D 364 ? 0.3842 0.7024 0.6684 0.1871  0.2088  0.0267  364 ASP D CB  
11635 C CG  . ASP D 364 ? 0.3781 0.6982 0.6928 0.1963  0.2022  0.0292  364 ASP D CG  
11636 O OD1 . ASP D 364 ? 0.4342 0.7267 0.7518 0.2000  0.1911  0.0300  364 ASP D OD1 
11637 O OD2 . ASP D 364 ? 0.3862 0.7369 0.7217 0.1998  0.2082  0.0315  364 ASP D OD2 
11638 N N   . GLY D 365 ? 0.3799 0.6059 0.6448 0.1919  0.1848  0.0154  365 GLY D N   
11639 C CA  . GLY D 365 ? 0.4049 0.5960 0.6657 0.2004  0.1821  0.0005  365 GLY D CA  
11640 C C   . GLY D 365 ? 0.4627 0.6559 0.7468 0.2150  0.1843  -0.0060 365 GLY D C   
11641 O O   . GLY D 365 ? 0.5144 0.6785 0.8009 0.2231  0.1826  -0.0170 365 GLY D O   
11642 N N   . GLY D 366 ? 0.4498 0.6771 0.7534 0.2181  0.1880  0.0020  366 GLY D N   
11643 C CA  . GLY D 366 ? 0.4203 0.6535 0.7481 0.2333  0.1908  -0.0039 366 GLY D CA  
11644 C C   . GLY D 366 ? 0.4615 0.6810 0.8065 0.2373  0.1776  0.0131  366 GLY D C   
11645 O O   . GLY D 366 ? 0.3937 0.6065 0.7327 0.2272  0.1671  0.0283  366 GLY D O   
11646 N N   . VAL D 367 ? 0.5276 0.7439 0.8940 0.2527  0.1783  0.0101  367 VAL D N   
11647 C CA  . VAL D 367 ? 0.5554 0.7660 0.9408 0.2593  0.1666  0.0288  367 VAL D CA  
11648 C C   . VAL D 367 ? 0.6017 0.7668 0.9803 0.2629  0.1609  0.0295  367 VAL D C   
11649 O O   . VAL D 367 ? 0.6250 0.7851 1.0147 0.2667  0.1508  0.0483  367 VAL D O   
11650 C CB  . VAL D 367 ? 0.5604 0.7939 0.9758 0.2755  0.1702  0.0294  367 VAL D CB  
11651 C CG1 . VAL D 367 ? 0.4990 0.7810 0.9264 0.2702  0.1739  0.0341  367 VAL D CG1 
11652 C CG2 . VAL D 367 ? 0.6131 0.8287 1.0309 0.2889  0.1820  0.0051  367 VAL D CG2 
11653 N N   . HIS D 368 ? 0.6318 0.7666 0.9935 0.2618  0.1674  0.0094  368 HIS D N   
11654 C CA  . HIS D 368 ? 0.6782 0.7693 1.0329 0.2609  0.1623  0.0109  368 HIS D CA  
11655 C C   . HIS D 368 ? 0.7033 0.7778 1.0301 0.2448  0.1602  0.0059  368 HIS D C   
11656 O O   . HIS D 368 ? 0.7250 0.7658 1.0409 0.2421  0.1619  -0.0071 368 HIS D O   
11657 C CB  . HIS D 368 ? 0.7610 0.8245 1.1241 0.2731  0.1704  -0.0086 368 HIS D CB  
11658 C CG  . HIS D 368 ? 0.8214 0.8947 1.2143 0.2910  0.1724  -0.0028 368 HIS D CG  
11659 N ND1 . HIS D 368 ? 0.8709 0.9335 1.2759 0.3050  0.1824  -0.0237 368 HIS D ND1 
11660 C CD2 . HIS D 368 ? 0.8501 0.9447 1.2636 0.2980  0.1653  0.0212  368 HIS D CD2 
11661 C CE1 . HIS D 368 ? 0.9214 0.9964 1.3546 0.3205  0.1820  -0.0120 368 HIS D CE1 
11662 N NE2 . HIS D 368 ? 0.9050 1.0008 1.3437 0.3164  0.1714  0.0156  368 HIS D NE2 
11663 N N   . ALA D 369 ? 0.6778 0.7768 0.9951 0.2337  0.1563  0.0164  369 ALA D N   
11664 C CA  . ALA D 369 ? 0.6102 0.6966 0.9032 0.2194  0.1537  0.0143  369 ALA D CA  
11665 C C   . ALA D 369 ? 0.6537 0.7105 0.9442 0.2158  0.1439  0.0268  369 ALA D C   
11666 O O   . ALA D 369 ? 0.6574 0.7193 0.9626 0.2207  0.1363  0.0459  369 ALA D O   
11667 C CB  . ALA D 369 ? 0.5249 0.6444 0.8135 0.2094  0.1518  0.0253  369 ALA D CB  
11668 N N   . ARG D 370 ? 0.7058 0.7355 0.9773 0.2068  0.1442  0.0166  370 ARG D N   
11669 C CA  . ARG D 370 ? 0.7504 0.7506 1.0181 0.2018  0.1369  0.0264  370 ARG D CA  
11670 C C   . ARG D 370 ? 0.7232 0.7398 0.9881 0.1948  0.1264  0.0483  370 ARG D C   
11671 O O   . ARG D 370 ? 0.7751 0.7816 1.0439 0.1954  0.1193  0.0645  370 ARG D O   
11672 C CB  . ARG D 370 ? 0.7815 0.7532 1.0316 0.1931  0.1406  0.0067  370 ARG D CB  
11673 C CG  . ARG D 370 ? 0.8285 0.7771 1.0691 0.1828  0.1340  0.0153  370 ARG D CG  
11674 C CD  . ARG D 370 ? 0.9045 0.8372 1.1277 0.1732  0.1381  -0.0077 370 ARG D CD  
11675 N NE  . ARG D 370 ? 0.9721 0.9306 1.1801 0.1689  0.1400  -0.0135 370 ARG D NE  
11676 C CZ  . ARG D 370 ? 1.0407 1.0048 1.2353 0.1669  0.1468  -0.0354 370 ARG D CZ  
11677 N NH1 . ARG D 370 ? 1.0760 1.0224 1.2707 0.1682  0.1513  -0.0576 370 ARG D NH1 
11678 N NH2 . ARG D 370 ? 1.0482 1.0389 1.2273 0.1618  0.1470  -0.0345 370 ARG D NH2 
11679 N N   . ALA D 371 ? 0.6194 0.6621 0.8775 0.1880  0.1259  0.0487  371 ALA D N   
11680 C CA  . ALA D 371 ? 0.5111 0.5745 0.7709 0.1815  0.1160  0.0660  371 ALA D CA  
11681 C C   . ALA D 371 ? 0.4993 0.6024 0.7699 0.1798  0.1163  0.0694  371 ALA D C   
11682 O O   . ALA D 371 ? 0.5343 0.6471 0.8057 0.1824  0.1265  0.0588  371 ALA D O   
11683 C CB  . ALA D 371 ? 0.4382 0.4857 0.6709 0.1637  0.1097  0.0602  371 ALA D CB  
11684 N N   . GLY D 372 ? 0.4467 0.5741 0.7236 0.1728  0.1047  0.0827  372 GLY D N   
11685 C CA  . GLY D 372 ? 0.3868 0.5525 0.6783 0.1681  0.1043  0.0861  372 GLY D CA  
11686 C C   . GLY D 372 ? 0.3306 0.4962 0.6064 0.1528  0.1083  0.0772  372 GLY D C   
11687 O O   . GLY D 372 ? 0.3175 0.5053 0.6032 0.1528  0.1170  0.0759  372 GLY D O   
11688 N N   . ILE D 373 ? 0.3129 0.4544 0.5653 0.1405  0.1025  0.0728  373 ILE D N   
11689 C CA  . ILE D 373 ? 0.3135 0.4488 0.5492 0.1275  0.1052  0.0665  373 ILE D CA  
11690 C C   . ILE D 373 ? 0.3309 0.4328 0.5427 0.1278  0.1068  0.0563  373 ILE D C   
11691 O O   . ILE D 373 ? 0.3188 0.4013 0.5242 0.1276  0.1001  0.0568  373 ILE D O   
11692 C CB  . ILE D 373 ? 0.3183 0.4602 0.5537 0.1108  0.0946  0.0707  373 ILE D CB  
11693 C CG1 . ILE D 373 ? 0.3121 0.4893 0.5745 0.1080  0.0909  0.0786  373 ILE D CG1 
11694 C CG2 . ILE D 373 ? 0.3362 0.4694 0.5580 0.0998  0.0985  0.0672  373 ILE D CG2 
11695 C CD1 . ILE D 373 ? 0.2887 0.4719 0.5538 0.0913  0.0791  0.0786  373 ILE D CD1 
11696 N N   . ALA D 374 ? 0.3639 0.4624 0.5632 0.1284  0.1160  0.0472  374 ALA D N   
11697 C CA  . ALA D 374 ? 0.3645 0.4367 0.5417 0.1260  0.1162  0.0357  374 ALA D CA  
11698 C C   . ALA D 374 ? 0.3741 0.4510 0.5351 0.1157  0.1166  0.0349  374 ALA D C   
11699 O O   . ALA D 374 ? 0.3736 0.4671 0.5308 0.1187  0.1257  0.0330  374 ALA D O   
11700 C CB  . ALA D 374 ? 0.3678 0.4309 0.5446 0.1388  0.1264  0.0218  374 ALA D CB  
11701 N N   . LEU D 375 ? 0.3766 0.4405 0.5286 0.1047  0.1074  0.0374  375 LEU D N   
11702 C CA  . LEU D 375 ? 0.3849 0.4509 0.5252 0.0959  0.1067  0.0398  375 LEU D CA  
11703 C C   . LEU D 375 ? 0.3990 0.4569 0.5184 0.0982  0.1097  0.0285  375 LEU D C   
11704 O O   . LEU D 375 ? 0.4237 0.4625 0.5355 0.0985  0.1062  0.0185  375 LEU D O   
11705 C CB  . LEU D 375 ? 0.3605 0.4159 0.5023 0.0848  0.0964  0.0442  375 LEU D CB  
11706 C CG  . LEU D 375 ? 0.3464 0.4133 0.5081 0.0808  0.0913  0.0514  375 LEU D CG  
11707 C CD1 . LEU D 375 ? 0.3664 0.4229 0.5269 0.0711  0.0812  0.0501  375 LEU D CD1 
11708 C CD2 . LEU D 375 ? 0.3356 0.4243 0.5133 0.0770  0.0963  0.0604  375 LEU D CD2 
11709 N N   . GLY D 376 ? 0.3721 0.4477 0.4828 0.0994  0.1164  0.0306  376 GLY D N   
11710 C CA  . GLY D 376 ? 0.3455 0.4228 0.4356 0.1027  0.1191  0.0182  376 GLY D CA  
11711 C C   . GLY D 376 ? 0.3583 0.4385 0.4342 0.0965  0.1145  0.0243  376 GLY D C   
11712 O O   . GLY D 376 ? 0.3559 0.4283 0.4389 0.0891  0.1084  0.0362  376 GLY D O   
11713 N N   . ALA D 377 ? 0.3756 0.4695 0.4325 0.1003  0.1174  0.0155  377 ALA D N   
11714 C CA  . ALA D 377 ? 0.3733 0.4731 0.4161 0.0967  0.1118  0.0211  377 ALA D CA  
11715 C C   . ALA D 377 ? 0.3339 0.4464 0.3825 0.0940  0.1136  0.0464  377 ALA D C   
11716 O O   . ALA D 377 ? 0.3814 0.4861 0.4314 0.0896  0.1072  0.0561  377 ALA D O   
11717 C CB  . ALA D 377 ? 0.3957 0.5157 0.4163 0.1019  0.1141  0.0055  377 ALA D CB  
11718 N N   A HIS D 378 ? 0.3607 0.4925 0.4157 0.0968  0.1235  0.0569  378 HIS D N   
11719 N N   B HIS D 378 ? 0.3607 0.4925 0.4157 0.0967  0.1234  0.0573  378 HIS D N   
11720 C CA  A HIS D 378 ? 0.3222 0.4665 0.3869 0.0934  0.1278  0.0826  378 HIS D CA  
11721 C CA  B HIS D 378 ? 0.3306 0.4743 0.3944 0.0932  0.1272  0.0831  378 HIS D CA  
11722 C C   A HIS D 378 ? 0.3612 0.4817 0.4500 0.0841  0.1217  0.0915  378 HIS D C   
11723 C C   B HIS D 378 ? 0.3612 0.4819 0.4507 0.0840  0.1219  0.0921  378 HIS D C   
11724 O O   A HIS D 378 ? 0.3640 0.4805 0.4614 0.0794  0.1204  0.1084  378 HIS D O   
11725 O O   B HIS D 378 ? 0.3656 0.4831 0.4655 0.0789  0.1213  0.1099  378 HIS D O   
11726 C CB  A HIS D 378 ? 0.3315 0.5024 0.4019 0.0972  0.1409  0.0903  378 HIS D CB  
11727 C CB  B HIS D 378 ? 0.3414 0.5153 0.4067 0.0976  0.1407  0.0927  378 HIS D CB  
11728 C CG  A HIS D 378 ? 0.3422 0.5328 0.4179 0.0946  0.1484  0.1182  378 HIS D CG  
11729 C CG  B HIS D 378 ? 0.3562 0.5615 0.3943 0.1056  0.1468  0.0907  378 HIS D CG  
11730 N ND1 A HIS D 378 ? 0.3622 0.5803 0.4159 0.1002  0.1535  0.1287  378 HIS D ND1 
11731 N ND1 B HIS D 378 ? 0.3727 0.6106 0.4068 0.1081  0.1581  0.1111  378 HIS D ND1 
11732 C CD2 A HIS D 378 ? 0.3385 0.5263 0.4409 0.0866  0.1519  0.1387  378 HIS D CD2 
11733 C CD2 B HIS D 378 ? 0.4238 0.6361 0.4375 0.1109  0.1431  0.0701  378 HIS D CD2 
11734 C CE1 A HIS D 378 ? 0.3709 0.6005 0.4374 0.0964  0.1607  0.1579  378 HIS D CE1 
11735 C CE1 B HIS D 378 ? 0.3923 0.6587 0.3976 0.1157  0.1609  0.1030  378 HIS D CE1 
11736 N NE2 A HIS D 378 ? 0.3568 0.5665 0.4547 0.0874  0.1602  0.1634  378 HIS D NE2 
11737 N NE2 B HIS D 378 ? 0.3888 0.6401 0.3819 0.1171  0.1515  0.0765  378 HIS D NE2 
11738 N N   . HIS D 379 ? 0.3219 0.4273 0.4224 0.0821  0.1181  0.0795  379 HIS D N   
11739 C CA  . HIS D 379 ? 0.3351 0.4219 0.4558 0.0731  0.1112  0.0828  379 HIS D CA  
11740 C C   . HIS D 379 ? 0.3730 0.4399 0.4876 0.0695  0.1021  0.0797  379 HIS D C   
11741 O O   . HIS D 379 ? 0.3926 0.4498 0.5219 0.0628  0.0994  0.0883  379 HIS D O   
11742 C CB  . HIS D 379 ? 0.3168 0.3968 0.4464 0.0735  0.1080  0.0710  379 HIS D CB  
11743 C CG  . HIS D 379 ? 0.3251 0.3923 0.4721 0.0643  0.1001  0.0714  379 HIS D CG  
11744 N ND1 . HIS D 379 ? 0.3314 0.4085 0.5024 0.0574  0.1015  0.0796  379 HIS D ND1 
11745 C CD2 . HIS D 379 ? 0.3562 0.4049 0.5003 0.0602  0.0911  0.0630  379 HIS D CD2 
11746 C CE1 . HIS D 379 ? 0.3225 0.3881 0.5036 0.0495  0.0929  0.0740  379 HIS D CE1 
11747 N NE2 . HIS D 379 ? 0.3458 0.3945 0.5098 0.0517  0.0870  0.0645  379 HIS D NE2 
11748 N N   . LEU D 380 ? 0.3847 0.4464 0.4802 0.0739  0.0982  0.0661  380 LEU D N   
11749 C CA  . LEU D 380 ? 0.3734 0.4196 0.4646 0.0710  0.0900  0.0613  380 LEU D CA  
11750 C C   . LEU D 380 ? 0.3573 0.4108 0.4446 0.0726  0.0896  0.0744  380 LEU D C   
11751 O O   . LEU D 380 ? 0.4030 0.4436 0.4975 0.0696  0.0841  0.0763  380 LEU D O   
11752 C CB  . LEU D 380 ? 0.3530 0.3932 0.4287 0.0738  0.0864  0.0427  380 LEU D CB  
11753 C CG  . LEU D 380 ? 0.3456 0.3745 0.4270 0.0735  0.0863  0.0325  380 LEU D CG  
11754 C CD1 . LEU D 380 ? 0.3405 0.3631 0.4103 0.0762  0.0856  0.0160  380 LEU D CD1 
11755 C CD2 . LEU D 380 ? 0.3230 0.3376 0.4171 0.0666  0.0804  0.0341  380 LEU D CD2 
11756 N N   . GLU D 381 ? 0.3382 0.4145 0.4144 0.0783  0.0958  0.0841  381 GLU D N   
11757 C CA  . GLU D 381 ? 0.3396 0.4287 0.4090 0.0822  0.0951  0.0996  381 GLU D CA  
11758 C C   . GLU D 381 ? 0.3756 0.4512 0.4689 0.0778  0.0955  0.1190  381 GLU D C   
11759 O O   . GLU D 381 ? 0.4175 0.4860 0.5307 0.0718  0.1003  0.1255  381 GLU D O   
11760 C CB  . GLU D 381 ? 0.3522 0.4733 0.4057 0.0888  0.1032  0.1094  381 GLU D CB  
11761 C CG  . GLU D 381 ? 0.3825 0.5198 0.4110 0.0941  0.1019  0.0880  381 GLU D CG  
11762 C CD  . GLU D 381 ? 0.4374 0.6082 0.4506 0.1003  0.1121  0.0917  381 GLU D CD  
11763 O OE1 . GLU D 381 ? 0.4228 0.6057 0.4448 0.1004  0.1207  0.1148  381 GLU D OE1 
11764 O OE2 . GLU D 381 ? 0.5022 0.6879 0.4963 0.1046  0.1126  0.0701  381 GLU D OE2 
11765 N N   . GLU D 382 ? 0.3792 0.4509 0.4730 0.0806  0.0900  0.1256  382 GLU D N   
11766 C CA  . GLU D 382 ? 0.3927 0.4481 0.5115 0.0785  0.0900  0.1423  382 GLU D CA  
11767 C C   . GLU D 382 ? 0.3740 0.4016 0.5150 0.0692  0.0875  0.1290  382 GLU D C   
11768 O O   . GLU D 382 ? 0.3556 0.3679 0.5233 0.0647  0.0901  0.1392  382 GLU D O   
11769 C CB  . GLU D 382 ? 0.4088 0.4750 0.5396 0.0793  0.0998  0.1713  382 GLU D CB  
11770 C CG  . GLU D 382 ? 0.4079 0.5067 0.5160 0.0895  0.1025  0.1891  382 GLU D CG  
11771 C CD  . GLU D 382 ? 0.4283 0.5327 0.5273 0.0977  0.0936  0.1915  382 GLU D CD  
11772 O OE1 . GLU D 382 ? 0.4409 0.5234 0.5615 0.0976  0.0899  0.1966  382 GLU D OE1 
11773 O OE2 . GLU D 382 ? 0.4699 0.6028 0.5408 0.1044  0.0901  0.1858  382 GLU D OE2 
11774 N N   . ASN D 383 ? 0.3851 0.4074 0.5156 0.0665  0.0826  0.1059  383 ASN D N   
11775 C CA  . ASN D 383 ? 0.3939 0.3958 0.5384 0.0589  0.0785  0.0907  383 ASN D CA  
11776 C C   . ASN D 383 ? 0.3707 0.3675 0.5027 0.0605  0.0714  0.0739  383 ASN D C   
11777 O O   . ASN D 383 ? 0.3685 0.3761 0.4802 0.0648  0.0698  0.0676  383 ASN D O   
11778 C CB  . ASN D 383 ? 0.3705 0.3737 0.5182 0.0532  0.0801  0.0822  383 ASN D CB  
11779 C CG  . ASN D 383 ? 0.3881 0.3962 0.5559 0.0486  0.0870  0.0966  383 ASN D CG  
11780 O OD1 . ASN D 383 ? 0.4174 0.4135 0.6098 0.0419  0.0876  0.1004  383 ASN D OD1 
11781 N ND2 . ASN D 383 ? 0.3689 0.3953 0.5288 0.0517  0.0930  0.1035  383 ASN D ND2 
11782 N N   . LEU D 384 ? 0.3923 0.3738 0.5378 0.0564  0.0681  0.0653  384 LEU D N   
11783 C CA  . LEU D 384 ? 0.3559 0.3340 0.4915 0.0562  0.0628  0.0488  384 LEU D CA  
11784 C C   . LEU D 384 ? 0.3419 0.3156 0.4744 0.0497  0.0616  0.0352  384 LEU D C   
11785 O O   . LEU D 384 ? 0.3272 0.2947 0.4738 0.0437  0.0616  0.0315  384 LEU D O   
11786 C CB  . LEU D 384 ? 0.3542 0.3228 0.5050 0.0572  0.0608  0.0467  384 LEU D CB  
11787 C CG  . LEU D 384 ? 0.3296 0.2976 0.4728 0.0561  0.0567  0.0300  384 LEU D CG  
11788 C CD1 . LEU D 384 ? 0.3243 0.3061 0.4506 0.0612  0.0539  0.0297  384 LEU D CD1 
11789 C CD2 . LEU D 384 ? 0.3459 0.3042 0.5091 0.0565  0.0566  0.0253  384 LEU D CD2 
11790 N N   . VAL D 385 ? 0.3449 0.3230 0.4603 0.0509  0.0606  0.0279  385 VAL D N   
11791 C CA  . VAL D 385 ? 0.3418 0.3175 0.4541 0.0469  0.0599  0.0201  385 VAL D CA  
11792 C C   . VAL D 385 ? 0.3649 0.3368 0.4687 0.0453  0.0573  0.0094  385 VAL D C   
11793 O O   . VAL D 385 ? 0.3366 0.3101 0.4303 0.0477  0.0574  0.0062  385 VAL D O   
11794 C CB  . VAL D 385 ? 0.3117 0.2939 0.4168 0.0502  0.0632  0.0235  385 VAL D CB  
11795 C CG1 . VAL D 385 ? 0.3154 0.2965 0.4216 0.0479  0.0621  0.0195  385 VAL D CG1 
11796 C CG2 . VAL D 385 ? 0.2474 0.2380 0.3611 0.0518  0.0675  0.0360  385 VAL D CG2 
11797 N N   . VAL D 386 ? 0.3830 0.3522 0.4914 0.0404  0.0555  0.0031  386 VAL D N   
11798 C CA  . VAL D 386 ? 0.3737 0.3419 0.4757 0.0381  0.0544  -0.0052 386 VAL D CA  
11799 C C   . VAL D 386 ? 0.3866 0.3554 0.4803 0.0364  0.0549  -0.0052 386 VAL D C   
11800 O O   . VAL D 386 ? 0.3684 0.3418 0.4643 0.0347  0.0537  -0.0032 386 VAL D O   
11801 C CB  . VAL D 386 ? 0.3346 0.3030 0.4461 0.0349  0.0533  -0.0127 386 VAL D CB  
11802 C CG1 . VAL D 386 ? 0.3498 0.3216 0.4550 0.0324  0.0538  -0.0209 386 VAL D CG1 
11803 C CG2 . VAL D 386 ? 0.2916 0.2568 0.4147 0.0387  0.0536  -0.0098 386 VAL D CG2 
11804 N N   . PHE D 387 ? 0.3680 0.3330 0.4544 0.0370  0.0567  -0.0065 387 PHE D N   
11805 C CA  . PHE D 387 ? 0.3493 0.3111 0.4309 0.0360  0.0586  -0.0038 387 PHE D CA  
11806 C C   . PHE D 387 ? 0.3458 0.3101 0.4250 0.0308  0.0592  -0.0070 387 PHE D C   
11807 O O   . PHE D 387 ? 0.3431 0.3046 0.4222 0.0284  0.0612  -0.0113 387 PHE D O   
11808 C CB  . PHE D 387 ? 0.3598 0.3132 0.4396 0.0387  0.0618  -0.0045 387 PHE D CB  
11809 C CG  . PHE D 387 ? 0.3755 0.3298 0.4563 0.0448  0.0630  -0.0016 387 PHE D CG  
11810 C CD1 . PHE D 387 ? 0.3553 0.3158 0.4352 0.0472  0.0624  -0.0031 387 PHE D CD1 
11811 C CD2 . PHE D 387 ? 0.4074 0.3596 0.4910 0.0490  0.0651  0.0046  387 PHE D CD2 
11812 C CE1 . PHE D 387 ? 0.3562 0.3215 0.4362 0.0525  0.0649  0.0003  387 PHE D CE1 
11813 C CE2 . PHE D 387 ? 0.3892 0.3455 0.4754 0.0550  0.0674  0.0065  387 PHE D CE2 
11814 C CZ  . PHE D 387 ? 0.3893 0.3527 0.4729 0.0561  0.0678  0.0039  387 PHE D CZ  
11815 N N   . ASP D 388 ? 0.3487 0.3221 0.4264 0.0287  0.0576  -0.0059 388 ASP D N   
11816 C CA  . ASP D 388 ? 0.3148 0.2969 0.3882 0.0241  0.0590  -0.0090 388 ASP D CA  
11817 C C   . ASP D 388 ? 0.3335 0.3161 0.4008 0.0236  0.0618  0.0023  388 ASP D C   
11818 O O   . ASP D 388 ? 0.3579 0.3501 0.4211 0.0251  0.0597  0.0098  388 ASP D O   
11819 C CB  . ASP D 388 ? 0.3198 0.3151 0.3944 0.0221  0.0558  -0.0164 388 ASP D CB  
11820 C CG  . ASP D 388 ? 0.3774 0.3859 0.4468 0.0179  0.0582  -0.0234 388 ASP D CG  
11821 O OD1 . ASP D 388 ? 0.4321 0.4409 0.4968 0.0160  0.0626  -0.0187 388 ASP D OD1 
11822 O OD2 . ASP D 388 ? 0.4137 0.4341 0.4847 0.0159  0.0565  -0.0344 388 ASP D OD2 
11823 N N   . LEU D 389 ? 0.3884 0.3611 0.4572 0.0215  0.0665  0.0044  389 LEU D N   
11824 C CA  . LEU D 389 ? 0.3945 0.3621 0.4622 0.0214  0.0708  0.0179  389 LEU D CA  
11825 C C   . LEU D 389 ? 0.4106 0.3954 0.4703 0.0172  0.0732  0.0242  389 LEU D C   
11826 O O   . LEU D 389 ? 0.4661 0.4538 0.5225 0.0188  0.0754  0.0403  389 LEU D O   
11827 C CB  . LEU D 389 ? 0.4109 0.3607 0.4874 0.0188  0.0759  0.0159  389 LEU D CB  
11828 C CG  . LEU D 389 ? 0.4285 0.3690 0.5091 0.0227  0.0733  0.0060  389 LEU D CG  
11829 C CD1 . LEU D 389 ? 0.4442 0.3744 0.5325 0.0184  0.0766  -0.0031 389 LEU D CD1 
11830 C CD2 . LEU D 389 ? 0.4417 0.3759 0.5237 0.0307  0.0727  0.0134  389 LEU D CD2 
11831 N N   . GLU D 390 ? 0.3832 0.3815 0.4401 0.0131  0.0731  0.0124  390 GLU D N   
11832 C CA  . GLU D 390 ? 0.3827 0.4024 0.4301 0.0092  0.0765  0.0157  390 GLU D CA  
11833 C C   . GLU D 390 ? 0.3853 0.4263 0.4212 0.0118  0.0714  0.0185  390 GLU D C   
11834 O O   . GLU D 390 ? 0.4254 0.4851 0.4503 0.0107  0.0739  0.0300  390 GLU D O   
11835 C CB  . GLU D 390 ? 0.4005 0.4305 0.4507 0.0051  0.0790  -0.0006 390 GLU D CB  
11836 C CG  . GLU D 390 ? 0.4617 0.4802 0.5234 0.0012  0.0838  -0.0028 390 GLU D CG  
11837 C CD  . GLU D 390 ? 0.4936 0.5288 0.5594 -0.0029 0.0886  -0.0139 390 GLU D CD  
11838 O OE1 . GLU D 390 ? 0.4890 0.5410 0.5503 -0.0012 0.0878  -0.0249 390 GLU D OE1 
11839 O OE2 . GLU D 390 ? 0.4765 0.5085 0.5526 -0.0081 0.0935  -0.0131 390 GLU D OE2 
11840 N N   . ARG D 391 ? 0.3700 0.4106 0.4093 0.0147  0.0643  0.0091  391 ARG D N   
11841 C CA  . ARG D 391 ? 0.3598 0.4231 0.3919 0.0156  0.0579  0.0076  391 ARG D CA  
11842 C C   . ARG D 391 ? 0.3748 0.4330 0.4111 0.0213  0.0531  0.0202  391 ARG D C   
11843 O O   . ARG D 391 ? 0.3976 0.4764 0.4314 0.0222  0.0466  0.0197  391 ARG D O   
11844 C CB  . ARG D 391 ? 0.3429 0.4124 0.3809 0.0128  0.0542  -0.0153 391 ARG D CB  
11845 C CG  . ARG D 391 ? 0.4045 0.4820 0.4409 0.0090  0.0593  -0.0300 391 ARG D CG  
11846 C CD  . ARG D 391 ? 0.4711 0.5552 0.5158 0.0070  0.0566  -0.0536 391 ARG D CD  
11847 N NE  . ARG D 391 ? 0.5398 0.6451 0.5802 0.0047  0.0500  -0.0603 391 ARG D NE  
11848 C CZ  . ARG D 391 ? 0.5755 0.6907 0.6236 0.0010  0.0476  -0.0836 391 ARG D CZ  
11849 N NH1 . ARG D 391 ? 0.5734 0.6769 0.6348 0.0009  0.0523  -0.1004 391 ARG D NH1 
11850 N NH2 . ARG D 391 ? 0.5890 0.7269 0.6344 -0.0024 0.0406  -0.0910 391 ARG D NH2 
11851 N N   . SER D 392 ? 0.3585 0.3920 0.4029 0.0251  0.0566  0.0296  392 SER D N   
11852 C CA  . SER D 392 ? 0.3572 0.3825 0.4088 0.0322  0.0544  0.0411  392 SER D CA  
11853 C C   . SER D 392 ? 0.3466 0.3795 0.4050 0.0332  0.0478  0.0318  392 SER D C   
11854 O O   . SER D 392 ? 0.3611 0.4113 0.4209 0.0364  0.0426  0.0386  392 SER D O   
11855 C CB  . SER D 392 ? 0.3663 0.4047 0.4128 0.0370  0.0542  0.0623  392 SER D CB  
11856 O OG  . SER D 392 ? 0.3606 0.3841 0.4183 0.0454  0.0554  0.0745  392 SER D OG  
11857 N N   . ARG D 393 ? 0.3342 0.3558 0.3990 0.0303  0.0483  0.0178  393 ARG D N   
11858 C CA  . ARG D 393 ? 0.3182 0.3447 0.3929 0.0293  0.0439  0.0097  393 ARG D CA  
11859 C C   . ARG D 393 ? 0.3289 0.3359 0.4118 0.0306  0.0470  0.0056  393 ARG D C   
11860 O O   . ARG D 393 ? 0.3547 0.3486 0.4348 0.0307  0.0509  0.0035  393 ARG D O   
11861 C CB  . ARG D 393 ? 0.3197 0.3625 0.3942 0.0224  0.0402  -0.0053 393 ARG D CB  
11862 C CG  . ARG D 393 ? 0.3171 0.3501 0.3907 0.0192  0.0443  -0.0170 393 ARG D CG  
11863 C CD  . ARG D 393 ? 0.3370 0.3854 0.4119 0.0135  0.0423  -0.0344 393 ARG D CD  
11864 N NE  . ARG D 393 ? 0.3802 0.4176 0.4591 0.0127  0.0470  -0.0449 393 ARG D NE  
11865 C CZ  . ARG D 393 ? 0.3924 0.4336 0.4803 0.0095  0.0473  -0.0631 393 ARG D CZ  
11866 N NH1 . ARG D 393 ? 0.4059 0.4609 0.4993 0.0049  0.0430  -0.0752 393 ARG D NH1 
11867 N NH2 . ARG D 393 ? 0.3800 0.4121 0.4739 0.0111  0.0519  -0.0704 393 ARG D NH2 
11868 N N   . VAL D 394 ? 0.3063 0.3152 0.4001 0.0313  0.0453  0.0053  394 VAL D N   
11869 C CA  . VAL D 394 ? 0.3251 0.3214 0.4259 0.0327  0.0483  0.0041  394 VAL D CA  
11870 C C   . VAL D 394 ? 0.3339 0.3323 0.4470 0.0273  0.0466  -0.0041 394 VAL D C   
11871 O O   . VAL D 394 ? 0.3480 0.3589 0.4701 0.0231  0.0431  -0.0072 394 VAL D O   
11872 C CB  . VAL D 394 ? 0.3656 0.3622 0.4718 0.0385  0.0504  0.0132  394 VAL D CB  
11873 C CG1 . VAL D 394 ? 0.3362 0.3260 0.4478 0.0397  0.0538  0.0136  394 VAL D CG1 
11874 C CG2 . VAL D 394 ? 0.3220 0.3123 0.4212 0.0449  0.0534  0.0195  394 VAL D CG2 
11875 N N   . GLY D 395 ? 0.3449 0.3320 0.4616 0.0275  0.0490  -0.0073 395 GLY D N   
11876 C CA  . GLY D 395 ? 0.3323 0.3164 0.4656 0.0237  0.0489  -0.0127 395 GLY D CA  
11877 C C   . GLY D 395 ? 0.3524 0.3290 0.4941 0.0273  0.0524  -0.0019 395 GLY D C   
11878 O O   . GLY D 395 ? 0.3526 0.3267 0.4837 0.0331  0.0545  0.0051  395 GLY D O   
11879 N N   . PHE D 396 ? 0.3525 0.3274 0.5139 0.0233  0.0535  -0.0006 396 PHE D N   
11880 C CA  . PHE D 396 ? 0.3278 0.2979 0.4979 0.0266  0.0580  0.0134  396 PHE D CA  
11881 C C   . PHE D 396 ? 0.3566 0.3168 0.5524 0.0219  0.0601  0.0131  396 PHE D C   
11882 O O   . PHE D 396 ? 0.3579 0.3171 0.5674 0.0143  0.0579  -0.0008 396 PHE D O   
11883 C CB  . PHE D 396 ? 0.3398 0.3210 0.5095 0.0273  0.0602  0.0233  396 PHE D CB  
11884 C CG  . PHE D 396 ? 0.3588 0.3509 0.5419 0.0197  0.0574  0.0175  396 PHE D CG  
11885 C CD1 . PHE D 396 ? 0.3627 0.3546 0.5719 0.0116  0.0590  0.0176  396 PHE D CD1 
11886 C CD2 . PHE D 396 ? 0.3220 0.3260 0.4939 0.0205  0.0531  0.0127  396 PHE D CD2 
11887 C CE1 . PHE D 396 ? 0.3250 0.3309 0.5481 0.0032  0.0552  0.0095  396 PHE D CE1 
11888 C CE2 . PHE D 396 ? 0.2885 0.3085 0.4725 0.0142  0.0489  0.0076  396 PHE D CE2 
11889 C CZ  . PHE D 396 ? 0.3134 0.3358 0.5227 0.0050  0.0495  0.0045  396 PHE D CZ  
11890 N N   . ASN D 397 ? 0.3669 0.3207 0.5705 0.0265  0.0647  0.0284  397 ASN D N   
11891 C CA  . ASN D 397 ? 0.3715 0.3119 0.6043 0.0231  0.0683  0.0325  397 ASN D CA  
11892 C C   . ASN D 397 ? 0.3593 0.3029 0.6136 0.0130  0.0705  0.0329  397 ASN D C   
11893 O O   . ASN D 397 ? 0.3704 0.3266 0.6199 0.0130  0.0728  0.0445  397 ASN D O   
11894 C CB  . ASN D 397 ? 0.3531 0.2892 0.5887 0.0318  0.0729  0.0544  397 ASN D CB  
11895 C CG  . ASN D 397 ? 0.3502 0.3024 0.5687 0.0363  0.0758  0.0710  397 ASN D CG  
11896 O OD1 . ASN D 397 ? 0.3237 0.2869 0.5163 0.0408  0.0730  0.0663  397 ASN D OD1 
11897 N ND2 . ASN D 397 ? 0.3693 0.3230 0.6038 0.0351  0.0825  0.0904  397 ASN D ND2 
11898 N N   . SER D 398 ? 0.3812 0.3151 0.6612 0.0039  0.0701  0.0185  398 SER D N   
11899 C CA  . SER D 398 ? 0.4254 0.3653 0.7294 -0.0083 0.0710  0.0146  398 SER D CA  
11900 C C   . SER D 398 ? 0.4790 0.4068 0.8141 -0.0117 0.0797  0.0339  398 SER D C   
11901 O O   . SER D 398 ? 0.5321 0.4667 0.8902 -0.0226 0.0821  0.0347  398 SER D O   
11902 C CB  . SER D 398 ? 0.4679 0.4075 0.7855 -0.0184 0.0660  -0.0138 398 SER D CB  
11903 O OG  . SER D 398 ? 0.5493 0.4664 0.8848 -0.0172 0.0690  -0.0220 398 SER D OG  
11904 N N   . ASN D 399 ? 0.4673 0.3796 0.8053 -0.0026 0.0846  0.0508  399 ASN D N   
11905 C CA  . ASN D 399 ? 0.4862 0.3905 0.8480 -0.0028 0.0941  0.0779  399 ASN D CA  
11906 C C   . ASN D 399 ? 0.4699 0.3844 0.8038 0.0116  0.0962  0.1024  399 ASN D C   
11907 O O   . ASN D 399 ? 0.4771 0.3972 0.7816 0.0207  0.0903  0.0952  399 ASN D O   
11908 C CB  . ASN D 399 ? 0.5462 0.4216 0.9470 -0.0055 0.0992  0.0784  399 ASN D CB  
11909 C CG  . ASN D 399 ? 0.6096 0.4754 1.0404 -0.0208 0.0973  0.0489  399 ASN D CG  
11910 O OD1 . ASN D 399 ? 0.6261 0.4974 1.0800 -0.0344 0.0998  0.0474  399 ASN D OD1 
11911 N ND2 . ASN D 399 ? 0.6136 0.4670 1.0467 -0.0190 0.0933  0.0246  399 ASN D ND2 
11912 N N   . SER D 400 ? 0.4645 0.3843 0.8075 0.0129  0.1047  0.1306  400 SER D N   
11913 C CA  . SER D 400 ? 0.4630 0.3987 0.7779 0.0264  0.1067  0.1529  400 SER D CA  
11914 C C   . SER D 400 ? 0.5163 0.4403 0.8285 0.0380  0.1040  0.1590  400 SER D C   
11915 O O   . SER D 400 ? 0.5577 0.4580 0.9006 0.0366  0.1059  0.1593  400 SER D O   
11916 C CB  . SER D 400 ? 0.4142 0.3611 0.7410 0.0254  0.1178  0.1841  400 SER D CB  
11917 O OG  . SER D 400 ? 0.4239 0.3497 0.7859 0.0243  0.1247  0.2043  400 SER D OG  
11918 N N   . LEU D 401 ? 0.5103 0.4523 0.7881 0.0496  0.0996  0.1627  401 LEU D N   
11919 C CA  . LEU D 401 ? 0.4937 0.4330 0.7679 0.0617  0.0962  0.1708  401 LEU D CA  
11920 C C   . LEU D 401 ? 0.5043 0.4371 0.8038 0.0670  0.1041  0.2044  401 LEU D C   
11921 O O   . LEU D 401 ? 0.4970 0.4130 0.8182 0.0736  0.1039  0.2111  401 LEU D O   
11922 C CB  . LEU D 401 ? 0.4716 0.4378 0.7057 0.0714  0.0905  0.1698  401 LEU D CB  
11923 C CG  . LEU D 401 ? 0.4640 0.4327 0.6762 0.0672  0.0833  0.1388  401 LEU D CG  
11924 C CD1 . LEU D 401 ? 0.4538 0.4440 0.6338 0.0759  0.0774  0.1346  401 LEU D CD1 
11925 C CD2 . LEU D 401 ? 0.4633 0.4097 0.6932 0.0621  0.0795  0.1171  401 LEU D CD2 
11926 N N   . LYS D 402 ? 0.4886 0.4354 0.7879 0.0642  0.1122  0.2266  402 LYS D N   
11927 C CA  . LYS D 402 ? 0.5136 0.4600 0.8329 0.0698  0.1212  0.2650  402 LYS D CA  
11928 C C   . LYS D 402 ? 0.5087 0.4268 0.8715 0.0608  0.1237  0.2570  402 LYS D C   
11929 O O   . LYS D 402 ? 0.5127 0.4278 0.8923 0.0667  0.1258  0.2733  402 LYS D O   
11930 C CB  . LYS D 402 ? 0.5534 0.5245 0.8631 0.0659  0.1304  0.2857  402 LYS D CB  
11931 C CG  . LYS D 402 ? 0.6685 0.6480 0.9986 0.0665  0.1386  0.3143  402 LYS D CG  
11932 C CD  . LYS D 402 ? 0.7195 0.7307 1.0331 0.0646  0.1473  0.3315  402 LYS D CD  
11933 C CE  . LYS D 402 ? 0.7738 0.7924 1.1119 0.0626  0.1565  0.3583  402 LYS D CE  
11934 N NZ  . LYS D 402 ? 0.7848 0.8456 1.0942 0.0689  0.1629  0.3803  402 LYS D NZ  
11935 N N   . SER D 403 ? 0.5085 0.4075 0.8891 0.0470  0.1230  0.2299  403 SER D N   
11936 C CA  . SER D 403 ? 0.5361 0.4102 0.9569 0.0378  0.1246  0.2150  403 SER D CA  
11937 C C   . SER D 403 ? 0.5744 0.4326 1.0009 0.0451  0.1187  0.1989  403 SER D C   
11938 O O   . SER D 403 ? 0.6289 0.4685 1.0882 0.0412  0.1212  0.1913  403 SER D O   
11939 C CB  . SER D 403 ? 0.5357 0.4008 0.9716 0.0206  0.1242  0.1877  403 SER D CB  
11940 O OG  . SER D 403 ? 0.5219 0.3781 0.9471 0.0196  0.1160  0.1563  403 SER D OG  
11941 N N   . TYR D 404 ? 0.5477 0.4141 0.9446 0.0557  0.1112  0.1921  404 TYR D N   
11942 C CA  . TYR D 404 ? 0.5421 0.3991 0.9439 0.0643  0.1062  0.1802  404 TYR D CA  
11943 C C   . TYR D 404 ? 0.5608 0.4324 0.9551 0.0800  0.1061  0.2109  404 TYR D C   
11944 O O   . TYR D 404 ? 0.5546 0.4229 0.9539 0.0891  0.1024  0.2074  404 TYR D O   
11945 C CB  . TYR D 404 ? 0.4825 0.3421 0.8610 0.0670  0.0981  0.1531  404 TYR D CB  
11946 C CG  . TYR D 404 ? 0.4456 0.2946 0.8292 0.0530  0.0971  0.1214  404 TYR D CG  
11947 C CD1 . TYR D 404 ? 0.4524 0.2855 0.8585 0.0459  0.0967  0.0940  404 TYR D CD1 
11948 C CD2 . TYR D 404 ? 0.4281 0.2932 0.7870 0.0458  0.0948  0.1156  404 TYR D CD2 
11949 C CE1 . TYR D 404 ? 0.4511 0.2804 0.8596 0.0332  0.0947  0.0642  404 TYR D CE1 
11950 C CE2 . TYR D 404 ? 0.4448 0.3096 0.8030 0.0329  0.0918  0.0867  404 TYR D CE2 
11951 C CZ  . TYR D 404 ? 0.4584 0.3047 0.8424 0.0267  0.0917  0.0618  404 TYR D CZ  
11952 O OH  . TYR D 404 ? 0.4478 0.3007 0.8279 0.0140  0.0876  0.0334  404 TYR D OH  
11953 N N   . GLY D 405 ? 0.5849 0.4762 0.9673 0.0830  0.1103  0.2410  405 GLY D N   
11954 C CA  . GLY D 405 ? 0.5831 0.4972 0.9523 0.0980  0.1093  0.2713  405 GLY D CA  
11955 C C   . GLY D 405 ? 0.5631 0.5028 0.8935 0.1099  0.1002  0.2702  405 GLY D C   
11956 O O   . GLY D 405 ? 0.5415 0.5020 0.8613 0.1233  0.0961  0.2879  405 GLY D O   
11957 N N   . LYS D 406 ? 0.5485 0.4891 0.8589 0.1051  0.0971  0.2497  406 LYS D N   
11958 C CA  . LYS D 406 ? 0.5093 0.4750 0.7834 0.1123  0.0874  0.2367  406 LYS D CA  
11959 C C   . LYS D 406 ? 0.4918 0.4866 0.7297 0.1087  0.0879  0.2380  406 LYS D C   
11960 O O   . LYS D 406 ? 0.5011 0.4937 0.7434 0.1003  0.0959  0.2455  406 LYS D O   
11961 C CB  . LYS D 406 ? 0.4628 0.4138 0.7355 0.1049  0.0815  0.1972  406 LYS D CB  
11962 C CG  . LYS D 406 ? 0.4998 0.4222 0.8084 0.1070  0.0824  0.1879  406 LYS D CG  
11963 C CD  . LYS D 406 ? 0.5906 0.5255 0.9014 0.1228  0.0770  0.1983  406 LYS D CD  
11964 C CE  . LYS D 406 ? 0.6906 0.6027 1.0332 0.1220  0.0789  0.1883  406 LYS D CE  
11965 N NZ  . LYS D 406 ? 0.7350 0.6234 1.0904 0.1098  0.0805  0.1537  406 LYS D NZ  
11966 N N   . THR D 407 ? 0.4546 0.4785 0.6592 0.1152  0.0798  0.2295  407 THR D N   
11967 C CA  . THR D 407 ? 0.4179 0.4676 0.5877 0.1118  0.0794  0.2201  407 THR D CA  
11968 C C   . THR D 407 ? 0.3999 0.4548 0.5491 0.1098  0.0699  0.1870  407 THR D C   
11969 O O   . THR D 407 ? 0.4118 0.4582 0.5709 0.1126  0.0639  0.1771  407 THR D O   
11970 C CB  . THR D 407 ? 0.4417 0.5296 0.5898 0.1223  0.0803  0.2462  407 THR D CB  
11971 O OG1 . THR D 407 ? 0.4519 0.5609 0.5885 0.1330  0.0700  0.2451  407 THR D OG1 
11972 C CG2 . THR D 407 ? 0.4885 0.5723 0.6605 0.1262  0.0902  0.2862  407 THR D CG2 
11973 N N   . CYS D 408 ? 0.3699 0.4392 0.4929 0.1052  0.0697  0.1706  408 CYS D N   
11974 C CA  . CYS D 408 ? 0.3736 0.4467 0.4794 0.1024  0.0622  0.1413  408 CYS D CA  
11975 C C   . CYS D 408 ? 0.4101 0.5122 0.5016 0.1116  0.0538  0.1427  408 CYS D C   
11976 O O   . CYS D 408 ? 0.4385 0.5428 0.5238 0.1093  0.0470  0.1205  408 CYS D O   
11977 C CB  . CYS D 408 ? 0.3700 0.4487 0.4559 0.0962  0.0652  0.1241  408 CYS D CB  
11978 S SG  . CYS D 408 ? 0.4176 0.4635 0.5182 0.0842  0.0683  0.1060  408 CYS D SG  
11979 N N   . SER D 409 ? 0.4234 0.5511 0.5102 0.1217  0.0541  0.1692  409 SER D N   
11980 C CA  . SER D 409 ? 0.4264 0.5864 0.5019 0.1309  0.0444  0.1713  409 SER D CA  
11981 C C   . SER D 409 ? 0.4514 0.6002 0.5536 0.1377  0.0399  0.1808  409 SER D C   
11982 O O   . SER D 409 ? 0.4729 0.6407 0.5719 0.1419  0.0305  0.1707  409 SER D O   
11983 C CB  . SER D 409 ? 0.4989 0.6997 0.5548 0.1406  0.0451  0.1962  409 SER D CB  
11984 O OG  . SER D 409 ? 0.5470 0.7640 0.5763 0.1355  0.0491  0.1819  409 SER D OG  
11985 N N   . ASN D 410 ? 0.4634 0.5821 0.5947 0.1388  0.0468  0.1986  410 ASN D N   
11986 C CA  . ASN D 410 ? 0.4592 0.5669 0.6195 0.1476  0.0439  0.2086  410 ASN D CA  
11987 C C   . ASN D 410 ? 0.4634 0.5312 0.6485 0.1393  0.0467  0.1867  410 ASN D C   
11988 O O   . ASN D 410 ? 0.4960 0.5501 0.7093 0.1462  0.0464  0.1914  410 ASN D O   
11989 C CB  . ASN D 410 ? 0.4662 0.5733 0.6469 0.1589  0.0496  0.2501  410 ASN D CB  
11990 C CG  . ASN D 410 ? 0.4849 0.5567 0.6868 0.1504  0.0619  0.2602  410 ASN D CG  
11991 O OD1 . ASN D 410 ? 0.5050 0.5447 0.7204 0.1389  0.0652  0.2369  410 ASN D OD1 
11992 N ND2 . ASN D 410 ? 0.4972 0.5778 0.7034 0.1559  0.0690  0.2962  410 ASN D ND2 
11993 N N   . LEU D 411 ? 0.4281 0.4799 0.6031 0.1256  0.0495  0.1627  411 LEU D N   
11994 C CA  . LEU D 411 ? 0.4068 0.4282 0.6006 0.1178  0.0513  0.1407  411 LEU D CA  
11995 C C   . LEU D 411 ? 0.4466 0.4782 0.6416 0.1216  0.0441  0.1240  411 LEU D C   
11996 O O   . LEU D 411 ? 0.4133 0.4277 0.6328 0.1233  0.0454  0.1163  411 LEU D O   
11997 C CB  . LEU D 411 ? 0.3639 0.3736 0.5439 0.1039  0.0543  0.1209  411 LEU D CB  
11998 C CG  . LEU D 411 ? 0.3888 0.3703 0.5872 0.0951  0.0570  0.1013  411 LEU D CG  
11999 C CD1 . LEU D 411 ? 0.3787 0.3360 0.6110 0.0955  0.0634  0.1131  411 LEU D CD1 
12000 C CD2 . LEU D 411 ? 0.4175 0.3956 0.5992 0.0836  0.0583  0.0858  411 LEU D CD2 
12001 N N   . PHE D 412 ? 0.4489 0.5107 0.6193 0.1227  0.0371  0.1175  412 PHE D N   
12002 C CA  . PHE D 412 ? 0.3807 0.4601 0.5523 0.1256  0.0298  0.1035  412 PHE D CA  
12003 C C   . PHE D 412 ? 0.4099 0.5289 0.5716 0.1368  0.0218  0.1191  412 PHE D C   
12004 O O   . PHE D 412 ? 0.4515 0.5874 0.5951 0.1393  0.0218  0.1338  412 PHE D O   
12005 C CB  . PHE D 412 ? 0.3575 0.4371 0.5113 0.1128  0.0284  0.0747  412 PHE D CB  
12006 C CG  . PHE D 412 ? 0.3460 0.3940 0.5033 0.1019  0.0351  0.0611  412 PHE D CG  
12007 C CD1 . PHE D 412 ? 0.3505 0.3812 0.5277 0.1002  0.0378  0.0503  412 PHE D CD1 
12008 C CD2 . PHE D 412 ? 0.3408 0.3801 0.4820 0.0942  0.0388  0.0590  412 PHE D CD2 
12009 C CE1 . PHE D 412 ? 0.3332 0.3413 0.5113 0.0903  0.0429  0.0373  412 PHE D CE1 
12010 C CE2 . PHE D 412 ? 0.3187 0.3344 0.4634 0.0851  0.0436  0.0479  412 PHE D CE2 
12011 C CZ  . PHE D 412 ? 0.3251 0.3263 0.4869 0.0827  0.0452  0.0371  412 PHE D CZ  
12012 N N   . ASP D 413 ? 0.4331 0.5713 0.6067 0.1438  0.0150  0.1155  413 ASP D N   
12013 C CA  . ASP D 413 ? 0.4495 0.6328 0.6148 0.1547  0.0051  0.1283  413 ASP D CA  
12014 C C   . ASP D 413 ? 0.4296 0.6403 0.5659 0.1448  -0.0011 0.1059  413 ASP D C   
12015 O O   . ASP D 413 ? 0.4067 0.6184 0.5451 0.1359  -0.0036 0.0805  413 ASP D O   
12016 C CB  . ASP D 413 ? 0.4534 0.6508 0.6455 0.1658  -0.0004 0.1307  413 ASP D CB  
12017 C CG  . ASP D 413 ? 0.4967 0.7429 0.6855 0.1807  -0.0111 0.1520  413 ASP D CG  
12018 O OD1 . ASP D 413 ? 0.5344 0.8125 0.6936 0.1779  -0.0168 0.1512  413 ASP D OD1 
12019 O OD2 . ASP D 413 ? 0.5093 0.7648 0.7254 0.1958  -0.0140 0.1685  413 ASP D OD2 
12020 N N   . LEU D 414 ? 0.4497 0.6834 0.5608 0.1463  -0.0027 0.1151  414 LEU D N   
12021 C CA  . LEU D 414 ? 0.4265 0.6851 0.5108 0.1369  -0.0075 0.0911  414 LEU D CA  
12022 C C   . LEU D 414 ? 0.4911 0.8060 0.5621 0.1456  -0.0191 0.0970  414 LEU D C   
12023 O O   . LEU D 414 ? 0.5178 0.8594 0.5639 0.1399  -0.0228 0.0804  414 LEU D O   
12024 C CB  . LEU D 414 ? 0.3942 0.6380 0.4572 0.1301  0.0008  0.0887  414 LEU D CB  
12025 C CG  . LEU D 414 ? 0.3681 0.5630 0.4401 0.1208  0.0114  0.0822  414 LEU D CG  
12026 C CD1 . LEU D 414 ? 0.3849 0.5771 0.4364 0.1170  0.0183  0.0823  414 LEU D CD1 
12027 C CD2 . LEU D 414 ? 0.3487 0.5247 0.4279 0.1091  0.0111  0.0537  414 LEU D CD2 
12028 N N   . ASN D 415 ? 0.5394 0.8743 0.6281 0.1602  -0.0251 0.1203  415 ASN D N   
12029 C CA  . ASN D 415 ? 0.6071 1.0026 0.6854 0.1705  -0.0383 0.1289  415 ASN D CA  
12030 C C   . ASN D 415 ? 0.6137 1.0362 0.6987 0.1632  -0.0489 0.0988  415 ASN D C   
12031 O O   . ASN D 415 ? 0.5721 0.9701 0.6822 0.1587  -0.0467 0.0869  415 ASN D O   
12032 C CB  . ASN D 415 ? 0.6596 1.0657 0.7579 0.1909  -0.0402 0.1696  415 ASN D CB  
12033 C CG  . ASN D 415 ? 0.6972 1.0730 0.7954 0.1963  -0.0281 0.2004  415 ASN D CG  
12034 O OD1 . ASN D 415 ? 0.7392 1.1204 0.8104 0.1915  -0.0234 0.2022  415 ASN D OD1 
12035 N ND2 . ASN D 415 ? 0.6795 1.0227 0.8108 0.2055  -0.0221 0.2230  415 ASN D ND2 
12036 N N   . ASN D 416 ? 0.6709 1.1458 0.7349 0.1612  -0.0599 0.0853  416 ASN D N   
12037 C CA  . ASN D 416 ? 0.7472 1.2430 0.8169 0.1482  -0.0681 0.0495  416 ASN D CA  
12038 C C   . ASN D 416 ? 0.7484 1.2919 0.8397 0.1586  -0.0819 0.0564  416 ASN D C   
12039 O O   . ASN D 416 ? 0.7781 1.3682 0.8625 0.1749  -0.0915 0.0815  416 ASN D O   
12040 C CB  . ASN D 416 ? 0.8431 1.3681 0.8816 0.1370  -0.0721 0.0225  416 ASN D CB  
12041 C CG  . ASN D 416 ? 0.9349 1.4941 0.9807 0.1242  -0.0828 -0.0131 416 ASN D CG  
12042 O OD1 . ASN D 416 ? 0.9716 1.5896 1.0024 0.1258  -0.0953 -0.0220 416 ASN D OD1 
12043 N ND2 . ASN D 416 ? 0.9708 1.4957 1.0392 0.1102  -0.0777 -0.0344 416 ASN D ND2 
12044 N N   . PRO D 417 ? 0.6915 1.2268 0.8095 0.1497  -0.0828 0.0355  417 PRO D N   
12045 C CA  . PRO D 417 ? 0.6906 1.2781 0.8303 0.1574  -0.0965 0.0362  417 PRO D CA  
12046 C C   . PRO D 417 ? 0.7195 1.3677 0.8447 0.1477  -0.1110 0.0098  417 PRO D C   
12047 O O   . PRO D 417 ? 0.7387 1.4460 0.8553 0.1607  -0.1246 0.0242  417 PRO D O   
12048 C CB  . PRO D 417 ? 0.6381 1.1934 0.8105 0.1492  -0.0894 0.0214  417 PRO D CB  
12049 C CG  . PRO D 417 ? 0.6029 1.1016 0.7643 0.1305  -0.0755 0.0009  417 PRO D CG  
12050 C CD  . PRO D 417 ? 0.6246 1.1070 0.7537 0.1325  -0.0710 0.0118  417 PRO D CD  
12051 N N   . LYS E 11  ? 0.7985 0.8883 1.3392 0.1341  -0.0218 0.2726  11  LYS E N   
12052 C CA  . LYS E 11  ? 0.7503 0.8513 1.2302 0.1267  -0.0302 0.2552  11  LYS E CA  
12053 C C   . LYS E 11  ? 0.7210 0.8583 1.2115 0.1249  -0.0402 0.2499  11  LYS E C   
12054 O O   . LYS E 11  ? 0.7238 0.8952 1.2268 0.1187  -0.0652 0.2748  11  LYS E O   
12055 C CB  . LYS E 11  ? 0.7301 0.8407 1.1493 0.1125  -0.0555 0.2749  11  LYS E CB  
12056 C CG  . LYS E 11  ? 0.6816 0.7533 1.0641 0.1120  -0.0397 0.2612  11  LYS E CG  
12057 C CD  . LYS E 11  ? 0.6704 0.7454 1.0006 0.0964  -0.0595 0.2834  11  LYS E CD  
12058 C CE  . LYS E 11  ? 0.8635 0.8959 1.1646 0.0932  -0.0390 0.2657  11  LYS E CE  
12059 N NZ  . LYS E 11  ? 0.8317 0.8369 1.1190 0.0944  -0.0108 0.2190  11  LYS E NZ  
12060 N N   . PRO E 12  ? 0.6652 0.7944 1.1521 0.1291  -0.0188 0.2164  12  PRO E N   
12061 C CA  . PRO E 12  ? 0.6324 0.7887 1.1350 0.1284  -0.0184 0.2034  12  PRO E CA  
12062 C C   . PRO E 12  ? 0.6059 0.8020 1.0646 0.1139  -0.0483 0.2119  12  PRO E C   
12063 O O   . PRO E 12  ? 0.6270 0.8167 1.0186 0.0998  -0.0584 0.2095  12  PRO E O   
12064 C CB  . PRO E 12  ? 0.6055 0.7315 1.0888 0.1294  0.0158  0.1612  12  PRO E CB  
12065 C CG  . PRO E 12  ? 0.6015 0.6962 1.0228 0.1209  0.0199  0.1498  12  PRO E CG  
12066 C CD  . PRO E 12  ? 0.6324 0.7220 1.0802 0.1275  0.0074  0.1834  12  PRO E CD  
12067 N N   . ASN E 13  ? 0.5519 0.7812 1.0357 0.1108  -0.0574 0.2131  13  ASN E N   
12068 C CA  . ASN E 13  ? 0.5016 0.7707 0.9480 0.0933  -0.0838 0.2180  13  ASN E CA  
12069 C C   . ASN E 13  ? 0.5132 0.7775 0.9255 0.0853  -0.0658 0.1793  13  ASN E C   
12070 O O   . ASN E 13  ? 0.5728 0.8610 0.9465 0.0677  -0.0796 0.1728  13  ASN E O   
12071 C CB  . ASN E 13  ? 0.4710 0.7735 0.9506 0.0876  -0.1055 0.2398  13  ASN E CB  
12072 C CG  . ASN E 13  ? 0.5215 0.8271 0.9989 0.0824  -0.1273 0.2746  13  ASN E CG  
12073 O OD1 . ASN E 13  ? 0.5396 0.8406 0.9637 0.0708  -0.1389 0.2830  13  ASN E OD1 
12074 N ND2 . ASN E 13  ? 0.5588 0.8718 1.0965 0.0902  -0.1313 0.2958  13  ASN E ND2 
12075 N N   . LEU E 14  ? 0.4329 0.6656 0.8587 0.0958  -0.0337 0.1533  14  LEU E N   
12076 C CA  . LEU E 14  ? 0.3451 0.5722 0.7401 0.0878  -0.0165 0.1207  14  LEU E CA  
12077 C C   . LEU E 14  ? 0.3026 0.4856 0.6827 0.0932  0.0163  0.0939  14  LEU E C   
12078 O O   . LEU E 14  ? 0.3228 0.4878 0.7468 0.1058  0.0335  0.0951  14  LEU E O   
12079 C CB  . LEU E 14  ? 0.2978 0.5587 0.7457 0.0894  -0.0175 0.1217  14  LEU E CB  
12080 C CG  . LEU E 14  ? 0.2645 0.5309 0.6831 0.0772  -0.0070 0.0949  14  LEU E CG  
12081 C CD1 . LEU E 14  ? 0.2319 0.5199 0.5993 0.0578  -0.0298 0.0961  14  LEU E CD1 
12082 C CD2 . LEU E 14  ? 0.2427 0.5348 0.7290 0.0829  0.0007  0.0943  14  LEU E CD2 
12083 N N   . LEU E 15  ? 0.2670 0.4333 0.5855 0.0818  0.0242  0.0712  15  LEU E N   
12084 C CA  . LEU E 15  ? 0.2653 0.3951 0.5584 0.0811  0.0509  0.0465  15  LEU E CA  
12085 C C   . LEU E 15  ? 0.2813 0.4132 0.5556 0.0728  0.0636  0.0263  15  LEU E C   
12086 O O   . LEU E 15  ? 0.3057 0.4600 0.5673 0.0650  0.0507  0.0280  15  LEU E O   
12087 C CB  . LEU E 15  ? 0.2771 0.3834 0.5152 0.0745  0.0467  0.0429  15  LEU E CB  
12088 C CG  . LEU E 15  ? 0.3222 0.4267 0.5697 0.0796  0.0321  0.0646  15  LEU E CG  
12089 C CD1 . LEU E 15  ? 0.2659 0.3520 0.4593 0.0707  0.0281  0.0590  15  LEU E CD1 
12090 C CD2 . LEU E 15  ? 0.3768 0.4636 0.6752 0.0925  0.0485  0.0682  15  LEU E CD2 
12091 N N   . VAL E 16  ? 0.2918 0.3992 0.5632 0.0720  0.0908  0.0066  16  VAL E N   
12092 C CA  . VAL E 16  ? 0.2799 0.3877 0.5377 0.0637  0.1061  -0.0102 16  VAL E CA  
12093 C C   . VAL E 16  ? 0.2977 0.3736 0.5024 0.0531  0.1228  -0.0281 16  VAL E C   
12094 O O   . VAL E 16  ? 0.3156 0.3676 0.5184 0.0530  0.1389  -0.0375 16  VAL E O   
12095 C CB  . VAL E 16  ? 0.2922 0.4093 0.6099 0.0700  0.1266  -0.0160 16  VAL E CB  
12096 C CG1 . VAL E 16  ? 0.2750 0.3926 0.5748 0.0592  0.1429  -0.0326 16  VAL E CG1 
12097 C CG2 . VAL E 16  ? 0.2681 0.4217 0.6482 0.0806  0.1067  0.0063  16  VAL E CG2 
12098 N N   . LEU E 17  ? 0.2878 0.3641 0.4512 0.0425  0.1187  -0.0319 17  LEU E N   
12099 C CA  . LEU E 17  ? 0.3101 0.3618 0.4230 0.0301  0.1298  -0.0433 17  LEU E CA  
12100 C C   . LEU E 17  ? 0.3360 0.3881 0.4374 0.0203  0.1452  -0.0522 17  LEU E C   
12101 O O   . LEU E 17  ? 0.3658 0.4316 0.4640 0.0181  0.1360  -0.0462 17  LEU E O   
12102 C CB  . LEU E 17  ? 0.3708 0.4188 0.4442 0.0259  0.1093  -0.0344 17  LEU E CB  
12103 C CG  . LEU E 17  ? 0.4211 0.4491 0.4455 0.0120  0.1149  -0.0405 17  LEU E CG  
12104 C CD1 . LEU E 17  ? 0.4358 0.4425 0.4469 0.0067  0.1281  -0.0521 17  LEU E CD1 
12105 C CD2 . LEU E 17  ? 0.4192 0.4498 0.4211 0.0100  0.0942  -0.0288 17  LEU E CD2 
12106 N N   . PRO E 18  ? 0.3591 0.3945 0.4543 0.0124  0.1717  -0.0678 18  PRO E N   
12107 C CA  . PRO E 18  ? 0.3751 0.4081 0.4526 0.0001  0.1885  -0.0754 18  PRO E CA  
12108 C C   . PRO E 18  ? 0.4052 0.4283 0.4244 -0.0134 0.1778  -0.0679 18  PRO E C   
12109 O O   . PRO E 18  ? 0.4186 0.4284 0.4020 -0.0194 0.1689  -0.0656 18  PRO E O   
12110 C CB  . PRO E 18  ? 0.4059 0.4204 0.4858 -0.0083 0.2219  -0.0962 18  PRO E CB  
12111 C CG  . PRO E 18  ? 0.3974 0.4122 0.5254 0.0066  0.2235  -0.0978 18  PRO E CG  
12112 C CD  . PRO E 18  ? 0.3551 0.3735 0.4663 0.0137  0.1915  -0.0808 18  PRO E CD  
12113 N N   . VAL E 19  ? 0.4055 0.4363 0.4215 -0.0180 0.1781  -0.0623 19  VAL E N   
12114 C CA  . VAL E 19  ? 0.3955 0.4184 0.3686 -0.0289 0.1677  -0.0499 19  VAL E CA  
12115 C C   . VAL E 19  ? 0.4429 0.4582 0.3972 -0.0438 0.1891  -0.0538 19  VAL E C   
12116 O O   . VAL E 19  ? 0.4286 0.4516 0.4143 -0.0422 0.2075  -0.0639 19  VAL E O   
12117 C CB  A VAL E 19  ? 0.3504 0.3883 0.3427 -0.0200 0.1468  -0.0363 19  VAL E CB  
12118 C CB  B VAL E 19  ? 0.3509 0.3881 0.3411 -0.0204 0.1463  -0.0358 19  VAL E CB  
12119 C CG1 A VAL E 19  ? 0.3437 0.3728 0.3060 -0.0290 0.1385  -0.0211 19  VAL E CG1 
12120 C CG1 B VAL E 19  ? 0.3314 0.3761 0.3366 -0.0085 0.1279  -0.0329 19  VAL E CG1 
12121 C CG2 A VAL E 19  ? 0.3314 0.3766 0.3379 -0.0083 0.1282  -0.0331 19  VAL E CG2 
12122 C CG2 B VAL E 19  ? 0.3349 0.3887 0.3621 -0.0173 0.1538  -0.0391 19  VAL E CG2 
12123 N N   . GLN E 20  ? 0.5168 0.5185 0.4212 -0.0596 0.1859  -0.0434 20  GLN E N   
12124 C CA  . GLN E 20  ? 0.5373 0.5292 0.4138 -0.0778 0.2063  -0.0442 20  GLN E CA  
12125 C C   . GLN E 20  ? 0.5161 0.5063 0.3735 -0.0841 0.1922  -0.0190 20  GLN E C   
12126 O O   . GLN E 20  ? 0.5093 0.4992 0.3534 -0.0824 0.1681  -0.0010 20  GLN E O   
12127 C CB  . GLN E 20  ? 0.6229 0.5973 0.4476 -0.0991 0.2218  -0.0560 20  GLN E CB  
12128 C CG  . GLN E 20  ? 0.7749 0.7395 0.5779 -0.1166 0.2394  -0.0595 20  GLN E CG  
12129 C CD  . GLN E 20  ? 0.8977 0.8459 0.6653 -0.1353 0.2507  -0.0767 20  GLN E CD  
12130 O OE1 . GLN E 20  ? 0.9130 0.8565 0.6916 -0.1318 0.2553  -0.0939 20  GLN E OE1 
12131 N NE2 . GLN E 20  ? 0.9781 0.9164 0.7035 -0.1569 0.2561  -0.0720 20  GLN E NE2 
12132 N N   . GLU E 21  ? 0.5240 0.5126 0.3857 -0.0913 0.2089  -0.0169 21  GLU E N   
12133 C CA  . GLU E 21  ? 0.5346 0.5182 0.3832 -0.0985 0.2006  0.0086  21  GLU E CA  
12134 C C   . GLU E 21  ? 0.5941 0.5628 0.3767 -0.1232 0.2006  0.0236  21  GLU E C   
12135 O O   . GLU E 21  ? 0.6288 0.5897 0.3804 -0.1384 0.2186  0.0077  21  GLU E O   
12136 C CB  . GLU E 21  ? 0.5426 0.5299 0.4249 -0.0975 0.2200  0.0043  21  GLU E CB  
12137 C CG  . GLU E 21  ? 0.5687 0.5529 0.4635 -0.0966 0.2103  0.0288  21  GLU E CG  
12138 C CD  . GLU E 21  ? 0.6756 0.6440 0.5330 -0.1168 0.2214  0.0480  21  GLU E CD  
12139 O OE1 . GLU E 21  ? 0.7349 0.6959 0.5502 -0.1335 0.2361  0.0398  21  GLU E OE1 
12140 O OE2 . GLU E 21  ? 0.7030 0.6660 0.5747 -0.1165 0.2155  0.0717  21  GLU E OE2 
12141 N N   . ASP E 22  ? 0.6148 0.5820 0.3826 -0.1260 0.1761  0.0542  22  ASP E N   
12142 C CA  . ASP E 22  ? 0.6445 0.6026 0.3512 -0.1512 0.1687  0.0775  22  ASP E CA  
12143 C C   . ASP E 22  ? 0.7107 0.6622 0.4207 -0.1583 0.1753  0.1021  22  ASP E C   
12144 O O   . ASP E 22  ? 0.6916 0.6460 0.4471 -0.1429 0.1645  0.1203  22  ASP E O   
12145 C CB  . ASP E 22  ? 0.6455 0.6097 0.3405 -0.1504 0.1343  0.1009  22  ASP E CB  
12146 C CG  . ASP E 22  ? 0.7272 0.6888 0.3684 -0.1741 0.1184  0.1276  22  ASP E CG  
12147 O OD1 . ASP E 22  ? 0.7678 0.7256 0.3677 -0.1902 0.1254  0.1088  22  ASP E OD1 
12148 O OD2 . ASP E 22  ? 0.7351 0.7000 0.3886 -0.1725 0.0965  0.1652  22  ASP E OD2 
12149 N N   . ALA E 23  ? 0.7929 0.7383 0.4734 -0.1732 0.1892  0.0972  23  ALA E N   
12150 C CA  . ALA E 23  ? 0.8225 0.7616 0.5109 -0.1783 0.1989  0.1165  23  ALA E CA  
12151 C C   . ALA E 23  ? 0.8652 0.8015 0.5463 -0.1821 0.1736  0.1637  23  ALA E C   
12152 O O   . ALA E 23  ? 0.8595 0.7906 0.5779 -0.1755 0.1763  0.1859  23  ALA E O   
12153 C CB  . ALA E 23  ? 0.8465 0.7794 0.4999 -0.1953 0.2177  0.1003  23  ALA E CB  
12154 N N   . SER E 24  ? 0.8967 0.8365 0.5367 -0.1920 0.1486  0.1776  24  SER E N   
12155 C CA  . SER E 24  ? 0.9163 0.8562 0.5531 -0.1945 0.1204  0.2218  24  SER E CA  
12156 C C   . SER E 24  ? 0.8524 0.7945 0.5503 -0.1744 0.1060  0.2445  24  SER E C   
12157 O O   . SER E 24  ? 0.8637 0.7980 0.5936 -0.1691 0.1021  0.2749  24  SER E O   
12158 C CB  . SER E 24  ? 0.9718 0.9210 0.5612 -0.2089 0.0940  0.2249  24  SER E CB  
12159 O OG  . SER E 24  ? 1.0263 0.9807 0.6244 -0.2089 0.0629  0.2674  24  SER E OG  
12160 N N   . THR E 25  ? 0.8148 0.7668 0.5333 -0.1634 0.0999  0.2281  25  THR E N   
12161 C CA  . THR E 25  ? 0.7543 0.7130 0.5377 -0.1424 0.0843  0.2452  25  THR E CA  
12162 C C   . THR E 25  ? 0.6816 0.6371 0.5266 -0.1205 0.1068  0.2173  25  THR E C   
12163 O O   . THR E 25  ? 0.6516 0.6078 0.5563 -0.1034 0.1017  0.2269  25  THR E O   
12164 C CB  . THR E 25  ? 0.7171 0.6894 0.5011 -0.1346 0.0615  0.2362  25  THR E CB  
12165 O OG1 . THR E 25  ? 0.6986 0.6723 0.4755 -0.1282 0.0783  0.1904  25  THR E OG1 
12166 C CG2 . THR E 25  ? 0.7698 0.7484 0.5009 -0.1530 0.0363  0.2529  25  THR E CG2 
12167 N N   . GLY E 26  ? 0.6678 0.6218 0.5010 -0.1223 0.1319  0.1811  26  GLY E N   
12168 C CA  . GLY E 26  ? 0.6227 0.5793 0.5106 -0.1052 0.1499  0.1540  26  GLY E CA  
12169 C C   . GLY E 26  ? 0.5753 0.5448 0.4903 -0.0873 0.1393  0.1313  26  GLY E C   
12170 O O   . GLY E 26  ? 0.5426 0.5182 0.5007 -0.0749 0.1491  0.1101  26  GLY E O   
12171 N N   . LEU E 27  ? 0.5613 0.5359 0.4482 -0.0888 0.1192  0.1356  27  LEU E N   
12172 C CA  . LEU E 27  ? 0.4785 0.4638 0.3860 -0.0739 0.1088  0.1170  27  LEU E CA  
12173 C C   . LEU E 27  ? 0.4645 0.4534 0.3464 -0.0760 0.1186  0.0866  27  LEU E C   
12174 O O   . LEU E 27  ? 0.5175 0.5002 0.3636 -0.0904 0.1329  0.0803  27  LEU E O   
12175 C CB  . LEU E 27  ? 0.5033 0.4924 0.4058 -0.0732 0.0816  0.1396  27  LEU E CB  
12176 C CG  . LEU E 27  ? 0.5396 0.5266 0.4802 -0.0690 0.0696  0.1744  27  LEU E CG  
12177 C CD1 . LEU E 27  ? 0.5514 0.5469 0.4883 -0.0699 0.0415  0.1965  27  LEU E CD1 
12178 C CD2 . LEU E 27  ? 0.5243 0.5106 0.5283 -0.0525 0.0819  0.1625  27  LEU E CD2 
12179 N N   . HIS E 28  ? 0.4850 0.4831 0.3885 -0.0622 0.1130  0.0685  28  HIS E N   
12180 C CA  . HIS E 28  ? 0.4726 0.4745 0.3663 -0.0604 0.1219  0.0420  28  HIS E CA  
12181 C C   . HIS E 28  ? 0.4746 0.4769 0.3487 -0.0598 0.1056  0.0408  28  HIS E C   
12182 O O   . HIS E 28  ? 0.4664 0.4723 0.3525 -0.0538 0.0869  0.0544  28  HIS E O   
12183 C CB  . HIS E 28  ? 0.4172 0.4315 0.3565 -0.0459 0.1292  0.0234  28  HIS E CB  
12184 C CG  . HIS E 28  ? 0.3903 0.4066 0.3505 -0.0486 0.1474  0.0186  28  HIS E CG  
12185 N ND1 . HIS E 28  ? 0.3868 0.4094 0.3577 -0.0495 0.1656  -0.0004 28  HIS E ND1 
12186 C CD2 . HIS E 28  ? 0.4031 0.4157 0.3805 -0.0512 0.1519  0.0305  28  HIS E CD2 
12187 C CE1 . HIS E 28  ? 0.4144 0.4385 0.4048 -0.0537 0.1795  -0.0007 28  HIS E CE1 
12188 N NE2 . HIS E 28  ? 0.4151 0.4318 0.4085 -0.0550 0.1721  0.0175  28  HIS E NE2 
12189 N N   . TRP E 29  ? 0.4909 0.4888 0.3394 -0.0667 0.1155  0.0232  29  TRP E N   
12190 C CA  . TRP E 29  ? 0.5182 0.5140 0.3465 -0.0692 0.1037  0.0189  29  TRP E CA  
12191 C C   . TRP E 29  ? 0.5291 0.5225 0.3668 -0.0643 0.1204  -0.0078 29  TRP E C   
12192 O O   . TRP E 29  ? 0.5269 0.5206 0.3809 -0.0625 0.1413  -0.0212 29  TRP E O   
12193 C CB  . TRP E 29  ? 0.5648 0.5534 0.3384 -0.0926 0.0964  0.0313  29  TRP E CB  
12194 C CG  . TRP E 29  ? 0.6105 0.5888 0.3476 -0.1115 0.1203  0.0189  29  TRP E CG  
12195 C CD1 . TRP E 29  ? 0.6464 0.6213 0.3743 -0.1204 0.1328  0.0277  29  TRP E CD1 
12196 C CD2 . TRP E 29  ? 0.6691 0.6373 0.3765 -0.1256 0.1396  -0.0071 29  TRP E CD2 
12197 N NE1 . TRP E 29  ? 0.6876 0.6517 0.3785 -0.1402 0.1589  0.0084  29  TRP E NE1 
12198 C CE2 . TRP E 29  ? 0.7164 0.6758 0.3955 -0.1439 0.1647  -0.0145 29  TRP E CE2 
12199 C CE3 . TRP E 29  ? 0.6820 0.6459 0.3864 -0.1256 0.1411  -0.0262 29  TRP E CE3 
12200 C CZ2 . TRP E 29  ? 0.7826 0.7304 0.4451 -0.1570 0.1853  -0.0414 29  TRP E CZ2 
12201 C CZ3 . TRP E 29  ? 0.7331 0.6831 0.4103 -0.1433 0.1688  -0.0534 29  TRP E CZ3 
12202 C CH2 . TRP E 29  ? 0.7787 0.7215 0.4433 -0.1563 0.1871  -0.0606 29  TRP E CH2 
12203 N N   . ALA E 30  ? 0.5345 0.5259 0.3686 -0.0618 0.1120  -0.0142 30  ALA E N   
12204 C CA  . ALA E 30  ? 0.5020 0.4888 0.3526 -0.0561 0.1279  -0.0363 30  ALA E CA  
12205 C C   . ALA E 30  ? 0.5616 0.5354 0.3787 -0.0699 0.1294  -0.0469 30  ALA E C   
12206 O O   . ALA E 30  ? 0.5815 0.5564 0.3754 -0.0770 0.1089  -0.0351 30  ALA E O   
12207 C CB  . ALA E 30  ? 0.4123 0.4111 0.3101 -0.0341 0.1178  -0.0343 30  ALA E CB  
12208 N N   . ASN E 31  ? 0.5844 0.5463 0.4032 -0.0751 0.1551  -0.0702 31  ASN E N   
12209 C CA  . ASN E 31  ? 0.6406 0.5887 0.4405 -0.0858 0.1604  -0.0853 31  ASN E CA  
12210 C C   . ASN E 31  ? 0.6352 0.5856 0.4797 -0.0644 0.1523  -0.0849 31  ASN E C   
12211 O O   . ASN E 31  ? 0.6430 0.5947 0.5347 -0.0479 0.1650  -0.0910 31  ASN E O   
12212 C CB  . ASN E 31  ? 0.7009 0.6313 0.4877 -0.1024 0.1968  -0.1137 31  ASN E CB  
12213 C CG  . ASN E 31  ? 0.7891 0.7123 0.5102 -0.1347 0.2004  -0.1166 31  ASN E CG  
12214 O OD1 . ASN E 31  ? 0.7969 0.7228 0.4743 -0.1508 0.1784  -0.1055 31  ASN E OD1 
12215 N ND2 . ASN E 31  ? 0.8580 0.7746 0.5821 -0.1431 0.2207  -0.1270 31  ASN E ND2 
12216 N N   . ILE E 32  ? 0.6232 0.5749 0.4535 -0.0662 0.1304  -0.0756 32  ILE E N   
12217 C CA  . ILE E 32  ? 0.5657 0.5180 0.4303 -0.0497 0.1221  -0.0732 32  ILE E CA  
12218 C C   . ILE E 32  ? 0.5709 0.5041 0.4231 -0.0620 0.1353  -0.0922 32  ILE E C   
12219 O O   . ILE E 32  ? 0.5597 0.4866 0.3656 -0.0856 0.1337  -0.0992 32  ILE E O   
12220 C CB  . ILE E 32  ? 0.5551 0.5212 0.4193 -0.0433 0.0922  -0.0518 32  ILE E CB  
12221 C CG1 . ILE E 32  ? 0.5293 0.5109 0.4054 -0.0348 0.0838  -0.0366 32  ILE E CG1 
12222 C CG2 . ILE E 32  ? 0.5215 0.4886 0.4185 -0.0276 0.0848  -0.0480 32  ILE E CG2 
12223 C CD1 . ILE E 32  ? 0.4962 0.4865 0.4152 -0.0164 0.0895  -0.0367 32  ILE E CD1 
12224 N N   . HIS E 33  ? 0.6083 0.5331 0.5033 -0.0476 0.1481  -0.0994 33  HIS E N   
12225 C CA  . HIS E 33  ? 0.6399 0.5432 0.5340 -0.0573 0.1643  -0.1184 33  HIS E CA  
12226 C C   . HIS E 33  ? 0.6026 0.5068 0.4984 -0.0534 0.1431  -0.1077 33  HIS E C   
12227 O O   . HIS E 33  ? 0.5441 0.4573 0.4751 -0.0327 0.1298  -0.0903 33  HIS E O   
12228 C CB  . HIS E 33  ? 0.6596 0.5509 0.6088 -0.0430 0.1915  -0.1294 33  HIS E CB  
12229 C CG  . HIS E 33  ? 0.7127 0.6003 0.6669 -0.0488 0.2192  -0.1452 33  HIS E CG  
12230 N ND1 . HIS E 33  ? 0.6895 0.5965 0.6528 -0.0398 0.2126  -0.1327 33  HIS E ND1 
12231 C CD2 . HIS E 33  ? 0.7635 0.6297 0.7169 -0.0644 0.2568  -0.1746 33  HIS E CD2 
12232 C CE1 . HIS E 33  ? 0.7313 0.6299 0.6995 -0.0487 0.2438  -0.1521 33  HIS E CE1 
12233 N NE2 . HIS E 33  ? 0.7767 0.6516 0.7404 -0.0639 0.2677  -0.1751 33  HIS E NE2 
12234 N N   . LYS E 34  ? 0.6223 0.5181 0.4787 -0.0762 0.1407  -0.1187 34  LYS E N   
12235 C CA  . LYS E 34  ? 0.6271 0.5247 0.4825 -0.0769 0.1214  -0.1106 34  LYS E CA  
12236 C C   . LYS E 34  ? 0.6792 0.5566 0.5149 -0.0997 0.1360  -0.1346 34  LYS E C   
12237 O O   . LYS E 34  ? 0.7395 0.6035 0.5479 -0.1213 0.1586  -0.1587 34  LYS E O   
12238 C CB  . LYS E 34  ? 0.6370 0.5569 0.4662 -0.0821 0.0905  -0.0905 34  LYS E CB  
12239 C CG  . LYS E 34  ? 0.6359 0.5734 0.4845 -0.0628 0.0794  -0.0703 34  LYS E CG  
12240 C CD  . LYS E 34  ? 0.6526 0.6085 0.4973 -0.0617 0.0520  -0.0496 34  LYS E CD  
12241 C CE  . LYS E 34  ? 0.6461 0.6018 0.5106 -0.0556 0.0423  -0.0451 34  LYS E CE  
12242 N NZ  . LYS E 34  ? 0.6442 0.6158 0.4992 -0.0643 0.0192  -0.0310 34  LYS E NZ  
12243 N N   . ARG E 35  ? 0.6582 0.5333 0.5072 -0.0970 0.1250  -0.1297 35  ARG E N   
12244 C CA  . ARG E 35  ? 0.6656 0.5251 0.4959 -0.1207 0.1334  -0.1506 35  ARG E CA  
12245 C C   . ARG E 35  ? 0.6890 0.5168 0.5489 -0.1207 0.1702  -0.1754 35  ARG E C   
12246 O O   . ARG E 35  ? 0.7015 0.5199 0.5985 -0.1029 0.1904  -0.1763 35  ARG E O   
12247 C CB  . ARG E 35  ? 0.6761 0.5436 0.4448 -0.1552 0.1272  -0.1627 35  ARG E CB  
12248 C CG  . ARG E 35  ? 0.6506 0.5491 0.4002 -0.1549 0.0899  -0.1341 35  ARG E CG  
12249 C CD  . ARG E 35  ? 0.7113 0.6227 0.4019 -0.1869 0.0788  -0.1357 35  ARG E CD  
12250 N NE  . ARG E 35  ? 0.7196 0.6582 0.4096 -0.1774 0.0479  -0.1027 35  ARG E NE  
12251 C CZ  . ARG E 35  ? 0.7565 0.7134 0.4050 -0.2001 0.0276  -0.0898 35  ARG E CZ  
12252 N NH1 . ARG E 35  ? 0.8187 0.7723 0.4125 -0.2376 0.0324  -0.1077 35  ARG E NH1 
12253 N NH2 . ARG E 35  ? 0.7128 0.6914 0.3752 -0.1870 0.0026  -0.0579 35  ARG E NH2 
12254 N N   . THR E 36  ? 0.6989 0.5107 0.5494 -0.1407 0.1788  -0.1944 36  THR E N   
12255 C CA  . THR E 36  ? 0.7067 0.4843 0.5837 -0.1468 0.2185  -0.2230 36  THR E CA  
12256 C C   . THR E 36  ? 0.7910 0.5652 0.6209 -0.1868 0.2295  -0.2507 36  THR E C   
12257 O O   . THR E 36  ? 0.8257 0.6069 0.6296 -0.2061 0.2126  -0.2532 36  THR E O   
12258 C CB  . THR E 36  ? 0.6797 0.4418 0.6071 -0.1297 0.2213  -0.2138 36  THR E CB  
12259 O OG1 . THR E 36  ? 0.6520 0.4296 0.6173 -0.0953 0.2014  -0.1779 36  THR E OG1 
12260 C CG2 . THR E 36  ? 0.6733 0.4037 0.6440 -0.1300 0.2625  -0.2352 36  THR E CG2 
12261 N N   . PRO E 37  ? 0.8287 0.6000 0.6550 -0.1992 0.2547  -0.2648 37  PRO E N   
12262 C CA  . PRO E 37  ? 0.8089 0.5740 0.6728 -0.1804 0.2773  -0.2638 37  PRO E CA  
12263 C C   . PRO E 37  ? 0.8003 0.5840 0.6446 -0.1669 0.2578  -0.2463 37  PRO E C   
12264 O O   . PRO E 37  ? 0.8294 0.6323 0.6195 -0.1808 0.2303  -0.2377 37  PRO E O   
12265 C CB  . PRO E 37  ? 0.8730 0.6321 0.7210 -0.2111 0.3062  -0.2876 37  PRO E CB  
12266 C CG  . PRO E 37  ? 0.9077 0.6805 0.6884 -0.2460 0.2873  -0.2937 37  PRO E CG  
12267 C CD  . PRO E 37  ? 0.8882 0.6638 0.6705 -0.2386 0.2626  -0.2840 37  PRO E CD  
12268 N N   . LEU E 38  ? 0.7412 0.5223 0.6347 -0.1398 0.2708  -0.2382 38  LEU E N   
12269 C CA  . LEU E 38  ? 0.7229 0.5224 0.6081 -0.1234 0.2552  -0.2211 38  LEU E CA  
12270 C C   . LEU E 38  ? 0.7502 0.5623 0.5811 -0.1488 0.2534  -0.2261 38  LEU E C   
12271 O O   . LEU E 38  ? 0.7868 0.5894 0.6132 -0.1695 0.2766  -0.2439 38  LEU E O   
12272 C CB  . LEU E 38  ? 0.7098 0.5072 0.6674 -0.0918 0.2709  -0.2114 38  LEU E CB  
12273 C CG  . LEU E 38  ? 0.6639 0.4876 0.6458 -0.0629 0.2439  -0.1785 38  LEU E CG  
12274 C CD1 . LEU E 38  ? 0.6022 0.4377 0.5892 -0.0497 0.2104  -0.1522 38  LEU E CD1 
12275 C CD2 . LEU E 38  ? 0.6782 0.4998 0.7325 -0.0389 0.2645  -0.1745 38  LEU E CD2 
12276 N N   . MET E 39  ? 0.7368 0.5694 0.5278 -0.1490 0.2268  -0.2092 39  MET E N   
12277 C CA  . MET E 39  ? 0.7602 0.6045 0.5060 -0.1702 0.2233  -0.2072 39  MET E CA  
12278 C C   . MET E 39  ? 0.7157 0.5803 0.4532 -0.1543 0.2040  -0.1836 39  MET E C   
12279 O O   . MET E 39  ? 0.6973 0.5751 0.4728 -0.1267 0.1822  -0.1599 39  MET E O   
12280 C CB  A MET E 39  ? 0.8062 0.6568 0.4931 -0.2055 0.2067  -0.2097 39  MET E CB  
12281 C CB  B MET E 39  ? 0.8057 0.6566 0.4925 -0.2053 0.2063  -0.2094 39  MET E CB  
12282 C CG  A MET E 39  ? 0.7844 0.6461 0.4566 -0.2048 0.1753  -0.1966 39  MET E CG  
12283 C CG  B MET E 39  ? 0.7835 0.6555 0.4408 -0.2053 0.1664  -0.1858 39  MET E CG  
12284 S SD  A MET E 39  ? 0.7434 0.6352 0.4077 -0.1873 0.1349  -0.1573 39  MET E SD  
12285 S SD  B MET E 39  ? 1.0818 0.9700 0.6788 -0.2468 0.1423  -0.1807 39  MET E SD  
12286 C CE  A MET E 39  ? 0.6964 0.6046 0.2945 -0.2237 0.1178  -0.1479 39  MET E CE  
12287 C CE  B MET E 39  ? 0.7252 0.6419 0.2962 -0.2433 0.1066  -0.1429 39  MET E CE  
12288 N N   . GLN E 40  ? 0.7530 0.6263 0.4591 -0.1688 0.2022  -0.1781 40  GLN E N   
12289 C CA  . GLN E 40  ? 0.7255 0.6159 0.4309 -0.1542 0.1894  -0.1563 40  GLN E CA  
12290 C C   . GLN E 40  ? 0.7450 0.6550 0.4090 -0.1653 0.1530  -0.1297 40  GLN E C   
12291 O O   . GLN E 40  ? 0.8092 0.7213 0.4268 -0.1940 0.1442  -0.1298 40  GLN E O   
12292 C CB  . GLN E 40  ? 0.7308 0.6183 0.4406 -0.1593 0.2101  -0.1625 40  GLN E CB  
12293 C CG  . GLN E 40  ? 0.7661 0.6416 0.5368 -0.1419 0.2405  -0.1790 40  GLN E CG  
12294 C CD  . GLN E 40  ? 0.8553 0.7280 0.6298 -0.1501 0.2605  -0.1861 40  GLN E CD  
12295 O OE1 . GLN E 40  ? 0.9323 0.7958 0.6680 -0.1792 0.2699  -0.1978 40  GLN E OE1 
12296 N NE2 . GLN E 40  ? 0.8569 0.7387 0.6785 -0.1265 0.2668  -0.1791 40  GLN E NE2 
12297 N N   . VAL E 41  ? 0.7016 0.6290 0.3994 -0.1396 0.1277  -0.1019 41  VAL E N   
12298 C CA  . VAL E 41  ? 0.6960 0.6426 0.3740 -0.1438 0.0943  -0.0725 41  VAL E CA  
12299 C C   . VAL E 41  ? 0.6590 0.6157 0.3517 -0.1307 0.0915  -0.0537 41  VAL E C   
12300 O O   . VAL E 41  ? 0.6367 0.5975 0.3771 -0.1045 0.0935  -0.0497 41  VAL E O   
12301 C CB  . VAL E 41  ? 0.6699 0.6272 0.3797 -0.1273 0.0687  -0.0571 41  VAL E CB  
12302 C CG1 . VAL E 41  ? 0.6883 0.6649 0.3835 -0.1351 0.0367  -0.0286 41  VAL E CG1 
12303 C CG2 . VAL E 41  ? 0.6546 0.5997 0.3621 -0.1357 0.0755  -0.0772 41  VAL E CG2 
12304 N N   . PRO E 42  ? 0.6831 0.6440 0.3336 -0.1511 0.0867  -0.0415 42  PRO E N   
12305 C CA  . PRO E 42  ? 0.6356 0.6043 0.3024 -0.1397 0.0843  -0.0222 42  PRO E CA  
12306 C C   . PRO E 42  ? 0.6062 0.5910 0.3037 -0.1236 0.0542  0.0075  42  PRO E C   
12307 O O   . PRO E 42  ? 0.5907 0.5848 0.2691 -0.1362 0.0299  0.0258  42  PRO E O   
12308 C CB  . PRO E 42  ? 0.7106 0.6767 0.3177 -0.1707 0.0884  -0.0166 42  PRO E CB  
12309 C CG  . PRO E 42  ? 0.7614 0.7295 0.3314 -0.1944 0.0723  -0.0183 42  PRO E CG  
12310 C CD  . PRO E 42  ? 0.7364 0.6950 0.3212 -0.1880 0.0839  -0.0447 42  PRO E CD  
12311 N N   . LEU E 43  ? 0.5882 0.5774 0.3353 -0.0979 0.0566  0.0110  43  LEU E N   
12312 C CA  . LEU E 43  ? 0.5328 0.5344 0.3160 -0.0824 0.0355  0.0332  43  LEU E CA  
12313 C C   . LEU E 43  ? 0.5171 0.5219 0.3292 -0.0701 0.0425  0.0420  43  LEU E C   
12314 O O   . LEU E 43  ? 0.5070 0.5081 0.3293 -0.0643 0.0622  0.0268  43  LEU E O   
12315 C CB  . LEU E 43  ? 0.4811 0.4851 0.2973 -0.0659 0.0310  0.0245  43  LEU E CB  
12316 C CG  . LEU E 43  ? 0.4966 0.4966 0.2942 -0.0757 0.0247  0.0150  43  LEU E CG  
12317 C CD1 . LEU E 43  ? 0.4964 0.4968 0.3299 -0.0577 0.0246  0.0078  43  LEU E CD1 
12318 C CD2 . LEU E 43  ? 0.5064 0.5166 0.2863 -0.0907 0.0002  0.0352  43  LEU E CD2 
12319 N N   . LEU E 44  ? 0.5094 0.5218 0.3407 -0.0668 0.0268  0.0667  44  LEU E N   
12320 C CA  . LEU E 44  ? 0.4828 0.4968 0.3467 -0.0565 0.0338  0.0753  44  LEU E CA  
12321 C C   . LEU E 44  ? 0.4305 0.4484 0.3346 -0.0382 0.0415  0.0592  44  LEU E C   
12322 O O   . LEU E 44  ? 0.4535 0.4757 0.3733 -0.0308 0.0326  0.0562  44  LEU E O   
12323 C CB  . LEU E 44  ? 0.4903 0.5097 0.3739 -0.0571 0.0164  0.1065  44  LEU E CB  
12324 C CG  . LEU E 44  ? 0.4789 0.4963 0.4007 -0.0482 0.0266  0.1155  44  LEU E CG  
12325 C CD1 . LEU E 44  ? 0.5199 0.5301 0.4117 -0.0616 0.0358  0.1246  44  LEU E CD1 
12326 C CD2 . LEU E 44  ? 0.4720 0.4941 0.4385 -0.0413 0.0135  0.1405  44  LEU E CD2 
12327 N N   . LEU E 45  ? 0.4155 0.4335 0.3349 -0.0334 0.0575  0.0499  45  LEU E N   
12328 C CA  . LEU E 45  ? 0.3932 0.4189 0.3476 -0.0207 0.0629  0.0370  45  LEU E CA  
12329 C C   . LEU E 45  ? 0.4127 0.4413 0.4004 -0.0160 0.0586  0.0482  45  LEU E C   
12330 O O   . LEU E 45  ? 0.4082 0.4336 0.4090 -0.0186 0.0654  0.0577  45  LEU E O   
12331 C CB  . LEU E 45  ? 0.3973 0.4256 0.3587 -0.0203 0.0805  0.0234  45  LEU E CB  
12332 C CG  . LEU E 45  ? 0.4156 0.4568 0.4116 -0.0117 0.0836  0.0124  45  LEU E CG  
12333 C CD1 . LEU E 45  ? 0.4314 0.4791 0.4301 -0.0048 0.0753  0.0043  45  LEU E CD1 
12334 C CD2 . LEU E 45  ? 0.3733 0.4212 0.3829 -0.0134 0.0989  0.0021  45  LEU E CD2 
12335 N N   . ASP E 46  ? 0.4251 0.4581 0.4293 -0.0100 0.0506  0.0463  46  ASP E N   
12336 C CA  . ASP E 46  ? 0.3907 0.4248 0.4317 -0.0068 0.0514  0.0532  46  ASP E CA  
12337 C C   . ASP E 46  ? 0.3805 0.4218 0.4391 -0.0033 0.0588  0.0341  46  ASP E C   
12338 O O   . ASP E 46  ? 0.3727 0.4171 0.4314 -0.0011 0.0527  0.0296  46  ASP E O   
12339 C CB  . ASP E 46  ? 0.3892 0.4227 0.4380 -0.0066 0.0366  0.0705  46  ASP E CB  
12340 C CG  . ASP E 46  ? 0.4346 0.4678 0.5331 -0.0025 0.0415  0.0780  46  ASP E CG  
12341 O OD1 . ASP E 46  ? 0.4689 0.4995 0.5914 -0.0019 0.0579  0.0692  46  ASP E OD1 
12342 O OD2 . ASP E 46  ? 0.4469 0.4827 0.5651 -0.0009 0.0308  0.0914  46  ASP E OD2 
12343 N N   . LEU E 47  ? 0.3803 0.4248 0.4528 -0.0054 0.0719  0.0236  47  LEU E N   
12344 C CA  . LEU E 47  ? 0.3470 0.4024 0.4285 -0.0076 0.0778  0.0050  47  LEU E CA  
12345 C C   . LEU E 47  ? 0.3411 0.3965 0.4389 -0.0089 0.0789  0.0006  47  LEU E C   
12346 O O   . LEU E 47  ? 0.3316 0.3954 0.4186 -0.0111 0.0754  -0.0094 47  LEU E O   
12347 C CB  . LEU E 47  ? 0.3372 0.3960 0.4361 -0.0137 0.0926  -0.0047 47  LEU E CB  
12348 C CG  . LEU E 47  ? 0.3202 0.3937 0.4263 -0.0219 0.0982  -0.0247 47  LEU E CG  
12349 C CD1 . LEU E 47  ? 0.2880 0.3772 0.3739 -0.0201 0.0861  -0.0282 47  LEU E CD1 
12350 C CD2 . LEU E 47  ? 0.3314 0.4074 0.4585 -0.0315 0.1147  -0.0365 47  LEU E CD2 
12351 N N   . ASN E 48  ? 0.3257 0.3717 0.4522 -0.0082 0.0846  0.0096  48  ASN E N   
12352 C CA  . ASN E 48  ? 0.3181 0.3630 0.4688 -0.0107 0.0921  0.0021  48  ASN E CA  
12353 C C   . ASN E 48  ? 0.3438 0.3872 0.4945 -0.0051 0.0788  0.0147  48  ASN E C   
12354 O O   . ASN E 48  ? 0.3822 0.4243 0.5581 -0.0066 0.0861  0.0102  48  ASN E O   
12355 C CB  . ASN E 48  ? 0.3395 0.3749 0.5364 -0.0131 0.1112  0.0019  48  ASN E CB  
12356 C CG  . ASN E 48  ? 0.3391 0.3765 0.5389 -0.0227 0.1279  -0.0169 48  ASN E CG  
12357 O OD1 . ASN E 48  ? 0.3665 0.4146 0.5483 -0.0326 0.1320  -0.0380 48  ASN E OD1 
12358 N ND2 . ASN E 48  ? 0.3489 0.3774 0.5696 -0.0216 0.1362  -0.0080 48  ASN E ND2 
12359 N N   . GLY E 49  ? 0.3219 0.3655 0.4460 -0.0008 0.0616  0.0286  49  GLY E N   
12360 C CA  . GLY E 49  ? 0.2826 0.3265 0.4048 0.0018  0.0473  0.0403  49  GLY E CA  
12361 C C   . GLY E 49  ? 0.2712 0.3187 0.3826 0.0005  0.0469  0.0271  49  GLY E C   
12362 O O   . GLY E 49  ? 0.3223 0.3731 0.4082 -0.0012 0.0480  0.0151  49  GLY E O   
12363 N N   . LYS E 50  ? 0.3074 0.3551 0.4411 0.0009  0.0447  0.0319  50  LYS E N   
12364 C CA  . LYS E 50  ? 0.2995 0.3490 0.4251 -0.0023 0.0477  0.0197  50  LYS E CA  
12365 C C   . LYS E 50  ? 0.3378 0.3869 0.4280 -0.0012 0.0330  0.0222  50  LYS E C   
12366 O O   . LYS E 50  ? 0.3617 0.4110 0.4367 -0.0037 0.0349  0.0136  50  LYS E O   
12367 C CB  . LYS E 50  ? 0.2842 0.3338 0.4521 -0.0030 0.0542  0.0220  50  LYS E CB  
12368 C CG  . LYS E 50  ? 0.3163 0.3630 0.5241 -0.0061 0.0766  0.0126  50  LYS E CG  
12369 C CD  . LYS E 50  ? 0.3471 0.3938 0.6025 -0.0068 0.0867  0.0125  50  LYS E CD  
12370 C CE  . LYS E 50  ? 0.4022 0.4430 0.7088 -0.0095 0.1132  0.0031  50  LYS E CE  
12371 N NZ  . LYS E 50  ? 0.4710 0.5119 0.8363 -0.0089 0.1258  0.0039  50  LYS E NZ  
12372 N N   . HIS E 51  ? 0.3364 0.3841 0.4136 0.0005  0.0197  0.0341  51  HIS E N   
12373 C CA  . HIS E 51  ? 0.3413 0.3857 0.3882 -0.0006 0.0100  0.0330  51  HIS E CA  
12374 C C   . HIS E 51  ? 0.3986 0.4403 0.4223 -0.0032 0.0017  0.0402  51  HIS E C   
12375 O O   . HIS E 51  ? 0.4409 0.4845 0.4720 -0.0041 0.0006  0.0503  51  HIS E O   
12376 C CB  . HIS E 51  ? 0.3069 0.3525 0.3656 -0.0033 0.0034  0.0362  51  HIS E CB  
12377 C CG  . HIS E 51  ? 0.3312 0.3836 0.4161 -0.0054 -0.0074 0.0521  51  HIS E CG  
12378 N ND1 . HIS E 51  ? 0.3463 0.4045 0.4778 -0.0037 -0.0023 0.0570  51  HIS E ND1 
12379 C CD2 . HIS E 51  ? 0.3548 0.4111 0.4285 -0.0106 -0.0233 0.0660  51  HIS E CD2 
12380 C CE1 . HIS E 51  ? 0.3497 0.4167 0.5043 -0.0052 -0.0170 0.0766  51  HIS E CE1 
12381 N NE2 . HIS E 51  ? 0.3517 0.4186 0.4673 -0.0108 -0.0316 0.0833  51  HIS E NE2 
12382 N N   . LEU E 52  ? 0.3995 0.4354 0.3956 -0.0061 -0.0016 0.0344  52  LEU E N   
12383 C CA  . LEU E 52  ? 0.3761 0.4080 0.3441 -0.0138 -0.0064 0.0368  52  LEU E CA  
12384 C C   . LEU E 52  ? 0.3961 0.4331 0.3625 -0.0238 -0.0223 0.0484  52  LEU E C   
12385 O O   . LEU E 52  ? 0.3877 0.4261 0.3636 -0.0250 -0.0271 0.0462  52  LEU E O   
12386 C CB  . LEU E 52  ? 0.3878 0.4094 0.3334 -0.0143 0.0019  0.0221  52  LEU E CB  
12387 C CG  . LEU E 52  ? 0.4186 0.4322 0.3324 -0.0246 0.0061  0.0162  52  LEU E CG  
12388 C CD1 . LEU E 52  ? 0.4106 0.4151 0.3237 -0.0187 0.0220  0.0015  52  LEU E CD1 
12389 C CD2 . LEU E 52  ? 0.4518 0.4627 0.3438 -0.0396 -0.0034 0.0158  52  LEU E CD2 
12390 N N   . TRP E 53  ? 0.4132 0.4550 0.3684 -0.0326 -0.0320 0.0625  53  TRP E N   
12391 C CA  . TRP E 53  ? 0.4470 0.4983 0.3971 -0.0456 -0.0515 0.0756  53  TRP E CA  
12392 C C   . TRP E 53  ? 0.5229 0.5728 0.4260 -0.0637 -0.0574 0.0783  53  TRP E C   
12393 O O   . TRP E 53  ? 0.5578 0.6016 0.4421 -0.0649 -0.0481 0.0780  53  TRP E O   
12394 C CB  . TRP E 53  ? 0.4106 0.4766 0.4063 -0.0416 -0.0645 0.0999  53  TRP E CB  
12395 C CG  . TRP E 53  ? 0.4079 0.4756 0.4150 -0.0387 -0.0639 0.1171  53  TRP E CG  
12396 C CD1 . TRP E 53  ? 0.3924 0.4550 0.4299 -0.0256 -0.0480 0.1146  53  TRP E CD1 
12397 C CD2 . TRP E 53  ? 0.4267 0.5013 0.4142 -0.0516 -0.0795 0.1407  53  TRP E CD2 
12398 N NE1 . TRP E 53  ? 0.4336 0.4973 0.4769 -0.0274 -0.0509 0.1346  53  TRP E NE1 
12399 C CE2 . TRP E 53  ? 0.4332 0.5042 0.4451 -0.0430 -0.0709 0.1529  53  TRP E CE2 
12400 C CE3 . TRP E 53  ? 0.4714 0.5547 0.4194 -0.0726 -0.0995 0.1523  53  TRP E CE3 
12401 C CZ2 . TRP E 53  ? 0.4587 0.5336 0.4595 -0.0524 -0.0818 0.1797  53  TRP E CZ2 
12402 C CZ3 . TRP E 53  ? 0.5151 0.6048 0.4468 -0.0843 -0.1122 0.1789  53  TRP E CZ3 
12403 C CH2 . TRP E 53  ? 0.5048 0.5896 0.4638 -0.0732 -0.1035 0.1941  53  TRP E CH2 
12404 N N   . VAL E 54  ? 0.5401 0.5954 0.4215 -0.0807 -0.0709 0.0782  54  VAL E N   
12405 C CA  . VAL E 54  ? 0.5654 0.6200 0.3942 -0.1044 -0.0759 0.0775  54  VAL E CA  
12406 C C   . VAL E 54  ? 0.6186 0.6930 0.4432 -0.1232 -0.1040 0.0953  54  VAL E C   
12407 O O   . VAL E 54  ? 0.6004 0.6841 0.4593 -0.1182 -0.1137 0.0978  54  VAL E O   
12408 C CB  . VAL E 54  ? 0.5481 0.5826 0.3405 -0.1118 -0.0537 0.0449  54  VAL E CB  
12409 C CG1 . VAL E 54  ? 0.5261 0.5574 0.3256 -0.1148 -0.0545 0.0299  54  VAL E CG1 
12410 C CG2 . VAL E 54  ? 0.6266 0.6573 0.3604 -0.1390 -0.0509 0.0397  54  VAL E CG2 
12411 N N   . THR E 55  ? 0.7004 0.7835 0.4837 -0.1467 -0.1181 0.1097  55  THR E N   
12412 C CA  . THR E 55  ? 0.7859 0.8906 0.5527 -0.1719 -0.1469 0.1248  55  THR E CA  
12413 C C   . THR E 55  ? 0.8184 0.9106 0.5435 -0.1907 -0.1344 0.0892  55  THR E C   
12414 O O   . THR E 55  ? 0.8404 0.9106 0.5249 -0.1976 -0.1088 0.0626  55  THR E O   
12415 C CB  . THR E 55  ? 0.8585 0.9748 0.5960 -0.1916 -0.1624 0.1503  55  THR E CB  
12416 O OG1 . THR E 55  ? 0.9181 1.0140 0.5996 -0.2040 -0.1385 0.1287  55  THR E OG1 
12417 C CG2 . THR E 55  ? 0.8152 0.9415 0.6058 -0.1712 -0.1726 0.1864  55  THR E CG2 
12418 N N   . CYS E 56  ? 0.8016 0.9061 0.5447 -0.1976 -0.1489 0.0871  56  CYS E N   
12419 C CA  . CYS E 56  ? 0.7679 0.8596 0.4789 -0.2164 -0.1365 0.0534  56  CYS E CA  
12420 C C   . CYS E 56  ? 0.8559 0.9656 0.5359 -0.2498 -0.1559 0.0594  56  CYS E C   
12421 O O   . CYS E 56  ? 0.8862 1.0226 0.5970 -0.2505 -0.1833 0.0904  56  CYS E O   
12422 C CB  . CYS E 56  ? 0.6565 0.7437 0.4180 -0.1971 -0.1302 0.0428  56  CYS E CB  
12423 S SG  . CYS E 56  ? 0.6445 0.7063 0.4418 -0.1589 -0.0997 0.0314  56  CYS E SG  
12424 N N   . SER E 57  ? 0.9187 1.0119 0.5507 -0.2737 -0.1361 0.0292  57  SER E N   
12425 C CA  . SER E 57  ? 0.9962 1.1041 0.5980 -0.3056 -0.1481 0.0338  57  SER E CA  
12426 C C   . SER E 57  ? 1.0596 1.1700 0.6577 -0.3247 -0.1485 0.0132  57  SER E C   
12427 O O   . SER E 57  ? 1.0048 1.1051 0.6284 -0.3127 -0.1403 -0.0045 57  SER E O   
12428 C CB  . SER E 57  ? 1.0203 1.1106 0.5680 -0.3252 -0.1244 0.0170  57  SER E CB  
12429 O OG  . SER E 57  ? 1.0843 1.1908 0.5975 -0.3589 -0.1373 0.0258  57  SER E OG  
12430 N N   . GLN E 58  ? 1.1755 1.3021 0.7446 -0.3555 -0.1609 0.0189  58  GLN E N   
12431 C CA  . GLN E 58  ? 1.2254 1.3503 0.7765 -0.3807 -0.1541 -0.0070 58  GLN E CA  
12432 C C   . GLN E 58  ? 1.2050 1.2932 0.7225 -0.3895 -0.1109 -0.0511 58  GLN E C   
12433 O O   . GLN E 58  ? 1.2003 1.2740 0.7194 -0.3973 -0.0929 -0.0808 58  GLN E O   
12434 C CB  . GLN E 58  ? 1.3266 1.4781 0.8473 -0.4156 -0.1761 0.0096  58  GLN E CB  
12435 C CG  . GLN E 58  ? 1.3728 1.5321 0.8655 -0.4250 -0.1842 0.0342  58  GLN E CG  
12436 C CD  . GLN E 58  ? 1.4409 1.6330 0.9145 -0.4567 -0.2148 0.0616  58  GLN E CD  
12437 O OE1 . GLN E 58  ? 1.4611 1.6710 0.9404 -0.4724 -0.2298 0.0608  58  GLN E OE1 
12438 N NE2 . GLN E 58  ? 1.4713 1.6724 0.9237 -0.4667 -0.2252 0.0870  58  GLN E NE2 
12439 N N   . HIS E 59  ? 1.1792 1.2523 0.6724 -0.3876 -0.0927 -0.0543 59  HIS E N   
12440 C CA  . HIS E 59  ? 1.1625 1.2017 0.6315 -0.3954 -0.0493 -0.0934 59  HIS E CA  
12441 C C   . HIS E 59  ? 1.0873 1.1004 0.5880 -0.3606 -0.0264 -0.1068 59  HIS E C   
12442 O O   . HIS E 59  ? 1.1173 1.1033 0.6098 -0.3591 0.0090  -0.1320 59  HIS E O   
12443 C CB  . HIS E 59  ? 1.2011 1.2392 0.6264 -0.4177 -0.0400 -0.0916 59  HIS E CB  
12444 C CG  . HIS E 59  ? 1.2643 1.3296 0.6542 -0.4544 -0.0643 -0.0745 59  HIS E CG  
12445 N ND1 . HIS E 59  ? 1.3114 1.3813 0.6797 -0.4861 -0.0607 -0.0932 59  HIS E ND1 
12446 C CD2 . HIS E 59  ? 1.2789 1.3684 0.6519 -0.4659 -0.0921 -0.0398 59  HIS E CD2 
12447 C CE1 . HIS E 59  ? 1.3664 1.4638 0.7033 -0.5165 -0.0868 -0.0704 59  HIS E CE1 
12448 N NE2 . HIS E 59  ? 1.3524 1.4618 0.6928 -0.5046 -0.1065 -0.0369 59  HIS E NE2 
12449 N N   . TYR E 60  ? 0.9991 1.0207 0.5395 -0.3341 -0.0457 -0.0904 60  TYR E N   
12450 C CA  . TYR E 60  ? 0.9378 0.9358 0.5078 -0.3044 -0.0260 -0.1036 60  TYR E CA  
12451 C C   . TYR E 60  ? 1.0014 0.9735 0.5791 -0.3113 0.0030  -0.1395 60  TYR E C   
12452 O O   . TYR E 60  ? 1.0452 1.0249 0.6359 -0.3196 -0.0087 -0.1419 60  TYR E O   
12453 C CB  . TYR E 60  ? 0.8343 0.8505 0.4439 -0.2803 -0.0547 -0.0770 60  TYR E CB  
12454 C CG  . TYR E 60  ? 0.7507 0.7472 0.4074 -0.2406 -0.0351 -0.0790 60  TYR E CG  
12455 C CD1 . TYR E 60  ? 0.7291 0.6988 0.4098 -0.2301 -0.0081 -0.1037 60  TYR E CD1 
12456 C CD2 . TYR E 60  ? 0.6723 0.6789 0.3581 -0.2120 -0.0442 -0.0518 60  TYR E CD2 
12457 C CE1 . TYR E 60  ? 0.6638 0.6199 0.3907 -0.1936 0.0063  -0.0987 60  TYR E CE1 
12458 C CE2 . TYR E 60  ? 0.6306 0.6234 0.3602 -0.1776 -0.0280 -0.0516 60  TYR E CE2 
12459 C CZ  . TYR E 60  ? 0.6089 0.5782 0.3570 -0.1690 -0.0046 -0.0734 60  TYR E CZ  
12460 O OH  . TYR E 60  ? 0.5595 0.5190 0.3480 -0.1377 0.0074  -0.0688 60  TYR E OH  
12461 N N   . SER E 61  ? 0.9896 0.9313 0.5657 -0.3075 0.0420  -0.1659 61  SER E N   
12462 C CA  . SER E 61  ? 0.9818 0.8955 0.5748 -0.3118 0.0749  -0.1983 61  SER E CA  
12463 C C   . SER E 61  ? 0.9676 0.8516 0.6051 -0.2791 0.1005  -0.2092 61  SER E C   
12464 O O   . SER E 61  ? 0.9639 0.8361 0.6082 -0.2643 0.1197  -0.2116 61  SER E O   
12465 C CB  . SER E 61  ? 0.9926 0.8961 0.5563 -0.3397 0.1033  -0.2205 61  SER E CB  
12466 O OG  . SER E 61  ? 1.0058 0.8822 0.5935 -0.3427 0.1382  -0.2504 61  SER E OG  
12467 N N   . SER E 62  ? 0.9338 0.8063 0.6051 -0.2684 0.1008  -0.2140 62  SER E N   
12468 C CA  . SER E 62  ? 0.8449 0.6931 0.5706 -0.2334 0.1214  -0.2135 62  SER E CA  
12469 C C   . SER E 62  ? 0.8102 0.6435 0.5712 -0.2303 0.1272  -0.2200 62  SER E C   
12470 O O   . SER E 62  ? 0.7909 0.6434 0.5508 -0.2379 0.1010  -0.2083 62  SER E O   
12471 C CB  . SER E 62  ? 0.7477 0.6174 0.4999 -0.1984 0.0979  -0.1763 62  SER E CB  
12472 O OG  . SER E 62  ? 0.6826 0.5367 0.4873 -0.1649 0.1126  -0.1685 62  SER E OG  
12473 N N   . SER E 63  ? 0.7872 0.5864 0.5850 -0.2188 0.1624  -0.2368 63  SER E N   
12474 C CA  . SER E 63  ? 0.7619 0.5422 0.5968 -0.2149 0.1721  -0.2413 63  SER E CA  
12475 C C   . SER E 63  ? 0.7413 0.5287 0.6225 -0.1772 0.1567  -0.2062 63  SER E C   
12476 O O   . SER E 63  ? 0.7878 0.5610 0.7014 -0.1704 0.1621  -0.2027 63  SER E O   
12477 C CB  . SER E 63  ? 0.7669 0.5168 0.6336 -0.2140 0.2141  -0.2623 63  SER E CB  
12478 O OG  . SER E 63  ? 0.7572 0.4917 0.6644 -0.1839 0.2314  -0.2532 63  SER E OG  
12479 N N   . THR E 64  ? 0.6849 0.4935 0.5669 -0.1552 0.1389  -0.1810 64  THR E N   
12480 C CA  . THR E 64  ? 0.5846 0.4019 0.5031 -0.1239 0.1250  -0.1498 64  THR E CA  
12481 C C   . THR E 64  ? 0.5469 0.3987 0.4513 -0.1201 0.0906  -0.1264 64  THR E C   
12482 O O   . THR E 64  ? 0.5511 0.4124 0.4786 -0.0974 0.0803  -0.1030 64  THR E O   
12483 C CB  . THR E 64  ? 0.5837 0.3943 0.5297 -0.0981 0.1377  -0.1394 64  THR E CB  
12484 O OG1 . THR E 64  ? 0.6401 0.4576 0.5577 -0.1067 0.1421  -0.1506 64  THR E OG1 
12485 C CG2 . THR E 64  ? 0.5586 0.3352 0.5453 -0.0918 0.1698  -0.1510 64  THR E CG2 
12486 N N   . TYR E 65  ? 0.5542 0.4251 0.4229 -0.1437 0.0735  -0.1319 65  TYR E N   
12487 C CA  . TYR E 65  ? 0.5748 0.4788 0.4400 -0.1403 0.0419  -0.1082 65  TYR E CA  
12488 C C   . TYR E 65  ? 0.5986 0.5117 0.4880 -0.1402 0.0289  -0.0987 65  TYR E C   
12489 O O   . TYR E 65  ? 0.6537 0.5551 0.5445 -0.1568 0.0363  -0.1144 65  TYR E O   
12490 C CB  . TYR E 65  ? 0.6105 0.5345 0.4334 -0.1658 0.0254  -0.1113 65  TYR E CB  
12491 C CG  . TYR E 65  ? 0.6307 0.5891 0.4595 -0.1669 -0.0081 -0.0863 65  TYR E CG  
12492 C CD1 . TYR E 65  ? 0.6291 0.6039 0.4716 -0.1466 -0.0206 -0.0624 65  TYR E CD1 
12493 C CD2 . TYR E 65  ? 0.6463 0.6215 0.4728 -0.1893 -0.0263 -0.0869 65  TYR E CD2 
12494 C CE1 . TYR E 65  ? 0.6287 0.6334 0.4881 -0.1466 -0.0479 -0.0391 65  TYR E CE1 
12495 C CE2 . TYR E 65  ? 0.6410 0.6497 0.4854 -0.1892 -0.0567 -0.0616 65  TYR E CE2 
12496 C CZ  . TYR E 65  ? 0.6263 0.6484 0.4893 -0.1671 -0.0662 -0.0376 65  TYR E CZ  
12497 O OH  . TYR E 65  ? 0.6035 0.6567 0.4947 -0.1664 -0.0929 -0.0126 65  TYR E OH  
12498 N N   . GLN E 66  ? 0.5471 0.4796 0.4578 -0.1228 0.0128  -0.0752 66  GLN E N   
12499 C CA  . GLN E 66  ? 0.5531 0.4985 0.4895 -0.1239 0.0011  -0.0657 66  GLN E CA  
12500 C C   . GLN E 66  ? 0.4899 0.4657 0.4411 -0.1166 -0.0207 -0.0443 66  GLN E C   
12501 O O   . GLN E 66  ? 0.4871 0.4686 0.4369 -0.1022 -0.0226 -0.0336 66  GLN E O   
12502 C CB  . GLN E 66  ? 0.6321 0.5580 0.5948 -0.1072 0.0173  -0.0618 66  GLN E CB  
12503 C CG  . GLN E 66  ? 0.7923 0.6880 0.7557 -0.1150 0.0386  -0.0794 66  GLN E CG  
12504 C CD  . GLN E 66  ? 0.9004 0.7766 0.8890 -0.0970 0.0530  -0.0686 66  GLN E CD  
12505 O OE1 . GLN E 66  ? 0.9283 0.8141 0.9326 -0.0899 0.0467  -0.0536 66  GLN E OE1 
12506 N NE2 . GLN E 66  ? 0.9410 0.7896 0.9360 -0.0909 0.0736  -0.0752 66  GLN E NE2 
12507 N N   . ALA E 67  ? 0.4823 0.4779 0.4537 -0.1271 -0.0360 -0.0385 67  ALA E N   
12508 C CA  . ALA E 67  ? 0.4642 0.4855 0.4669 -0.1171 -0.0509 -0.0180 67  ALA E CA  
12509 C C   . ALA E 67  ? 0.4643 0.4812 0.5021 -0.1074 -0.0399 -0.0157 67  ALA E C   
12510 O O   . ALA E 67  ? 0.4988 0.5181 0.5523 -0.1199 -0.0410 -0.0214 67  ALA E O   
12511 C CB  . ALA E 67  ? 0.4727 0.5249 0.4831 -0.1356 -0.0777 -0.0084 67  ALA E CB  
12512 N N   . PRO E 68  ? 0.4257 0.4361 0.4729 -0.0881 -0.0282 -0.0086 68  PRO E N   
12513 C CA  . PRO E 68  ? 0.3996 0.4046 0.4718 -0.0829 -0.0152 -0.0071 68  PRO E CA  
12514 C C   . PRO E 68  ? 0.3910 0.4191 0.5046 -0.0910 -0.0241 -0.0022 68  PRO E C   
12515 O O   . PRO E 68  ? 0.3903 0.4424 0.5220 -0.0928 -0.0413 0.0075  68  PRO E O   
12516 C CB  . PRO E 68  ? 0.3783 0.3816 0.4490 -0.0665 -0.0065 0.0002  68  PRO E CB  
12517 C CG  . PRO E 68  ? 0.3825 0.3784 0.4224 -0.0609 -0.0089 -0.0011 68  PRO E CG  
12518 C CD  . PRO E 68  ? 0.3966 0.4032 0.4274 -0.0739 -0.0246 -0.0037 68  PRO E CD  
12519 N N   . PHE E 69  ? 0.3912 0.4131 0.5238 -0.0963 -0.0128 -0.0069 69  PHE E N   
12520 C CA  . PHE E 69  ? 0.3896 0.4348 0.5699 -0.1042 -0.0190 -0.0032 69  PHE E CA  
12521 C C   . PHE E 69  ? 0.4199 0.4749 0.6340 -0.0929 -0.0088 0.0042  69  PHE E C   
12522 O O   . PHE E 69  ? 0.4536 0.4938 0.6477 -0.0827 0.0064  0.0034  69  PHE E O   
12523 C CB  . PHE E 69  ? 0.3851 0.4208 0.5767 -0.1172 -0.0092 -0.0130 69  PHE E CB  
12524 C CG  . PHE E 69  ? 0.4085 0.4154 0.5848 -0.1119 0.0163  -0.0167 69  PHE E CG  
12525 C CD1 . PHE E 69  ? 0.4005 0.4088 0.5982 -0.1076 0.0328  -0.0133 69  PHE E CD1 
12526 C CD2 . PHE E 69  ? 0.4285 0.4071 0.5724 -0.1142 0.0248  -0.0232 69  PHE E CD2 
12527 C CE1 . PHE E 69  ? 0.4191 0.4028 0.5965 -0.1071 0.0537  -0.0135 69  PHE E CE1 
12528 C CE2 . PHE E 69  ? 0.4428 0.3965 0.5758 -0.1102 0.0450  -0.0204 69  PHE E CE2 
12529 C CZ  . PHE E 69  ? 0.4296 0.3869 0.5754 -0.1077 0.0577  -0.0143 69  PHE E CZ  
12530 N N   . CYS E 70  ? 0.3885 0.4700 0.6567 -0.0960 -0.0169 0.0113  70  CYS E N   
12531 C CA  . CYS E 70  ? 0.3305 0.4201 0.6388 -0.0864 -0.0027 0.0155  70  CYS E CA  
12532 C C   . CYS E 70  ? 0.3263 0.3964 0.6298 -0.0874 0.0279  0.0040  70  CYS E C   
12533 O O   . CYS E 70  ? 0.3171 0.3789 0.6194 -0.0974 0.0355  -0.0026 70  CYS E O   
12534 C CB  . CYS E 70  ? 0.3043 0.4258 0.6848 -0.0893 -0.0146 0.0264  70  CYS E CB  
12535 S SG  . CYS E 70  ? 0.4081 0.5382 0.8388 -0.0750 -0.0002 0.0333  70  CYS E SG  
12536 N N   . HIS E 71  ? 0.2914 0.5353 0.5426 0.0190  0.0660  0.0960  71  HIS E N   
12537 C CA  . HIS E 71  ? 0.2911 0.5319 0.5357 0.0280  0.0913  0.0962  71  HIS E CA  
12538 C C   . HIS E 71  ? 0.2784 0.5057 0.4962 0.0200  0.0952  0.0952  71  HIS E C   
12539 O O   . HIS E 71  ? 0.2883 0.5153 0.4985 0.0222  0.1119  0.1011  71  HIS E O   
12540 C CB  . HIS E 71  ? 0.3160 0.5796 0.6087 0.0307  0.1075  0.1055  71  HIS E CB  
12541 C CG  . HIS E 71  ? 0.3420 0.6243 0.6864 0.0371  0.1027  0.1124  71  HIS E CG  
12542 N ND1 . HIS E 71  ? 0.3357 0.6126 0.6869 0.0509  0.1120  0.1097  71  HIS E ND1 
12543 C CD2 . HIS E 71  ? 0.3331 0.6404 0.7346 0.0305  0.0888  0.1242  71  HIS E CD2 
12544 C CE1 . HIS E 71  ? 0.3287 0.6271 0.7452 0.0542  0.1047  0.1224  71  HIS E CE1 
12545 N NE2 . HIS E 71  ? 0.3186 0.6369 0.7654 0.0413  0.0880  0.1326  71  HIS E NE2 
12546 N N   . SER E 72  ? 0.2909 0.5057 0.4966 0.0095  0.0816  0.0893  72  SER E N   
12547 C CA  . SER E 72  ? 0.2830 0.4840 0.4803 0.0025  0.0862  0.0905  72  SER E CA  
12548 C C   . SER E 72  ? 0.3044 0.4883 0.4689 0.0101  0.0871  0.0918  72  SER E C   
12549 O O   . SER E 72  ? 0.3303 0.5084 0.4729 0.0191  0.0839  0.0859  72  SER E O   
12550 C CB  . SER E 72  ? 0.2756 0.4646 0.4758 -0.0125 0.0783  0.0800  72  SER E CB  
12551 O OG  . SER E 72  ? 0.3077 0.4823 0.4801 -0.0110 0.0681  0.0711  72  SER E OG  
12552 N N   . THR E 73  ? 0.3129 0.4890 0.4798 0.0050  0.0895  0.1011  73  THR E N   
12553 C CA  . THR E 73  ? 0.3468 0.5079 0.4872 0.0080  0.0833  0.1056  73  THR E CA  
12554 C C   . THR E 73  ? 0.3640 0.5066 0.4953 0.0093  0.0733  0.0926  73  THR E C   
12555 O O   . THR E 73  ? 0.3635 0.4959 0.4693 0.0149  0.0666  0.0903  73  THR E O   
12556 C CB  . THR E 73  ? 0.3475 0.5061 0.5072 0.0003  0.0830  0.1250  73  THR E CB  
12557 O OG1 . THR E 73  ? 0.3341 0.4882 0.5367 -0.0080 0.0874  0.1213  73  THR E OG1 
12558 C CG2 . THR E 73  ? 0.2690 0.4433 0.4265 -0.0013 0.0927  0.1422  73  THR E CG2 
12559 N N   . GLN E 74  ? 0.3371 0.4734 0.4857 0.0019  0.0739  0.0829  74  GLN E N   
12560 C CA  . GLN E 74  ? 0.3117 0.4294 0.4472 0.0021  0.0686  0.0714  74  GLN E CA  
12561 C C   . GLN E 74  ? 0.3201 0.4418 0.4316 0.0121  0.0620  0.0656  74  GLN E C   
12562 O O   . GLN E 74  ? 0.3471 0.4551 0.4439 0.0181  0.0572  0.0615  74  GLN E O   
12563 C CB  . GLN E 74  ? 0.3299 0.4369 0.4758 -0.0121 0.0745  0.0594  74  GLN E CB  
12564 C CG  . GLN E 74  ? 0.3432 0.4397 0.5246 -0.0224 0.0870  0.0612  74  GLN E CG  
12565 C CD  . GLN E 74  ? 0.3627 0.4731 0.5666 -0.0322 0.0943  0.0614  74  GLN E CD  
12566 O OE1 . GLN E 74  ? 0.3624 0.4949 0.5616 -0.0274 0.0888  0.0677  74  GLN E OE1 
12567 N NE2 . GLN E 74  ? 0.3937 0.4898 0.6278 -0.0470 0.1098  0.0523  74  GLN E NE2 
12568 N N   . CYS E 75  ? 0.3234 0.4641 0.4408 0.0138  0.0621  0.0667  75  CYS E N   
12569 C CA  . CYS E 75  ? 0.3083 0.4550 0.4203 0.0238  0.0574  0.0651  75  CYS E CA  
12570 C C   . CYS E 75  ? 0.3063 0.4494 0.4048 0.0360  0.0645  0.0639  75  CYS E C   
12571 O O   . CYS E 75  ? 0.3228 0.4573 0.4132 0.0442  0.0627  0.0581  75  CYS E O   
12572 C CB  . CYS E 75  ? 0.3197 0.4904 0.4573 0.0222  0.0554  0.0710  75  CYS E CB  
12573 S SG  . CYS E 75  ? 0.4374 0.6130 0.5806 0.0009  0.0417  0.0699  75  CYS E SG  
12574 N N   . SER E 76  ? 0.2886 0.4365 0.3819 0.0345  0.0732  0.0692  76  SER E N   
12575 C CA  . SER E 76  ? 0.3535 0.4943 0.4191 0.0391  0.0802  0.0660  76  SER E CA  
12576 C C   . SER E 76  ? 0.3938 0.5138 0.4380 0.0381  0.0680  0.0612  76  SER E C   
12577 O O   . SER E 76  ? 0.4004 0.5100 0.4268 0.0433  0.0693  0.0504  76  SER E O   
12578 C CB  . SER E 76  ? 0.3685 0.5167 0.4236 0.0324  0.0891  0.0771  76  SER E CB  
12579 O OG  . SER E 76  ? 0.4582 0.5972 0.4727 0.0314  0.0962  0.0722  76  SER E OG  
12580 N N   . ARG E 77  ? 0.3834 0.4964 0.4375 0.0309  0.0581  0.0686  77  ARG E N   
12581 C CA  . ARG E 77  ? 0.3925 0.4873 0.4399 0.0296  0.0463  0.0671  77  ARG E CA  
12582 C C   . ARG E 77  ? 0.3997 0.4830 0.4481 0.0371  0.0448  0.0539  77  ARG E C   
12583 O O   . ARG E 77  ? 0.3680 0.4379 0.4049 0.0399  0.0387  0.0475  77  ARG E O   
12584 C CB  . ARG E 77  ? 0.3898 0.4790 0.4659 0.0212  0.0412  0.0787  77  ARG E CB  
12585 C CG  . ARG E 77  ? 0.4496 0.5227 0.5296 0.0193  0.0278  0.0820  77  ARG E CG  
12586 C CD  . ARG E 77  ? 0.4917 0.5579 0.6168 0.0118  0.0255  0.0958  77  ARG E CD  
12587 N NE  . ARG E 77  ? 0.5643 0.6166 0.7015 0.0107  0.0107  0.1000  77  ARG E NE  
12588 C CZ  . ARG E 77  ? 0.5911 0.6316 0.7803 0.0067  0.0106  0.1088  77  ARG E CZ  
12589 N NH1 . ARG E 77  ? 0.5343 0.5725 0.7650 0.0023  0.0280  0.1114  77  ARG E NH1 
12590 N NH2 . ARG E 77  ? 0.6439 0.6737 0.8494 0.0059  -0.0049 0.1137  77  ARG E NH2 
12591 N N   . ALA E 78  ? 0.3723 0.4615 0.4342 0.0385  0.0486  0.0517  78  ALA E N   
12592 C CA  . ALA E 78  ? 0.3418 0.4220 0.4049 0.0437  0.0460  0.0456  78  ALA E CA  
12593 C C   . ALA E 78  ? 0.3781 0.4637 0.4405 0.0550  0.0501  0.0406  78  ALA E C   
12594 O O   . ALA E 78  ? 0.4214 0.5001 0.4912 0.0610  0.0480  0.0384  78  ALA E O   
12595 C CB  . ALA E 78  ? 0.3236 0.4087 0.3939 0.0363  0.0450  0.0483  78  ALA E CB  
12596 N N   . ASN E 79  ? 0.4109 0.5075 0.4685 0.0571  0.0595  0.0393  79  ASN E N   
12597 C CA  . ASN E 79  ? 0.4805 0.5789 0.5442 0.0666  0.0722  0.0308  79  ASN E CA  
12598 C C   . ASN E 79  ? 0.5162 0.6287 0.6185 0.0737  0.0727  0.0384  79  ASN E C   
12599 O O   . ASN E 79  ? 0.5006 0.6087 0.6235 0.0829  0.0772  0.0351  79  ASN E O   
12600 C CB  . ASN E 79  ? 0.5430 0.6201 0.5922 0.0697  0.0716  0.0173  79  ASN E CB  
12601 C CG  . ASN E 79  ? 0.6025 0.6756 0.6527 0.0754  0.0919  0.0021  79  ASN E CG  
12602 O OD1 . ASN E 79  ? 0.6413 0.7243 0.6903 0.0746  0.1094  0.0002  79  ASN E OD1 
12603 N ND2 . ASN E 79  ? 0.6212 0.6774 0.6768 0.0803  0.0938  -0.0105 79  ASN E ND2 
12604 N N   . THR E 80  ? 0.5654 0.6953 0.6818 0.0676  0.0660  0.0505  80  THR E N   
12605 C CA  . THR E 80  ? 0.6193 0.7684 0.7754 0.0703  0.0608  0.0632  80  THR E CA  
12606 C C   . THR E 80  ? 0.7378 0.9090 0.9165 0.0675  0.0682  0.0695  80  THR E C   
12607 O O   . THR E 80  ? 0.7621 0.9374 0.9268 0.0569  0.0645  0.0711  80  THR E O   
12608 C CB  . THR E 80  ? 0.5678 0.7172 0.7187 0.0599  0.0391  0.0737  80  THR E CB  
12609 O OG1 . THR E 80  ? 0.5893 0.7629 0.7769 0.0570  0.0278  0.0906  80  THR E OG1 
12610 C CG2 . THR E 80  ? 0.5147 0.6571 0.6358 0.0450  0.0356  0.0692  80  THR E CG2 
12611 N N   . HIS E 81  ? 0.8336 1.0185 1.0564 0.0770  0.0813  0.0735  81  HIS E N   
12612 C CA  . HIS E 81  ? 0.8911 1.0977 1.1462 0.0751  0.0911  0.0809  81  HIS E CA  
12613 C C   . HIS E 81  ? 0.8484 1.0798 1.1701 0.0769  0.0780  0.1008  81  HIS E C   
12614 O O   . HIS E 81  ? 0.8634 1.1149 1.2353 0.0790  0.0887  0.1091  81  HIS E O   
12615 C CB  . HIS E 81  ? 0.9821 1.1820 1.2328 0.0818  0.1260  0.0677  81  HIS E CB  
12616 C CG  . HIS E 81  ? 1.0589 1.2397 1.2432 0.0747  0.1316  0.0556  81  HIS E CG  
12617 N ND1 . HIS E 81  ? 1.0954 1.2526 1.2379 0.0751  0.1296  0.0422  81  HIS E ND1 
12618 C CD2 . HIS E 81  ? 1.0688 1.2525 1.2279 0.0657  0.1359  0.0591  81  HIS E CD2 
12619 C CE1 . HIS E 81  ? 1.1083 1.2560 1.2026 0.0657  0.1293  0.0396  81  HIS E CE1 
12620 N NE2 . HIS E 81  ? 1.0969 1.2602 1.2005 0.0603  0.1336  0.0510  81  HIS E NE2 
12621 N N   . GLN E 82  ? 0.7844 1.0144 1.1086 0.0749  0.0535  0.1113  82  GLN E N   
12622 C CA  . GLN E 82  ? 0.7013 0.9556 1.0813 0.0714  0.0293  0.1374  82  GLN E CA  
12623 C C   . GLN E 82  ? 0.5929 0.8556 0.9417 0.0486  -0.0024 0.1462  82  GLN E C   
12624 O O   . GLN E 82  ? 0.5969 0.8409 0.8885 0.0383  -0.0136 0.1393  82  GLN E O   
12625 C CB  . GLN E 82  ? 0.7504 0.9967 1.1506 0.0809  0.0228  0.1467  82  GLN E CB  
12626 C CG  . GLN E 82  ? 0.8289 1.0957 1.2656 0.0719  -0.0133 0.1795  82  GLN E CG  
12627 C CD  . GLN E 82  ? 0.9169 1.1779 1.3947 0.0855  -0.0128 0.1927  82  GLN E CD  
12628 O OE1 . GLN E 82  ? 0.9826 1.2345 1.5001 0.1042  0.0191  0.1803  82  GLN E OE1 
12629 N NE2 . GLN E 82  ? 0.9205 1.1841 1.3864 0.0744  -0.0456 0.2168  82  GLN E NE2 
12630 N N   . CYS E 83  ? 0.5107 0.8003 0.9007 0.0390  -0.0155 0.1607  83  CYS E N   
12631 C CA  . CYS E 83  ? 0.4745 0.7697 0.8310 0.0132  -0.0408 0.1620  83  CYS E CA  
12632 C C   . CYS E 83  ? 0.5141 0.8121 0.8486 -0.0064 -0.0784 0.1792  83  CYS E C   
12633 O O   . CYS E 83  ? 0.5611 0.8697 0.9329 -0.0002 -0.0941 0.2028  83  CYS E O   
12634 C CB  . CYS E 83  ? 0.4359 0.7592 0.8466 0.0068  -0.0436 0.1709  83  CYS E CB  
12635 S SG  . CYS E 83  ? 0.5060 0.8243 0.9232 0.0199  -0.0008 0.1518  83  CYS E SG  
12636 N N   . PHE E 84  ? 0.5070 0.7938 0.7807 -0.0323 -0.0910 0.1678  84  PHE E N   
12637 C CA  . PHE E 84  ? 0.5079 0.7910 0.7389 -0.0570 -0.1234 0.1804  84  PHE E CA  
12638 C C   . PHE E 84  ? 0.5325 0.8406 0.7729 -0.0873 -0.1586 0.1950  84  PHE E C   
12639 O O   . PHE E 84  ? 0.5404 0.8518 0.7788 -0.1000 -0.1530 0.1789  84  PHE E O   
12640 C CB  . PHE E 84  ? 0.4941 0.7395 0.6408 -0.0695 -0.1090 0.1543  84  PHE E CB  
12641 C CG  . PHE E 84  ? 0.5301 0.7652 0.6202 -0.0964 -0.1347 0.1649  84  PHE E CG  
12642 C CD1 . PHE E 84  ? 0.5621 0.7872 0.6441 -0.0860 -0.1385 0.1802  84  PHE E CD1 
12643 C CD2 . PHE E 84  ? 0.5431 0.7763 0.5845 -0.1348 -0.1535 0.1589  84  PHE E CD2 
12644 C CE1 . PHE E 84  ? 0.6200 0.8351 0.6447 -0.1130 -0.1615 0.1939  84  PHE E CE1 
12645 C CE2 . PHE E 84  ? 0.5984 0.8197 0.5749 -0.1644 -0.1757 0.1683  84  PHE E CE2 
12646 C CZ  . PHE E 84  ? 0.6423 0.8551 0.6089 -0.1536 -0.1802 0.1879  84  PHE E CZ  
12647 N N   . THR E 85  ? 0.5599 0.8852 0.8112 -0.1007 -0.1973 0.2276  85  THR E N   
12648 C CA  . THR E 85  ? 0.6284 0.9779 0.8805 -0.1358 -0.2411 0.2466  85  THR E CA  
12649 C C   . THR E 85  ? 0.7185 1.0536 0.8870 -0.1686 -0.2717 0.2574  85  THR E C   
12650 O O   . THR E 85  ? 0.7506 1.0851 0.9246 -0.1590 -0.2826 0.2832  85  THR E O   
12651 C CB  . THR E 85  ? 0.7178 1.1050 1.0749 -0.1247 -0.2649 0.2856  85  THR E CB  
12652 O OG1 . THR E 85  ? 0.6774 1.0779 1.1128 -0.0958 -0.2326 0.2767  85  THR E OG1 
12653 C CG2 . THR E 85  ? 0.7531 1.1468 1.0951 -0.1606 -0.3031 0.2987  85  THR E CG2 
12654 N N   . CYS E 86  ? 0.7662 1.0869 0.8559 -0.2089 -0.2826 0.2373  86  CYS E N   
12655 C CA  . CYS E 86  ? 0.8488 1.1520 0.8465 -0.2454 -0.3077 0.2454  86  CYS E CA  
12656 C C   . CYS E 86  ? 0.9482 1.2558 0.9259 -0.2816 -0.3418 0.2586  86  CYS E C   
12657 O O   . CYS E 86  ? 0.9869 1.2924 0.9380 -0.3089 -0.3446 0.2348  86  CYS E O   
12658 C CB  . CYS E 86  ? 0.8766 1.1314 0.7762 -0.2616 -0.2695 0.1993  86  CYS E CB  
12659 S SG  . CYS E 86  ? 1.0859 1.3116 0.8692 -0.3008 -0.2868 0.2090  86  CYS E SG  
12660 N N   . THR E 87  ? 1.0008 1.3142 0.9959 -0.2825 -0.3672 0.2974  87  THR E N   
12661 C CA  . THR E 87  ? 1.0865 1.4037 1.0571 -0.3203 -0.4037 0.3154  87  THR E CA  
12662 C C   . THR E 87  ? 1.1448 1.4366 1.0289 -0.3461 -0.4121 0.3263  87  THR E C   
12663 O O   . THR E 87  ? 1.2252 1.5219 1.0936 -0.3747 -0.4462 0.3548  87  THR E O   
12664 C CB  . THR E 87  ? 1.1498 1.5021 1.2347 -0.3041 -0.4300 0.3558  87  THR E CB  
12665 O OG1 . THR E 87  ? 1.2482 1.6074 1.3140 -0.3424 -0.4662 0.3675  87  THR E OG1 
12666 C CG2 . THR E 87  ? 1.1156 1.4751 1.2599 -0.2794 -0.4341 0.3951  87  THR E CG2 
12667 N N   . ASP E 88  ? 1.1060 1.3710 0.9373 -0.3363 -0.3803 0.3043  88  ASP E N   
12668 C CA  . ASP E 88  ? 1.1674 1.4002 0.9032 -0.3630 -0.3763 0.3028  88  ASP E CA  
12669 C C   . ASP E 88  ? 1.2336 1.4496 0.8863 -0.4131 -0.3848 0.2800  88  ASP E C   
12670 O O   . ASP E 88  ? 1.2824 1.5111 0.9310 -0.4408 -0.4218 0.3067  88  ASP E O   
12671 C CB  . ASP E 88  ? 1.2244 1.4265 0.9193 -0.3437 -0.3332 0.2749  88  ASP E CB  
12672 C CG  . ASP E 88  ? 1.3010 1.4614 0.8867 -0.3767 -0.3176 0.2599  88  ASP E CG  
12673 O OD1 . ASP E 88  ? 1.3200 1.4785 0.9015 -0.3753 -0.3284 0.2892  88  ASP E OD1 
12674 O OD2 . ASP E 88  ? 1.3343 1.4628 0.8443 -0.4038 -0.2906 0.2173  88  ASP E OD2 
12675 N N   . SER E 89  ? 1.2508 1.4354 0.8359 -0.4278 -0.3491 0.2308  89  SER E N   
12676 C CA  . SER E 89  ? 1.3393 1.5127 0.8707 -0.4703 -0.3539 0.2051  89  SER E CA  
12677 C C   . SER E 89  ? 1.3066 1.5172 0.9279 -0.4536 -0.3720 0.2098  89  SER E C   
12678 O O   . SER E 89  ? 1.2344 1.4677 0.9392 -0.4110 -0.3637 0.2170  89  SER E O   
12679 C CB  . SER E 89  ? 1.3636 1.4904 0.8122 -0.4902 -0.3036 0.1488  89  SER E CB  
12680 O OG  . SER E 89  ? 1.3961 1.5167 0.8279 -0.5166 -0.2967 0.1147  89  SER E OG  
12681 N N   . THR E 90  ? 1.3613 1.5781 0.9688 -0.4862 -0.3952 0.2062  90  THR E N   
12682 C CA  . THR E 90  ? 1.3127 1.5593 1.0002 -0.4741 -0.4059 0.2027  90  THR E CA  
12683 C C   . THR E 90  ? 1.3657 1.5878 1.0085 -0.4975 -0.3741 0.1454  90  THR E C   
12684 O O   . THR E 90  ? 1.3656 1.6081 1.0607 -0.4990 -0.3852 0.1389  90  THR E O   
12685 C CB  . THR E 90  ? 1.4730 1.7509 1.2077 -0.4875 -0.4577 0.2442  90  THR E CB  
12686 O OG1 . THR E 90  ? 1.6133 1.8694 1.2509 -0.5372 -0.4763 0.2446  90  THR E OG1 
12687 C CG2 . THR E 90  ? 1.4156 1.7221 1.2338 -0.4568 -0.4825 0.2993  90  THR E CG2 
12688 N N   . THR E 91  ? 1.3759 1.5529 0.9287 -0.5173 -0.3330 0.1046  91  THR E N   
12689 C CA  . THR E 91  ? 1.3315 1.4809 0.8620 -0.5312 -0.2894 0.0475  91  THR E CA  
12690 C C   . THR E 91  ? 1.2121 1.3442 0.7521 -0.5013 -0.2456 0.0284  91  THR E C   
12691 O O   . THR E 91  ? 1.2191 1.3442 0.7361 -0.4879 -0.2448 0.0486  91  THR E O   
12692 C CB  . THR E 91  ? 1.4310 1.5365 0.8561 -0.5820 -0.2699 0.0126  91  THR E CB  
12693 O OG1 . THR E 91  ? 1.5163 1.6369 0.9135 -0.6135 -0.3192 0.0419  91  THR E OG1 
12694 C CG2 . THR E 91  ? 1.3610 1.4461 0.7951 -0.5933 -0.2293 -0.0420 91  THR E CG2 
12695 N N   . THR E 92  ? 1.1011 1.2215 0.6711 -0.4940 -0.2062 -0.0117 92  THR E N   
12696 C CA  . THR E 92  ? 1.0019 1.1110 0.5936 -0.4643 -0.1705 -0.0238 92  THR E CA  
12697 C C   . THR E 92  ? 1.0912 1.1434 0.6005 -0.4793 -0.1219 -0.0568 92  THR E C   
12698 O O   . THR E 92  ? 1.1989 1.2168 0.6444 -0.5142 -0.1011 -0.0832 92  THR E O   
12699 C CB  . THR E 92  ? 0.8676 0.9836 0.5532 -0.4312 -0.1364 -0.0420 92  THR E CB  
12700 O OG1 . THR E 92  ? 0.8827 0.9630 0.5412 -0.4634 -0.0987 -0.0918 92  THR E OG1 
12701 C CG2 . THR E 92  ? 0.7937 0.9616 0.5657 -0.4149 -0.1743 -0.0114 92  THR E CG2 
12702 N N   . ARG E 93  ? 1.0523 1.0947 0.5800 -0.4423 -0.0982 -0.0487 93  ARG E N   
12703 C CA  . ARG E 93  ? 1.0904 1.0817 0.5583 -0.4497 -0.0503 -0.0752 93  ARG E CA  
12704 C C   . ARG E 93  ? 1.0117 1.0060 0.5548 -0.3914 -0.0253 -0.0622 93  ARG E C   
12705 O O   . ARG E 93  ? 0.9526 0.9868 0.5694 -0.3533 -0.0505 -0.0309 93  ARG E O   
12706 C CB  . ARG E 93  ? 1.1318 1.1096 0.5157 -0.4742 -0.0685 -0.0544 93  ARG E CB  
12707 C CG  . ARG E 93  ? 1.0835 1.1006 0.4963 -0.4462 -0.1157 -0.0007 93  ARG E CG  
12708 C CD  . ARG E 93  ? 1.1700 1.1706 0.5260 -0.4592 -0.1244 0.0227  93  ARG E CD  
12709 N NE  . ARG E 93  ? 1.1610 1.2031 0.5633 -0.4335 -0.1724 0.0773  93  ARG E NE  
12710 C CZ  . ARG E 93  ? 1.1272 1.1767 0.5668 -0.3945 -0.1683 0.0984  93  ARG E CZ  
12711 N NH1 . ARG E 93  ? 1.0746 1.0949 0.5116 -0.3749 -0.1207 0.0710  93  ARG E NH1 
12712 N NH2 . ARG E 93  ? 1.1240 1.2097 0.6171 -0.3725 -0.2084 0.1473  93  ARG E NH2 
12713 N N   . PRO E 94  ? 1.0106 0.9620 0.5389 -0.3860 0.0255  -0.0870 94  PRO E N   
12714 C CA  . PRO E 94  ? 0.9018 0.8589 0.4971 -0.3337 0.0399  -0.0699 94  PRO E CA  
12715 C C   . PRO E 94  ? 0.8410 0.8262 0.4333 -0.3148 -0.0015 -0.0260 94  PRO E C   
12716 O O   . PRO E 94  ? 0.8850 0.8587 0.4040 -0.3413 -0.0158 -0.0155 94  PRO E O   
12717 C CB  . PRO E 94  ? 0.9531 0.8583 0.5215 -0.3415 0.0945  -0.0996 94  PRO E CB  
12718 C CG  . PRO E 94  ? 1.0412 0.9149 0.5670 -0.3877 0.1235  -0.1424 94  PRO E CG  
12719 C CD  . PRO E 94  ? 1.1042 1.0011 0.5680 -0.4248 0.0747  -0.1321 94  PRO E CD  
12720 N N   . GLY E 95  ? 0.7503 0.7705 0.4213 -0.2717 -0.0185 -0.0006 95  GLY E N   
12721 C CA  . GLY E 95  ? 0.7305 0.7776 0.4169 -0.2512 -0.0533 0.0399  95  GLY E CA  
12722 C C   . GLY E 95  ? 0.7346 0.8263 0.4446 -0.2574 -0.1039 0.0716  95  GLY E C   
12723 O O   . GLY E 95  ? 0.7152 0.8314 0.4605 -0.2357 -0.1294 0.1071  95  GLY E O   
12724 N N   . CYS E 96  ? 0.7645 0.8660 0.4608 -0.2886 -0.1183 0.0601  96  CYS E N   
12725 C CA  . CYS E 96  ? 0.7670 0.9133 0.4979 -0.2968 -0.1685 0.0915  96  CYS E CA  
12726 C C   . CYS E 96  ? 0.7205 0.8816 0.4929 -0.3038 -0.1653 0.0720  96  CYS E C   
12727 O O   . CYS E 96  ? 0.7497 0.8963 0.4692 -0.3466 -0.1670 0.0476  96  CYS E O   
12728 C CB  . CYS E 96  ? 0.8798 1.0272 0.5317 -0.3438 -0.2104 0.1115  96  CYS E CB  
12729 S SG  . CYS E 96  ? 0.8723 1.0752 0.5768 -0.3570 -0.2791 0.1593  96  CYS E SG  
12730 N N   . HIS E 97  ? 0.6440 0.8303 0.5064 -0.2640 -0.1571 0.0807  97  HIS E N   
12731 C CA  . HIS E 97  ? 0.6379 0.8445 0.5567 -0.2638 -0.1552 0.0713  97  HIS E CA  
12732 C C   . HIS E 97  ? 0.6153 0.8651 0.6231 -0.2304 -0.1763 0.1083  97  HIS E C   
12733 O O   . HIS E 97  ? 0.5784 0.8340 0.6004 -0.2071 -0.1828 0.1320  97  HIS E O   
12734 C CB  . HIS E 97  ? 0.5945 0.7779 0.5345 -0.2451 -0.1054 0.0398  97  HIS E CB  
12735 C CG  . HIS E 97  ? 0.6378 0.7741 0.5132 -0.2630 -0.0712 0.0065  97  HIS E CG  
12736 N ND1 . HIS E 97  ? 0.6752 0.7861 0.5104 -0.3021 -0.0554 -0.0276 97  HIS E ND1 
12737 C CD2 . HIS E 97  ? 0.6481 0.7563 0.4999 -0.2469 -0.0459 0.0011  97  HIS E CD2 
12738 C CE1 . HIS E 97  ? 0.6966 0.7651 0.4891 -0.3085 -0.0185 -0.0524 97  HIS E CE1 
12739 N NE2 . HIS E 97  ? 0.6820 0.7494 0.4852 -0.2751 -0.0140 -0.0339 97  HIS E NE2 
12740 N N   . ASN E 98  ? 0.6420 0.9201 0.7156 -0.2274 -0.1831 0.1130  98  ASN E N   
12741 C CA  . ASN E 98  ? 0.6270 0.9357 0.7878 -0.1890 -0.1835 0.1403  98  ASN E CA  
12742 C C   . ASN E 98  ? 0.5571 0.8593 0.7542 -0.1633 -0.1411 0.1209  98  ASN E C   
12743 O O   . ASN E 98  ? 0.5585 0.8373 0.7241 -0.1759 -0.1181 0.0920  98  ASN E O   
12744 C CB  . ASN E 98  ? 0.6899 1.0415 0.9193 -0.1969 -0.2228 0.1722  98  ASN E CB  
12745 C CG  . ASN E 98  ? 0.8101 1.1723 1.0022 -0.2319 -0.2746 0.1965  98  ASN E CG  
12746 O OD1 . ASN E 98  ? 0.8631 1.2457 1.0696 -0.2616 -0.3070 0.2036  98  ASN E OD1 
12747 N ND2 . ASN E 98  ? 0.8590 1.1990 0.9828 -0.2370 -0.2799 0.2018  98  ASN E ND2 
12748 N N   . ASN E 99  ? 0.4961 0.8184 0.7615 -0.1295 -0.1298 0.1381  99  ASN E N   
12749 C CA  . ASN E 99  ? 0.4297 0.7473 0.7257 -0.1033 -0.0903 0.1264  99  ASN E CA  
12750 C C   . ASN E 99  ? 0.4013 0.6821 0.6404 -0.0933 -0.0619 0.1050  99  ASN E C   
12751 O O   . ASN E 99  ? 0.4030 0.6719 0.6448 -0.0842 -0.0332 0.0913  99  ASN E O   
12752 C CB  . ASN E 99  ? 0.4502 0.7782 0.7770 -0.1174 -0.0839 0.1169  99  ASN E CB  
12753 C CG  . ASN E 99  ? 0.4188 0.7575 0.8015 -0.0900 -0.0527 0.1215  99  ASN E CG  
12754 O OD1 . ASN E 99  ? 0.3999 0.7455 0.8093 -0.0636 -0.0411 0.1344  99  ASN E OD1 
12755 N ND2 . ASN E 99  ? 0.4157 0.7557 0.8187 -0.0983 -0.0378 0.1115  99  ASN E ND2 
12756 N N   . THR E 100 ? 0.3869 0.6517 0.5822 -0.0943 -0.0713 0.1069  100 THR E N   
12757 C CA  . THR E 100 ? 0.3983 0.6315 0.5529 -0.0819 -0.0477 0.0919  100 THR E CA  
12758 C C   . THR E 100 ? 0.4049 0.6424 0.5815 -0.0521 -0.0432 0.1057  100 THR E C   
12759 O O   . THR E 100 ? 0.4377 0.7008 0.6659 -0.0404 -0.0514 0.1241  100 THR E O   
12760 C CB  . THR E 100 ? 0.4532 0.6600 0.5415 -0.1066 -0.0554 0.0807  100 THR E CB  
12761 O OG1 . THR E 100 ? 0.4898 0.7127 0.5690 -0.1221 -0.0907 0.1015  100 THR E OG1 
12762 C CG2 . THR E 100 ? 0.4769 0.6670 0.5386 -0.1354 -0.0449 0.0560  100 THR E CG2 
12763 N N   . CYS E 101 ? 0.4196 0.6313 0.5644 -0.0406 -0.0285 0.0962  101 CYS E N   
12764 C CA  . CYS E 101 ? 0.4066 0.6194 0.5710 -0.0155 -0.0237 0.1056  101 CYS E CA  
12765 C C   . CYS E 101 ? 0.3937 0.5881 0.5266 -0.0157 -0.0319 0.1087  101 CYS E C   
12766 O O   . CYS E 101 ? 0.4263 0.5973 0.5123 -0.0304 -0.0301 0.0975  101 CYS E O   
12767 C CB  . CYS E 101 ? 0.4248 0.6288 0.5953 0.0040  0.0036  0.0941  101 CYS E CB  
12768 S SG  . CYS E 101 ? 0.7501 0.9252 0.8806 -0.0021 0.0194  0.0753  101 CYS E SG  
12769 N N   . GLY E 102 ? 0.3791 0.5837 0.5461 0.0007  -0.0374 0.1247  102 GLY E N   
12770 C CA  . GLY E 102 ? 0.4136 0.6066 0.5669 0.0021  -0.0478 0.1354  102 GLY E CA  
12771 C C   . GLY E 102 ? 0.4230 0.5924 0.5692 0.0214  -0.0276 0.1231  102 GLY E C   
12772 O O   . GLY E 102 ? 0.4163 0.5849 0.5846 0.0394  -0.0083 0.1125  102 GLY E O   
12773 N N   . LEU E 103 ? 0.4479 0.5969 0.5601 0.0148  -0.0321 0.1244  103 LEU E N   
12774 C CA  . LEU E 103 ? 0.4549 0.5796 0.5606 0.0296  -0.0157 0.1126  103 LEU E CA  
12775 C C   . LEU E 103 ? 0.4800 0.5984 0.5900 0.0309  -0.0266 0.1312  103 LEU E C   
12776 O O   . LEU E 103 ? 0.5330 0.6483 0.6102 0.0112  -0.0420 0.1445  103 LEU E O   
12777 C CB  . LEU E 103 ? 0.4479 0.5475 0.5112 0.0198  -0.0019 0.0914  103 LEU E CB  
12778 C CG  . LEU E 103 ? 0.4702 0.5479 0.5344 0.0339  0.0140  0.0770  103 LEU E CG  
12779 C CD1 . LEU E 103 ? 0.4843 0.5722 0.5771 0.0519  0.0217  0.0712  103 LEU E CD1 
12780 C CD2 . LEU E 103 ? 0.4602 0.5194 0.5017 0.0229  0.0255  0.0620  103 LEU E CD2 
12781 N N   . LEU E 104 ? 0.4216 0.5368 0.5704 0.0517  -0.0180 0.1327  104 LEU E N   
12782 C CA  . LEU E 104 ? 0.4528 0.5609 0.6138 0.0543  -0.0264 0.1524  104 LEU E CA  
12783 C C   . LEU E 104 ? 0.4278 0.5037 0.5488 0.0511  -0.0146 0.1385  104 LEU E C   
12784 O O   . LEU E 104 ? 0.4192 0.4793 0.5416 0.0620  0.0028  0.1154  104 LEU E O   
12785 C CB  . LEU E 104 ? 0.5004 0.6165 0.7304 0.0769  -0.0185 0.1589  104 LEU E CB  
12786 C CG  . LEU E 104 ? 0.5697 0.6908 0.8351 0.0782  -0.0342 0.1927  104 LEU E CG  
12787 C CD1 . LEU E 104 ? 0.5799 0.7298 0.8546 0.0618  -0.0655 0.2275  104 LEU E CD1 
12788 C CD2 . LEU E 104 ? 0.5993 0.7222 0.9419 0.1019  -0.0172 0.1917  104 LEU E CD2 
12789 N N   . SER E 105 ? 0.4326 0.4985 0.5165 0.0333  -0.0245 0.1534  105 SER E N   
12790 C CA  . SER E 105 ? 0.4337 0.4676 0.4844 0.0281  -0.0100 0.1434  105 SER E CA  
12791 C C   . SER E 105 ? 0.4453 0.4724 0.5164 0.0343  -0.0146 0.1671  105 SER E C   
12792 O O   . SER E 105 ? 0.4614 0.5065 0.5459 0.0291  -0.0355 0.1985  105 SER E O   
12793 C CB  . SER E 105 ? 0.4559 0.4766 0.4419 -0.0006 -0.0081 0.1378  105 SER E CB  
12794 O OG  . SER E 105 ? 0.4608 0.4871 0.4386 -0.0054 -0.0018 0.1166  105 SER E OG  
12795 N N   . SER E 106 ? 0.4700 0.4716 0.5481 0.0437  0.0030  0.1558  106 SER E N   
12796 C CA  . SER E 106 ? 0.4907 0.4852 0.5969 0.0510  0.0009  0.1789  106 SER E CA  
12797 C C   . SER E 106 ? 0.5176 0.4820 0.5808 0.0364  0.0135  0.1812  106 SER E C   
12798 O O   . SER E 106 ? 0.5220 0.4637 0.5670 0.0338  0.0337  0.1552  106 SER E O   
12799 C CB  A SER E 106 ? 0.4735 0.4648 0.6436 0.0772  0.0123  0.1657  106 SER E CB  
12800 C CB  B SER E 106 ? 0.4734 0.4641 0.6426 0.0771  0.0127  0.1652  106 SER E CB  
12801 O OG  A SER E 106 ? 0.5022 0.4911 0.7162 0.0861  0.0097  0.1912  106 SER E OG  
12802 O OG  B SER E 106 ? 0.4532 0.4680 0.6649 0.0895  0.0078  0.1639  106 SER E OG  
12803 N N   . ASN E 107 ? 0.4642 0.4769 0.5703 -0.0588 -0.0573 0.1211  107 ASN E N   
12804 C CA  . ASN E 107 ? 0.4643 0.4658 0.5451 -0.0695 -0.0535 0.1344  107 ASN E CA  
12805 C C   . ASN E 107 ? 0.4679 0.4561 0.5919 -0.0614 -0.0453 0.1320  107 ASN E C   
12806 O O   . ASN E 107 ? 0.4817 0.4657 0.6523 -0.0547 -0.0538 0.1468  107 ASN E O   
12807 C CB  . ASN E 107 ? 0.4904 0.4960 0.5525 -0.0816 -0.0711 0.1683  107 ASN E CB  
12808 C CG  . ASN E 107 ? 0.5465 0.5422 0.5781 -0.0948 -0.0652 0.1837  107 ASN E CG  
12809 O OD1 . ASN E 107 ? 0.5555 0.5383 0.6061 -0.0917 -0.0527 0.1795  107 ASN E OD1 
12810 N ND2 . ASN E 107 ? 0.5982 0.6018 0.5813 -0.1109 -0.0733 0.2000  107 ASN E ND2 
12811 N N   . PRO E 108 ? 0.4578 0.4393 0.5702 -0.0621 -0.0288 0.1122  108 PRO E N   
12812 C CA  . PRO E 108 ? 0.4538 0.4250 0.6086 -0.0548 -0.0196 0.1013  108 PRO E CA  
12813 C C   . PRO E 108 ? 0.4832 0.4401 0.6569 -0.0611 -0.0222 0.1276  108 PRO E C   
12814 O O   . PRO E 108 ? 0.5172 0.4633 0.7383 -0.0550 -0.0182 0.1237  108 PRO E O   
12815 C CB  . PRO E 108 ? 0.4453 0.4184 0.5747 -0.0563 -0.0039 0.0752  108 PRO E CB  
12816 C CG  . PRO E 108 ? 0.4455 0.4222 0.5199 -0.0685 -0.0031 0.0837  108 PRO E CG  
12817 C CD  . PRO E 108 ? 0.4513 0.4360 0.5138 -0.0701 -0.0181 0.0983  108 PRO E CD  
12818 N N   . VAL E 109 ? 0.4926 0.4497 0.6299 -0.0742 -0.0287 0.1545  109 VAL E N   
12819 C CA  . VAL E 109 ? 0.4983 0.4432 0.6485 -0.0821 -0.0319 0.1854  109 VAL E CA  
12820 C C   . VAL E 109 ? 0.5123 0.4553 0.7034 -0.0766 -0.0506 0.2142  109 VAL E C   
12821 O O   . VAL E 109 ? 0.5645 0.4930 0.8051 -0.0727 -0.0515 0.2287  109 VAL E O   
12822 C CB  . VAL E 109 ? 0.5115 0.4602 0.6018 -0.1004 -0.0303 0.2040  109 VAL E CB  
12823 C CG1 . VAL E 109 ? 0.5546 0.4934 0.6567 -0.1096 -0.0364 0.2429  109 VAL E CG1 
12824 C CG2 . VAL E 109 ? 0.4964 0.4449 0.5583 -0.1055 -0.0096 0.1784  109 VAL E CG2 
12825 N N   . THR E 110 ? 0.5230 0.4809 0.6965 -0.0767 -0.0660 0.2238  110 THR E N   
12826 C CA  . THR E 110 ? 0.5489 0.5095 0.7605 -0.0720 -0.0868 0.2549  110 THR E CA  
12827 C C   . THR E 110 ? 0.5612 0.5246 0.8326 -0.0535 -0.0887 0.2371  110 THR E C   
12828 O O   . THR E 110 ? 0.6194 0.5827 0.9404 -0.0460 -0.1030 0.2599  110 THR E O   
12829 C CB  . THR E 110 ? 0.5536 0.5324 0.7182 -0.0834 -0.1047 0.2764  110 THR E CB  
12830 O OG1 . THR E 110 ? 0.5558 0.5492 0.7001 -0.0800 -0.1031 0.2478  110 THR E OG1 
12831 C CG2 . THR E 110 ? 0.5629 0.5411 0.6625 -0.1034 -0.0992 0.2890  110 THR E CG2 
12832 N N   . GLN E 111 ? 0.5120 0.4793 0.7791 -0.0466 -0.0738 0.1973  111 GLN E N   
12833 C CA  . GLN E 111 ? 0.5229 0.4964 0.8368 -0.0309 -0.0711 0.1739  111 GLN E CA  
12834 C C   . GLN E 111 ? 0.5358 0.5288 0.8500 -0.0282 -0.0861 0.1820  111 GLN E C   
12835 O O   . GLN E 111 ? 0.5377 0.5395 0.8896 -0.0161 -0.0834 0.1640  111 GLN E O   
12836 C CB  . GLN E 111 ? 0.6387 0.5974 1.0270 -0.0198 -0.0699 0.1786  111 GLN E CB  
12837 C CG  . GLN E 111 ? 0.7671 0.7087 1.1681 -0.0200 -0.0520 0.1580  111 GLN E CG  
12838 C CD  . GLN E 111 ? 0.8826 0.8330 1.2736 -0.0144 -0.0362 0.1134  111 GLN E CD  
12839 O OE1 . GLN E 111 ? 0.9299 0.8845 1.2709 -0.0216 -0.0276 0.0984  111 GLN E OE1 
12840 N NE2 . GLN E 111 ? 0.9160 0.8709 1.3553 -0.0015 -0.0320 0.0926  111 GLN E NE2 
12841 N N   . GLU E 112 ? 0.5667 0.5690 0.8359 -0.0410 -0.1006 0.2059  112 GLU E N   
12842 C CA  . GLU E 112 ? 0.5872 0.6109 0.8483 -0.0417 -0.1148 0.2097  112 GLU E CA  
12843 C C   . GLU E 112 ? 0.5517 0.5837 0.7832 -0.0410 -0.1013 0.1748  112 GLU E C   
12844 O O   . GLU E 112 ? 0.5302 0.5540 0.7247 -0.0455 -0.0855 0.1553  112 GLU E O   
12845 C CB  . GLU E 112 ? 0.6874 0.7208 0.9019 -0.0582 -0.1337 0.2402  112 GLU E CB  
12846 C CG  . GLU E 112 ? 0.8061 0.8389 1.0544 -0.0584 -0.1540 0.2823  112 GLU E CG  
12847 C CD  . GLU E 112 ? 0.9173 0.9590 1.1071 -0.0782 -0.1699 0.3117  112 GLU E CD  
12848 O OE1 . GLU E 112 ? 0.9328 0.9701 1.0602 -0.0915 -0.1573 0.2989  112 GLU E OE1 
12849 O OE2 . GLU E 112 ? 0.9942 1.0490 1.2011 -0.0807 -0.1949 0.3471  112 GLU E OE2 
12850 N N   . SER E 113 ? 0.5545 0.6039 0.8064 -0.0354 -0.1079 0.1689  113 SER E N   
12851 C CA  . SER E 113 ? 0.5577 0.6172 0.7815 -0.0366 -0.0979 0.1419  113 SER E CA  
12852 C C   . SER E 113 ? 0.5232 0.6034 0.7370 -0.0436 -0.1147 0.1524  113 SER E C   
12853 O O   . SER E 113 ? 0.5396 0.6301 0.7805 -0.0438 -0.1345 0.1781  113 SER E O   
12854 C CB  . SER E 113 ? 0.5725 0.6330 0.8363 -0.0217 -0.0810 0.1136  113 SER E CB  
12855 O OG  . SER E 113 ? 0.5924 0.6625 0.9190 -0.0105 -0.0882 0.1206  113 SER E OG  
12856 N N   . GLY E 114 ? 0.4941 0.5806 0.6702 -0.0500 -0.1077 0.1335  114 GLY E N   
12857 C CA  . GLY E 114 ? 0.4931 0.5983 0.6580 -0.0591 -0.1225 0.1401  114 GLY E CA  
12858 C C   . GLY E 114 ? 0.4661 0.5768 0.6200 -0.0584 -0.1083 0.1134  114 GLY E C   
12859 O O   . GLY E 114 ? 0.4558 0.5545 0.5907 -0.0553 -0.0894 0.0933  114 GLY E O   
12860 N N   . LEU E 115 ? 0.4597 0.5898 0.6292 -0.0612 -0.1180 0.1148  115 LEU E N   
12861 C CA  . LEU E 115 ? 0.4564 0.5920 0.6185 -0.0616 -0.1045 0.0926  115 LEU E CA  
12862 C C   . LEU E 115 ? 0.4570 0.5879 0.5635 -0.0783 -0.1049 0.0864  115 LEU E C   
12863 O O   . LEU E 115 ? 0.4546 0.5962 0.5474 -0.0916 -0.1223 0.0974  115 LEU E O   
12864 C CB  . LEU E 115 ? 0.4680 0.6275 0.6790 -0.0570 -0.1112 0.0945  115 LEU E CB  
12865 C CG  . LEU E 115 ? 0.4948 0.6584 0.7047 -0.0548 -0.0919 0.0717  115 LEU E CG  
12866 C CD1 . LEU E 115 ? 0.5036 0.6621 0.7373 -0.0392 -0.0719 0.0564  115 LEU E CD1 
12867 C CD2 . LEU E 115 ? 0.5109 0.6990 0.7520 -0.0583 -0.0992 0.0735  115 LEU E CD2 
12868 N N   . GLY E 116 ? 0.4753 0.5912 0.5525 -0.0778 -0.0858 0.0680  116 GLY E N   
12869 C CA  . GLY E 116 ? 0.5083 0.6168 0.5398 -0.0918 -0.0822 0.0585  116 GLY E CA  
12870 C C   . GLY E 116 ? 0.4751 0.5883 0.5123 -0.0921 -0.0716 0.0434  116 GLY E C   
12871 O O   . GLY E 116 ? 0.4544 0.5792 0.5278 -0.0823 -0.0668 0.0407  116 GLY E O   
12872 N N   . GLU E 117 ? 0.4723 0.5760 0.4745 -0.1040 -0.0667 0.0334  117 GLU E N   
12873 C CA  . GLU E 117 ? 0.4584 0.5626 0.4643 -0.1062 -0.0561 0.0213  117 GLU E CA  
12874 C C   . GLU E 117 ? 0.4684 0.5535 0.4540 -0.1005 -0.0362 0.0090  117 GLU E C   
12875 O O   . GLU E 117 ? 0.5025 0.5722 0.4575 -0.1048 -0.0323 0.0050  117 GLU E O   
12876 C CB  . GLU E 117 ? 0.4626 0.5698 0.4512 -0.1250 -0.0661 0.0184  117 GLU E CB  
12877 C CG  . GLU E 117 ? 0.4419 0.5505 0.4420 -0.1296 -0.0575 0.0086  117 GLU E CG  
12878 C CD  . GLU E 117 ? 0.5156 0.6233 0.4964 -0.1501 -0.0660 0.0017  117 GLU E CD  
12879 O OE1 . GLU E 117 ? 0.5669 0.6593 0.5103 -0.1594 -0.0641 -0.0063 117 GLU E OE1 
12880 O OE2 . GLU E 117 ? 0.5529 0.6764 0.5571 -0.1579 -0.0740 0.0025  117 GLU E OE2 
12881 N N   . LEU E 118 ? 0.4144 0.5026 0.4176 -0.0916 -0.0236 0.0038  118 LEU E N   
12882 C CA  . LEU E 118 ? 0.3794 0.4528 0.3666 -0.0861 -0.0073 -0.0046 118 LEU E CA  
12883 C C   . LEU E 118 ? 0.4255 0.4830 0.3881 -0.0982 -0.0034 -0.0117 118 LEU E C   
12884 O O   . LEU E 118 ? 0.4167 0.4777 0.3829 -0.1097 -0.0083 -0.0130 118 LEU E O   
12885 C CB  . LEU E 118 ? 0.3471 0.4304 0.3546 -0.0769 0.0038  -0.0061 118 LEU E CB  
12886 C CG  . LEU E 118 ? 0.3383 0.4112 0.3324 -0.0695 0.0180  -0.0108 118 LEU E CG  
12887 C CD1 . LEU E 118 ? 0.3201 0.3893 0.3081 -0.0605 0.0188  -0.0130 118 LEU E CD1 
12888 C CD2 . LEU E 118 ? 0.3173 0.4037 0.3271 -0.0642 0.0274  -0.0096 118 LEU E CD2 
12889 N N   . ALA E 119 ? 0.4330 0.4737 0.3744 -0.0961 0.0059  -0.0178 119 ALA E N   
12890 C CA  . ALA E 119 ? 0.4135 0.4367 0.3349 -0.1061 0.0126  -0.0275 119 ALA E CA  
12891 C C   . ALA E 119 ? 0.4649 0.4758 0.3873 -0.0961 0.0281  -0.0313 119 ALA E C   
12892 O O   . ALA E 119 ? 0.4825 0.4989 0.4125 -0.0831 0.0316  -0.0271 119 ALA E O   
12893 C CB  . ALA E 119 ? 0.3852 0.4019 0.2792 -0.1159 0.0080  -0.0314 119 ALA E CB  
12894 N N   . GLN E 120 ? 0.4968 0.4915 0.4140 -0.1026 0.0368  -0.0394 120 GLN E N   
12895 C CA  . GLN E 120 ? 0.5047 0.4863 0.4272 -0.0937 0.0505  -0.0411 120 GLN E CA  
12896 C C   . GLN E 120 ? 0.5131 0.4739 0.4231 -0.1023 0.0595  -0.0553 120 GLN E C   
12897 O O   . GLN E 120 ? 0.4908 0.4449 0.3958 -0.1165 0.0583  -0.0642 120 GLN E O   
12898 C CB  . GLN E 120 ? 0.5122 0.4959 0.4546 -0.0908 0.0546  -0.0334 120 GLN E CB  
12899 C CG  . GLN E 120 ? 0.5306 0.5021 0.4819 -0.0822 0.0663  -0.0302 120 GLN E CG  
12900 C CD  . GLN E 120 ? 0.5677 0.5403 0.5367 -0.0830 0.0699  -0.0199 120 GLN E CD  
12901 O OE1 . GLN E 120 ? 0.5516 0.5425 0.5272 -0.0772 0.0679  -0.0088 120 GLN E OE1 
12902 N NE2 . GLN E 120 ? 0.6019 0.5551 0.5796 -0.0919 0.0764  -0.0247 120 GLN E NE2 
12903 N N   . ASP E 121 ? 0.5194 0.4714 0.4266 -0.0946 0.0691  -0.0594 121 ASP E N   
12904 C CA  . ASP E 121 ? 0.5436 0.4766 0.4427 -0.1021 0.0808  -0.0755 121 ASP E CA  
12905 C C   . ASP E 121 ? 0.5137 0.4407 0.4256 -0.0881 0.0922  -0.0748 121 ASP E C   
12906 O O   . ASP E 121 ? 0.4750 0.4139 0.3971 -0.0750 0.0884  -0.0620 121 ASP E O   
12907 C CB  . ASP E 121 ? 0.5900 0.5259 0.4595 -0.1155 0.0767  -0.0852 121 ASP E CB  
12908 C CG  . ASP E 121 ? 0.6386 0.5589 0.4946 -0.1313 0.0859  -0.1060 121 ASP E CG  
12909 O OD1 . ASP E 121 ? 0.6636 0.5661 0.5362 -0.1287 0.1004  -0.1160 121 ASP E OD1 
12910 O OD2 . ASP E 121 ? 0.6553 0.5818 0.4842 -0.1471 0.0783  -0.1125 121 ASP E OD2 
12911 N N   . VAL E 122 ? 0.5156 0.4258 0.4283 -0.0913 0.1062  -0.0898 122 VAL E N   
12912 C CA  . VAL E 122 ? 0.4630 0.3687 0.3920 -0.0786 0.1177  -0.0907 122 VAL E CA  
12913 C C   . VAL E 122 ? 0.4786 0.3972 0.3927 -0.0762 0.1161  -0.0906 122 VAL E C   
12914 O O   . VAL E 122 ? 0.4891 0.4096 0.3769 -0.0887 0.1150  -0.0986 122 VAL E O   
12915 C CB  . VAL E 122 ? 0.4357 0.3194 0.3747 -0.0836 0.1357  -0.1100 122 VAL E CB  
12916 C CG1 . VAL E 122 ? 0.4362 0.3182 0.3952 -0.0709 0.1479  -0.1122 122 VAL E CG1 
12917 C CG2 . VAL E 122 ? 0.4499 0.3179 0.4124 -0.0839 0.1388  -0.1082 122 VAL E CG2 
12918 N N   . LEU E 123 ? 0.4461 0.3750 0.3770 -0.0615 0.1149  -0.0802 123 LEU E N   
12919 C CA  . LEU E 123 ? 0.4299 0.3674 0.3571 -0.0585 0.1182  -0.0825 123 LEU E CA  
12920 C C   . LEU E 123 ? 0.4638 0.3979 0.4197 -0.0469 0.1305  -0.0854 123 LEU E C   
12921 O O   . LEU E 123 ? 0.4568 0.3913 0.4370 -0.0358 0.1284  -0.0756 123 LEU E O   
12922 C CB  . LEU E 123 ? 0.3998 0.3560 0.3252 -0.0526 0.1043  -0.0695 123 LEU E CB  
12923 C CG  . LEU E 123 ? 0.4546 0.4205 0.3822 -0.0493 0.1063  -0.0700 123 LEU E CG  
12924 C CD1 . LEU E 123 ? 0.4403 0.4174 0.3565 -0.0522 0.0938  -0.0624 123 LEU E CD1 
12925 C CD2 . LEU E 123 ? 0.4284 0.4035 0.3839 -0.0349 0.1076  -0.0657 123 LEU E CD2 
12926 N N   . ALA E 124 ? 0.4674 0.3999 0.4222 -0.0499 0.1432  -0.0974 124 ALA E N   
12927 C CA  . ALA E 124 ? 0.4470 0.3798 0.4347 -0.0384 0.1551  -0.1004 124 ALA E CA  
12928 C C   . ALA E 124 ? 0.4656 0.4148 0.4564 -0.0355 0.1554  -0.0989 124 ALA E C   
12929 O O   . ALA E 124 ? 0.4728 0.4265 0.4373 -0.0458 0.1535  -0.1006 124 ALA E O   
12930 C CB  . ALA E 124 ? 0.4601 0.3749 0.4547 -0.0442 0.1755  -0.1200 124 ALA E CB  
12931 N N   . ILE E 125 ? 0.4242 0.3830 0.4498 -0.0220 0.1571  -0.0942 125 ILE E N   
12932 C CA  . ILE E 125 ? 0.3901 0.3661 0.4248 -0.0194 0.1569  -0.0932 125 ILE E CA  
12933 C C   . ILE E 125 ? 0.4087 0.3907 0.4870 -0.0074 0.1665  -0.0952 125 ILE E C   
12934 O O   . ILE E 125 ? 0.4368 0.4141 0.5401 0.0027  0.1656  -0.0895 125 ILE E O   
12935 C CB  . ILE E 125 ? 0.3496 0.3425 0.3791 -0.0153 0.1366  -0.0792 125 ILE E CB  
12936 C CG1 . ILE E 125 ? 0.3367 0.3447 0.3741 -0.0163 0.1369  -0.0807 125 ILE E CG1 
12937 C CG2 . ILE E 125 ? 0.3334 0.3351 0.3841 -0.0022 0.1251  -0.0666 125 ILE E CG2 
12938 C CD1 . ILE E 125 ? 0.3268 0.3498 0.3617 -0.0138 0.1197  -0.0722 125 ILE E CD1 
12939 N N   . HIS E 126 ? 0.4050 0.3979 0.4962 -0.0085 0.1760  -0.1019 126 HIS E N   
12940 C CA  . HIS E 126 ? 0.3909 0.3927 0.5297 0.0029  0.1859  -0.1046 126 HIS E CA  
12941 C C   . HIS E 126 ? 0.3743 0.3953 0.5450 0.0182  0.1675  -0.0875 126 HIS E C   
12942 O O   . HIS E 126 ? 0.3733 0.4092 0.5317 0.0181  0.1500  -0.0782 126 HIS E O   
12943 C CB  . HIS E 126 ? 0.4065 0.4190 0.5522 -0.0036 0.2003  -0.1151 126 HIS E CB  
12944 C CG  . HIS E 126 ? 0.4767 0.4728 0.6034 -0.0163 0.2189  -0.1304 126 HIS E CG  
12945 N ND1 . HIS E 126 ? 0.5441 0.5308 0.6972 -0.0127 0.2318  -0.1396 126 HIS E ND1 
12946 C CD2 . HIS E 126 ? 0.4987 0.4866 0.5810 -0.0335 0.2218  -0.1352 126 HIS E CD2 
12947 C CE1 . HIS E 126 ? 0.5500 0.5250 0.6744 -0.0280 0.2432  -0.1521 126 HIS E CE1 
12948 N NE2 . HIS E 126 ? 0.5324 0.5087 0.6128 -0.0406 0.2366  -0.1486 126 HIS E NE2 
12949 N N   . SER E 127 ? 0.3980 0.4186 0.6101 0.0309  0.1714  -0.0835 127 SER E N   
12950 C CA  . SER E 127 ? 0.3602 0.4048 0.6089 0.0451  0.1553  -0.0670 127 SER E CA  
12951 C C   . SER E 127 ? 0.3937 0.4569 0.6824 0.0488  0.1646  -0.0744 127 SER E C   
12952 O O   . SER E 127 ? 0.4318 0.4899 0.7136 0.0391  0.1834  -0.0914 127 SER E O   
12953 C CB  . SER E 127 ? 0.3398 0.3762 0.6163 0.0576  0.1516  -0.0530 127 SER E CB  
12954 O OG  . SER E 127 ? 0.3630 0.3785 0.6656 0.0593  0.1745  -0.0663 127 SER E OG  
12955 N N   . THR E 128 ? 0.3792 0.4660 0.7105 0.0621  0.1517  -0.0609 128 THR E N   
12956 C CA  . THR E 128 ? 0.3261 0.4329 0.7039 0.0663  0.1607  -0.0677 128 THR E CA  
12957 C C   . THR E 128 ? 0.3734 0.4834 0.8117 0.0827  0.1653  -0.0604 128 THR E C   
12958 O O   . THR E 128 ? 0.3897 0.4969 0.8389 0.0932  0.1518  -0.0418 128 THR E O   
12959 C CB  . THR E 128 ? 0.3113 0.4513 0.6950 0.0658  0.1403  -0.0609 128 THR E CB  
12960 O OG1 . THR E 128 ? 0.3299 0.4884 0.7270 0.0771  0.1150  -0.0396 128 THR E OG1 
12961 C CG2 . THR E 128 ? 0.2751 0.4099 0.6050 0.0506  0.1357  -0.0676 128 THR E CG2 
12962 N N   . HIS E 129 ? 0.4079 0.5207 0.8763 0.0821  0.1804  -0.0719 129 HIS E N   
12963 C CA  . HIS E 129 ? 0.4240 0.5356 0.9432 0.0943  0.1824  -0.0653 129 HIS E CA  
12964 C C   . HIS E 129 ? 0.3904 0.5282 0.9464 0.0958  0.1808  -0.0670 129 HIS E C   
12965 O O   . HIS E 129 ? 0.3898 0.5205 0.9402 0.0853  0.1993  -0.0846 129 HIS E O   
12966 C CB  . HIS E 129 ? 0.4906 0.5659 0.9998 0.0878  0.2061  -0.0816 129 HIS E CB  
12967 C CG  . HIS E 129 ? 0.5825 0.6515 1.1457 0.0996  0.2105  -0.0761 129 HIS E CG  
12968 N ND1 . HIS E 129 ? 0.6157 0.6887 1.2141 0.1158  0.1940  -0.0518 129 HIS E ND1 
12969 C CD2 . HIS E 129 ? 0.6478 0.7069 1.2372 0.0970  0.2297  -0.0908 129 HIS E CD2 
12970 C CE1 . HIS E 129 ? 0.6643 0.7290 1.3099 0.1228  0.2024  -0.0512 129 HIS E CE1 
12971 N NE2 . HIS E 129 ? 0.6887 0.7453 1.3311 0.1118  0.2249  -0.0762 129 HIS E NE2 
12972 N N   . GLY E 130 ? 0.3896 0.5593 0.9831 0.1079  0.1578  -0.0477 130 GLY E N   
12973 C CA  . GLY E 130 ? 0.4024 0.6016 1.0304 0.1083  0.1528  -0.0489 130 GLY E CA  
12974 C C   . GLY E 130 ? 0.3810 0.5911 0.9784 0.0929  0.1558  -0.0628 130 GLY E C   
12975 O O   . GLY E 130 ? 0.3659 0.5838 0.9326 0.0882  0.1437  -0.0601 130 GLY E O   
12976 N N   . SER E 131 ? 0.3746 0.5835 0.9802 0.0843  0.1732  -0.0775 131 SER E N   
12977 C CA  . SER E 131 ? 0.3844 0.6009 0.9638 0.0688  0.1769  -0.0883 131 SER E CA  
12978 C C   . SER E 131 ? 0.4026 0.5858 0.9271 0.0546  0.1976  -0.1022 131 SER E C   
12979 O O   . SER E 131 ? 0.4369 0.6196 0.9335 0.0404  0.2032  -0.1096 131 SER E O   
12980 C CB  . SER E 131 ? 0.3725 0.6068 0.9884 0.0654  0.1845  -0.0947 131 SER E CB  
12981 O OG  . SER E 131 ? 0.3964 0.6070 1.0083 0.0593  0.2121  -0.1089 131 SER E OG  
12982 N N   . LYS E 132 ? 0.3895 0.5454 0.8992 0.0576  0.2074  -0.1045 132 LYS E N   
12983 C CA  . LYS E 132 ? 0.4032 0.5289 0.8615 0.0431  0.2261  -0.1182 132 LYS E CA  
12984 C C   . LYS E 132 ? 0.4100 0.5200 0.8258 0.0417  0.2181  -0.1139 132 LYS E C   
12985 O O   . LYS E 132 ? 0.4045 0.5255 0.8335 0.0533  0.2003  -0.1003 132 LYS E O   
12986 C CB  . LYS E 132 ? 0.4245 0.5304 0.8979 0.0437  0.2464  -0.1293 132 LYS E CB  
12987 C CG  . LYS E 132 ? 0.4358 0.5574 0.9568 0.0462  0.2561  -0.1342 132 LYS E CG  
12988 C CD  . LYS E 132 ? 0.4733 0.5745 0.9878 0.0368  0.2829  -0.1529 132 LYS E CD  
12989 C CE  . LYS E 132 ? 0.4881 0.6032 1.0607 0.0433  0.2932  -0.1571 132 LYS E CE  
12990 N NZ  . LYS E 132 ? 0.5176 0.6121 1.1092 0.0449  0.3126  -0.1700 132 LYS E NZ  
12991 N N   . LEU E 133 ? 0.4234 0.5100 0.7882 0.0272  0.2302  -0.1243 133 LEU E N   
12992 C CA  . LEU E 133 ? 0.4306 0.4977 0.7567 0.0253  0.2258  -0.1224 133 LEU E CA  
12993 C C   . LEU E 133 ? 0.4710 0.5210 0.8174 0.0353  0.2297  -0.1219 133 LEU E C   
12994 O O   . LEU E 133 ? 0.5196 0.5610 0.8897 0.0359  0.2439  -0.1309 133 LEU E O   
12995 C CB  . LEU E 133 ? 0.4381 0.4858 0.7066 0.0062  0.2362  -0.1329 133 LEU E CB  
12996 C CG  . LEU E 133 ? 0.4181 0.4753 0.6570 -0.0052 0.2310  -0.1301 133 LEU E CG  
12997 C CD1 . LEU E 133 ? 0.4463 0.4841 0.6308 -0.0228 0.2397  -0.1368 133 LEU E CD1 
12998 C CD2 . LEU E 133 ? 0.3641 0.4327 0.6018 0.0018  0.2121  -0.1188 133 LEU E CD2 
12999 N N   . GLY E 134 ? 0.4432 0.4878 0.7828 0.0427  0.2182  -0.1116 134 GLY E N   
13000 C CA  . GLY E 134 ? 0.4779 0.5036 0.8385 0.0517  0.2217  -0.1088 134 GLY E CA  
13001 C C   . GLY E 134 ? 0.5229 0.5197 0.8371 0.0395  0.2296  -0.1193 134 GLY E C   
13002 O O   . GLY E 134 ? 0.4896 0.4817 0.7554 0.0235  0.2330  -0.1289 134 GLY E O   
13003 N N   . PRO E 135 ? 0.5946 0.5723 0.9254 0.0463  0.2316  -0.1162 135 PRO E N   
13004 C CA  . PRO E 135 ? 0.6150 0.5656 0.9065 0.0338  0.2385  -0.1274 135 PRO E CA  
13005 C C   . PRO E 135 ? 0.5536 0.5051 0.8000 0.0285  0.2263  -0.1207 135 PRO E C   
13006 O O   . PRO E 135 ? 0.5382 0.5086 0.7843 0.0355  0.2040  -0.0998 135 PRO E O   
13007 C CB  . PRO E 135 ? 0.6584 0.5909 0.9914 0.0450  0.2414  -0.1214 135 PRO E CB  
13008 C CG  . PRO E 135 ? 0.6520 0.6051 1.0379 0.0656  0.2289  -0.0986 135 PRO E CG  
13009 C CD  . PRO E 135 ? 0.6193 0.5989 1.0101 0.0644  0.2279  -0.1020 135 PRO E CD  
13010 N N   . MET E 136 ? 0.5306 0.4643 0.7307 0.0119  0.2316  -0.1339 136 MET E N   
13011 C CA  . MET E 136 ? 0.4970 0.4296 0.6502 0.0031  0.2144  -0.1248 136 MET E CA  
13012 C C   . MET E 136 ? 0.4783 0.4059 0.6445 0.0125  0.1986  -0.1051 136 MET E C   
13013 O O   . MET E 136 ? 0.5195 0.4305 0.7171 0.0189  0.2069  -0.1059 136 MET E O   
13014 C CB  . MET E 136 ? 0.5681 0.4827 0.6787 -0.0158 0.2251  -0.1441 136 MET E CB  
13015 C CG  . MET E 136 ? 0.6245 0.5441 0.7167 -0.0292 0.2344  -0.1571 136 MET E CG  
13016 S SD  . MET E 136 ? 0.6450 0.5835 0.6986 -0.0370 0.2223  -0.1477 136 MET E SD  
13017 C CE  . MET E 136 ? 0.6153 0.5414 0.6193 -0.0513 0.2125  -0.1485 136 MET E CE  
13018 N N   . VAL E 137 ? 0.4572 0.3990 0.6007 0.0130  0.1771  -0.0874 137 VAL E N   
13019 C CA  . VAL E 137 ? 0.4465 0.3859 0.5913 0.0184  0.1623  -0.0681 137 VAL E CA  
13020 C C   . VAL E 137 ? 0.4845 0.4204 0.5833 0.0052  0.1534  -0.0687 137 VAL E C   
13021 O O   . VAL E 137 ? 0.4904 0.4353 0.5601 -0.0035 0.1503  -0.0753 137 VAL E O   
13022 C CB  . VAL E 137 ? 0.3853 0.3501 0.5493 0.0320  0.1447  -0.0456 137 VAL E CB  
13023 C CG1 . VAL E 137 ? 0.3831 0.3510 0.6003 0.0465  0.1507  -0.0401 137 VAL E CG1 
13024 C CG2 . VAL E 137 ? 0.3524 0.3400 0.4963 0.0286  0.1357  -0.0479 137 VAL E CG2 
13025 N N   . LYS E 138 ? 0.5016 0.4254 0.5984 0.0037  0.1491  -0.0603 138 LYS E N   
13026 C CA  . LYS E 138 ? 0.4974 0.4159 0.5579 -0.0098 0.1432  -0.0634 138 LYS E CA  
13027 C C   . LYS E 138 ? 0.4603 0.3928 0.5107 -0.0068 0.1260  -0.0433 138 LYS E C   
13028 O O   . LYS E 138 ? 0.4425 0.3800 0.5137 0.0035  0.1208  -0.0255 138 LYS E O   
13029 C CB  . LYS E 138 ? 0.5568 0.4486 0.6208 -0.0188 0.1552  -0.0760 138 LYS E CB  
13030 C CG  . LYS E 138 ? 0.6211 0.4986 0.6887 -0.0254 0.1750  -0.1016 138 LYS E CG  
13031 C CD  . LYS E 138 ? 0.7215 0.5726 0.7943 -0.0354 0.1867  -0.1169 138 LYS E CD  
13032 C CE  . LYS E 138 ? 0.7960 0.6339 0.8722 -0.0426 0.2092  -0.1462 138 LYS E CE  
13033 N NZ  . LYS E 138 ? 0.8224 0.6524 0.9514 -0.0269 0.2233  -0.1468 138 LYS E NZ  
13034 N N   . VAL E 139 ? 0.4912 0.4311 0.5103 -0.0163 0.1179  -0.0459 139 VAL E N   
13035 C CA  . VAL E 139 ? 0.4795 0.4287 0.4874 -0.0176 0.1060  -0.0326 139 VAL E CA  
13036 C C   . VAL E 139 ? 0.4920 0.4255 0.4869 -0.0312 0.1086  -0.0405 139 VAL E C   
13037 O O   . VAL E 139 ? 0.5369 0.4716 0.5090 -0.0417 0.1061  -0.0507 139 VAL E O   
13038 C CB  . VAL E 139 ? 0.3679 0.3392 0.3576 -0.0174 0.0945  -0.0304 139 VAL E CB  
13039 C CG1 . VAL E 139 ? 0.3539 0.3373 0.3370 -0.0174 0.0852  -0.0182 139 VAL E CG1 
13040 C CG2 . VAL E 139 ? 0.3442 0.3315 0.3459 -0.0070 0.0919  -0.0278 139 VAL E CG2 
13041 N N   . PRO E 140 ? 0.4950 0.4148 0.5060 -0.0319 0.1126  -0.0344 140 PRO E N   
13042 C CA  . PRO E 140 ? 0.5099 0.4126 0.5150 -0.0461 0.1166  -0.0447 140 PRO E CA  
13043 C C   . PRO E 140 ? 0.5443 0.4600 0.5296 -0.0550 0.1052  -0.0409 140 PRO E C   
13044 O O   . PRO E 140 ? 0.5921 0.4997 0.5666 -0.0691 0.1053  -0.0526 140 PRO E O   
13045 C CB  . PRO E 140 ? 0.4945 0.3812 0.5299 -0.0418 0.1231  -0.0340 140 PRO E CB  
13046 C CG  . PRO E 140 ? 0.4912 0.3840 0.5484 -0.0253 0.1241  -0.0210 140 PRO E CG  
13047 C CD  . PRO E 140 ? 0.4739 0.3935 0.5123 -0.0197 0.1133  -0.0161 140 PRO E CD  
13048 N N   . GLN E 141 ? 0.5544 0.4911 0.5371 -0.0476 0.0959  -0.0257 141 GLN E N   
13049 C CA  . GLN E 141 ? 0.5575 0.5091 0.5274 -0.0542 0.0864  -0.0229 141 GLN E CA  
13050 C C   . GLN E 141 ? 0.5311 0.5019 0.4879 -0.0497 0.0783  -0.0236 141 GLN E C   
13051 O O   . GLN E 141 ? 0.5244 0.5135 0.4823 -0.0448 0.0727  -0.0147 141 GLN E O   
13052 C CB  . GLN E 141 ? 0.5786 0.5394 0.5598 -0.0513 0.0850  -0.0059 141 GLN E CB  
13053 C CG  . GLN E 141 ? 0.6916 0.6334 0.6900 -0.0570 0.0924  -0.0016 141 GLN E CG  
13054 C CD  . GLN E 141 ? 0.8127 0.7435 0.8305 -0.0462 0.0993  0.0092  141 GLN E CD  
13055 O OE1 . GLN E 141 ? 0.8219 0.7663 0.8393 -0.0341 0.0962  0.0178  141 GLN E OE1 
13056 N NE2 . GLN E 141 ? 0.8834 0.7900 0.9217 -0.0506 0.1081  0.0088  141 GLN E NE2 
13057 N N   . PHE E 142 ? 0.5261 0.4931 0.4720 -0.0518 0.0791  -0.0345 142 PHE E N   
13058 C CA  . PHE E 142 ? 0.4794 0.4617 0.4171 -0.0484 0.0719  -0.0345 142 PHE E CA  
13059 C C   . PHE E 142 ? 0.3759 0.3673 0.3058 -0.0563 0.0621  -0.0336 142 PHE E C   
13060 O O   . PHE E 142 ? 0.3697 0.3536 0.2899 -0.0680 0.0600  -0.0387 142 PHE E O   
13061 C CB  . PHE E 142 ? 0.4276 0.4032 0.3581 -0.0493 0.0771  -0.0438 142 PHE E CB  
13062 C CG  . PHE E 142 ? 0.3844 0.3733 0.3120 -0.0456 0.0710  -0.0425 142 PHE E CG  
13063 C CD1 . PHE E 142 ? 0.3334 0.3343 0.2735 -0.0343 0.0702  -0.0390 142 PHE E CD1 
13064 C CD2 . PHE E 142 ? 0.3969 0.3869 0.3110 -0.0541 0.0653  -0.0439 142 PHE E CD2 
13065 C CE1 . PHE E 142 ? 0.3369 0.3484 0.2782 -0.0321 0.0654  -0.0401 142 PHE E CE1 
13066 C CE2 . PHE E 142 ? 0.3513 0.3507 0.2680 -0.0507 0.0604  -0.0414 142 PHE E CE2 
13067 C CZ  . PHE E 142 ? 0.3192 0.3282 0.2506 -0.0400 0.0613  -0.0410 142 PHE E CZ  
13068 N N   . LEU E 143 ? 0.3657 0.3745 0.3019 -0.0499 0.0559  -0.0278 143 LEU E N   
13069 C CA  . LEU E 143 ? 0.3856 0.4049 0.3235 -0.0547 0.0469  -0.0258 143 LEU E CA  
13070 C C   . LEU E 143 ? 0.4218 0.4438 0.3553 -0.0557 0.0403  -0.0272 143 LEU E C   
13071 O O   . LEU E 143 ? 0.4315 0.4565 0.3678 -0.0486 0.0418  -0.0286 143 LEU E O   
13072 C CB  . LEU E 143 ? 0.3162 0.3534 0.2680 -0.0479 0.0462  -0.0205 143 LEU E CB  
13073 C CG  . LEU E 143 ? 0.3203 0.3579 0.2773 -0.0485 0.0520  -0.0144 143 LEU E CG  
13074 C CD1 . LEU E 143 ? 0.3112 0.3700 0.2768 -0.0420 0.0536  -0.0100 143 LEU E CD1 
13075 C CD2 . LEU E 143 ? 0.3361 0.3673 0.2956 -0.0604 0.0498  -0.0144 143 LEU E CD2 
13076 N N   . PHE E 144 ? 0.4119 0.4341 0.3405 -0.0653 0.0320  -0.0253 144 PHE E N   
13077 C CA  . PHE E 144 ? 0.4189 0.4419 0.3426 -0.0677 0.0251  -0.0223 144 PHE E CA  
13078 C C   . PHE E 144 ? 0.4326 0.4642 0.3611 -0.0752 0.0120  -0.0151 144 PHE E C   
13079 O O   . PHE E 144 ? 0.4401 0.4779 0.3774 -0.0780 0.0097  -0.0147 144 PHE E O   
13080 C CB  . PHE E 144 ? 0.3822 0.3914 0.2835 -0.0747 0.0310  -0.0274 144 PHE E CB  
13081 C CG  . PHE E 144 ? 0.4213 0.4221 0.3036 -0.0885 0.0313  -0.0327 144 PHE E CG  
13082 C CD1 . PHE E 144 ? 0.4386 0.4299 0.3218 -0.0896 0.0406  -0.0408 144 PHE E CD1 
13083 C CD2 . PHE E 144 ? 0.4722 0.4743 0.3354 -0.1015 0.0225  -0.0297 144 PHE E CD2 
13084 C CE1 . PHE E 144 ? 0.4643 0.4464 0.3322 -0.1037 0.0421  -0.0497 144 PHE E CE1 
13085 C CE2 . PHE E 144 ? 0.5050 0.5013 0.3475 -0.1166 0.0226  -0.0382 144 PHE E CE2 
13086 C CZ  . PHE E 144 ? 0.4999 0.4853 0.3457 -0.1179 0.0331  -0.0502 144 PHE E CZ  
13087 N N   . SER E 145 ? 0.4399 0.4736 0.3661 -0.0784 0.0029  -0.0076 145 SER E N   
13088 C CA  . SER E 145 ? 0.4355 0.4801 0.3702 -0.0849 -0.0123 0.0024  145 SER E CA  
13089 C C   . SER E 145 ? 0.4331 0.4736 0.3387 -0.1003 -0.0202 0.0063  145 SER E C   
13090 O O   . SER E 145 ? 0.4609 0.4933 0.3476 -0.1033 -0.0168 0.0075  145 SER E O   
13091 C CB  . SER E 145 ? 0.4479 0.5017 0.4114 -0.0753 -0.0193 0.0119  145 SER E CB  
13092 O OG  . SER E 145 ? 0.4865 0.5519 0.4631 -0.0807 -0.0359 0.0247  145 SER E OG  
13093 N N   . CYS E 146 ? 0.4294 0.4774 0.3308 -0.1116 -0.0305 0.0076  146 CYS E N   
13094 C CA  . CYS E 146 ? 0.4418 0.4927 0.3159 -0.1278 -0.0427 0.0135  146 CYS E CA  
13095 C C   . CYS E 146 ? 0.4674 0.5330 0.3633 -0.1246 -0.0607 0.0341  146 CYS E C   
13096 O O   . CYS E 146 ? 0.4899 0.5708 0.4133 -0.1233 -0.0726 0.0405  146 CYS E O   
13097 C CB  . CYS E 146 ? 0.4659 0.5205 0.3280 -0.1428 -0.0477 0.0043  146 CYS E CB  
13098 S SG  . CYS E 146 ? 0.5795 0.6131 0.4145 -0.1506 -0.0273 -0.0199 146 CYS E SG  
13099 N N   . ALA E 147 ? 0.4844 0.5457 0.3729 -0.1230 -0.0623 0.0455  147 ALA E N   
13100 C CA  . ALA E 147 ? 0.4644 0.5356 0.3817 -0.1170 -0.0774 0.0670  147 ALA E CA  
13101 C C   . ALA E 147 ? 0.5408 0.6248 0.4400 -0.1325 -0.0989 0.0850  147 ALA E C   
13102 O O   . ALA E 147 ? 0.5910 0.6734 0.4459 -0.1493 -0.0989 0.0790  147 ALA E O   
13103 C CB  . ALA E 147 ? 0.4529 0.5122 0.3750 -0.1086 -0.0688 0.0723  147 ALA E CB  
13104 N N   . PRO E 148 ? 0.5530 0.6512 0.4875 -0.1275 -0.1176 0.1067  148 PRO E N   
13105 C CA  . PRO E 148 ? 0.5888 0.7028 0.5081 -0.1421 -0.1421 0.1295  148 PRO E CA  
13106 C C   . PRO E 148 ? 0.6662 0.7715 0.5414 -0.1535 -0.1415 0.1416  148 PRO E C   
13107 O O   . PRO E 148 ? 0.6851 0.7747 0.5657 -0.1446 -0.1275 0.1426  148 PRO E O   
13108 C CB  . PRO E 148 ? 0.5418 0.6691 0.5203 -0.1289 -0.1585 0.1516  148 PRO E CB  
13109 C CG  . PRO E 148 ? 0.5073 0.6216 0.5255 -0.1082 -0.1390 0.1390  148 PRO E CG  
13110 C CD  . PRO E 148 ? 0.5105 0.6135 0.5031 -0.1087 -0.1172 0.1097  148 PRO E CD  
13111 N N   . SER E 149 ? 0.7373 0.8541 0.5681 -0.1744 -0.1549 0.1484  149 SER E N   
13112 C CA  . SER E 149 ? 0.8101 0.9214 0.5890 -0.1892 -0.1510 0.1561  149 SER E CA  
13113 C C   . SER E 149 ? 0.8539 0.9612 0.6494 -0.1829 -0.1567 0.1877  149 SER E C   
13114 O O   . SER E 149 ? 0.8681 0.9625 0.6358 -0.1874 -0.1419 0.1889  149 SER E O   
13115 C CB  . SER E 149 ? 0.8663 0.9966 0.5959 -0.2145 -0.1684 0.1593  149 SER E CB  
13116 O OG  . SER E 149 ? 0.8923 1.0431 0.6467 -0.2153 -0.1952 0.1875  149 SER E OG  
13117 N N   . PHE E 150 ? 0.8123 0.9302 0.6572 -0.1724 -0.1769 0.2131  150 PHE E N   
13118 C CA  . PHE E 150 ? 0.7810 0.8947 0.6495 -0.1666 -0.1851 0.2463  150 PHE E CA  
13119 C C   . PHE E 150 ? 0.7643 0.8533 0.6538 -0.1523 -0.1602 0.2355  150 PHE E C   
13120 O O   . PHE E 150 ? 0.8206 0.9003 0.7120 -0.1530 -0.1588 0.2567  150 PHE E O   
13121 C CB  . PHE E 150 ? 0.7450 0.8736 0.6762 -0.1545 -0.2093 0.2713  150 PHE E CB  
13122 C CG  . PHE E 150 ? 0.6900 0.8096 0.6867 -0.1306 -0.1972 0.2548  150 PHE E CG  
13123 C CD1 . PHE E 150 ? 0.6927 0.7950 0.7326 -0.1150 -0.1874 0.2620  150 PHE E CD1 
13124 C CD2 . PHE E 150 ? 0.6341 0.7640 0.6498 -0.1253 -0.1953 0.2320  150 PHE E CD2 
13125 C CE1 . PHE E 150 ? 0.6436 0.7400 0.7403 -0.0949 -0.1754 0.2434  150 PHE E CE1 
13126 C CE2 . PHE E 150 ? 0.5886 0.7133 0.6604 -0.1050 -0.1828 0.2164  150 PHE E CE2 
13127 C CZ  . PHE E 150 ? 0.5938 0.7023 0.7039 -0.0901 -0.1728 0.2209  150 PHE E CZ  
13128 N N   . LEU E 151 ? 0.7004 0.7800 0.6040 -0.1410 -0.1410 0.2028  151 LEU E N   
13129 C CA  . LEU E 151 ? 0.6700 0.7310 0.6054 -0.1249 -0.1211 0.1905  151 LEU E CA  
13130 C C   . LEU E 151 ? 0.6695 0.7158 0.5693 -0.1329 -0.1035 0.1877  151 LEU E C   
13131 O O   . LEU E 151 ? 0.6591 0.6923 0.5859 -0.1242 -0.0941 0.1916  151 LEU E O   
13132 C CB  . LEU E 151 ? 0.6206 0.6799 0.5723 -0.1134 -0.1069 0.1577  151 LEU E CB  
13133 C CG  . LEU E 151 ? 0.5755 0.6240 0.5733 -0.0946 -0.0929 0.1450  151 LEU E CG  
13134 C CD1 . LEU E 151 ? 0.6040 0.6562 0.6589 -0.0836 -0.1065 0.1657  151 LEU E CD1 
13135 C CD2 . LEU E 151 ? 0.5251 0.5775 0.5302 -0.0870 -0.0826 0.1180  151 LEU E CD2 
13136 N N   . ALA E 152 ? 0.7070 0.7563 0.5489 -0.1502 -0.0983 0.1798  152 ALA E N   
13137 C CA  . ALA E 152 ? 0.7482 0.7862 0.5563 -0.1588 -0.0791 0.1752  152 ALA E CA  
13138 C C   . ALA E 152 ? 0.8415 0.8857 0.6151 -0.1767 -0.0890 0.2064  152 ALA E C   
13139 O O   . ALA E 152 ? 0.8908 0.9290 0.6317 -0.1872 -0.0731 0.2054  152 ALA E O   
13140 C CB  . ALA E 152 ? 0.7172 0.7531 0.4868 -0.1658 -0.0613 0.1427  152 ALA E CB  
13141 N N   . GLN E 153 ? 0.8814 0.9393 0.6643 -0.1801 -0.1155 0.2358  153 GLN E N   
13142 C CA  . GLN E 153 ? 0.9130 0.9823 0.6609 -0.1975 -0.1282 0.2644  153 GLN E CA  
13143 C C   . GLN E 153 ? 0.9002 0.9578 0.6729 -0.1934 -0.1247 0.2916  153 GLN E C   
13144 O O   . GLN E 153 ? 0.9432 1.0072 0.6924 -0.2041 -0.1263 0.3062  153 GLN E O   
13145 C CB  . GLN E 153 ? 0.9592 1.0502 0.7196 -0.1993 -0.1572 0.2790  153 GLN E CB  
13146 C CG  . GLN E 153 ? 1.0609 1.1617 0.8434 -0.1999 -0.1770 0.3155  153 GLN E CG  
13147 C CD  . GLN E 153 ? 1.1241 1.2414 0.9513 -0.1919 -0.2040 0.3312  153 GLN E CD  
13148 O OE1 . GLN E 153 ? 1.1282 1.2623 0.9400 -0.1990 -0.2141 0.3181  153 GLN E OE1 
13149 N NE2 . GLN E 153 ? 1.1618 1.2739 1.0502 -0.1767 -0.2144 0.3580  153 GLN E NE2 
13150 N N   . LYS E 154 ? 0.8605 0.9007 0.6851 -0.1768 -0.1174 0.2927  154 LYS E N   
13151 C CA  . LYS E 154 ? 0.8803 0.9049 0.7393 -0.1721 -0.1125 0.3168  154 LYS E CA  
13152 C C   . LYS E 154 ? 0.9037 0.9082 0.7935 -0.1596 -0.0861 0.2895  154 LYS E C   
13153 O O   . LYS E 154 ? 0.8885 0.8892 0.8103 -0.1438 -0.0799 0.2606  154 LYS E O   
13154 C CB  . LYS E 154 ? 0.9073 0.9323 0.8293 -0.1591 -0.1357 0.3478  154 LYS E CB  
13155 C CG  . LYS E 154 ? 0.9874 1.0283 0.9050 -0.1661 -0.1555 0.3779  154 LYS E CG  
13156 C CD  . LYS E 154 ? 1.0396 1.1062 0.9150 -0.1783 -0.1716 0.3747  154 LYS E CD  
13157 C CE  . LYS E 154 ? 1.0956 1.1785 0.9690 -0.1864 -0.1912 0.4066  154 LYS E CE  
13158 N NZ  . LYS E 154 ? 1.1087 1.2173 0.9419 -0.2000 -0.2063 0.4004  154 LYS E NZ  
13159 N N   . GLY E 155 ? 0.8867 0.8807 0.7676 -0.1679 -0.0716 0.3004  155 GLY E N   
13160 C CA  . GLY E 155 ? 0.8420 0.8186 0.7612 -0.1574 -0.0510 0.2820  155 GLY E CA  
13161 C C   . GLY E 155 ? 0.7964 0.7712 0.6889 -0.1600 -0.0250 0.2456  155 GLY E C   
13162 O O   . GLY E 155 ? 0.7642 0.7277 0.6831 -0.1556 -0.0085 0.2351  155 GLY E O   
13163 N N   . LEU E 156 ? 0.7842 0.7703 0.6280 -0.1672 -0.0217 0.2264  156 LEU E N   
13164 C CA  . LEU E 156 ? 0.7444 0.7293 0.5706 -0.1666 0.0014  0.1906  156 LEU E CA  
13165 C C   . LEU E 156 ? 0.7488 0.7367 0.5267 -0.1859 0.0186  0.1939  156 LEU E C   
13166 O O   . LEU E 156 ? 0.8218 0.8164 0.5665 -0.2020 0.0103  0.2220  156 LEU E O   
13167 C CB  . LEU E 156 ? 0.7170 0.7102 0.5253 -0.1625 -0.0028 0.1659  156 LEU E CB  
13168 C CG  . LEU E 156 ? 0.6623 0.6576 0.5099 -0.1471 -0.0211 0.1660  156 LEU E CG  
13169 C CD1 . LEU E 156 ? 0.6310 0.6337 0.4607 -0.1449 -0.0219 0.1413  156 LEU E CD1 
13170 C CD2 . LEU E 156 ? 0.6411 0.6260 0.5462 -0.1295 -0.0161 0.1581  156 LEU E CD2 
13171 N N   . PRO E 157 ? 0.6732 0.6583 0.4482 -0.1849 0.0428  0.1664  157 PRO E N   
13172 C CA  . PRO E 157 ? 0.7185 0.7094 0.4459 -0.2039 0.0620  0.1649  157 PRO E CA  
13173 C C   . PRO E 157 ? 0.8105 0.8134 0.4898 -0.2121 0.0534  0.1576  157 PRO E C   
13174 O O   . PRO E 157 ? 0.8088 0.8142 0.4844 -0.2083 0.0407  0.1487  157 PRO E O   
13175 C CB  . PRO E 157 ? 0.6489 0.6369 0.3923 -0.1959 0.0859  0.1307  157 PRO E CB  
13176 C CG  . PRO E 157 ? 0.5688 0.5484 0.3725 -0.1760 0.0795  0.1259  157 PRO E CG  
13177 C CD  . PRO E 157 ? 0.5785 0.5573 0.3948 -0.1678 0.0538  0.1385  157 PRO E CD  
13178 N N   . ASN E 158 ? 0.8949 0.9057 0.5410 -0.2230 0.0602  0.1595  158 ASN E N   
13179 C CA  . ASN E 158 ? 0.9640 0.9872 0.5703 -0.2322 0.0480  0.1547  158 ASN E CA  
13180 C C   . ASN E 158 ? 0.9306 0.9541 0.5260 -0.2300 0.0574  0.1171  158 ASN E C   
13181 O O   . ASN E 158 ? 0.8420 0.8592 0.4472 -0.2248 0.0799  0.0922  158 ASN E O   
13182 C CB  . ASN E 158 ? 1.0662 1.0991 0.6378 -0.2465 0.0539  0.1644  158 ASN E CB  
13183 C CG  . ASN E 158 ? 1.1309 1.1625 0.6940 -0.2493 0.0839  0.1406  158 ASN E CG  
13184 O OD1 . ASN E 158 ? 1.1693 1.1917 0.7632 -0.2409 0.1002  0.1344  158 ASN E OD1 
13185 N ND2 . ASN E 158 ? 1.1577 1.1998 0.6816 -0.2619 0.0915  0.1272  158 ASN E ND2 
13186 N N   . ASN E 159 ? 1.0112 1.0416 0.5935 -0.2327 0.0384  0.1152  159 ASN E N   
13187 C CA  . ASN E 159 ? 1.0468 1.0769 0.6201 -0.2322 0.0430  0.0828  159 ASN E CA  
13188 C C   . ASN E 159 ? 0.9210 0.9399 0.5260 -0.2171 0.0489  0.0676  159 ASN E C   
13189 O O   . ASN E 159 ? 0.9155 0.9315 0.5192 -0.2147 0.0543  0.0416  159 ASN E O   
13190 C CB  . ASN E 159 ? 1.1483 1.1796 0.6978 -0.2405 0.0653  0.0564  159 ASN E CB  
13191 C CG  . ASN E 159 ? 1.2537 1.2994 0.7634 -0.2584 0.0571  0.0634  159 ASN E CG  
13192 O OD1 . ASN E 159 ? 1.2903 1.3412 0.7799 -0.2672 0.0560  0.0435  159 ASN E OD1 
13193 N ND2 . ASN E 159 ? 1.2886 1.3408 0.7878 -0.2647 0.0518  0.0923  159 ASN E ND2 
13194 N N   . VAL E 160 ? 0.8262 0.8383 0.4611 -0.2078 0.0484  0.0838  160 VAL E N   
13195 C CA  . VAL E 160 ? 0.7372 0.7413 0.4074 -0.1915 0.0508  0.0695  160 VAL E CA  
13196 C C   . VAL E 160 ? 0.7262 0.7357 0.4039 -0.1877 0.0258  0.0773  160 VAL E C   
13197 O O   . VAL E 160 ? 0.7340 0.7505 0.4092 -0.1929 0.0060  0.1047  160 VAL E O   
13198 C CB  . VAL E 160 ? 0.6510 0.6476 0.3696 -0.1764 0.0548  0.0773  160 VAL E CB  
13199 C CG1 . VAL E 160 ? 0.5830 0.5760 0.3445 -0.1563 0.0471  0.0666  160 VAL E CG1 
13200 C CG2 . VAL E 160 ? 0.6124 0.6056 0.3312 -0.1781 0.0811  0.0621  160 VAL E CG2 
13201 N N   . GLN E 161 ? 0.7154 0.7228 0.4029 -0.1795 0.0268  0.0547  161 GLN E N   
13202 C CA  . GLN E 161 ? 0.7011 0.7162 0.3888 -0.1805 0.0063  0.0580  161 GLN E CA  
13203 C C   . GLN E 161 ? 0.6509 0.6633 0.3877 -0.1600 0.0000  0.0545  161 GLN E C   
13204 O O   . GLN E 161 ? 0.6321 0.6496 0.3750 -0.1584 -0.0105 0.0491  161 GLN E O   
13205 C CB  . GLN E 161 ? 0.7493 0.7660 0.4019 -0.1933 0.0125  0.0343  161 GLN E CB  
13206 C CG  . GLN E 161 ? 0.8552 0.8793 0.4659 -0.2126 0.0142  0.0337  161 GLN E CG  
13207 C CD  . GLN E 161 ? 0.9371 0.9771 0.5348 -0.2230 -0.0120 0.0600  161 GLN E CD  
13208 O OE1 . GLN E 161 ? 0.9661 1.0149 0.5672 -0.2254 -0.0305 0.0623  161 GLN E OE1 
13209 N NE2 . GLN E 161 ? 0.9723 1.0173 0.5568 -0.2297 -0.0133 0.0797  161 GLN E NE2 
13210 N N   . GLY E 162 ? 0.5981 0.6039 0.3693 -0.1456 0.0071  0.0561  162 GLY E N   
13211 C CA  . GLY E 162 ? 0.5326 0.5379 0.3467 -0.1275 0.0030  0.0508  162 GLY E CA  
13212 C C   . GLY E 162 ? 0.4792 0.4777 0.3209 -0.1158 0.0155  0.0453  162 GLY E C   
13213 O O   . GLY E 162 ? 0.4712 0.4658 0.3050 -0.1217 0.0237  0.0517  162 GLY E O   
13214 N N   . ALA E 163 ? 0.4875 0.4057 0.3446 -0.0942 -0.0771 0.0406  163 ALA E N   
13215 C CA  . ALA E 163 ? 0.4602 0.3893 0.3323 -0.0802 -0.0573 0.0355  163 ALA E CA  
13216 C C   . ALA E 163 ? 0.4533 0.3983 0.3471 -0.0671 -0.0366 0.0232  163 ALA E C   
13217 O O   . ALA E 163 ? 0.4583 0.4114 0.3723 -0.0650 -0.0399 0.0209  163 ALA E O   
13218 C CB  . ALA E 163 ? 0.4526 0.3914 0.3616 -0.0718 -0.0695 0.0453  163 ALA E CB  
13219 N N   . LEU E 164 ? 0.4368 0.3854 0.3264 -0.0597 -0.0165 0.0161  164 LEU E N   
13220 C CA  . LEU E 164 ? 0.4052 0.3675 0.3157 -0.0474 -0.0003 0.0073  164 LEU E CA  
13221 C C   . LEU E 164 ? 0.4005 0.3765 0.3404 -0.0360 0.0022  0.0087  164 LEU E C   
13222 O O   . LEU E 164 ? 0.4415 0.4154 0.3768 -0.0360 0.0028  0.0117  164 LEU E O   
13223 C CB  . LEU E 164 ? 0.4454 0.4013 0.3337 -0.0477 0.0187  -0.0017 164 LEU E CB  
13224 C CG  . LEU E 164 ? 0.5431 0.4953 0.4179 -0.0489 0.0279  -0.0020 164 LEU E CG  
13225 C CD1 . LEU E 164 ? 0.5563 0.5224 0.4528 -0.0364 0.0410  -0.0065 164 LEU E CD1 
13226 C CD2 . LEU E 164 ? 0.6072 0.5409 0.4449 -0.0614 0.0373  -0.0071 164 LEU E CD2 
13227 N N   . GLY E 165 ? 0.3854 0.3735 0.3540 -0.0282 0.0044  0.0062  165 GLY E N   
13228 C CA  . GLY E 165 ? 0.3737 0.3719 0.3685 -0.0196 0.0079  0.0058  165 GLY E CA  
13229 C C   . GLY E 165 ? 0.3639 0.3674 0.3577 -0.0129 0.0237  -0.0015 165 GLY E C   
13230 O O   . GLY E 165 ? 0.3919 0.3958 0.3812 -0.0122 0.0305  -0.0056 165 GLY E O   
13231 N N   . LEU E 166 ? 0.3498 0.3558 0.3469 -0.0090 0.0280  -0.0022 166 LEU E N   
13232 C CA  . LEU E 166 ? 0.3523 0.3623 0.3473 -0.0044 0.0391  -0.0073 166 LEU E CA  
13233 C C   . LEU E 166 ? 0.3580 0.3720 0.3703 -0.0010 0.0427  -0.0105 166 LEU E C   
13234 O O   . LEU E 166 ? 0.3804 0.3950 0.3876 0.0004  0.0484  -0.0135 166 LEU E O   
13235 C CB  . LEU E 166 ? 0.3513 0.3599 0.3326 -0.0050 0.0423  -0.0069 166 LEU E CB  
13236 C CG  . LEU E 166 ? 0.4163 0.4192 0.3801 -0.0088 0.0450  -0.0071 166 LEU E CG  
13237 C CD1 . LEU E 166 ? 0.4705 0.4746 0.4302 -0.0094 0.0502  -0.0074 166 LEU E CD1 
13238 C CD2 . LEU E 166 ? 0.4227 0.4254 0.3845 -0.0062 0.0510  -0.0107 166 LEU E CD2 
13239 N N   . GLY E 167 ? 0.3389 0.3548 0.3729 -0.0005 0.0396  -0.0102 167 GLY E N   
13240 C CA  . GLY E 167 ? 0.3490 0.3665 0.4022 0.0021  0.0462  -0.0152 167 GLY E CA  
13241 C C   . GLY E 167 ? 0.3663 0.3843 0.4146 0.0016  0.0591  -0.0225 167 GLY E C   
13242 O O   . GLY E 167 ? 0.3862 0.4034 0.4182 0.0001  0.0608  -0.0219 167 GLY E O   
13243 N N   . GLN E 168 ? 0.3891 0.4052 0.4481 0.0016  0.0691  -0.0294 168 GLN E N   
13244 C CA  . GLN E 168 ? 0.4158 0.4285 0.4669 -0.0019 0.0834  -0.0371 168 GLN E CA  
13245 C C   . GLN E 168 ? 0.4290 0.4468 0.5068 -0.0023 0.0897  -0.0400 168 GLN E C   
13246 O O   . GLN E 168 ? 0.4607 0.4804 0.5681 -0.0012 0.0979  -0.0460 168 GLN E O   
13247 C CB  . GLN E 168 ? 0.4465 0.4516 0.4931 -0.0044 0.0938  -0.0453 168 GLN E CB  
13248 C CG  . GLN E 168 ? 0.4671 0.4674 0.4849 -0.0066 0.0882  -0.0430 168 GLN E CG  
13249 C CD  . GLN E 168 ? 0.5374 0.5348 0.5280 -0.0102 0.0874  -0.0401 168 GLN E CD  
13250 O OE1 . GLN E 168 ? 0.5918 0.5815 0.5685 -0.0162 0.0975  -0.0450 168 GLN E OE1 
13251 N NE2 . GLN E 168 ? 0.5619 0.5639 0.5455 -0.0072 0.0763  -0.0320 168 GLN E NE2 
13252 N N   . ALA E 169 ? 0.3930 0.4135 0.4648 -0.0038 0.0859  -0.0360 169 ALA E N   
13253 C CA  . ALA E 169 ? 0.3328 0.3600 0.4330 -0.0051 0.0890  -0.0375 169 ALA E CA  
13254 C C   . ALA E 169 ? 0.2968 0.3212 0.3761 -0.0092 0.0894  -0.0352 169 ALA E C   
13255 O O   . ALA E 169 ? 0.3303 0.3498 0.3828 -0.0086 0.0817  -0.0302 169 ALA E O   
13256 C CB  . ALA E 169 ? 0.3256 0.3607 0.4561 -0.0017 0.0729  -0.0310 169 ALA E CB  
13257 N N   . PRO E 170 ? 0.3176 0.3446 0.4122 -0.0135 0.0992  -0.0391 170 PRO E N   
13258 C CA  . PRO E 170 ? 0.3480 0.3680 0.4191 -0.0187 0.1030  -0.0377 170 PRO E CA  
13259 C C   . PRO E 170 ? 0.3549 0.3736 0.4144 -0.0182 0.0885  -0.0307 170 PRO E C   
13260 O O   . PRO E 170 ? 0.3357 0.3445 0.3682 -0.0200 0.0902  -0.0286 170 PRO E O   
13261 C CB  . PRO E 170 ? 0.3658 0.3909 0.4646 -0.0243 0.1172  -0.0439 170 PRO E CB  
13262 C CG  . PRO E 170 ? 0.3436 0.3819 0.4886 -0.0202 0.1151  -0.0464 170 PRO E CG  
13263 C CD  . PRO E 170 ? 0.3106 0.3456 0.4463 -0.0144 0.1107  -0.0461 170 PRO E CD  
13264 N N   . ILE E 171 ? 0.3594 0.3849 0.4360 -0.0168 0.0745  -0.0269 171 ILE E N   
13265 C CA  . ILE E 171 ? 0.3317 0.3509 0.3881 -0.0186 0.0642  -0.0225 171 ILE E CA  
13266 C C   . ILE E 171 ? 0.3651 0.3820 0.4075 -0.0154 0.0530  -0.0184 171 ILE E C   
13267 O O   . ILE E 171 ? 0.3858 0.3984 0.4186 -0.0188 0.0428  -0.0155 171 ILE E O   
13268 C CB  . ILE E 171 ? 0.2663 0.2893 0.3411 -0.0248 0.0568  -0.0214 171 ILE E CB  
13269 C CG1 . ILE E 171 ? 0.2799 0.3144 0.3895 -0.0250 0.0445  -0.0186 171 ILE E CG1 
13270 C CG2 . ILE E 171 ? 0.2562 0.2798 0.3410 -0.0295 0.0702  -0.0256 171 ILE E CG2 
13271 C CD1 . ILE E 171 ? 0.2986 0.3340 0.4165 -0.0327 0.0295  -0.0150 171 ILE E CD1 
13272 N N   . SER E 172 ? 0.3328 0.3502 0.3705 -0.0107 0.0562  -0.0189 172 SER E N   
13273 C CA  . SER E 172 ? 0.3463 0.3607 0.3690 -0.0087 0.0491  -0.0155 172 SER E CA  
13274 C C   . SER E 172 ? 0.3783 0.3845 0.3760 -0.0091 0.0512  -0.0154 172 SER E C   
13275 O O   . SER E 172 ? 0.4097 0.4119 0.4015 -0.0092 0.0577  -0.0170 172 SER E O   
13276 C CB  . SER E 172 ? 0.3451 0.3615 0.3694 -0.0046 0.0530  -0.0167 172 SER E CB  
13277 O OG  . SER E 172 ? 0.4027 0.4160 0.4142 -0.0039 0.0626  -0.0198 172 SER E OG  
13278 N N   . LEU E 173 ? 0.3705 0.3726 0.3547 -0.0097 0.0469  -0.0136 173 LEU E N   
13279 C CA  . LEU E 173 ? 0.3651 0.3593 0.3320 -0.0098 0.0516  -0.0152 173 LEU E CA  
13280 C C   . LEU E 173 ? 0.3922 0.3870 0.3583 -0.0040 0.0585  -0.0156 173 LEU E C   
13281 O O   . LEU E 173 ? 0.3914 0.3800 0.3535 -0.0031 0.0625  -0.0162 173 LEU E O   
13282 C CB  . LEU E 173 ? 0.3743 0.3636 0.3276 -0.0130 0.0495  -0.0148 173 LEU E CB  
13283 C CG  . LEU E 173 ? 0.4011 0.3831 0.3425 -0.0120 0.0588  -0.0184 173 LEU E CG  
13284 C CD1 . LEU E 173 ? 0.4012 0.3727 0.3347 -0.0150 0.0626  -0.0222 173 LEU E CD1 
13285 C CD2 . LEU E 173 ? 0.4442 0.4212 0.3714 -0.0174 0.0597  -0.0189 173 LEU E CD2 
13286 N N   . GLN E 174 ? 0.4170 0.4177 0.3870 -0.0009 0.0583  -0.0145 174 GLN E N   
13287 C CA  . GLN E 174 ? 0.4173 0.4177 0.3853 0.0027  0.0608  -0.0132 174 GLN E CA  
13288 C C   . GLN E 174 ? 0.4264 0.4226 0.3913 0.0013  0.0631  -0.0127 174 GLN E C   
13289 O O   . GLN E 174 ? 0.4611 0.4512 0.4205 0.0026  0.0633  -0.0099 174 GLN E O   
13290 C CB  . GLN E 174 ? 0.3906 0.3973 0.3617 0.0041  0.0586  -0.0124 174 GLN E CB  
13291 C CG  . GLN E 174 ? 0.3788 0.3870 0.3514 0.0022  0.0590  -0.0139 174 GLN E CG  
13292 C CD  . GLN E 174 ? 0.3523 0.3632 0.3356 0.0008  0.0582  -0.0157 174 GLN E CD  
13293 O OE1 . GLN E 174 ? 0.3719 0.3828 0.3569 0.0000  0.0543  -0.0141 174 GLN E OE1 
13294 N NE2 . GLN E 174 ? 0.3463 0.3578 0.3370 -0.0003 0.0618  -0.0189 174 GLN E NE2 
13295 N N   . ASN E 175 ? 0.3846 0.3828 0.3547 -0.0020 0.0655  -0.0151 175 ASN E N   
13296 C CA  . ASN E 175 ? 0.3860 0.3787 0.3508 -0.0058 0.0714  -0.0158 175 ASN E CA  
13297 C C   . ASN E 175 ? 0.3969 0.3817 0.3571 -0.0071 0.0724  -0.0141 175 ASN E C   
13298 O O   . ASN E 175 ? 0.4119 0.3872 0.3606 -0.0096 0.0750  -0.0114 175 ASN E O   
13299 C CB  A ASN E 175 ? 0.3892 0.3867 0.3675 -0.0092 0.0776  -0.0208 175 ASN E CB  
13300 C CB  B ASN E 175 ? 0.3910 0.3887 0.3701 -0.0091 0.0773  -0.0207 175 ASN E CB  
13301 C CG  A ASN E 175 ? 0.3912 0.3902 0.3688 -0.0092 0.0803  -0.0238 175 ASN E CG  
13302 C CG  B ASN E 175 ? 0.4029 0.3937 0.3748 -0.0153 0.0879  -0.0232 175 ASN E CG  
13303 O OD1 A ASN E 175 ? 0.4058 0.3997 0.3661 -0.0099 0.0784  -0.0219 175 ASN E OD1 
13304 O OD1 B ASN E 175 ? 0.3917 0.3785 0.3637 -0.0187 0.0910  -0.0226 175 ASN E OD1 
13305 N ND2 A ASN E 175 ? 0.3524 0.3577 0.3510 -0.0088 0.0834  -0.0281 175 ASN E ND2 
13306 N ND2 B ASN E 175 ? 0.4418 0.4290 0.4051 -0.0187 0.0946  -0.0266 175 ASN E ND2 
13307 N N   . GLN E 176 ? 0.3929 0.3788 0.3591 -0.0070 0.0697  -0.0153 176 GLN E N   
13308 C CA  . GLN E 176 ? 0.4062 0.3823 0.3675 -0.0092 0.0713  -0.0150 176 GLN E CA  
13309 C C   . GLN E 176 ? 0.3915 0.3590 0.3453 -0.0044 0.0708  -0.0124 176 GLN E C   
13310 O O   . GLN E 176 ? 0.4027 0.3589 0.3517 -0.0050 0.0728  -0.0101 176 GLN E O   
13311 C CB  . GLN E 176 ? 0.4080 0.3852 0.3746 -0.0132 0.0678  -0.0179 176 GLN E CB  
13312 C CG  . GLN E 176 ? 0.3694 0.3551 0.3529 -0.0182 0.0669  -0.0193 176 GLN E CG  
13313 C CD  . GLN E 176 ? 0.3818 0.3665 0.3701 -0.0245 0.0598  -0.0204 176 GLN E CD  
13314 O OE1 . GLN E 176 ? 0.4037 0.3797 0.3868 -0.0292 0.0617  -0.0217 176 GLN E OE1 
13315 N NE2 . GLN E 176 ? 0.3722 0.3642 0.3699 -0.0261 0.0500  -0.0190 176 GLN E NE2 
13316 N N   . LEU E 177 ? 0.3263 0.2985 0.2824 0.0003  0.0688  -0.0125 177 LEU E N   
13317 C CA  . LEU E 177 ? 0.3392 0.3060 0.2981 0.0059  0.0693  -0.0104 177 LEU E CA  
13318 C C   . LEU E 177 ? 0.3494 0.3133 0.3071 0.0081  0.0647  -0.0032 177 LEU E C   
13319 O O   . LEU E 177 ? 0.3775 0.3315 0.3378 0.0109  0.0632  0.0011  177 LEU E O   
13320 C CB  . LEU E 177 ? 0.3377 0.3120 0.3028 0.0090  0.0702  -0.0128 177 LEU E CB  
13321 C CG  . LEU E 177 ? 0.3059 0.2775 0.2646 0.0045  0.0743  -0.0189 177 LEU E CG  
13322 C CD1 . LEU E 177 ? 0.3193 0.2975 0.2809 0.0055  0.0763  -0.0203 177 LEU E CD1 
13323 C CD2 . LEU E 177 ? 0.3239 0.2815 0.2793 0.0035  0.0812  -0.0235 177 LEU E CD2 
13324 N N   . PHE E 178 ? 0.3589 0.3295 0.3116 0.0057  0.0617  -0.0018 178 PHE E N   
13325 C CA  . PHE E 178 ? 0.3527 0.3175 0.2955 0.0037  0.0560  0.0049  178 PHE E CA  
13326 C C   . PHE E 178 ? 0.3647 0.3144 0.2948 -0.0010 0.0575  0.0088  178 PHE E C   
13327 O O   . PHE E 178 ? 0.4180 0.3565 0.3426 -0.0007 0.0505  0.0173  178 PHE E O   
13328 C CB  . PHE E 178 ? 0.3788 0.3489 0.3123 -0.0015 0.0566  0.0024  178 PHE E CB  
13329 C CG  . PHE E 178 ? 0.3820 0.3642 0.3252 0.0016  0.0535  0.0002  178 PHE E CG  
13330 C CD1 . PHE E 178 ? 0.4040 0.3919 0.3614 0.0077  0.0490  0.0026  178 PHE E CD1 
13331 C CD2 . PHE E 178 ? 0.3748 0.3618 0.3154 -0.0020 0.0568  -0.0048 178 PHE E CD2 
13332 C CE1 . PHE E 178 ? 0.3824 0.3808 0.3481 0.0088  0.0474  0.0006  178 PHE E CE1 
13333 C CE2 . PHE E 178 ? 0.3600 0.3557 0.3083 -0.0002 0.0540  -0.0063 178 PHE E CE2 
13334 C CZ  . PHE E 178 ? 0.3682 0.3697 0.3276 0.0046  0.0490  -0.0033 178 PHE E CZ  
13335 N N   . SER E 179 ? 0.3791 0.3281 0.3057 -0.0063 0.0658  0.0036  179 SER E N   
13336 C CA  . SER E 179 ? 0.4632 0.3981 0.3759 -0.0135 0.0696  0.0066  179 SER E CA  
13337 C C   . SER E 179 ? 0.4128 0.3359 0.3299 -0.0108 0.0686  0.0098  179 SER E C   
13338 O O   . SER E 179 ? 0.4154 0.3222 0.3205 -0.0142 0.0663  0.0173  179 SER E O   
13339 C CB  . SER E 179 ? 0.5424 0.4826 0.4570 -0.0207 0.0804  -0.0008 179 SER E CB  
13340 O OG  . SER E 179 ? 0.5829 0.5290 0.5138 -0.0193 0.0824  -0.0057 179 SER E OG  
13341 N N   . HIS E 180 ? 0.3841 0.3123 0.3158 -0.0057 0.0703  0.0044  180 HIS E N   
13342 C CA  . HIS E 180 ? 0.4274 0.3418 0.3628 -0.0039 0.0717  0.0050  180 HIS E CA  
13343 C C   . HIS E 180 ? 0.4302 0.3357 0.3726 0.0038  0.0647  0.0131  180 HIS E C   
13344 O O   . HIS E 180 ? 0.4417 0.3301 0.3834 0.0039  0.0633  0.0187  180 HIS E O   
13345 C CB  . HIS E 180 ? 0.4527 0.3711 0.3965 -0.0030 0.0763  -0.0043 180 HIS E CB  
13346 C CG  . HIS E 180 ? 0.5360 0.4374 0.4799 -0.0044 0.0805  -0.0065 180 HIS E CG  
13347 N ND1 . HIS E 180 ? 0.5600 0.4515 0.5133 0.0024  0.0831  -0.0083 180 HIS E ND1 
13348 C CD2 . HIS E 180 ? 0.5900 0.4815 0.5280 -0.0124 0.0837  -0.0082 180 HIS E CD2 
13349 C CE1 . HIS E 180 ? 0.5909 0.4653 0.5416 -0.0012 0.0878  -0.0113 180 HIS E CE1 
13350 N NE2 . HIS E 180 ? 0.6182 0.4924 0.5586 -0.0106 0.0873  -0.0108 180 HIS E NE2 
13351 N N   . PHE E 181 ? 0.4207 0.3378 0.3735 0.0100  0.0595  0.0144  181 PHE E N   
13352 C CA  . PHE E 181 ? 0.4115 0.3241 0.3819 0.0183  0.0519  0.0218  181 PHE E CA  
13353 C C   . PHE E 181 ? 0.4338 0.3442 0.3964 0.0165  0.0372  0.0345  181 PHE E C   
13354 O O   . PHE E 181 ? 0.4486 0.3549 0.4287 0.0227  0.0264  0.0436  181 PHE E O   
13355 C CB  . PHE E 181 ? 0.3795 0.3057 0.3725 0.0258  0.0565  0.0147  181 PHE E CB  
13356 C CG  . PHE E 181 ? 0.3647 0.2871 0.3608 0.0258  0.0701  0.0030  181 PHE E CG  
13357 C CD1 . PHE E 181 ? 0.4042 0.3108 0.4118 0.0296  0.0758  0.0011  181 PHE E CD1 
13358 C CD2 . PHE E 181 ? 0.3704 0.3024 0.3562 0.0209  0.0762  -0.0059 181 PHE E CD2 
13359 C CE1 . PHE E 181 ? 0.4191 0.3188 0.4233 0.0268  0.0891  -0.0113 181 PHE E CE1 
13360 C CE2 . PHE E 181 ? 0.3486 0.2738 0.3300 0.0177  0.0863  -0.0159 181 PHE E CE2 
13361 C CZ  . PHE E 181 ? 0.3771 0.2858 0.3656 0.0200  0.0936  -0.0195 181 PHE E CZ  
13362 N N   . GLY E 182 ? 0.4140 0.3258 0.3512 0.0071  0.0365  0.0349  182 GLY E N   
13363 C CA  . GLY E 182 ? 0.4332 0.3394 0.3538 0.0017  0.0232  0.0453  182 GLY E CA  
13364 C C   . GLY E 182 ? 0.4316 0.3533 0.3697 0.0071  0.0138  0.0467  182 GLY E C   
13365 O O   . GLY E 182 ? 0.4602 0.3768 0.3999 0.0068  -0.0030 0.0585  182 GLY E O   
13366 N N   . LEU E 183 ? 0.4090 0.3486 0.3603 0.0110  0.0230  0.0357  183 LEU E N   
13367 C CA  . LEU E 183 ? 0.3981 0.3535 0.3678 0.0151  0.0166  0.0356  183 LEU E CA  
13368 C C   . LEU E 183 ? 0.4327 0.3890 0.3791 0.0059  0.0098  0.0371  183 LEU E C   
13369 O O   . LEU E 183 ? 0.4727 0.4223 0.3927 -0.0024 0.0171  0.0327  183 LEU E O   
13370 C CB  . LEU E 183 ? 0.3760 0.3462 0.3615 0.0198  0.0295  0.0239  183 LEU E CB  
13371 C CG  . LEU E 183 ? 0.3811 0.3497 0.3828 0.0258  0.0412  0.0174  183 LEU E CG  
13372 C CD1 . LEU E 183 ? 0.3780 0.3579 0.3806 0.0249  0.0514  0.0072  183 LEU E CD1 
13373 C CD2 . LEU E 183 ? 0.4014 0.3703 0.4345 0.0345  0.0378  0.0217  183 LEU E CD2 
13374 N N   . LYS E 184 ? 0.4195 0.3843 0.3776 0.0067  -0.0026 0.0418  184 LYS E N   
13375 C CA  . LYS E 184 ? 0.4759 0.4423 0.4127 -0.0027 -0.0069 0.0399  184 LYS E CA  
13376 C C   . LYS E 184 ? 0.4627 0.4395 0.3997 -0.0022 0.0098  0.0264  184 LYS E C   
13377 O O   . LYS E 184 ? 0.4072 0.3944 0.3667 0.0058  0.0183  0.0212  184 LYS E O   
13378 C CB  . LYS E 184 ? 0.5360 0.5118 0.4912 -0.0021 -0.0243 0.0470  184 LYS E CB  
13379 C CG  . LYS E 184 ? 0.5908 0.5695 0.5274 -0.0117 -0.0270 0.0424  184 LYS E CG  
13380 C CD  . LYS E 184 ? 0.6397 0.6233 0.5870 -0.0155 -0.0492 0.0519  184 LYS E CD  
13381 C CE  . LYS E 184 ? 0.8330 0.8170 0.7590 -0.0266 -0.0500 0.0450  184 LYS E CE  
13382 N NZ  . LYS E 184 ? 0.7990 0.7946 0.7339 -0.0227 -0.0304 0.0310  184 LYS E NZ  
13383 N N   . ARG E 185 ? 0.4448 0.4162 0.3564 -0.0113 0.0150  0.0207  185 ARG E N   
13384 C CA  . ARG E 185 ? 0.3815 0.3611 0.2975 -0.0105 0.0287  0.0095  185 ARG E CA  
13385 C C   . ARG E 185 ? 0.3827 0.3750 0.3133 -0.0087 0.0256  0.0067  185 ARG E C   
13386 O O   . ARG E 185 ? 0.4189 0.4084 0.3364 -0.0158 0.0238  0.0037  185 ARG E O   
13387 C CB  . ARG E 185 ? 0.3724 0.3411 0.2635 -0.0201 0.0386  0.0031  185 ARG E CB  
13388 C CG  . ARG E 185 ? 0.3996 0.3555 0.2761 -0.0240 0.0445  0.0050  185 ARG E CG  
13389 C CD  . ARG E 185 ? 0.4800 0.4283 0.3413 -0.0327 0.0607  -0.0043 185 ARG E CD  
13390 N NE  . ARG E 185 ? 0.5406 0.4892 0.4118 -0.0304 0.0697  -0.0055 185 ARG E NE  
13391 C CZ  . ARG E 185 ? 0.5950 0.5543 0.4887 -0.0263 0.0792  -0.0128 185 ARG E CZ  
13392 N NH1 . ARG E 185 ? 0.6168 0.5862 0.5257 -0.0235 0.0821  -0.0193 185 ARG E NH1 
13393 N NH2 . ARG E 185 ? 0.6612 0.6198 0.5627 -0.0260 0.0844  -0.0127 185 ARG E NH2 
13394 N N   . GLN E 186 ? 0.3615 0.3656 0.3174 -0.0006 0.0264  0.0069  186 GLN E N   
13395 C CA  . GLN E 186 ? 0.3602 0.3760 0.3316 0.0003  0.0242  0.0053  186 GLN E CA  
13396 C C   . GLN E 186 ? 0.3538 0.3776 0.3440 0.0068  0.0330  0.0023  186 GLN E C   
13397 O O   . GLN E 186 ? 0.3740 0.3963 0.3726 0.0117  0.0357  0.0039  186 GLN E O   
13398 C CB  . GLN E 186 ? 0.3854 0.4055 0.3681 -0.0003 0.0098  0.0130  186 GLN E CB  
13399 C CG  . GLN E 186 ? 0.4030 0.4354 0.4026 -0.0017 0.0066  0.0117  186 GLN E CG  
13400 C CD  . GLN E 186 ? 0.4266 0.4680 0.4519 0.0002  -0.0072 0.0199  186 GLN E CD  
13401 O OE1 . GLN E 186 ? 0.4580 0.5084 0.5131 0.0082  -0.0031 0.0212  186 GLN E OE1 
13402 N NE2 . GLN E 186 ? 0.4507 0.4878 0.4647 -0.0078 -0.0238 0.0257  186 GLN E NE2 
13403 N N   . PHE E 187 ? 0.3337 0.3629 0.3277 0.0057  0.0381  -0.0021 187 PHE E N   
13404 C CA  . PHE E 187 ? 0.3036 0.3379 0.3105 0.0088  0.0458  -0.0041 187 PHE E CA  
13405 C C   . PHE E 187 ? 0.3401 0.3821 0.3563 0.0060  0.0464  -0.0051 187 PHE E C   
13406 O O   . PHE E 187 ? 0.3300 0.3718 0.3406 0.0019  0.0418  -0.0055 187 PHE E O   
13407 C CB  . PHE E 187 ? 0.3243 0.3519 0.3199 0.0084  0.0528  -0.0075 187 PHE E CB  
13408 C CG  . PHE E 187 ? 0.3613 0.3868 0.3488 0.0047  0.0523  -0.0094 187 PHE E CG  
13409 C CD1 . PHE E 187 ? 0.3703 0.3913 0.3506 0.0033  0.0509  -0.0107 187 PHE E CD1 
13410 C CD2 . PHE E 187 ? 0.3523 0.3783 0.3402 0.0021  0.0543  -0.0100 187 PHE E CD2 
13411 C CE1 . PHE E 187 ? 0.3388 0.3580 0.3199 0.0013  0.0516  -0.0131 187 PHE E CE1 
13412 C CE2 . PHE E 187 ? 0.3064 0.3290 0.2917 -0.0004 0.0518  -0.0102 187 PHE E CE2 
13413 C CZ  . PHE E 187 ? 0.3126 0.3328 0.2981 0.0002  0.0506  -0.0121 187 PHE E CZ  
13414 N N   . SER E 188 ? 0.3794 0.4267 0.4098 0.0072  0.0539  -0.0064 188 SER E N   
13415 C CA  . SER E 188 ? 0.3849 0.4398 0.4266 0.0034  0.0566  -0.0072 188 SER E CA  
13416 C C   . SER E 188 ? 0.3976 0.4474 0.4307 -0.0003 0.0689  -0.0108 188 SER E C   
13417 O O   . SER E 188 ? 0.4092 0.4545 0.4404 0.0011  0.0779  -0.0136 188 SER E O   
13418 C CB  . SER E 188 ? 0.3943 0.4620 0.4672 0.0061  0.0550  -0.0053 188 SER E CB  
13419 O OG  . SER E 188 ? 0.3810 0.4513 0.4589 0.0072  0.0397  0.0002  188 SER E OG  
13420 N N   . VAL E 189 ? 0.4096 0.4577 0.4355 -0.0064 0.0691  -0.0104 189 VAL E N   
13421 C CA  . VAL E 189 ? 0.3958 0.4350 0.4062 -0.0130 0.0778  -0.0115 189 VAL E CA  
13422 C C   . VAL E 189 ? 0.3757 0.4198 0.3964 -0.0193 0.0869  -0.0126 189 VAL E C   
13423 O O   . VAL E 189 ? 0.4002 0.4497 0.4298 -0.0218 0.0816  -0.0105 189 VAL E O   
13424 C CB  . VAL E 189 ? 0.3666 0.3955 0.3585 -0.0163 0.0696  -0.0082 189 VAL E CB  
13425 C CG1 . VAL E 189 ? 0.3462 0.3629 0.3182 -0.0251 0.0746  -0.0067 189 VAL E CG1 
13426 C CG2 . VAL E 189 ? 0.3634 0.3891 0.3503 -0.0108 0.0624  -0.0080 189 VAL E CG2 
13427 N N   . CYS E 190 ? 0.3743 0.4149 0.3924 -0.0234 0.1021  -0.0167 190 CYS E N   
13428 C CA  . CYS E 190 ? 0.3722 0.4156 0.3979 -0.0316 0.1148  -0.0188 190 CYS E CA  
13429 C C   . CYS E 190 ? 0.4173 0.4416 0.4081 -0.0436 0.1262  -0.0202 190 CYS E C   
13430 O O   . CYS E 190 ? 0.4116 0.4296 0.3960 -0.0470 0.1426  -0.0269 190 CYS E O   
13431 C CB  . CYS E 190 ? 0.3517 0.4109 0.4156 -0.0271 0.1266  -0.0240 190 CYS E CB  
13432 S SG  . CYS E 190 ? 0.4584 0.5329 0.5537 -0.0343 0.1348  -0.0246 190 CYS E SG  
13433 N N   . LEU E 191 ? 0.4088 0.4212 0.3755 -0.0510 0.1171  -0.0137 191 LEU E N   
13434 C CA  . LEU E 191 ? 0.4400 0.4308 0.3682 -0.0648 0.1232  -0.0121 191 LEU E CA  
13435 C C   . LEU E 191 ? 0.4569 0.4447 0.3824 -0.0775 0.1433  -0.0157 191 LEU E C   
13436 O O   . LEU E 191 ? 0.4485 0.4482 0.3978 -0.0780 0.1454  -0.0148 191 LEU E O   
13437 C CB  . LEU E 191 ? 0.4460 0.4238 0.3536 -0.0682 0.1040  -0.0018 191 LEU E CB  
13438 C CG  . LEU E 191 ? 0.4787 0.4603 0.3936 -0.0566 0.0871  0.0006  191 LEU E CG  
13439 C CD1 . LEU E 191 ? 0.4919 0.4602 0.3933 -0.0600 0.0698  0.0105  191 LEU E CD1 
13440 C CD2 . LEU E 191 ? 0.4727 0.4506 0.3767 -0.0545 0.0906  -0.0041 191 LEU E CD2 
13441 N N   . SER E 192 ? 0.4873 0.4573 0.3813 -0.0896 0.1588  -0.0203 192 SER E N   
13442 C CA  . SER E 192 ? 0.4997 0.4622 0.3837 -0.1049 0.1819  -0.0249 192 SER E CA  
13443 C C   . SER E 192 ? 0.5637 0.5025 0.4043 -0.1218 0.1746  -0.0147 192 SER E C   
13444 O O   . SER E 192 ? 0.5834 0.5018 0.3858 -0.1273 0.1590  -0.0072 192 SER E O   
13445 C CB  . SER E 192 ? 0.5001 0.4521 0.3716 -0.1097 0.2022  -0.0369 192 SER E CB  
13446 O OG  . SER E 192 ? 0.4770 0.4185 0.3392 -0.1221 0.2174  -0.0417 192 SER E OG  
13447 N N   . ARG E 193 ? 0.5632 0.5047 0.4129 -0.1302 0.1841  -0.0132 193 ARG E N   
13448 C CA  . ARG E 193 ? 0.5557 0.4723 0.3649 -0.1486 0.1807  -0.0032 193 ARG E CA  
13449 C C   . ARG E 193 ? 0.6040 0.4945 0.3698 -0.1621 0.1877  -0.0075 193 ARG E C   
13450 O O   . ARG E 193 ? 0.6471 0.5114 0.3696 -0.1762 0.1759  0.0026  193 ARG E O   
13451 C CB  . ARG E 193 ? 0.5673 0.4961 0.4050 -0.1523 0.1890  -0.0025 193 ARG E CB  
13452 C CG  . ARG E 193 ? 0.6470 0.5519 0.4510 -0.1698 0.1896  0.0042  193 ARG E CG  
13453 C CD  . ARG E 193 ? 0.7024 0.6225 0.5411 -0.1719 0.1971  0.0043  193 ARG E CD  
13454 N NE  . ARG E 193 ? 0.7725 0.7075 0.6406 -0.1593 0.1771  0.0107  193 ARG E NE  
13455 C CZ  . ARG E 193 ? 0.8049 0.7639 0.7195 -0.1521 0.1765  0.0076  193 ARG E CZ  
13456 N NH1 . ARG E 193 ? 0.8004 0.7738 0.7416 -0.1598 0.1997  -0.0003 193 ARG E NH1 
13457 N NH2 . ARG E 193 ? 0.7931 0.7612 0.7284 -0.1384 0.1532  0.0118  193 ARG E NH2 
13458 N N   . TYR E 194 ? 0.6077 0.5035 0.3856 -0.1585 0.2057  -0.0224 194 TYR E N   
13459 C CA  . TYR E 194 ? 0.6598 0.5300 0.4000 -0.1735 0.2178  -0.0302 194 TYR E CA  
13460 C C   . TYR E 194 ? 0.6858 0.5387 0.3935 -0.1755 0.2100  -0.0327 194 TYR E C   
13461 O O   . TYR E 194 ? 0.6624 0.5295 0.3929 -0.1614 0.2083  -0.0370 194 TYR E O   
13462 C CB  . TYR E 194 ? 0.6071 0.4894 0.3820 -0.1715 0.2457  -0.0461 194 TYR E CB  
13463 C CG  . TYR E 194 ? 0.5842 0.4890 0.4007 -0.1676 0.2513  -0.0438 194 TYR E CG  
13464 C CD1 . TYR E 194 ? 0.6150 0.5068 0.4111 -0.1828 0.2546  -0.0388 194 TYR E CD1 
13465 C CD2 . TYR E 194 ? 0.5334 0.4712 0.4076 -0.1499 0.2500  -0.0450 194 TYR E CD2 
13466 C CE1 . TYR E 194 ? 0.6463 0.5583 0.4806 -0.1806 0.2587  -0.0363 194 TYR E CE1 
13467 C CE2 . TYR E 194 ? 0.5142 0.4726 0.4268 -0.1482 0.2524  -0.0424 194 TYR E CE2 
13468 C CZ  . TYR E 194 ? 0.5906 0.5362 0.4837 -0.1636 0.2571  -0.0383 194 TYR E CZ  
13469 O OH  . TYR E 194 ? 0.5878 0.5532 0.5195 -0.1633 0.2591  -0.0358 194 TYR E OH  
13470 N N   . SER E 195 ? 0.7576 0.5786 0.4109 -0.1943 0.2037  -0.0292 195 SER E N   
13471 C CA  . SER E 195 ? 0.7908 0.5917 0.4088 -0.2007 0.1956  -0.0317 195 SER E CA  
13472 C C   . SER E 195 ? 0.8109 0.6094 0.4387 -0.2012 0.2219  -0.0511 195 SER E C   
13473 O O   . SER E 195 ? 0.8280 0.6156 0.4401 -0.2025 0.2196  -0.0565 195 SER E O   
13474 C CB  . SER E 195 ? 0.8535 0.6196 0.4111 -0.2229 0.1787  -0.0214 195 SER E CB  
13475 O OG  . SER E 195 ? 0.9126 0.6618 0.4496 -0.2394 0.1963  -0.0272 195 SER E OG  
13476 N N   . THR E 196 ? 0.7858 0.5934 0.4413 -0.2008 0.2466  -0.0613 196 THR E N   
13477 C CA  . THR E 196 ? 0.7834 0.5870 0.4531 -0.2020 0.2737  -0.0800 196 THR E CA  
13478 C C   . THR E 196 ? 0.7194 0.5539 0.4521 -0.1787 0.2820  -0.0873 196 THR E C   
13479 O O   . THR E 196 ? 0.7014 0.5322 0.4498 -0.1775 0.3014  -0.1014 196 THR E O   
13480 C CB  . THR E 196 ? 0.7758 0.5711 0.4457 -0.2150 0.2983  -0.0887 196 THR E CB  
13481 O OG1 . THR E 196 ? 0.7357 0.5611 0.4548 -0.2028 0.3010  -0.0846 196 THR E OG1 
13482 C CG2 . THR E 196 ? 0.8482 0.6099 0.4538 -0.2397 0.2914  -0.0821 196 THR E CG2 
13483 N N   . SER E 197 ? 0.6787 0.5409 0.4458 -0.1613 0.2664  -0.0775 197 SER E N   
13484 C CA  . SER E 197 ? 0.6349 0.5240 0.4580 -0.1402 0.2699  -0.0825 197 SER E CA  
13485 C C   . SER E 197 ? 0.6005 0.5041 0.4296 -0.1271 0.2461  -0.0711 197 SER E C   
13486 O O   . SER E 197 ? 0.6650 0.5695 0.4779 -0.1300 0.2299  -0.0588 197 SER E O   
13487 C CB  . SER E 197 ? 0.6094 0.5247 0.4898 -0.1315 0.2836  -0.0861 197 SER E CB  
13488 O OG  . SER E 197 ? 0.6033 0.5326 0.4913 -0.1311 0.2721  -0.0746 197 SER E OG  
13489 N N   . ASN E 198 ? 0.5854 0.4987 0.4387 -0.1131 0.2449  -0.0755 198 ASN E N   
13490 C CA  . ASN E 198 ? 0.5611 0.4849 0.4173 -0.1017 0.2248  -0.0668 198 ASN E CA  
13491 C C   . ASN E 198 ? 0.4915 0.4457 0.3952 -0.0866 0.2185  -0.0611 198 ASN E C   
13492 O O   . ASN E 198 ? 0.5116 0.4831 0.4578 -0.0808 0.2294  -0.0651 198 ASN E O   
13493 C CB  . ASN E 198 ? 0.6252 0.5445 0.4854 -0.0941 0.2258  -0.0738 198 ASN E CB  
13494 C CG  . ASN E 198 ? 0.7206 0.6092 0.5275 -0.1098 0.2244  -0.0769 198 ASN E CG  
13495 O OD1 . ASN E 198 ? 0.8087 0.6793 0.5723 -0.1257 0.2168  -0.0710 198 ASN E OD1 
13496 N ND2 . ASN E 198 ? 0.7191 0.6003 0.5285 -0.1062 0.2293  -0.0849 198 ASN E ND2 
13497 N N   . GLY E 199 ? 0.4483 0.4077 0.3442 -0.0817 0.2005  -0.0516 199 GLY E N   
13498 C CA  . GLY E 199 ? 0.4727 0.4579 0.4130 -0.0650 0.1873  -0.0465 199 GLY E CA  
13499 C C   . GLY E 199 ? 0.4605 0.4488 0.4114 -0.0517 0.1773  -0.0474 199 GLY E C   
13500 O O   . GLY E 199 ? 0.4539 0.4270 0.3852 -0.0553 0.1871  -0.0546 199 GLY E O   
13501 N N   . ALA E 200 ? 0.4343 0.4396 0.4129 -0.0382 0.1587  -0.0406 200 ALA E N   
13502 C CA  . ALA E 200 ? 0.4417 0.4494 0.4309 -0.0266 0.1500  -0.0406 200 ALA E CA  
13503 C C   . ALA E 200 ? 0.4609 0.4773 0.4552 -0.0186 0.1264  -0.0312 200 ALA E C   
13504 O O   . ALA E 200 ? 0.4545 0.4801 0.4571 -0.0187 0.1174  -0.0259 200 ALA E O   
13505 C CB  . ALA E 200 ? 0.3918 0.4113 0.4238 -0.0169 0.1620  -0.0464 200 ALA E CB  
13506 N N   . ILE E 201 ? 0.4427 0.4546 0.4312 -0.0130 0.1184  -0.0304 201 ILE E N   
13507 C CA  . ILE E 201 ? 0.3767 0.3962 0.3740 -0.0051 0.1014  -0.0240 201 ILE E CA  
13508 C C   . ILE E 201 ? 0.3616 0.3861 0.3827 0.0044  0.1022  -0.0248 201 ILE E C   
13509 O O   . ILE E 201 ? 0.3617 0.3775 0.3819 0.0055  0.1120  -0.0301 201 ILE E O   
13510 C CB  . ILE E 201 ? 0.3794 0.3891 0.3529 -0.0073 0.0912  -0.0214 201 ILE E CB  
13511 C CG1 . ILE E 201 ? 0.3802 0.3783 0.3268 -0.0181 0.0902  -0.0202 201 ILE E CG1 
13512 C CG2 . ILE E 201 ? 0.2877 0.3050 0.2699 -0.0014 0.0776  -0.0162 201 ILE E CG2 
13513 C CD1 . ILE E 201 ? 0.3690 0.3707 0.3160 -0.0210 0.0829  -0.0149 201 ILE E CD1 
13514 N N   . LEU E 202 ? 0.3415 0.3773 0.3822 0.0103  0.0910  -0.0193 202 LEU E N   
13515 C CA  . LEU E 202 ? 0.3652 0.4042 0.4286 0.0186  0.0872  -0.0168 202 LEU E CA  
13516 C C   . LEU E 202 ? 0.3552 0.3899 0.4039 0.0200  0.0730  -0.0110 202 LEU E C   
13517 O O   . LEU E 202 ? 0.3723 0.4093 0.4093 0.0165  0.0646  -0.0084 202 LEU E O   
13518 C CB  . LEU E 202 ? 0.4144 0.4687 0.5131 0.0220  0.0837  -0.0136 202 LEU E CB  
13519 C CG  . LEU E 202 ? 0.4538 0.5137 0.5832 0.0238  0.1006  -0.0199 202 LEU E CG  
13520 C CD1 . LEU E 202 ? 0.4919 0.5476 0.6029 0.0145  0.1167  -0.0272 202 LEU E CD1 
13521 C CD2 . LEU E 202 ? 0.4568 0.5348 0.6264 0.0271  0.0917  -0.0145 202 LEU E CD2 
13522 N N   . PHE E 203 ? 0.3411 0.3674 0.3894 0.0240  0.0723  -0.0100 203 PHE E N   
13523 C CA  . PHE E 203 ? 0.3258 0.3457 0.3574 0.0234  0.0619  -0.0050 203 PHE E CA  
13524 C C   . PHE E 203 ? 0.3121 0.3310 0.3591 0.0284  0.0520  0.0026  203 PHE E C   
13525 O O   . PHE E 203 ? 0.3472 0.3622 0.4123 0.0339  0.0560  0.0027  203 PHE E O   
13526 C CB  . PHE E 203 ? 0.3771 0.3849 0.3898 0.0212  0.0676  -0.0088 203 PHE E CB  
13527 C CG  . PHE E 203 ? 0.3693 0.3756 0.3662 0.0152  0.0733  -0.0142 203 PHE E CG  
13528 C CD1 . PHE E 203 ? 0.3870 0.3948 0.3715 0.0112  0.0674  -0.0130 203 PHE E CD1 
13529 C CD2 . PHE E 203 ? 0.3768 0.3777 0.3708 0.0126  0.0843  -0.0203 203 PHE E CD2 
13530 C CE1 . PHE E 203 ? 0.4075 0.4127 0.3808 0.0057  0.0686  -0.0153 203 PHE E CE1 
13531 C CE2 . PHE E 203 ? 0.3960 0.3921 0.3705 0.0048  0.0860  -0.0231 203 PHE E CE2 
13532 C CZ  . PHE E 203 ? 0.4268 0.4255 0.3924 0.0019  0.0762  -0.0193 203 PHE E CZ  
13533 N N   . GLY E 204 ? 0.3374 0.3571 0.3760 0.0254  0.0387  0.0092  204 GLY E N   
13534 C CA  . GLY E 204 ? 0.3235 0.3401 0.3724 0.0277  0.0247  0.0192  204 GLY E CA  
13535 C C   . GLY E 204 ? 0.3614 0.3896 0.4241 0.0256  0.0122  0.0241  204 GLY E C   
13536 O O   . GLY E 204 ? 0.3470 0.3848 0.4102 0.0225  0.0165  0.0188  204 GLY E O   
13537 N N   . ASP E 205 ? 0.3985 0.4238 0.4707 0.0260  -0.0052 0.0352  205 ASP E N   
13538 C CA  . ASP E 205 ? 0.4200 0.4543 0.5028 0.0217  -0.0222 0.0418  205 ASP E CA  
13539 C C   . ASP E 205 ? 0.4388 0.4921 0.5719 0.0288  -0.0199 0.0409  205 ASP E C   
13540 O O   . ASP E 205 ? 0.4789 0.5343 0.6470 0.0375  -0.0203 0.0447  205 ASP E O   
13541 C CB  . ASP E 205 ? 0.4667 0.4886 0.5389 0.0176  -0.0448 0.0559  205 ASP E CB  
13542 C CG  . ASP E 205 ? 0.5444 0.5719 0.6176 0.0094  -0.0656 0.0631  205 ASP E CG  
13543 O OD1 . ASP E 205 ? 0.5270 0.5661 0.6021 0.0056  -0.0608 0.0557  205 ASP E OD1 
13544 O OD2 . ASP E 205 ? 0.6195 0.6380 0.6917 0.0060  -0.0884 0.0772  205 ASP E OD2 
13545 N N   . ILE E 206 ? 0.4338 0.5005 0.5746 0.0247  -0.0176 0.0362  206 ILE E N   
13546 C CA  . ILE E 206 ? 0.4424 0.5277 0.6335 0.0303  -0.0118 0.0343  206 ILE E CA  
13547 C C   . ILE E 206 ? 0.4138 0.5098 0.6383 0.0294  -0.0359 0.0461  206 ILE E C   
13548 O O   . ILE E 206 ? 0.4233 0.5358 0.7002 0.0353  -0.0338 0.0466  206 ILE E O   
13549 C CB  . ILE E 206 ? 0.4527 0.5472 0.6400 0.0253  0.0031  0.0243  206 ILE E CB  
13550 C CG1 . ILE E 206 ? 0.4665 0.5574 0.6217 0.0148  -0.0096 0.0260  206 ILE E CG1 
13551 C CG2 . ILE E 206 ? 0.4770 0.5622 0.6400 0.0262  0.0254  0.0139  206 ILE E CG2 
13552 C CD1 . ILE E 206 ? 0.4908 0.5876 0.6412 0.0097  0.0022  0.0180  206 ILE E CD1 
13553 N N   . ASN E 207 ? 0.4353 0.5200 0.6301 0.0216  -0.0589 0.0561  207 ASN E N   
13554 C CA  . ASN E 207 ? 0.4888 0.5806 0.7071 0.0174  -0.0876 0.0694  207 ASN E CA  
13555 C C   . ASN E 207 ? 0.5167 0.5960 0.7414 0.0218  -0.1053 0.0833  207 ASN E C   
13556 O O   . ASN E 207 ? 0.5656 0.6418 0.7942 0.0160  -0.1350 0.0982  207 ASN E O   
13557 C CB  . ASN E 207 ? 0.5903 0.6731 0.7624 0.0014  -0.1031 0.0712  207 ASN E CB  
13558 C CG  . ASN E 207 ? 0.6289 0.7201 0.7917 -0.0039 -0.0873 0.0582  207 ASN E CG  
13559 O OD1 . ASN E 207 ? 0.6494 0.7604 0.8539 -0.0004 -0.0792 0.0540  207 ASN E OD1 
13560 N ND2 . ASN E 207 ? 0.6321 0.7073 0.7419 -0.0129 -0.0816 0.0517  207 ASN E ND2 
13561 N N   . ASP E 208 ? 0.5221 0.5937 0.7509 0.0319  -0.0879 0.0791  208 ASP E N   
13562 C CA  . ASP E 208 ? 0.5554 0.6115 0.7881 0.0368  -0.1010 0.0914  208 ASP E CA  
13563 C C   . ASP E 208 ? 0.6126 0.6854 0.9208 0.0504  -0.1015 0.0948  208 ASP E C   
13564 O O   . ASP E 208 ? 0.6127 0.6965 0.9505 0.0589  -0.0744 0.0811  208 ASP E O   
13565 C CB  . ASP E 208 ? 0.5716 0.6087 0.7672 0.0390  -0.0811 0.0840  208 ASP E CB  
13566 C CG  . ASP E 208 ? 0.6322 0.6497 0.8291 0.0430  -0.0944 0.0975  208 ASP E CG  
13567 O OD1 . ASP E 208 ? 0.6408 0.6598 0.8752 0.0469  -0.1179 0.1127  208 ASP E OD1 
13568 O OD2 . ASP E 208 ? 0.6582 0.6579 0.8207 0.0420  -0.0820 0.0935  208 ASP E OD2 
13569 N N   . PRO E 209 ? 0.6865 0.7618 1.0275 0.0507  -0.1330 0.1128  209 PRO E N   
13570 C CA  . PRO E 209 ? 0.6865 0.7783 1.1108 0.0639  -0.1400 0.1197  209 PRO E CA  
13571 C C   . PRO E 209 ? 0.6391 0.7246 1.0921 0.0789  -0.1138 0.1111  209 PRO E C   
13572 O O   . PRO E 209 ? 0.5691 0.6714 1.0923 0.0907  -0.1019 0.1063  209 PRO E O   
13573 C CB  . PRO E 209 ? 0.7398 0.8210 1.1682 0.0591  -0.1836 0.1448  209 PRO E CB  
13574 C CG  . PRO E 209 ? 0.7780 0.8301 1.1164 0.0441  -0.1922 0.1489  209 PRO E CG  
13575 C CD  . PRO E 209 ? 0.7461 0.8037 1.0406 0.0365  -0.1657 0.1291  209 PRO E CD  
13576 N N   . ASN E 210 ? 0.6825 0.7433 1.0840 0.0776  -0.1041 0.1084  210 ASN E N   
13577 C CA  . ASN E 210 ? 0.7033 0.7559 1.1254 0.0895  -0.0771 0.0975  210 ASN E CA  
13578 C C   . ASN E 210 ? 0.6661 0.7321 1.0940 0.0913  -0.0398 0.0744  210 ASN E C   
13579 O O   . ASN E 210 ? 0.6704 0.7368 1.1358 0.1011  -0.0159 0.0633  210 ASN E O   
13580 C CB  . ASN E 210 ? 0.7449 0.7679 1.1098 0.0859  -0.0754 0.0996  210 ASN E CB  
13581 C CG  . ASN E 210 ? 0.8043 0.8085 1.1678 0.0851  -0.1081 0.1225  210 ASN E CG  
13582 O OD1 . ASN E 210 ? 0.8446 0.8318 1.1479 0.0722  -0.1238 0.1315  210 ASN E OD1 
13583 N ND2 . ASN E 210 ? 0.7983 0.8034 1.2280 0.0982  -0.1180 0.1323  210 ASN E ND2 
13584 N N   . ASN E 211 ? 0.6283 0.7031 1.0188 0.0807  -0.0344 0.0669  211 ASN E N   
13585 C CA  . ASN E 211 ? 0.5692 0.6524 0.9588 0.0804  -0.0015 0.0474  211 ASN E CA  
13586 C C   . ASN E 211 ? 0.5534 0.6625 0.9982 0.0821  0.0027  0.0442  211 ASN E C   
13587 O O   . ASN E 211 ? 0.5297 0.6473 0.9755 0.0793  0.0283  0.0295  211 ASN E O   
13588 C CB  . ASN E 211 ? 0.5225 0.5988 0.8442 0.0686  0.0044  0.0406  211 ASN E CB  
13589 C CG  . ASN E 211 ? 0.4953 0.5483 0.7678 0.0662  0.0021  0.0429  211 ASN E CG  
13590 O OD1 . ASN E 211 ? 0.5022 0.5427 0.7853 0.0731  0.0101  0.0416  211 ASN E OD1 
13591 N ND2 . ASN E 211 ? 0.5002 0.5465 0.7212 0.0560  -0.0071 0.0453  211 ASN E ND2 
13592 N N   . ASN E 212 ? 0.5750 0.6956 1.0705 0.0867  -0.0224 0.0588  212 ASN E N   
13593 C CA  . ASN E 212 ? 0.5710 0.7190 1.1211 0.0862  -0.0247 0.0586  212 ASN E CA  
13594 C C   . ASN E 212 ? 0.5091 0.6712 1.1115 0.0927  0.0119  0.0411  212 ASN E C   
13595 O O   . ASN E 212 ? 0.4605 0.6391 1.0739 0.0859  0.0224  0.0338  212 ASN E O   
13596 C CB  . ASN E 212 ? 0.6174 0.7747 1.2194 0.0902  -0.0618 0.0793  212 ASN E CB  
13597 C CG  . ASN E 212 ? 0.6693 0.8508 1.3013 0.0826  -0.0755 0.0826  212 ASN E CG  
13598 O OD1 . ASN E 212 ? 0.6814 0.8775 1.3279 0.0799  -0.0502 0.0680  212 ASN E OD1 
13599 N ND2 . ASN E 212 ? 0.7118 0.8928 1.3443 0.0762  -0.1150 0.1013  212 ASN E ND2 
13600 N N   . ASN E 213 ? 0.5312 0.6779 1.1441 0.0998  0.0325  0.0325  213 ASN E N   
13601 C CA  . ASN E 213 ? 0.5571 0.7071 1.1929 0.0976  0.0653  0.0150  213 ASN E CA  
13602 C C   . ASN E 213 ? 0.4766 0.6219 1.0647 0.0892  0.0950  -0.0018 213 ASN E C   
13603 O O   . ASN E 213 ? 0.4430 0.5946 1.0346 0.0815  0.1169  -0.0138 213 ASN E O   
13604 C CB  . ASN E 213 ? 0.6520 0.7860 1.3116 0.1043  0.0818  0.0081  213 ASN E CB  
13605 C CG  . ASN E 213 ? 0.7260 0.8639 1.4415 0.1119  0.0564  0.0233  213 ASN E CG  
13606 O OD1 . ASN E 213 ? 0.7787 0.9027 1.5148 0.1180  0.0660  0.0200  213 ASN E OD1 
13607 N ND2 . ASN E 213 ? 0.7326 0.8830 1.4588 0.1108  0.0191  0.0424  213 ASN E ND2 
13608 N N   . TYR E 214 ? 0.4177 0.5492 0.9577 0.0894  0.0954  -0.0020 214 TYR E N   
13609 C CA  . TYR E 214 ? 0.4042 0.5268 0.8939 0.0800  0.1224  -0.0173 214 TYR E CA  
13610 C C   . TYR E 214 ? 0.3886 0.5259 0.8596 0.0687  0.1174  -0.0162 214 TYR E C   
13611 O O   . TYR E 214 ? 0.3982 0.5370 0.8590 0.0605  0.1425  -0.0287 214 TYR E O   
13612 C CB  . TYR E 214 ? 0.3701 0.4670 0.7896 0.0765  0.1185  -0.0171 214 TYR E CB  
13613 C CG  . TYR E 214 ? 0.3593 0.4447 0.7297 0.0655  0.1449  -0.0324 214 TYR E CG  
13614 C CD1 . TYR E 214 ? 0.3785 0.4501 0.7500 0.0643  0.1748  -0.0480 214 TYR E CD1 
13615 C CD2 . TYR E 214 ? 0.3818 0.4673 0.7025 0.0545  0.1381  -0.0308 214 TYR E CD2 
13616 C CE1 . TYR E 214 ? 0.4053 0.4622 0.7232 0.0505  0.1939  -0.0598 214 TYR E CE1 
13617 C CE2 . TYR E 214 ? 0.4016 0.4751 0.6783 0.0436  0.1583  -0.0421 214 TYR E CE2 
13618 C CZ  . TYR E 214 ? 0.4086 0.4686 0.6850 0.0416  0.1872  -0.0567 214 TYR E CZ  
13619 O OH  . TYR E 214 ? 0.4068 0.4516 0.6318 0.0277  0.2028  -0.0658 214 TYR E OH  
13620 N N   . ILE E 215 ? 0.3745 0.5207 0.8419 0.0670  0.0852  -0.0013 215 ILE E N   
13621 C CA  . ILE E 215 ? 0.3631 0.5194 0.8081 0.0558  0.0783  0.0000  215 ILE E CA  
13622 C C   . ILE E 215 ? 0.3786 0.5618 0.8883 0.0558  0.0728  0.0034  215 ILE E C   
13623 O O   . ILE E 215 ? 0.3629 0.5557 0.8620 0.0464  0.0637  0.0058  215 ILE E O   
13624 C CB  . ILE E 215 ? 0.2817 0.4280 0.6748 0.0506  0.0489  0.0118  215 ILE E CB  
13625 C CG1 . ILE E 215 ? 0.3084 0.4564 0.7272 0.0568  0.0185  0.0276  215 ILE E CG1 
13626 C CG2 . ILE E 215 ? 0.3009 0.4234 0.6324 0.0490  0.0569  0.0071  215 ILE E CG2 
13627 C CD1 . ILE E 215 ? 0.3228 0.4871 0.7637 0.0512  -0.0075 0.0383  215 ILE E CD1 
13628 N N   . HIS E 216 ? 0.4173 0.6105 0.9927 0.0654  0.0786  0.0028  216 HIS E N   
13629 C CA  . HIS E 216 ? 0.4390 0.6505 1.0649 0.0635  0.0672  0.0078  216 HIS E CA  
13630 C C   . HIS E 216 ? 0.4226 0.6446 1.0456 0.0518  0.0856  -0.0020 216 HIS E C   
13631 O O   . HIS E 216 ? 0.4223 0.6620 1.0690 0.0464  0.0680  0.0051  216 HIS E O   
13632 C CB  . HIS E 216 ? 0.5167 0.7239 1.1907 0.0717  0.0749  0.0056  216 HIS E CB  
13633 C CG  . HIS E 216 ? 0.5775 0.8033 1.3092 0.0706  0.0622  0.0115  216 HIS E CG  
13634 N ND1 . HIS E 216 ? 0.5919 0.8264 1.3552 0.0738  0.0241  0.0299  216 HIS E ND1 
13635 C CD2 . HIS E 216 ? 0.5727 0.8088 1.3336 0.0651  0.0815  0.0020  216 HIS E CD2 
13636 C CE1 . HIS E 216 ? 0.5837 0.8339 1.3965 0.0711  0.0206  0.0311  216 HIS E CE1 
13637 N NE2 . HIS E 216 ? 0.5760 0.8285 1.3904 0.0663  0.0559  0.0141  216 HIS E NE2 
13638 N N   . ASN E 217 ? 0.4043 0.6131 0.9947 0.0463  0.1192  -0.0175 217 ASN E N   
13639 C CA  . ASN E 217 ? 0.4195 0.6337 1.0019 0.0340  0.1370  -0.0257 217 ASN E CA  
13640 C C   . ASN E 217 ? 0.3865 0.6082 0.9359 0.0242  0.1250  -0.0207 217 ASN E C   
13641 O O   . ASN E 217 ? 0.3693 0.5960 0.9127 0.0131  0.1350  -0.0249 217 ASN E O   
13642 C CB  . ASN E 217 ? 0.4938 0.6866 1.0433 0.0284  0.1732  -0.0421 217 ASN E CB  
13643 C CG  . ASN E 217 ? 0.5394 0.7342 1.0794 0.0147  0.1921  -0.0498 217 ASN E CG  
13644 O OD1 . ASN E 217 ? 0.5514 0.7604 1.1381 0.0135  0.1941  -0.0504 217 ASN E OD1 
13645 N ND2 . ASN E 217 ? 0.5589 0.7373 1.0382 0.0038  0.2058  -0.0554 217 ASN E ND2 
13646 N N   . SER E 218 ? 0.3792 0.5955 0.8979 0.0268  0.1033  -0.0119 218 SER E N   
13647 C CA  . SER E 218 ? 0.3345 0.5436 0.7998 0.0159  0.0879  -0.0075 218 SER E CA  
13648 C C   . SER E 218 ? 0.3333 0.5537 0.8133 0.0141  0.0514  0.0060  218 SER E C   
13649 O O   . SER E 218 ? 0.3340 0.5462 0.7703 0.0053  0.0374  0.0092  218 SER E O   
13650 C CB  . SER E 218 ? 0.3120 0.4945 0.7052 0.0154  0.0877  -0.0086 218 SER E CB  
13651 O OG  . SER E 218 ? 0.2939 0.4693 0.6762 0.0224  0.0634  0.0010  218 SER E OG  
13652 N N   . LEU E 219 ? 0.3273 0.5654 0.8695 0.0214  0.0357  0.0139  219 LEU E N   
13653 C CA  . LEU E 219 ? 0.3115 0.5551 0.8602 0.0186  -0.0036 0.0288  219 LEU E CA  
13654 C C   . LEU E 219 ? 0.3109 0.5651 0.8578 0.0046  -0.0164 0.0307  219 LEU E C   
13655 O O   . LEU E 219 ? 0.3129 0.5593 0.8279 -0.0028 -0.0449 0.0393  219 LEU E O   
13656 C CB  . LEU E 219 ? 0.2800 0.5410 0.9039 0.0290  -0.0193 0.0385  219 LEU E CB  
13657 C CG  . LEU E 219 ? 0.2682 0.5129 0.8843 0.0413  -0.0251 0.0440  219 LEU E CG  
13658 C CD1 . LEU E 219 ? 0.2733 0.5245 0.9519 0.0505  -0.0372 0.0521  219 LEU E CD1 
13659 C CD2 . LEU E 219 ? 0.2448 0.4674 0.7932 0.0354  -0.0536 0.0547  219 LEU E CD2 
13660 N N   . ASP E 220 ? 0.3300 0.6002 0.9101 -0.0005 0.0053  0.0222  220 ASP E N   
13661 C CA  . ASP E 220 ? 0.3773 0.6566 0.9571 -0.0147 -0.0062 0.0236  220 ASP E CA  
13662 C C   . ASP E 220 ? 0.3527 0.6072 0.8524 -0.0237 -0.0038 0.0196  220 ASP E C   
13663 O O   . ASP E 220 ? 0.4018 0.6519 0.8778 -0.0340 -0.0255 0.0240  220 ASP E O   
13664 C CB  . ASP E 220 ? 0.4525 0.7533 1.0865 -0.0194 0.0183  0.0155  220 ASP E CB  
13665 C CG  . ASP E 220 ? 0.5536 0.8650 1.2447 -0.0102 0.0137  0.0186  220 ASP E CG  
13666 O OD1 . ASP E 220 ? 0.5968 0.9134 1.3091 -0.0072 -0.0203 0.0316  220 ASP E OD1 
13667 O OD2 . ASP E 220 ? 0.5734 0.8855 1.2862 -0.0075 0.0436  0.0084  220 ASP E OD2 
13668 N N   . VAL E 221 ? 0.2826 0.5197 0.7423 -0.0202 0.0218  0.0111  221 VAL E N   
13669 C CA  . VAL E 221 ? 0.2536 0.4668 0.6434 -0.0267 0.0248  0.0077  221 VAL E CA  
13670 C C   . VAL E 221 ? 0.2815 0.4784 0.6274 -0.0264 -0.0010 0.0143  221 VAL E C   
13671 O O   . VAL E 221 ? 0.3068 0.4922 0.6160 -0.0358 -0.0103 0.0139  221 VAL E O   
13672 C CB  . VAL E 221 ? 0.2300 0.4279 0.5898 -0.0224 0.0533  -0.0007 221 VAL E CB  
13673 C CG1 . VAL E 221 ? 0.2431 0.4182 0.5401 -0.0281 0.0541  -0.0026 221 VAL E CG1 
13674 C CG2 . VAL E 221 ? 0.2254 0.4344 0.6184 -0.0262 0.0822  -0.0087 221 VAL E CG2 
13675 N N   . LEU E 222 ? 0.2664 0.4603 0.6161 -0.0167 -0.0106 0.0197  222 LEU E N   
13676 C CA  . LEU E 222 ? 0.2807 0.4572 0.5876 -0.0174 -0.0319 0.0259  222 LEU E CA  
13677 C C   . LEU E 222 ? 0.3319 0.5117 0.6405 -0.0280 -0.0615 0.0338  222 LEU E C   
13678 O O   . LEU E 222 ? 0.3975 0.5590 0.6574 -0.0357 -0.0744 0.0349  222 LEU E O   
13679 C CB  . LEU E 222 ? 0.2740 0.4469 0.5906 -0.0057 -0.0357 0.0313  222 LEU E CB  
13680 C CG  . LEU E 222 ? 0.2752 0.4391 0.5797 0.0035  -0.0095 0.0235  222 LEU E CG  
13681 C CD1 . LEU E 222 ? 0.3246 0.4827 0.6385 0.0135  -0.0179 0.0302  222 LEU E CD1 
13682 C CD2 . LEU E 222 ? 0.2737 0.4180 0.5190 -0.0010 -0.0006 0.0175  222 LEU E CD2 
13683 N N   . HIS E 223 ? 0.3556 0.5584 0.7224 -0.0293 -0.0718 0.0389  223 HIS E N   
13684 C CA  . HIS E 223 ? 0.4352 0.6442 0.8120 -0.0411 -0.1030 0.0475  223 HIS E CA  
13685 C C   . HIS E 223 ? 0.4433 0.6412 0.7792 -0.0558 -0.1021 0.0405  223 HIS E C   
13686 O O   . HIS E 223 ? 0.4847 0.6716 0.7912 -0.0682 -0.1259 0.0445  223 HIS E O   
13687 C CB  . HIS E 223 ? 0.4571 0.6975 0.9162 -0.0390 -0.1093 0.0526  223 HIS E CB  
13688 C CG  . HIS E 223 ? 0.5590 0.8090 1.0372 -0.0521 -0.1446 0.0627  223 HIS E CG  
13689 N ND1 . HIS E 223 ? 0.6240 0.8663 1.0933 -0.0554 -0.1806 0.0770  223 HIS E ND1 
13690 C CD2 . HIS E 223 ? 0.5968 0.8629 1.1037 -0.0643 -0.1507 0.0613  223 HIS E CD2 
13691 C CE1 . HIS E 223 ? 0.6530 0.9056 1.1418 -0.0697 -0.2089 0.0840  223 HIS E CE1 
13692 N NE2 . HIS E 223 ? 0.6298 0.8979 1.1437 -0.0750 -0.1911 0.0743  223 HIS E NE2 
13693 N N   . ASP E 224 ? 0.4077 0.6056 0.7390 -0.0554 -0.0741 0.0300  224 ASP E N   
13694 C CA  . ASP E 224 ? 0.4163 0.6044 0.7187 -0.0683 -0.0707 0.0234  224 ASP E CA  
13695 C C   . ASP E 224 ? 0.3803 0.5414 0.6212 -0.0678 -0.0568 0.0160  224 ASP E C   
13696 O O   . ASP E 224 ? 0.3904 0.5411 0.6098 -0.0767 -0.0504 0.0099  224 ASP E O   
13697 C CB  . ASP E 224 ? 0.4516 0.6572 0.7939 -0.0713 -0.0513 0.0184  224 ASP E CB  
13698 C CG  . ASP E 224 ? 0.5048 0.7395 0.9152 -0.0742 -0.0642 0.0243  224 ASP E CG  
13699 O OD1 . ASP E 224 ? 0.5611 0.8001 0.9813 -0.0787 -0.0951 0.0332  224 ASP E OD1 
13700 O OD2 . ASP E 224 ? 0.4988 0.7512 0.9529 -0.0735 -0.0436 0.0202  224 ASP E OD2 
13701 N N   . LEU E 225 ? 0.3530 0.5024 0.5692 -0.0579 -0.0529 0.0167  225 LEU E N   
13702 C CA  . LEU E 225 ? 0.3439 0.4703 0.5099 -0.0570 -0.0405 0.0101  225 LEU E CA  
13703 C C   . LEU E 225 ? 0.3704 0.4780 0.4970 -0.0692 -0.0519 0.0067  225 LEU E C   
13704 O O   . LEU E 225 ? 0.3910 0.4957 0.5093 -0.0773 -0.0734 0.0112  225 LEU E O   
13705 C CB  . LEU E 225 ? 0.3515 0.4688 0.4989 -0.0465 -0.0375 0.0119  225 LEU E CB  
13706 C CG  . LEU E 225 ? 0.3435 0.4669 0.5076 -0.0339 -0.0199 0.0112  225 LEU E CG  
13707 C CD1 . LEU E 225 ? 0.3577 0.4639 0.4856 -0.0286 -0.0187 0.0109  225 LEU E CD1 
13708 C CD2 . LEU E 225 ? 0.3268 0.4521 0.4958 -0.0334 0.0026  0.0049  225 LEU E CD2 
13709 N N   . VAL E 226 ? 0.3694 0.4617 0.4701 -0.0710 -0.0371 -0.0012 226 VAL E N   
13710 C CA  . VAL E 226 ? 0.3898 0.4606 0.4533 -0.0813 -0.0408 -0.0078 226 VAL E CA  
13711 C C   . VAL E 226 ? 0.3990 0.4511 0.4287 -0.0747 -0.0292 -0.0126 226 VAL E C   
13712 O O   . VAL E 226 ? 0.3943 0.4486 0.4297 -0.0641 -0.0151 -0.0126 226 VAL E O   
13713 C CB  . VAL E 226 ? 0.4443 0.5115 0.5132 -0.0889 -0.0328 -0.0132 226 VAL E CB  
13714 C CG1 . VAL E 226 ? 0.5025 0.5433 0.5344 -0.0960 -0.0292 -0.0225 226 VAL E CG1 
13715 C CG2 . VAL E 226 ? 0.4186 0.5007 0.5152 -0.0997 -0.0468 -0.0100 226 VAL E CG2 
13716 N N   . TYR E 227 ? 0.4194 0.4527 0.4140 -0.0825 -0.0350 -0.0170 227 TYR E N   
13717 C CA  . TYR E 227 ? 0.4312 0.4483 0.3980 -0.0776 -0.0234 -0.0222 227 TYR E CA  
13718 C C   . TYR E 227 ? 0.4305 0.4254 0.3729 -0.0844 -0.0125 -0.0342 227 TYR E C   
13719 O O   . TYR E 227 ? 0.4537 0.4394 0.3864 -0.0969 -0.0181 -0.0392 227 TYR E O   
13720 C CB  . TYR E 227 ? 0.4721 0.4833 0.4167 -0.0807 -0.0350 -0.0176 227 TYR E CB  
13721 C CG  . TYR E 227 ? 0.5044 0.5343 0.4756 -0.0711 -0.0436 -0.0059 227 TYR E CG  
13722 C CD1 . TYR E 227 ? 0.5106 0.5441 0.4884 -0.0580 -0.0316 -0.0045 227 TYR E CD1 
13723 C CD2 . TYR E 227 ? 0.5759 0.6193 0.5690 -0.0754 -0.0640 0.0033  227 TYR E CD2 
13724 C CE1 . TYR E 227 ? 0.5458 0.5933 0.5485 -0.0493 -0.0373 0.0045  227 TYR E CE1 
13725 C CE2 . TYR E 227 ? 0.6040 0.6637 0.6281 -0.0654 -0.0705 0.0133  227 TYR E CE2 
13726 C CZ  . TYR E 227 ? 0.6105 0.6710 0.6380 -0.0523 -0.0558 0.0131  227 TYR E CZ  
13727 O OH  . TYR E 227 ? 0.6588 0.7326 0.7177 -0.0424 -0.0603 0.0215  227 TYR E OH  
13728 N N   . THR E 228 ? 0.4334 0.4192 0.3691 -0.0764 0.0033  -0.0393 228 THR E N   
13729 C CA  . THR E 228 ? 0.4841 0.4481 0.4026 -0.0810 0.0162  -0.0517 228 THR E CA  
13730 C C   . THR E 228 ? 0.4717 0.4280 0.3783 -0.0748 0.0284  -0.0556 228 THR E C   
13731 O O   . THR E 228 ? 0.4537 0.4228 0.3723 -0.0643 0.0287  -0.0482 228 THR E O   
13732 C CB  . THR E 228 ? 0.4660 0.4288 0.4071 -0.0766 0.0246  -0.0539 228 THR E CB  
13733 O OG1 . THR E 228 ? 0.5149 0.4550 0.4440 -0.0829 0.0350  -0.0666 228 THR E OG1 
13734 C CG2 . THR E 228 ? 0.4040 0.3760 0.3650 -0.0623 0.0320  -0.0481 228 THR E CG2 
13735 N N   . PRO E 229 ? 0.5053 0.4399 0.3889 -0.0824 0.0403  -0.0682 229 PRO E N   
13736 C CA  . PRO E 229 ? 0.4965 0.4244 0.3707 -0.0784 0.0537  -0.0727 229 PRO E CA  
13737 C C   . PRO E 229 ? 0.4731 0.4113 0.3801 -0.0627 0.0634  -0.0704 229 PRO E C   
13738 O O   . PRO E 229 ? 0.4647 0.4038 0.3958 -0.0570 0.0667  -0.0711 229 PRO E O   
13739 C CB  . PRO E 229 ? 0.5220 0.4236 0.3707 -0.0909 0.0686  -0.0894 229 PRO E CB  
13740 C CG  . PRO E 229 ? 0.5497 0.4428 0.3781 -0.1058 0.0556  -0.0910 229 PRO E CG  
13741 C CD  . PRO E 229 ? 0.5158 0.4298 0.3786 -0.0971 0.0428  -0.0800 229 PRO E CD  
13742 N N   . LEU E 230 ? 0.4823 0.4267 0.3887 -0.0569 0.0661  -0.0665 230 LEU E N   
13743 C CA  . LEU E 230 ? 0.4628 0.4166 0.3971 -0.0440 0.0726  -0.0636 230 LEU E CA  
13744 C C   . LEU E 230 ? 0.5021 0.4444 0.4374 -0.0444 0.0908  -0.0747 230 LEU E C   
13745 O O   . LEU E 230 ? 0.5222 0.4548 0.4310 -0.0527 0.0976  -0.0800 230 LEU E O   
13746 C CB  . LEU E 230 ? 0.4183 0.3874 0.3557 -0.0374 0.0638  -0.0521 230 LEU E CB  
13747 C CG  . LEU E 230 ? 0.3649 0.3432 0.3251 -0.0266 0.0673  -0.0479 230 LEU E CG  
13748 C CD1 . LEU E 230 ? 0.3323 0.3153 0.3146 -0.0214 0.0633  -0.0437 230 LEU E CD1 
13749 C CD2 . LEU E 230 ? 0.3405 0.3288 0.2960 -0.0231 0.0606  -0.0393 230 LEU E CD2 
13750 N N   . THR E 231 ? 0.4905 0.4331 0.4576 -0.0365 0.0986  -0.0779 231 THR E N   
13751 C CA  . THR E 231 ? 0.4890 0.4251 0.4712 -0.0346 0.1168  -0.0881 231 THR E CA  
13752 C C   . THR E 231 ? 0.4728 0.4240 0.4901 -0.0224 0.1134  -0.0798 231 THR E C   
13753 O O   . THR E 231 ? 0.4593 0.4197 0.4915 -0.0158 0.0994  -0.0687 231 THR E O   
13754 C CB  . THR E 231 ? 0.4728 0.3929 0.4697 -0.0368 0.1308  -0.1016 231 THR E CB  
13755 O OG1 . THR E 231 ? 0.4429 0.3659 0.4619 -0.0309 0.1192  -0.0944 231 THR E OG1 
13756 C CG2 . THR E 231 ? 0.4753 0.3752 0.4316 -0.0526 0.1398  -0.1143 231 THR E CG2 
13757 N N   . ILE E 232 ? 0.4674 0.4194 0.4966 -0.0211 0.1265  -0.0855 232 ILE E N   
13758 C CA  . ILE E 232 ? 0.4312 0.3977 0.4905 -0.0119 0.1215  -0.0774 232 ILE E CA  
13759 C C   . ILE E 232 ? 0.4278 0.3932 0.5314 -0.0070 0.1348  -0.0856 232 ILE E C   
13760 O O   . ILE E 232 ? 0.4816 0.4368 0.5846 -0.0125 0.1562  -0.1002 232 ILE E O   
13761 C CB  . ILE E 232 ? 0.3748 0.3467 0.4146 -0.0148 0.1227  -0.0746 232 ILE E CB  
13762 C CG1 . ILE E 232 ? 0.3515 0.3240 0.3540 -0.0189 0.1095  -0.0666 232 ILE E CG1 
13763 C CG2 . ILE E 232 ? 0.3610 0.3469 0.4306 -0.0070 0.1157  -0.0666 232 ILE E CG2 
13764 C CD1 . ILE E 232 ? 0.3265 0.3094 0.3370 -0.0125 0.0919  -0.0546 232 ILE E CD1 
13765 N N   . SER E 233 ? 0.3787 0.3532 0.5210 0.0023  0.1227  -0.0764 233 SER E N   
13766 C CA  . SER E 233 ? 0.3744 0.3497 0.5695 0.0084  0.1327  -0.0825 233 SER E CA  
13767 C C   . SER E 233 ? 0.3646 0.3503 0.5772 0.0083  0.1426  -0.0858 233 SER E C   
13768 O O   . SER E 233 ? 0.3538 0.3457 0.5382 0.0048  0.1375  -0.0804 233 SER E O   
13769 C CB  . SER E 233 ? 0.3403 0.3203 0.5727 0.0172  0.1124  -0.0690 233 SER E CB  
13770 O OG  . SER E 233 ? 0.3280 0.3215 0.5648 0.0196  0.0948  -0.0554 233 SER E OG  
13771 N N   . LYS E 234 ? 0.4035 0.3912 0.6676 0.0125  0.1567  -0.0943 234 LYS E N   
13772 C CA  . LYS E 234 ? 0.4675 0.4664 0.7570 0.0118  0.1686  -0.0986 234 LYS E CA  
13773 C C   . LYS E 234 ? 0.5104 0.5260 0.8119 0.0161  0.1432  -0.0812 234 LYS E C   
13774 O O   . LYS E 234 ? 0.5094 0.5351 0.8211 0.0138  0.1476  -0.0816 234 LYS E O   
13775 C CB  . LYS E 234 ? 0.4984 0.4955 0.8405 0.0132  0.1835  -0.1081 234 LYS E CB  
13776 C CG  . LYS E 234 ? 0.5095 0.5213 0.9187 0.0239  0.1661  -0.0971 234 LYS E CG  
13777 C CD  . LYS E 234 ? 0.5236 0.5288 0.9791 0.0241  0.1767  -0.1044 234 LYS E CD  
13778 C CE  . LYS E 234 ? 0.4898 0.5068 1.0111 0.0344  0.1536  -0.0905 234 LYS E CE  
13779 N NZ  . LYS E 234 ? 0.4453 0.4646 0.9626 0.0429  0.1251  -0.0739 234 LYS E NZ  
13780 N N   . GLN E 235 ? 0.5494 0.5657 0.8467 0.0205  0.1174  -0.0665 235 GLN E N   
13781 C CA  . GLN E 235 ? 0.5406 0.5678 0.8380 0.0216  0.0933  -0.0508 235 GLN E CA  
13782 C C   . GLN E 235 ? 0.4668 0.4909 0.7040 0.0164  0.0831  -0.0436 235 GLN E C   
13783 O O   . GLN E 235 ? 0.4412 0.4701 0.6689 0.0156  0.0644  -0.0318 235 GLN E O   
13784 C CB  . GLN E 235 ? 0.6167 0.6458 0.9543 0.0279  0.0713  -0.0383 235 GLN E CB  
13785 C CG  . GLN E 235 ? 0.7214 0.7650 1.1160 0.0309  0.0670  -0.0359 235 GLN E CG  
13786 C CD  . GLN E 235 ? 0.8271 0.8728 1.2675 0.0364  0.0408  -0.0211 235 GLN E CD  
13787 O OE1 . GLN E 235 ? 0.8656 0.8995 1.2999 0.0389  0.0301  -0.0144 235 GLN E OE1 
13788 N NE2 . GLN E 235 ? 0.8683 0.9282 1.3567 0.0377  0.0291  -0.0150 235 GLN E NE2 
13789 N N   . GLY E 236 ? 0.3895 0.4046 0.5874 0.0121  0.0957  -0.0514 236 GLY E N   
13790 C CA  . GLY E 236 ? 0.3433 0.3569 0.4933 0.0079  0.0890  -0.0462 236 GLY E CA  
13791 C C   . GLY E 236 ? 0.3268 0.3366 0.4560 0.0085  0.0740  -0.0374 236 GLY E C   
13792 O O   . GLY E 236 ? 0.3112 0.3224 0.4114 0.0064  0.0665  -0.0314 236 GLY E O   
13793 N N   . GLU E 237 ? 0.3428 0.3469 0.4889 0.0110  0.0712  -0.0370 237 GLU E N   
13794 C CA  . GLU E 237 ? 0.3443 0.3433 0.4724 0.0100  0.0589  -0.0290 237 GLU E CA  
13795 C C   . GLU E 237 ? 0.3596 0.3521 0.4593 0.0057  0.0673  -0.0359 237 GLU E C   
13796 O O   . GLU E 237 ? 0.3779 0.3649 0.4756 0.0033  0.0820  -0.0475 237 GLU E O   
13797 C CB  . GLU E 237 ? 0.3569 0.3504 0.5164 0.0137  0.0493  -0.0231 237 GLU E CB  
13798 C CG  . GLU E 237 ? 0.3745 0.3731 0.5657 0.0170  0.0347  -0.0131 237 GLU E CG  
13799 C CD  . GLU E 237 ? 0.4313 0.4243 0.6683 0.0224  0.0302  -0.0109 237 GLU E CD  
13800 O OE1 . GLU E 237 ? 0.4608 0.4537 0.7276 0.0263  0.0472  -0.0234 237 GLU E OE1 
13801 O OE2 . GLU E 237 ? 0.4706 0.4571 0.7132 0.0221  0.0106  0.0029  237 GLU E OE2 
13802 N N   . TYR E 238 ? 0.3426 0.3348 0.4201 0.0032  0.0582  -0.0291 238 TYR E N   
13803 C CA  . TYR E 238 ? 0.3426 0.3310 0.3967 -0.0018 0.0619  -0.0334 238 TYR E CA  
13804 C C   . TYR E 238 ? 0.3396 0.3182 0.4019 -0.0033 0.0614  -0.0350 238 TYR E C   
13805 O O   . TYR E 238 ? 0.3167 0.2929 0.3890 -0.0020 0.0520  -0.0265 238 TYR E O   
13806 C CB  . TYR E 238 ? 0.3232 0.3186 0.3564 -0.0037 0.0543  -0.0260 238 TYR E CB  
13807 C CG  . TYR E 238 ? 0.3460 0.3483 0.3700 -0.0024 0.0551  -0.0247 238 TYR E CG  
13808 C CD1 . TYR E 238 ? 0.3526 0.3549 0.3621 -0.0047 0.0611  -0.0298 238 TYR E CD1 
13809 C CD2 . TYR E 238 ? 0.3165 0.3226 0.3444 -0.0003 0.0491  -0.0182 238 TYR E CD2 
13810 C CE1 . TYR E 238 ? 0.3390 0.3452 0.3407 -0.0037 0.0614  -0.0278 238 TYR E CE1 
13811 C CE2 . TYR E 238 ? 0.3221 0.3324 0.3421 0.0003  0.0505  -0.0178 238 TYR E CE2 
13812 C CZ  . TYR E 238 ? 0.3275 0.3381 0.3362 -0.0007 0.0570  -0.0225 238 TYR E CZ  
13813 O OH  . TYR E 238 ? 0.3267 0.3392 0.3283 -0.0002 0.0580  -0.0213 238 TYR E OH  
13814 N N   . PHE E 239 ? 0.3564 0.3266 0.4113 -0.0076 0.0714  -0.0460 239 PHE E N   
13815 C CA  . PHE E 239 ? 0.3799 0.3379 0.4417 -0.0102 0.0731  -0.0501 239 PHE E CA  
13816 C C   . PHE E 239 ? 0.3878 0.3419 0.4214 -0.0194 0.0739  -0.0552 239 PHE E C   
13817 O O   . PHE E 239 ? 0.3974 0.3533 0.4094 -0.0240 0.0773  -0.0597 239 PHE E O   
13818 C CB  . PHE E 239 ? 0.3807 0.3274 0.4672 -0.0078 0.0870  -0.0618 239 PHE E CB  
13819 C CG  . PHE E 239 ? 0.3797 0.3281 0.5069 0.0014  0.0825  -0.0554 239 PHE E CG  
13820 C CD1 . PHE E 239 ? 0.3694 0.3284 0.5136 0.0064  0.0836  -0.0537 239 PHE E CD1 
13821 C CD2 . PHE E 239 ? 0.3709 0.3097 0.5210 0.0042  0.0752  -0.0499 239 PHE E CD2 
13822 C CE1 . PHE E 239 ? 0.3546 0.3162 0.5398 0.0139  0.0757  -0.0464 239 PHE E CE1 
13823 C CE2 . PHE E 239 ? 0.3667 0.3061 0.5563 0.0122  0.0667  -0.0414 239 PHE E CE2 
13824 C CZ  . PHE E 239 ? 0.3409 0.2926 0.5492 0.0170  0.0660  -0.0395 239 PHE E CZ  
13825 N N   . ILE E 240 ? 0.3999 0.3477 0.4338 -0.0232 0.0691  -0.0536 240 ILE E N   
13826 C CA  . ILE E 240 ? 0.3981 0.3392 0.4108 -0.0335 0.0699  -0.0605 240 ILE E CA  
13827 C C   . ILE E 240 ? 0.4448 0.3675 0.4679 -0.0369 0.0761  -0.0688 240 ILE E C   
13828 O O   . ILE E 240 ? 0.4958 0.4126 0.5456 -0.0299 0.0777  -0.0665 240 ILE E O   
13829 C CB  . ILE E 240 ? 0.3602 0.3132 0.3636 -0.0375 0.0579  -0.0511 240 ILE E CB  
13830 C CG1 . ILE E 240 ? 0.3706 0.3249 0.3906 -0.0342 0.0523  -0.0410 240 ILE E CG1 
13831 C CG2 . ILE E 240 ? 0.3638 0.3322 0.3574 -0.0348 0.0536  -0.0455 240 ILE E CG2 
13832 C CD1 . ILE E 240 ? 0.3689 0.3318 0.3839 -0.0403 0.0452  -0.0345 240 ILE E CD1 
13833 N N   . GLN E 241 ? 0.4538 0.3659 0.4566 -0.0481 0.0782  -0.0778 241 GLN E N   
13834 C CA  . GLN E 241 ? 0.4952 0.3864 0.5047 -0.0531 0.0856  -0.0879 241 GLN E CA  
13835 C C   . GLN E 241 ? 0.5111 0.4012 0.5218 -0.0588 0.0748  -0.0811 241 GLN E C   
13836 O O   . GLN E 241 ? 0.5039 0.4014 0.4959 -0.0679 0.0660  -0.0789 241 GLN E O   
13837 C CB  . GLN E 241 ? 0.5510 0.4250 0.5326 -0.0652 0.0974  -0.1054 241 GLN E CB  
13838 C CG  . GLN E 241 ? 0.6048 0.4541 0.5857 -0.0739 0.1055  -0.1183 241 GLN E CG  
13839 C CD  . GLN E 241 ? 0.6104 0.4480 0.6309 -0.0631 0.1165  -0.1216 241 GLN E CD  
13840 O OE1 . GLN E 241 ? 0.5999 0.4449 0.6453 -0.0512 0.1220  -0.1191 241 GLN E OE1 
13841 N NE2 . GLN E 241 ? 0.6059 0.4247 0.6357 -0.0673 0.1186  -0.1267 241 GLN E NE2 
13842 N N   . VAL E 242 ? 0.3859 0.5136 0.5171 0.0332  0.0761  -0.0657 242 VAL E N   
13843 C CA  . VAL E 242 ? 0.3575 0.4631 0.5114 0.0360  0.0770  -0.0733 242 VAL E CA  
13844 C C   . VAL E 242 ? 0.3770 0.4836 0.5438 0.0422  0.0804  -0.0952 242 VAL E C   
13845 O O   . VAL E 242 ? 0.3838 0.4938 0.5606 0.0504  0.0866  -0.0996 242 VAL E O   
13846 C CB  . VAL E 242 ? 0.3308 0.4145 0.4932 0.0380  0.0823  -0.0582 242 VAL E CB  
13847 C CG1 . VAL E 242 ? 0.3280 0.3884 0.5120 0.0375  0.0866  -0.0636 242 VAL E CG1 
13848 C CG2 . VAL E 242 ? 0.3190 0.4004 0.4695 0.0321  0.0800  -0.0433 242 VAL E CG2 
13849 N N   . ASN E 243 ? 0.4046 0.5088 0.5749 0.0388  0.0737  -0.1112 243 ASN E N   
13850 C CA  . ASN E 243 ? 0.4145 0.5166 0.5968 0.0441  0.0744  -0.1369 243 ASN E CA  
13851 C C   . ASN E 243 ? 0.3604 0.4360 0.5789 0.0493  0.0768  -0.1385 243 ASN E C   
13852 O O   . ASN E 243 ? 0.3551 0.4254 0.5911 0.0575  0.0785  -0.1561 243 ASN E O   
13853 C CB  . ASN E 243 ? 0.4539 0.5585 0.6248 0.0372  0.0613  -0.1534 243 ASN E CB  
13854 C CG  . ASN E 243 ? 0.4874 0.6147 0.6139 0.0320  0.0595  -0.1600 243 ASN E CG  
13855 O OD1 . ASN E 243 ? 0.5137 0.6591 0.6231 0.0329  0.0716  -0.1527 243 ASN E OD1 
13856 N ND2 . ASN E 243 ? 0.4975 0.6233 0.6038 0.0246  0.0436  -0.1729 243 ASN E ND2 
13857 N N   . ALA E 244 ? 0.3406 0.3985 0.5706 0.0432  0.0774  -0.1208 244 ALA E N   
13858 C CA  . ALA E 244 ? 0.3327 0.3615 0.5903 0.0428  0.0809  -0.1160 244 ALA E CA  
13859 C C   . ALA E 244 ? 0.3360 0.3512 0.5909 0.0337  0.0888  -0.0927 244 ALA E C   
13860 O O   . ALA E 244 ? 0.3492 0.3772 0.5953 0.0283  0.0895  -0.0876 244 ALA E O   
13861 C CB  . ALA E 244 ? 0.3213 0.3398 0.6076 0.0400  0.0742  -0.1370 244 ALA E CB  
13862 N N   . ILE E 245 ? 0.3624 0.3496 0.6243 0.0315  0.0944  -0.0793 245 ILE E N   
13863 C CA  . ILE E 245 ? 0.3903 0.3601 0.6489 0.0191  0.1067  -0.0614 245 ILE E CA  
13864 C C   . ILE E 245 ? 0.4105 0.3611 0.7041 0.0090  0.1112  -0.0664 245 ILE E C   
13865 O O   . ILE E 245 ? 0.4065 0.3317 0.7131 0.0099  0.1066  -0.0647 245 ILE E O   
13866 C CB  . ILE E 245 ? 0.4168 0.3637 0.6468 0.0190  0.1092  -0.0384 245 ILE E CB  
13867 C CG1 . ILE E 245 ? 0.4369 0.4042 0.6432 0.0293  0.1014  -0.0360 245 ILE E CG1 
13868 C CG2 . ILE E 245 ? 0.4193 0.3494 0.6323 0.0040  0.1259  -0.0217 245 ILE E CG2 
13869 C CD1 . ILE E 245 ? 0.4744 0.4201 0.6606 0.0327  0.0947  -0.0173 245 ILE E CD1 
13870 N N   . ARG E 246 ? 0.4311 0.3927 0.7463 -0.0011 0.1191  -0.0719 246 ARG E N   
13871 C CA  . ARG E 246 ? 0.4606 0.4100 0.8195 -0.0128 0.1236  -0.0786 246 ARG E CA  
13872 C C   . ARG E 246 ? 0.4439 0.3744 0.8040 -0.0304 0.1478  -0.0593 246 ARG E C   
13873 O O   . ARG E 246 ? 0.4436 0.3860 0.7895 -0.0353 0.1632  -0.0532 246 ARG E O   
13874 C CB  . ARG E 246 ? 0.4766 0.4519 0.8706 -0.0138 0.1143  -0.0998 246 ARG E CB  
13875 C CG  . ARG E 246 ? 0.5453 0.5123 0.9946 -0.0264 0.1162  -0.1091 246 ARG E CG  
13876 C CD  . ARG E 246 ? 0.5978 0.5917 1.0875 -0.0318 0.1139  -0.1217 246 ARG E CD  
13877 N NE  . ARG E 246 ? 0.6073 0.6189 1.1010 -0.0223 0.0843  -0.1423 246 ARG E NE  
13878 C CZ  . ARG E 246 ? 0.6092 0.6439 1.1146 -0.0205 0.0723  -0.1487 246 ARG E CZ  
13879 N NH1 . ARG E 246 ? 0.5787 0.6251 1.1009 -0.0251 0.0892  -0.1401 246 ARG E NH1 
13880 N NH2 . ARG E 246 ? 0.6320 0.6760 1.1306 -0.0146 0.0419  -0.1643 246 ARG E NH2 
13881 N N   . VAL E 247 ? 0.4623 0.3617 0.8373 -0.0409 0.1516  -0.0503 247 VAL E N   
13882 C CA  . VAL E 247 ? 0.4586 0.3383 0.8368 -0.0633 0.1775  -0.0321 247 VAL E CA  
13883 C C   . VAL E 247 ? 0.4608 0.3353 0.9007 -0.0757 0.1778  -0.0426 247 VAL E C   
13884 O O   . VAL E 247 ? 0.4813 0.3313 0.9368 -0.0733 0.1607  -0.0440 247 VAL E O   
13885 C CB  . VAL E 247 ? 0.4990 0.3355 0.8291 -0.0701 0.1803  -0.0023 247 VAL E CB  
13886 C CG1 . VAL E 247 ? 0.5295 0.3460 0.8504 -0.0979 0.2116  0.0178  247 VAL E CG1 
13887 C CG2 . VAL E 247 ? 0.4777 0.3169 0.7518 -0.0566 0.1728  0.0068  247 VAL E CG2 
13888 N N   . ASN E 248 ? 0.4778 0.3764 0.9597 -0.0879 0.1951  -0.0524 248 ASN E N   
13889 C CA  . ASN E 248 ? 0.4903 0.3944 1.0376 -0.0966 0.1904  -0.0667 248 ASN E CA  
13890 C C   . ASN E 248 ? 0.4866 0.3933 1.0569 -0.0808 0.1553  -0.0908 248 ASN E C   
13891 O O   . ASN E 248 ? 0.4784 0.4125 1.0401 -0.0653 0.1394  -0.1073 248 ASN E O   
13892 C CB  . ASN E 248 ? 0.6001 0.4723 1.1427 -0.1128 0.2009  -0.0454 248 ASN E CB  
13893 C CG  . ASN E 248 ? 0.6704 0.5426 1.1816 -0.1297 0.2353  -0.0261 248 ASN E CG  
13894 O OD1 . ASN E 248 ? 0.6605 0.5624 1.1712 -0.1272 0.2515  -0.0357 248 ASN E OD1 
13895 N ND2 . ASN E 248 ? 0.7413 0.5777 1.2231 -0.1469 0.2442  0.0001  248 ASN E ND2 
13896 N N   . LYS E 249 ? 0.5043 0.3836 1.0890 -0.0813 0.1404  -0.0918 249 LYS E N   
13897 C CA  . LYS E 249 ? 0.4939 0.3756 1.0913 -0.0647 0.1086  -0.1193 249 LYS E CA  
13898 C C   . LYS E 249 ? 0.4984 0.3558 1.0561 -0.0484 0.0958  -0.1167 249 LYS E C   
13899 O O   . LYS E 249 ? 0.4730 0.3260 1.0418 -0.0360 0.0734  -0.1395 249 LYS E O   
13900 C CB  . LYS E 249 ? 0.5207 0.4033 1.1673 -0.0699 0.0938  -0.1317 249 LYS E CB  
13901 C CG  . LYS E 249 ? 0.5208 0.4320 1.2130 -0.0812 0.1034  -0.1349 249 LYS E CG  
13902 C CD  . LYS E 249 ? 0.5357 0.4466 1.2769 -0.0831 0.0823  -0.1506 249 LYS E CD  
13903 C CE  . LYS E 249 ? 0.5269 0.4583 1.3200 -0.0948 0.0940  -0.1498 249 LYS E CE  
13904 N NZ  . LYS E 249 ? 0.5149 0.4447 1.3571 -0.0954 0.0688  -0.1666 249 LYS E NZ  
13905 N N   . HIS E 250 ? 0.4992 0.3463 1.0093 -0.0466 0.1084  -0.0912 250 HIS E N   
13906 C CA  . HIS E 250 ? 0.5042 0.3347 0.9848 -0.0292 0.0942  -0.0891 250 HIS E CA  
13907 C C   . HIS E 250 ? 0.5021 0.3662 0.9406 -0.0125 0.0929  -0.0951 250 HIS E C   
13908 O O   . HIS E 250 ? 0.5163 0.3935 0.9249 -0.0172 0.1076  -0.0789 250 HIS E O   
13909 C CB  . HIS E 250 ? 0.5252 0.3138 0.9844 -0.0397 0.1016  -0.0543 250 HIS E CB  
13910 C CG  . HIS E 250 ? 0.5584 0.3093 1.0559 -0.0575 0.1001  -0.0449 250 HIS E CG  
13911 N ND1 . HIS E 250 ? 0.5725 0.2851 1.0449 -0.0735 0.1060  -0.0091 250 HIS E ND1 
13912 C CD2 . HIS E 250 ? 0.5316 0.2902 1.0737 -0.0606 0.0895  -0.0634 250 HIS E CD2 
13913 C CE1 . HIS E 250 ? 0.6090 0.3060 1.1109 -0.0857 0.1000  -0.0062 250 HIS E CE1 
13914 N NE2 . HIS E 250 ? 0.5825 0.3077 1.1303 -0.0776 0.0904  -0.0392 250 HIS E NE2 
13915 N N   . LEU E 251 ? 0.4943 0.3712 0.9300 0.0059  0.0768  -0.1187 251 LEU E N   
13916 C CA  . LEU E 251 ? 0.4431 0.3524 0.8409 0.0189  0.0765  -0.1237 251 LEU E CA  
13917 C C   . LEU E 251 ? 0.3739 0.2773 0.7557 0.0342  0.0711  -0.1209 251 LEU E C   
13918 O O   . LEU E 251 ? 0.3886 0.2871 0.7909 0.0460  0.0605  -0.1424 251 LEU E O   
13919 C CB  . LEU E 251 ? 0.4211 0.3590 0.8219 0.0245  0.0659  -0.1545 251 LEU E CB  
13920 C CG  . LEU E 251 ? 0.4251 0.3788 0.8401 0.0125  0.0651  -0.1582 251 LEU E CG  
13921 C CD1 . LEU E 251 ? 0.4537 0.3915 0.9174 0.0039  0.0559  -0.1739 251 LEU E CD1 
13922 C CD2 . LEU E 251 ? 0.4131 0.3980 0.7995 0.0186  0.0546  -0.1728 251 LEU E CD2 
13923 N N   . VAL E 252 ? 0.3828 0.2916 0.7309 0.0350  0.0779  -0.0984 252 VAL E N   
13924 C CA  . VAL E 252 ? 0.3916 0.2987 0.7288 0.0487  0.0713  -0.0925 252 VAL E CA  
13925 C C   . VAL E 252 ? 0.3860 0.3347 0.7066 0.0596  0.0726  -0.1085 252 VAL E C   
13926 O O   . VAL E 252 ? 0.4337 0.4042 0.7272 0.0539  0.0794  -0.1011 252 VAL E O   
13927 C CB  . VAL E 252 ? 0.3828 0.2674 0.6902 0.0410  0.0745  -0.0573 252 VAL E CB  
13928 C CG1 . VAL E 252 ? 0.3817 0.2644 0.6850 0.0550  0.0622  -0.0510 252 VAL E CG1 
13929 C CG2 . VAL E 252 ? 0.4272 0.2675 0.7432 0.0261  0.0755  -0.0384 252 VAL E CG2 
13930 N N   . ILE E 253 ? 0.3769 0.3364 0.7163 0.0743  0.0672  -0.1314 253 ILE E N   
13931 C CA  . ILE E 253 ? 0.4025 0.4035 0.7263 0.0815  0.0728  -0.1498 253 ILE E CA  
13932 C C   . ILE E 253 ? 0.4473 0.4590 0.7699 0.0904  0.0728  -0.1370 253 ILE E C   
13933 O O   . ILE E 253 ? 0.4756 0.4773 0.8318 0.1030  0.0658  -0.1442 253 ILE E O   
13934 C CB  . ILE E 253 ? 0.3988 0.4117 0.7411 0.0903  0.0718  -0.1883 253 ILE E CB  
13935 C CG1 . ILE E 253 ? 0.3649 0.3579 0.7204 0.0828  0.0649  -0.2020 253 ILE E CG1 
13936 C CG2 . ILE E 253 ? 0.3966 0.4522 0.7073 0.0908  0.0814  -0.2033 253 ILE E CG2 
13937 C CD1 . ILE E 253 ? 0.3480 0.3473 0.6812 0.0683  0.0660  -0.1909 253 ILE E CD1 
13938 N N   . PRO E 254 ? 0.4469 0.4772 0.7367 0.0839  0.0778  -0.1182 254 PRO E N   
13939 C CA  . PRO E 254 ? 0.4845 0.5242 0.7719 0.0890  0.0752  -0.1024 254 PRO E CA  
13940 C C   . PRO E 254 ? 0.5539 0.6293 0.8636 0.1006  0.0804  -0.1232 254 PRO E C   
13941 O O   . PRO E 254 ? 0.5383 0.6431 0.8400 0.0995  0.0923  -0.1463 254 PRO E O   
13942 C CB  . PRO E 254 ? 0.4052 0.4567 0.6525 0.0769  0.0797  -0.0833 254 PRO E CB  
13943 C CG  . PRO E 254 ? 0.3516 0.3921 0.5874 0.0666  0.0829  -0.0845 254 PRO E CG  
13944 C CD  . PRO E 254 ? 0.3836 0.4263 0.6417 0.0712  0.0830  -0.1123 254 PRO E CD  
13945 N N   . THR E 255 ? 0.6331 0.7034 0.9723 0.1109  0.0707  -0.1155 255 THR E N   
13946 C CA  . THR E 255 ? 0.6558 0.7620 1.0224 0.1199  0.0747  -0.1271 255 THR E CA  
13947 C C   . THR E 255 ? 0.6567 0.7406 1.0619 0.1311  0.0534  -0.1125 255 THR E C   
13948 O O   . THR E 255 ? 0.6700 0.7142 1.0944 0.1367  0.0373  -0.1089 255 THR E O   
13949 C CB  . THR E 255 ? 0.8867 1.0147 1.2604 0.1221  0.0850  -0.1581 255 THR E CB  
13950 O OG1 . THR E 255 ? 0.9234 1.0556 1.2623 0.1130  0.0957  -0.1718 255 THR E OG1 
13951 C CG2 . THR E 255 ? 0.8433 1.0138 1.2239 0.1219  0.0970  -0.1640 255 THR E CG2 
13952 N N   . GLY E 271 ? 1.0191 1.3664 0.7864 -0.1020 0.1869  -0.0854 271 GLY E N   
13953 C CA  . GLY E 271 ? 0.9698 1.3343 0.7841 -0.1029 0.1978  -0.0647 271 GLY E CA  
13954 C C   . GLY E 271 ? 0.8911 1.2698 0.7877 -0.0765 0.2115  -0.0846 271 GLY E C   
13955 O O   . GLY E 271 ? 0.8937 1.2922 0.8217 -0.0730 0.2346  -0.0952 271 GLY E O   
13956 N N   . GLU E 272 ? 0.8138 1.1803 0.7457 -0.0585 0.1949  -0.0876 272 GLU E N   
13957 C CA  . GLU E 272 ? 0.7440 1.1117 0.7502 -0.0338 0.1968  -0.0985 272 GLU E CA  
13958 C C   . GLU E 272 ? 0.6721 1.0197 0.6957 -0.0298 0.1714  -0.0719 272 GLU E C   
13959 O O   . GLU E 272 ? 0.7061 1.0232 0.6977 -0.0336 0.1484  -0.0600 272 GLU E O   
13960 C CB  . GLU E 272 ? 0.7731 1.1282 0.7990 -0.0135 0.1982  -0.1325 272 GLU E CB  
13961 C CG  . GLU E 272 ? 0.8495 1.2177 0.9125 -0.0019 0.2178  -0.1566 272 GLU E CG  
13962 C CD  . GLU E 272 ? 0.8809 1.2576 1.0121 0.0112  0.2171  -0.1469 272 GLU E CD  
13963 O OE1 . GLU E 272 ? 0.8782 1.2434 1.0292 0.0154  0.1995  -0.1262 272 GLU E OE1 
13964 O OE2 . GLU E 272 ? 0.9000 1.2958 1.0659 0.0176  0.2330  -0.1614 272 GLU E OE2 
13965 N N   . ILE E 273 ? 0.6079 0.9617 0.6815 -0.0216 0.1695  -0.0608 273 ILE E N   
13966 C CA  . ILE E 273 ? 0.5750 0.8968 0.6574 -0.0176 0.1421  -0.0352 273 ILE E CA  
13967 C C   . ILE E 273 ? 0.5660 0.8547 0.6585 0.0001  0.1285  -0.0460 273 ILE E C   
13968 O O   . ILE E 273 ? 0.5864 0.8781 0.7039 0.0141  0.1378  -0.0697 273 ILE E O   
13969 C CB  . ILE E 273 ? 0.5022 0.8350 0.6314 -0.0137 0.1398  -0.0221 273 ILE E CB  
13970 C CG1 . ILE E 273 ? 0.6154 0.9849 0.7455 -0.0331 0.1561  -0.0122 273 ILE E CG1 
13971 C CG2 . ILE E 273 ? 0.4213 0.7199 0.5479 -0.0125 0.1128  0.0019  273 ILE E CG2 
13972 C CD1 . ILE E 273 ? 0.6588 1.0374 0.8367 -0.0319 0.1482  0.0027  273 ILE E CD1 
13973 N N   . GLY E 274 ? 0.5288 0.7863 0.6054 -0.0014 0.1073  -0.0297 274 GLY E N   
13974 C CA  . GLY E 274 ? 0.4872 0.7150 0.5763 0.0118  0.0977  -0.0369 274 GLY E CA  
13975 C C   . GLY E 274 ? 0.4746 0.6945 0.6015 0.0260  0.0983  -0.0376 274 GLY E C   
13976 O O   . GLY E 274 ? 0.4630 0.6957 0.6077 0.0260  0.0988  -0.0281 274 GLY E O   
13977 N N   . GLY E 275 ? 0.4741 0.6701 0.6136 0.0367  0.0952  -0.0468 275 GLY E N   
13978 C CA  . GLY E 275 ? 0.4508 0.6323 0.6198 0.0486  0.0918  -0.0451 275 GLY E CA  
13979 C C   . GLY E 275 ? 0.4273 0.5769 0.5872 0.0481  0.0792  -0.0256 275 GLY E C   
13980 O O   . GLY E 275 ? 0.4496 0.5819 0.6236 0.0553  0.0723  -0.0197 275 GLY E O   
13981 N N   . ALA E 276 ? 0.3873 0.5269 0.5232 0.0395  0.0752  -0.0168 276 ALA E N   
13982 C CA  . ALA E 276 ? 0.3211 0.4318 0.4463 0.0384  0.0685  -0.0040 276 ALA E CA  
13983 C C   . ALA E 276 ? 0.3496 0.4643 0.4627 0.0320  0.0597  0.0104  276 ALA E C   
13984 O O   . ALA E 276 ? 0.3301 0.4558 0.4349 0.0244  0.0568  0.0132  276 ALA E O   
13985 C CB  . ALA E 276 ? 0.2533 0.3480 0.3729 0.0352  0.0720  -0.0096 276 ALA E CB  
13986 N N   . LEU E 277 ? 0.3665 0.4693 0.4794 0.0345  0.0517  0.0203  277 LEU E N   
13987 C CA  . LEU E 277 ? 0.3375 0.4391 0.4409 0.0286  0.0405  0.0323  277 LEU E CA  
13988 C C   . LEU E 277 ? 0.3715 0.4472 0.4531 0.0252  0.0396  0.0331  277 LEU E C   
13989 O O   . LEU E 277 ? 0.4270 0.4805 0.4984 0.0275  0.0465  0.0294  277 LEU E O   
13990 C CB  . LEU E 277 ? 0.3309 0.4258 0.4415 0.0323  0.0280  0.0405  277 LEU E CB  
13991 C CG  . LEU E 277 ? 0.3322 0.4189 0.4317 0.0261  0.0126  0.0514  277 LEU E CG  
13992 C CD1 . LEU E 277 ? 0.2966 0.4153 0.4151 0.0183  0.0113  0.0558  277 LEU E CD1 
13993 C CD2 . LEU E 277 ? 0.3536 0.4211 0.4511 0.0299  -0.0050 0.0589  277 LEU E CD2 
13994 N N   . ILE E 278 ? 0.3663 0.4445 0.4438 0.0191  0.0320  0.0374  278 ILE E N   
13995 C CA  . ILE E 278 ? 0.3523 0.4065 0.4158 0.0175  0.0304  0.0347  278 ILE E CA  
13996 C C   . ILE E 278 ? 0.3848 0.4259 0.4360 0.0151  0.0158  0.0420  278 ILE E C   
13997 O O   . ILE E 278 ? 0.4006 0.4561 0.4634 0.0106  0.0032  0.0505  278 ILE E O   
13998 C CB  . ILE E 278 ? 0.3318 0.3925 0.4066 0.0141  0.0282  0.0304  278 ILE E CB  
13999 C CG1 . ILE E 278 ? 0.2935 0.3675 0.3797 0.0153  0.0370  0.0229  278 ILE E CG1 
14000 C CG2 . ILE E 278 ? 0.3594 0.3984 0.4305 0.0148  0.0302  0.0217  278 ILE E CG2 
14001 C CD1 . ILE E 278 ? 0.2873 0.3684 0.3849 0.0111  0.0271  0.0218  278 ILE E CD1 
14002 N N   . THR E 279 ? 0.4102 0.4227 0.4354 0.0161  0.0174  0.0388  279 THR E N   
14003 C CA  . THR E 279 ? 0.3997 0.3939 0.4053 0.0139  0.0007  0.0435  279 THR E CA  
14004 C C   . THR E 279 ? 0.4408 0.4036 0.4122 0.0120  0.0073  0.0325  279 THR E C   
14005 O O   . THR E 279 ? 0.4603 0.4141 0.4207 0.0120  0.0279  0.0242  279 THR E O   
14006 C CB  . THR E 279 ? 0.4085 0.3970 0.4072 0.0163  -0.0104 0.0535  279 THR E CB  
14007 O OG1 . THR E 279 ? 0.4586 0.4282 0.4387 0.0132  -0.0317 0.0576  279 THR E OG1 
14008 C CG2 . THR E 279 ? 0.4158 0.3813 0.3890 0.0182  0.0019  0.0525  279 THR E CG2 
14009 N N   . THR E 280 ? 0.4538 0.4002 0.4088 0.0093  -0.0088 0.0308  280 THR E N   
14010 C CA  . THR E 280 ? 0.4883 0.4043 0.4052 0.0069  -0.0009 0.0160  280 THR E CA  
14011 C C   . THR E 280 ? 0.5257 0.4105 0.3915 0.0031  -0.0152 0.0215  280 THR E C   
14012 O O   . THR E 280 ? 0.5795 0.4355 0.4009 -0.0010 -0.0107 0.0088  280 THR E O   
14013 C CB  . THR E 280 ? 0.4922 0.4069 0.4271 0.0069  -0.0093 0.0027  280 THR E CB  
14014 O OG1 . THR E 280 ? 0.5000 0.4176 0.4478 0.0046  -0.0385 0.0137  280 THR E OG1 
14015 C CG2 . THR E 280 ? 0.4433 0.3808 0.4242 0.0101  0.0005  -0.0028 280 THR E CG2 
14016 N N   . THR E 281 ? 0.5211 0.4107 0.3930 0.0044  -0.0336 0.0389  281 THR E N   
14017 C CA  . THR E 281 ? 0.5738 0.4334 0.4052 0.0011  -0.0586 0.0462  281 THR E CA  
14018 C C   . THR E 281 ? 0.6309 0.4631 0.4185 -0.0012 -0.0557 0.0564  281 THR E C   
14019 O O   . THR E 281 ? 0.6823 0.4874 0.4372 -0.0038 -0.0827 0.0671  281 THR E O   
14020 C CB  . THR E 281 ? 0.5557 0.4354 0.4296 0.0031  -0.0893 0.0585  281 THR E CB  
14021 O OG1 . THR E 281 ? 0.5097 0.4245 0.4334 0.0086  -0.0818 0.0676  281 THR E OG1 
14022 C CG2 . THR E 281 ? 0.5419 0.4341 0.4429 0.0004  -0.0976 0.0511  281 THR E CG2 
14023 N N   . HIS E 282 ? 0.6116 0.4487 0.4011 -0.0011 -0.0266 0.0547  282 HIS E N   
14024 C CA  . HIS E 282 ? 0.6344 0.4368 0.3700 -0.0084 -0.0157 0.0618  282 HIS E CA  
14025 C C   . HIS E 282 ? 0.6001 0.4093 0.3366 -0.0124 0.0249  0.0484  282 HIS E C   
14026 O O   . HIS E 282 ? 0.5508 0.3948 0.3431 -0.0060 0.0378  0.0405  282 HIS E O   
14027 C CB  . HIS E 282 ? 0.6655 0.4649 0.4182 -0.0040 -0.0327 0.0817  282 HIS E CB  
14028 C CG  . HIS E 282 ? 0.6597 0.5014 0.4844 0.0062  -0.0239 0.0800  282 HIS E CG  
14029 N ND1 . HIS E 282 ? 0.6526 0.5101 0.4971 0.0061  0.0065  0.0712  282 HIS E ND1 
14030 C CD2 . HIS E 282 ? 0.6495 0.5199 0.5291 0.0158  -0.0413 0.0846  282 HIS E CD2 
14031 C CE1 . HIS E 282 ? 0.6023 0.4935 0.5032 0.0151  0.0057  0.0700  282 HIS E CE1 
14032 N NE2 . HIS E 282 ? 0.6127 0.5137 0.5352 0.0208  -0.0202 0.0774  282 HIS E NE2 
14033 N N   . PRO E 283 ? 0.6453 0.4215 0.3199 -0.0247 0.0449  0.0459  283 PRO E N   
14034 C CA  . PRO E 283 ? 0.6332 0.4156 0.3093 -0.0313 0.0870  0.0306  283 PRO E CA  
14035 C C   . PRO E 283 ? 0.6470 0.4434 0.3610 -0.0311 0.1030  0.0391  283 PRO E C   
14036 O O   . PRO E 283 ? 0.6227 0.4482 0.3864 -0.0280 0.1251  0.0246  283 PRO E O   
14037 C CB  . PRO E 283 ? 0.7297 0.4687 0.3174 -0.0481 0.1012  0.0298  283 PRO E CB  
14038 C CG  . PRO E 283 ? 0.7842 0.4887 0.3232 -0.0506 0.0631  0.0533  283 PRO E CG  
14039 C CD  . PRO E 283 ? 0.7261 0.4559 0.3207 -0.0349 0.0271  0.0557  283 PRO E CD  
14040 N N   . TYR E 284 ? 0.6918 0.4655 0.3861 -0.0341 0.0888  0.0616  284 TYR E N   
14041 C CA  . TYR E 284 ? 0.6874 0.4671 0.4136 -0.0356 0.1036  0.0683  284 TYR E CA  
14042 C C   . TYR E 284 ? 0.6335 0.4461 0.4284 -0.0193 0.0849  0.0691  284 TYR E C   
14043 O O   . TYR E 284 ? 0.6555 0.4809 0.4661 -0.0094 0.0591  0.0709  284 TYR E O   
14044 C CB  . TYR E 284 ? 0.7656 0.4982 0.4354 -0.0491 0.0990  0.0923  284 TYR E CB  
14045 C CG  . TYR E 284 ? 0.8385 0.5366 0.4265 -0.0689 0.1206  0.0917  284 TYR E CG  
14046 C CD1 . TYR E 284 ? 0.8610 0.5728 0.4517 -0.0793 0.1657  0.0724  284 TYR E CD1 
14047 C CD2 . TYR E 284 ? 0.8903 0.5436 0.3993 -0.0777 0.0963  0.1079  284 TYR E CD2 
14048 C CE1 . TYR E 284 ? 0.9291 0.6131 0.4445 -0.0987 0.1922  0.0674  284 TYR E CE1 
14049 C CE2 . TYR E 284 ? 0.9738 0.5942 0.3966 -0.0980 0.1189  0.1049  284 TYR E CE2 
14050 C CZ  . TYR E 284 ? 0.9973 0.6347 0.4231 -0.1087 0.1699  0.0833  284 TYR E CZ  
14051 O OH  . TYR E 284 ? 1.0825 0.7072 0.4529 -0.1243 0.1897  0.0719  284 TYR E OH  
14052 N N   . THR E 285 ? 0.5845 0.4131 0.4220 -0.0178 0.1000  0.0654  285 THR E N   
14053 C CA  . THR E 285 ? 0.5008 0.3589 0.3964 -0.0039 0.0862  0.0628  285 THR E CA  
14054 C C   . THR E 285 ? 0.5365 0.3742 0.4329 0.0009  0.0619  0.0799  285 THR E C   
14055 O O   . THR E 285 ? 0.5845 0.3853 0.4525 -0.0081 0.0620  0.0946  285 THR E O   
14056 C CB  . THR E 285 ? 0.4562 0.3369 0.3962 -0.0039 0.1074  0.0493  285 THR E CB  
14057 O OG1 . THR E 285 ? 0.4835 0.3855 0.4348 -0.0054 0.1227  0.0328  285 THR E OG1 
14058 C CG2 . THR E 285 ? 0.4092 0.3172 0.3979 0.0091  0.0937  0.0442  285 THR E CG2 
14059 N N   . VAL E 286 ? 0.5256 0.3867 0.4568 0.0141  0.0403  0.0783  286 VAL E N   
14060 C CA  . VAL E 286 ? 0.5323 0.3802 0.4781 0.0222  0.0132  0.0904  286 VAL E CA  
14061 C C   . VAL E 286 ? 0.5136 0.3889 0.5219 0.0344  0.0147  0.0789  286 VAL E C   
14062 O O   . VAL E 286 ? 0.4690 0.3857 0.5115 0.0406  0.0237  0.0628  286 VAL E O   
14063 C CB  . VAL E 286 ? 0.5214 0.3769 0.4663 0.0275  -0.0128 0.0949  286 VAL E CB  
14064 C CG1 . VAL E 286 ? 0.5227 0.3696 0.4986 0.0379  -0.0429 0.1047  286 VAL E CG1 
14065 C CG2 . VAL E 286 ? 0.5615 0.3840 0.4389 0.0155  -0.0179 0.1038  286 VAL E CG2 
14066 N N   . LEU E 287 ? 0.5553 0.4036 0.5746 0.0367  0.0044  0.0871  287 LEU E N   
14067 C CA  . LEU E 287 ? 0.5045 0.3716 0.5822 0.0488  0.0048  0.0730  287 LEU E CA  
14068 C C   . LEU E 287 ? 0.5157 0.3776 0.6303 0.0625  -0.0243 0.0771  287 LEU E C   
14069 O O   . LEU E 287 ? 0.5830 0.4048 0.6729 0.0596  -0.0492 0.0984  287 LEU E O   
14070 C CB  . LEU E 287 ? 0.4874 0.3280 0.5634 0.0410  0.0177  0.0744  287 LEU E CB  
14071 C CG  . LEU E 287 ? 0.4681 0.3153 0.5178 0.0271  0.0466  0.0692  287 LEU E CG  
14072 C CD1 . LEU E 287 ? 0.4852 0.3045 0.5338 0.0152  0.0603  0.0738  287 LEU E CD1 
14073 C CD2 . LEU E 287 ? 0.4186 0.3153 0.5013 0.0347  0.0582  0.0458  287 LEU E CD2 
14074 N N   . SER E 288 ? 0.4945 0.3960 0.6683 0.0768  -0.0220 0.0557  288 SER E N   
14075 C CA  . SER E 288 ? 0.5452 0.4475 0.7723 0.0924  -0.0468 0.0532  288 SER E CA  
14076 C C   . SER E 288 ? 0.5968 0.4505 0.8304 0.0935  -0.0617 0.0631  288 SER E C   
14077 O O   . SER E 288 ? 0.5989 0.4347 0.8120 0.0840  -0.0450 0.0633  288 SER E O   
14078 C CB  . SER E 288 ? 0.5474 0.5050 0.8365 0.1059  -0.0328 0.0229  288 SER E CB  
14079 O OG  . SER E 288 ? 0.5542 0.5191 0.8575 0.1077  -0.0127 0.0025  288 SER E OG  
14080 N N   . HIS E 289 ? 0.6432 0.4733 0.9086 0.1039  -0.0956 0.0730  289 HIS E N   
14081 C CA  . HIS E 289 ? 0.7333 0.5052 0.9955 0.1016  -0.1165 0.0907  289 HIS E CA  
14082 C C   . HIS E 289 ? 0.6857 0.4590 0.9851 0.1057  -0.0989 0.0703  289 HIS E C   
14083 O O   . HIS E 289 ? 0.7136 0.4443 0.9819 0.0919  -0.0962 0.0859  289 HIS E O   
14084 C CB  . HIS E 289 ? 0.8208 0.5689 1.1264 0.1156  -0.1618 0.1017  289 HIS E CB  
14085 C CG  . HIS E 289 ? 0.9397 0.6328 1.2301 0.1077  -0.1829 0.1199  289 HIS E CG  
14086 N ND1 . HIS E 289 ? 1.0241 0.6608 1.2318 0.0856  -0.1905 0.1546  289 HIS E ND1 
14087 C CD2 . HIS E 289 ? 0.9773 0.6658 1.3213 0.1165  -0.1951 0.1071  289 HIS E CD2 
14088 C CE1 . HIS E 289 ? 1.0820 0.6818 1.2944 0.0814  -0.2072 0.1647  289 HIS E CE1 
14089 N NE2 . HIS E 289 ? 1.0566 0.6853 1.3536 0.1006  -0.2128 0.1368  289 HIS E NE2 
14090 N N   . SER E 290 ? 0.6293 0.4506 0.9920 0.1224  -0.0858 0.0350  290 SER E N   
14091 C CA  . SER E 290 ? 0.6419 0.4624 1.0413 0.1276  -0.0734 0.0115  290 SER E CA  
14092 C C   . SER E 290 ? 0.5704 0.3892 0.9217 0.1092  -0.0446 0.0122  290 SER E C   
14093 O O   . SER E 290 ? 0.6171 0.4035 0.9721 0.1026  -0.0439 0.0142  290 SER E O   
14094 C CB  . SER E 290 ? 0.6662 0.5441 1.1271 0.1456  -0.0589 -0.0306 290 SER E CB  
14095 O OG  . SER E 290 ? 0.6573 0.5853 1.0936 0.1405  -0.0306 -0.0428 290 SER E OG  
14096 N N   . ILE E 291 ? 0.4846 0.3376 0.7973 0.1006  -0.0229 0.0107  291 ILE E N   
14097 C CA  . ILE E 291 ? 0.4443 0.2991 0.7186 0.0842  0.0020  0.0110  291 ILE E CA  
14098 C C   . ILE E 291 ? 0.4993 0.3055 0.7219 0.0647  0.0004  0.0433  291 ILE E C   
14099 O O   . ILE E 291 ? 0.4801 0.2683 0.6959 0.0520  0.0139  0.0450  291 ILE E O   
14100 C CB  . ILE E 291 ? 0.3930 0.2943 0.6460 0.0817  0.0202  0.0015  291 ILE E CB  
14101 C CG1 . ILE E 291 ? 0.3742 0.3222 0.6700 0.0960  0.0274  -0.0306 291 ILE E CG1 
14102 C CG2 . ILE E 291 ? 0.3870 0.2882 0.6070 0.0658  0.0410  0.0031  291 ILE E CG2 
14103 C CD1 . ILE E 291 ? 0.3698 0.3611 0.6449 0.0921  0.0422  -0.0368 291 ILE E CD1 
14104 N N   . PHE E 292 ? 0.5491 0.3341 0.7355 0.0610  -0.0159 0.0681  292 PHE E N   
14105 C CA  . PHE E 292 ? 0.6305 0.3665 0.7552 0.0404  -0.0169 0.0994  292 PHE E CA  
14106 C C   . PHE E 292 ? 0.7195 0.4036 0.8510 0.0320  -0.0272 0.1154  292 PHE E C   
14107 O O   . PHE E 292 ? 0.7729 0.4365 0.8760 0.0121  -0.0068 0.1253  292 PHE E O   
14108 C CB  . PHE E 292 ? 0.6447 0.3615 0.7303 0.0401  -0.0419 0.1214  292 PHE E CB  
14109 C CG  . PHE E 292 ? 0.7068 0.3655 0.7189 0.0180  -0.0474 0.1549  292 PHE E CG  
14110 C CD1 . PHE E 292 ? 0.7013 0.3594 0.6513 -0.0010 -0.0193 0.1597  292 PHE E CD1 
14111 C CD2 . PHE E 292 ? 0.7735 0.3763 0.7779 0.0154  -0.0809 0.1812  292 PHE E CD2 
14112 C CE1 . PHE E 292 ? 0.7467 0.3518 0.6214 -0.0239 -0.0194 0.1885  292 PHE E CE1 
14113 C CE2 . PHE E 292 ? 0.8350 0.3800 0.7594 -0.0087 -0.0860 0.2149  292 PHE E CE2 
14114 C CZ  . PHE E 292 ? 0.8107 0.3584 0.6670 -0.0292 -0.0524 0.2176  292 PHE E CZ  
14115 N N   . GLU E 293 ? 0.7349 0.3993 0.9120 0.0469  -0.0581 0.1162  293 GLU E N   
14116 C CA  . GLU E 293 ? 0.8126 0.4201 0.9979 0.0387  -0.0747 0.1352  293 GLU E CA  
14117 C C   . GLU E 293 ? 0.7677 0.3853 0.9856 0.0333  -0.0496 0.1153  293 GLU E C   
14118 O O   . GLU E 293 ? 0.7841 0.3605 0.9830 0.0128  -0.0439 0.1350  293 GLU E O   
14119 C CB  . GLU E 293 ? 0.9287 0.5177 1.1679 0.0591  -0.1159 0.1349  293 GLU E CB  
14120 C CG  . GLU E 293 ? 1.0111 0.6475 1.3332 0.0839  -0.1128 0.0918  293 GLU E CG  
14121 C CD  . GLU E 293 ? 1.1703 0.7901 1.5369 0.0923  -0.1392 0.0855  293 GLU E CD  
14122 O OE1 . GLU E 293 ? 1.2797 0.8489 1.6152 0.0792  -0.1615 0.1168  293 GLU E OE1 
14123 O OE2 . GLU E 293 ? 1.1736 0.8320 1.6040 0.1104  -0.1360 0.0484  293 GLU E OE2 
14124 N N   . VAL E 294 ? 0.6820 0.3527 0.9473 0.0496  -0.0354 0.0769  294 VAL E N   
14125 C CA  . VAL E 294 ? 0.6277 0.3094 0.9240 0.0455  -0.0164 0.0548  294 VAL E CA  
14126 C C   . VAL E 294 ? 0.5960 0.2873 0.8499 0.0228  0.0152  0.0618  294 VAL E C   
14127 O O   . VAL E 294 ? 0.6371 0.3063 0.8978 0.0063  0.0258  0.0672  294 VAL E O   
14128 C CB  . VAL E 294 ? 0.5774 0.3130 0.9212 0.0665  -0.0096 0.0116  294 VAL E CB  
14129 C CG1 . VAL E 294 ? 0.5772 0.3247 0.9414 0.0595  0.0086  -0.0114 294 VAL E CG1 
14130 C CG2 . VAL E 294 ? 0.5398 0.2709 0.9414 0.0903  -0.0356 -0.0043 294 VAL E CG2 
14131 N N   . PHE E 295 ? 0.5599 0.2851 0.7775 0.0219  0.0298  0.0607  295 PHE E N   
14132 C CA  . PHE E 295 ? 0.5422 0.2819 0.7302 0.0038  0.0595  0.0621  295 PHE E CA  
14133 C C   . PHE E 295 ? 0.5931 0.2872 0.7373 -0.0216 0.0692  0.0937  295 PHE E C   
14134 O O   . PHE E 295 ? 0.5947 0.2897 0.7422 -0.0392 0.0938  0.0925  295 PHE E O   
14135 C CB  . PHE E 295 ? 0.5350 0.3132 0.6937 0.0083  0.0691  0.0560  295 PHE E CB  
14136 C CG  . PHE E 295 ? 0.5916 0.3779 0.7202 -0.0099 0.0973  0.0595  295 PHE E CG  
14137 C CD1 . PHE E 295 ? 0.5878 0.4028 0.7493 -0.0134 0.1153  0.0384  295 PHE E CD1 
14138 C CD2 . PHE E 295 ? 0.6182 0.3828 0.6885 -0.0235 0.1049  0.0814  295 PHE E CD2 
14139 C CE1 . PHE E 295 ? 0.5788 0.4040 0.7267 -0.0285 0.1411  0.0384  295 PHE E CE1 
14140 C CE2 . PHE E 295 ? 0.6300 0.4042 0.6794 -0.0394 0.1346  0.0793  295 PHE E CE2 
14141 C CZ  . PHE E 295 ? 0.6044 0.4108 0.6983 -0.0410 0.1530  0.0573  295 PHE E CZ  
14142 N N   . THR E 296 ? 0.6497 0.3054 0.7508 -0.0252 0.0506  0.1218  296 THR E N   
14143 C CA  . THR E 296 ? 0.7659 0.3746 0.8078 -0.0527 0.0607  0.1547  296 THR E CA  
14144 C C   . THR E 296 ? 0.8433 0.4132 0.9099 -0.0686 0.0616  0.1672  296 THR E C   
14145 O O   . THR E 296 ? 0.9108 0.4636 0.9505 -0.0959 0.0890  0.1818  296 THR E O   
14146 C CB  . THR E 296 ? 0.8281 0.3971 0.8149 -0.0531 0.0318  0.1835  296 THR E CB  
14147 O OG1 . THR E 296 ? 0.8349 0.4382 0.7958 -0.0431 0.0340  0.1728  296 THR E OG1 
14148 C CG2 . THR E 296 ? 0.9212 0.4355 0.8354 -0.0846 0.0412  0.2193  296 THR E CG2 
14149 N N   . GLN E 297 ? 0.8343 0.3935 0.9588 -0.0517 0.0337  0.1584  297 GLN E N   
14150 C CA  . GLN E 297 ? 0.8539 0.3733 1.0123 -0.0640 0.0279  0.1680  297 GLN E CA  
14151 C C   . GLN E 297 ? 0.7862 0.3400 0.9861 -0.0721 0.0587  0.1427  297 GLN E C   
14152 O O   . GLN E 297 ? 0.8092 0.3406 1.0061 -0.0975 0.0749  0.1569  297 GLN E O   
14153 C CB  . GLN E 297 ? 0.8846 0.3907 1.0972 -0.0392 -0.0118 0.1563  297 GLN E CB  
14154 C CG  . GLN E 297 ? 0.9522 0.4265 1.1898 -0.0477 -0.0240 0.1592  297 GLN E CG  
14155 C CD  . GLN E 297 ? 1.0452 0.4622 1.2176 -0.0760 -0.0263 0.2016  297 GLN E CD  
14156 O OE1 . GLN E 297 ? 1.1322 0.5201 1.2581 -0.0746 -0.0471 0.2260  297 GLN E OE1 
14157 N NE2 . GLN E 297 ? 1.0314 0.4337 1.2006 -0.1021 -0.0048 0.2091  297 GLN E NE2 
14158 N N   . VAL E 298 ? 0.7104 0.3208 0.9455 -0.0517 0.0649  0.1052  298 VAL E N   
14159 C CA  . VAL E 298 ? 0.6647 0.3099 0.9393 -0.0575 0.0880  0.0795  298 VAL E CA  
14160 C C   . VAL E 298 ? 0.7055 0.3569 0.9480 -0.0842 0.1238  0.0931  298 VAL E C   
14161 O O   . VAL E 298 ? 0.7590 0.4108 1.0339 -0.1023 0.1421  0.0898  298 VAL E O   
14162 C CB  . VAL E 298 ? 0.5738 0.2762 0.8711 -0.0339 0.0872  0.0426  298 VAL E CB  
14163 C CG1 . VAL E 298 ? 0.5306 0.2677 0.8573 -0.0424 0.1084  0.0208  298 VAL E CG1 
14164 C CG2 . VAL E 298 ? 0.5593 0.2612 0.9004 -0.0107 0.0606  0.0203  298 VAL E CG2 
14165 N N   . PHE E 299 ? 0.6916 0.3481 0.8740 -0.0872 0.1343  0.1066  299 PHE E N   
14166 C CA  . PHE E 299 ? 0.7324 0.3979 0.8845 -0.1107 0.1715  0.1140  299 PHE E CA  
14167 C C   . PHE E 299 ? 0.8187 0.4383 0.9483 -0.1419 0.1849  0.1440  299 PHE E C   
14168 O O   . PHE E 299 ? 0.8448 0.4855 0.9958 -0.1589 0.2089  0.1365  299 PHE E O   
14169 C CB  . PHE E 299 ? 0.7747 0.4502 0.8625 -0.1068 0.1771  0.1199  299 PHE E CB  
14170 C CG  . PHE E 299 ? 0.8001 0.4951 0.8656 -0.1257 0.2177  0.1162  299 PHE E CG  
14171 C CD1 . PHE E 299 ? 0.7165 0.4645 0.8223 -0.1159 0.2324  0.0856  299 PHE E CD1 
14172 C CD2 . PHE E 299 ? 0.8904 0.5548 0.8960 -0.1524 0.2374  0.1406  299 PHE E CD2 
14173 C CE1 . PHE E 299 ? 0.7170 0.4846 0.8148 -0.1312 0.2695  0.0781  299 PHE E CE1 
14174 C CE2 . PHE E 299 ? 0.8762 0.5722 0.8671 -0.1641 0.2702  0.1281  299 PHE E CE2 
14175 C CZ  . PHE E 299 ? 0.7972 0.5439 0.8377 -0.1519 0.2860  0.0956  299 PHE E CZ  
14176 N N   . ALA E 300 ? 0.8763 0.4444 0.9625 -0.1456 0.1588  0.1744  300 ALA E N   
14177 C CA  . ALA E 300 ? 0.9666 0.4943 1.0138 -0.1748 0.1575  0.2055  300 ALA E CA  
14178 C C   . ALA E 300 ? 0.9910 0.5195 1.1001 -0.1847 0.1590  0.1970  300 ALA E C   
14179 O O   . ALA E 300 ? 0.9489 0.4696 1.0432 -0.2137 0.1765  0.2125  300 ALA E O   
14180 C CB  . ALA E 300 ? 1.0079 0.4759 1.0102 -0.1727 0.1167  0.2370  300 ALA E CB  
14181 N N   . ASN E 301 ? 0.9480 0.4905 1.1281 -0.1603 0.1402  0.1703  301 ASN E N   
14182 C CA  . ASN E 301 ? 0.9394 0.4867 1.1845 -0.1642 0.1363  0.1552  301 ASN E CA  
14183 C C   . ASN E 301 ? 0.8763 0.4739 1.1576 -0.1748 0.1708  0.1338  301 ASN E C   
14184 O O   . ASN E 301 ? 0.8177 0.4186 1.1444 -0.1856 0.1727  0.1270  301 ASN E O   
14185 C CB  . ASN E 301 ? 0.9252 0.4815 1.2317 -0.1323 0.1055  0.1259  301 ASN E CB  
14186 C CG  . ASN E 301 ? 0.9780 0.4885 1.2699 -0.1184 0.0670  0.1409  301 ASN E CG  
14187 O OD1 . ASN E 301 ? 1.0698 0.5314 1.3084 -0.1352 0.0584  0.1760  301 ASN E OD1 
14188 N ND2 . ASN E 301 ? 0.9178 0.4458 1.2558 -0.0874 0.0433  0.1118  301 ASN E ND2 
14189 N N   . ASN E 302 ? 0.8558 0.4933 1.1221 -0.1695 0.1951  0.1210  302 ASN E N   
14190 C CA  . ASN E 302 ? 0.8469 0.5337 1.1507 -0.1765 0.2247  0.0987  302 ASN E CA  
14191 C C   . ASN E 302 ? 0.9021 0.5949 1.1548 -0.2002 0.2591  0.1147  302 ASN E C   
14192 O O   . ASN E 302 ? 0.9034 0.6399 1.1758 -0.2010 0.2857  0.0947  302 ASN E O   
14193 C CB  . ASN E 302 ? 0.6477 0.3791 0.9846 -0.1522 0.2240  0.0661  302 ASN E CB  
14194 C CG  . ASN E 302 ? 0.6099 0.3471 1.0082 -0.1334 0.1948  0.0416  302 ASN E CG  
14195 O OD1 . ASN E 302 ? 0.5915 0.3539 1.0471 -0.1339 0.1938  0.0200  302 ASN E OD1 
14196 N ND2 . ASN E 302 ? 0.6375 0.3521 1.0236 -0.1153 0.1690  0.0427  302 ASN E ND2 
14197 N N   . MET E 303 ? 0.9501 0.5978 1.1396 -0.2195 0.2553  0.1499  303 MET E N   
14198 C CA  . MET E 303 ? 1.0088 0.6591 1.1406 -0.2429 0.2851  0.1664  303 MET E CA  
14199 C C   . MET E 303 ? 1.1329 0.7433 1.2412 -0.2736 0.2826  0.2006  303 MET E C   
14200 O O   . MET E 303 ? 1.1905 0.7570 1.3075 -0.2751 0.2497  0.2177  303 MET E O   
14201 C CB  . MET E 303 ? 1.0114 0.6492 1.0650 -0.2357 0.2818  0.1778  303 MET E CB  
14202 C CG  . MET E 303 ? 0.9369 0.6177 1.0050 -0.2120 0.2919  0.1460  303 MET E CG  
14203 S SD  . MET E 303 ? 1.4360 1.1659 1.5234 -0.2254 0.3378  0.1237  303 MET E SD  
14204 C CE  . MET E 303 ? 0.9482 0.6523 0.9288 -0.2456 0.3538  0.1496  303 MET E CE  
14205 N N   . PRO E 304 ? 1.1907 0.8144 1.2677 -0.2982 0.3165  0.2108  304 PRO E N   
14206 C CA  . PRO E 304 ? 1.2704 0.8539 1.3150 -0.3308 0.3136  0.2513  304 PRO E CA  
14207 C C   . PRO E 304 ? 1.3004 0.8272 1.2760 -0.3313 0.2775  0.2901  304 PRO E C   
14208 O O   . PRO E 304 ? 1.2976 0.8230 1.2089 -0.3248 0.2817  0.2970  304 PRO E O   
14209 C CB  . PRO E 304 ? 1.3159 0.9315 1.3342 -0.3513 0.3614  0.2498  304 PRO E CB  
14210 C CG  . PRO E 304 ? 1.2604 0.9173 1.2681 -0.3271 0.3802  0.2145  304 PRO E CG  
14211 C CD  . PRO E 304 ? 1.1703 0.8449 1.2474 -0.2973 0.3577  0.1850  304 PRO E CD  
14212 N N   . LYS E 305 ? 1.3248 0.8040 1.3211 -0.3360 0.2387  0.3110  305 LYS E N   
14213 C CA  . LYS E 305 ? 1.3581 0.7836 1.3197 -0.3270 0.1928  0.3423  305 LYS E CA  
14214 C C   . LYS E 305 ? 1.4596 0.8597 1.3607 -0.3386 0.1997  0.3896  305 LYS E C   
14215 O O   . LYS E 305 ? 1.4995 0.8698 1.3625 -0.3173 0.1811  0.4033  305 LYS E O   
14216 C CB  . LYS E 305 ? 1.3733 0.7440 1.3646 -0.3318 0.1526  0.3435  305 LYS E CB  
14217 C CG  . LYS E 305 ? 1.3847 0.7657 1.4190 -0.3558 0.1761  0.3355  305 LYS E CG  
14218 C CD  . LYS E 305 ? 1.4297 0.7398 1.4715 -0.3593 0.1493  0.3332  305 LYS E CD  
14219 C CE  . LYS E 305 ? 1.4225 0.7601 1.5343 -0.3768 0.1705  0.3216  305 LYS E CE  
14220 N NZ  . LYS E 305 ? 1.4939 0.8402 1.5736 -0.4219 0.1945  0.3594  305 LYS E NZ  
14221 N N   . GLN E 306 ? 1.5291 0.9365 1.4104 -0.3695 0.2343  0.4070  306 GLN E N   
14222 C CA  . GLN E 306 ? 1.6377 1.0104 1.4375 -0.3845 0.2493  0.4462  306 GLN E CA  
14223 C C   . GLN E 306 ? 1.6556 1.0591 1.3752 -0.3931 0.2880  0.4313  306 GLN E C   
14224 O O   . GLN E 306 ? 1.7440 1.1340 1.4038 -0.4181 0.3135  0.4535  306 GLN E O   
14225 C CB  . GLN E 306 ? 1.6738 1.0214 1.4898 -0.4164 0.2632  0.4825  306 GLN E CB  
14226 C CG  . GLN E 306 ? 1.6495 1.0415 1.5278 -0.4423 0.2876  0.4667  306 GLN E CG  
14227 C CD  . GLN E 306 ? 1.5747 0.9735 1.5354 -0.4341 0.2547  0.4402  306 GLN E CD  
14228 O OE1 . GLN E 306 ? 1.5475 0.9153 1.5266 -0.4105 0.2101  0.4400  306 GLN E OE1 
14229 N NE2 . GLN E 306 ? 1.5528 0.9867 1.5584 -0.4507 0.2791  0.4107  306 GLN E NE2 
14230 N N   . ALA E 307 ? 1.5821 1.0273 1.3063 -0.3733 0.2962  0.3906  307 ALA E N   
14231 C CA  . ALA E 307 ? 1.6100 1.0805 1.2660 -0.3759 0.3300  0.3717  307 ALA E CA  
14232 C C   . ALA E 307 ? 1.6002 1.0477 1.1965 -0.3525 0.2985  0.3718  307 ALA E C   
14233 O O   . ALA E 307 ? 1.6135 1.0732 1.1472 -0.3505 0.3150  0.3557  307 ALA E O   
14234 C CB  . ALA E 307 ? 1.5366 1.0708 1.2481 -0.3689 0.3657  0.3235  307 ALA E CB  
14235 N N   . GLN E 308 ? 1.5705 0.9854 1.1941 -0.3334 0.2522  0.3861  308 GLN E N   
14236 C CA  . GLN E 308 ? 1.5581 0.9542 1.1410 -0.3088 0.2178  0.3838  308 GLN E CA  
14237 C C   . GLN E 308 ? 1.6850 1.0365 1.1635 -0.3191 0.2045  0.4109  308 GLN E C   
14238 O O   . GLN E 308 ? 1.7609 1.0760 1.2038 -0.3416 0.2071  0.4428  308 GLN E O   
14239 C CB  . GLN E 308 ? 1.4949 0.8683 1.1444 -0.2849 0.1746  0.3883  308 GLN E CB  
14240 C CG  . GLN E 308 ? 1.3960 0.8095 1.1407 -0.2789 0.1850  0.3596  308 GLN E CG  
14241 C CD  . GLN E 308 ? 1.3331 0.7269 1.1451 -0.2537 0.1455  0.3557  308 GLN E CD  
14242 O OE1 . GLN E 308 ? 1.3634 0.7154 1.1542 -0.2354 0.1141  0.3696  308 GLN E OE1 
14243 N NE2 . GLN E 308 ? 1.2449 0.6646 1.1283 -0.2519 0.1465  0.3282  308 GLN E NE2 
14244 N N   . VAL E 309 ? 1.7164 1.0692 1.1464 -0.3029 0.1875  0.3973  309 VAL E N   
14245 C CA  . VAL E 309 ? 1.8209 1.1330 1.1513 -0.3099 0.1663  0.4163  309 VAL E CA  
14246 C C   . VAL E 309 ? 1.7695 1.0613 1.1080 -0.2811 0.1108  0.4170  309 VAL E C   
14247 O O   . VAL E 309 ? 1.6449 0.9665 1.0489 -0.2564 0.1023  0.3939  309 VAL E O   
14248 C CB  . VAL E 309 ? 1.6608 0.9990 0.9222 -0.3209 0.2027  0.3922  309 VAL E CB  
14249 C CG1 . VAL E 309 ? 1.7398 1.0379 0.9015 -0.3239 0.1734  0.4042  309 VAL E CG1 
14250 C CG2 . VAL E 309 ? 1.7038 1.0605 0.9561 -0.3505 0.2576  0.3912  309 VAL E CG2 
14251 N N   . LYS E 310 ? 1.8494 1.0909 1.1245 -0.2849 0.0719  0.4430  310 LYS E N   
14252 C CA  . LYS E 310 ? 1.8166 1.0421 1.0981 -0.2591 0.0172  0.4417  310 LYS E CA  
14253 C C   . LYS E 310 ? 1.7551 1.0214 1.0278 -0.2449 0.0269  0.4090  310 LYS E C   
14254 O O   . LYS E 310 ? 1.7923 1.0690 0.9990 -0.2603 0.0561  0.3981  310 LYS E O   
14255 C CB  . LYS E 310 ? 1.9264 1.0936 1.1344 -0.2697 -0.0261 0.4725  310 LYS E CB  
14256 C CG  . LYS E 310 ? 2.2416 1.3646 1.4580 -0.2858 -0.0347 0.5066  310 LYS E CG  
14257 C CD  . LYS E 310 ? 2.0040 1.1153 1.3160 -0.2617 -0.0724 0.5090  310 LYS E CD  
14258 C CE  . LYS E 310 ? 1.9645 1.0717 1.3020 -0.2325 -0.1301 0.4997  310 LYS E CE  
14259 N NZ  . LYS E 310 ? 1.9461 1.0286 1.3589 -0.2162 -0.1712 0.5076  310 LYS E NZ  
14260 N N   . ALA E 311 ? 1.6585 0.9474 1.0010 -0.2159 0.0046  0.3917  311 ALA E N   
14261 C CA  . ALA E 311 ? 1.5775 0.9063 0.9272 -0.2002 0.0124  0.3610  311 ALA E CA  
14262 C C   . ALA E 311 ? 1.6347 0.9510 0.9015 -0.2048 -0.0021 0.3581  311 ALA E C   
14263 O O   . ALA E 311 ? 1.7043 0.9801 0.9278 -0.2079 -0.0426 0.3788  311 ALA E O   
14264 C CB  . ALA E 311 ? 1.4930 0.8369 0.9240 -0.1693 -0.0198 0.3503  311 ALA E CB  
14265 N N   . VAL E 312 ? 1.6103 0.9607 0.8596 -0.2048 0.0296  0.3302  312 VAL E N   
14266 C CA  . VAL E 312 ? 1.6634 1.0031 0.8336 -0.2113 0.0237  0.3216  312 VAL E CA  
14267 C C   . VAL E 312 ? 1.5722 0.9464 0.7722 -0.1897 0.0189  0.2930  312 VAL E C   
14268 O O   . VAL E 312 ? 1.5081 0.9209 0.7740 -0.1769 0.0405  0.2747  312 VAL E O   
14269 C CB  . VAL E 312 ? 1.5552 0.8967 0.6588 -0.2383 0.0744  0.3129  312 VAL E CB  
14270 C CG1 . VAL E 312 ? 1.6524 0.9587 0.7208 -0.2628 0.0809  0.3439  312 VAL E CG1 
14271 C CG2 . VAL E 312 ? 1.4727 0.8665 0.6285 -0.2357 0.1270  0.2821  312 VAL E CG2 
14272 N N   . GLY E 313 ? 1.4744 1.1015 0.7721 -0.3212 0.0068  0.2167  313 GLY E N   
14273 C CA  . GLY E 313 ? 1.4115 1.0351 0.7166 -0.3104 -0.0005 0.1699  313 GLY E CA  
14274 C C   . GLY E 313 ? 1.3085 0.9523 0.7281 -0.2852 -0.0381 0.1815  313 GLY E C   
14275 O O   . GLY E 313 ? 1.2965 0.9506 0.7522 -0.2835 -0.0763 0.2275  313 GLY E O   
14276 N N   . PRO E 314 ? 1.2310 0.8789 0.7082 -0.2628 -0.0243 0.1405  314 PRO E N   
14277 C CA  . PRO E 314 ? 1.1380 0.8071 0.7213 -0.2367 -0.0481 0.1412  314 PRO E CA  
14278 C C   . PRO E 314 ? 1.0598 0.7388 0.7361 -0.2094 -0.0289 0.1504  314 PRO E C   
14279 O O   . PRO E 314 ? 0.9849 0.6781 0.7444 -0.1859 -0.0445 0.1514  314 PRO E O   
14280 C CB  . PRO E 314 ? 1.1308 0.7892 0.7098 -0.2313 -0.0331 0.0916  314 PRO E CB  
14281 C CG  . PRO E 314 ? 1.1872 0.8219 0.7041 -0.2337 0.0182  0.0616  314 PRO E CG  
14282 C CD  . PRO E 314 ? 1.2536 0.8810 0.6840 -0.2611 0.0190  0.0889  314 PRO E CD  
14283 N N   . PHE E 315 ? 1.0782 0.7503 0.7368 -0.2156 0.0052  0.1571  315 PHE E N   
14284 C CA  . PHE E 315 ? 1.0171 0.6959 0.7553 -0.1977 0.0261  0.1586  315 PHE E CA  
14285 C C   . PHE E 315 ? 1.0198 0.6870 0.7933 -0.1975 0.0014  0.2041  315 PHE E C   
14286 O O   . PHE E 315 ? 1.0810 0.7367 0.8075 -0.2136 -0.0247 0.2420  315 PHE E O   
14287 C CB  . PHE E 315 ? 1.0480 0.7341 0.7627 -0.2067 0.0766  0.1437  315 PHE E CB  
14288 C CG  . PHE E 315 ? 1.0488 0.7379 0.7309 -0.1994 0.1051  0.0983  315 PHE E CG  
14289 C CD1 . PHE E 315 ? 0.9913 0.6859 0.7317 -0.1734 0.1068  0.0657  315 PHE E CD1 
14290 C CD2 . PHE E 315 ? 1.1375 0.8165 0.7236 -0.2175 0.1297  0.0878  315 PHE E CD2 
14291 C CE1 . PHE E 315 ? 1.0383 0.7241 0.7480 -0.1638 0.1312  0.0258  315 PHE E CE1 
14292 C CE2 . PHE E 315 ? 1.1726 0.8412 0.7252 -0.2062 0.1573  0.0424  315 PHE E CE2 
14293 C CZ  . PHE E 315 ? 1.1332 0.8026 0.7504 -0.1784 0.1568  0.0127  315 PHE E CZ  
14294 N N   . GLY E 316 ? 0.9786 0.6435 0.8318 -0.1787 0.0073  0.1997  316 GLY E N   
14295 C CA  . GLY E 316 ? 1.0300 0.6684 0.9217 -0.1740 -0.0133 0.2361  316 GLY E CA  
14296 C C   . GLY E 316 ? 1.0831 0.7063 0.9817 -0.1933 0.0127  0.2502  316 GLY E C   
14297 O O   . GLY E 316 ? 1.1404 0.7273 1.0474 -0.2000 -0.0028 0.2875  316 GLY E O   
14298 N N   . LEU E 317 ? 1.0581 0.7094 0.9593 -0.2018 0.0517  0.2217  317 LEU E N   
14299 C CA  . LEU E 317 ? 1.0763 0.7304 0.9955 -0.2245 0.0787  0.2340  317 LEU E CA  
14300 C C   . LEU E 317 ? 1.1395 0.8353 1.0173 -0.2433 0.1243  0.2222  317 LEU E C   
14301 O O   . LEU E 317 ? 1.1071 0.8376 1.0053 -0.2272 0.1484  0.1830  317 LEU E O   
14302 C CB  . LEU E 317 ? 0.9863 0.6420 0.9884 -0.2104 0.0796  0.2109  317 LEU E CB  
14303 C CG  . LEU E 317 ? 0.9922 0.6564 1.0275 -0.2385 0.1013  0.2221  317 LEU E CG  
14304 C CD1 . LEU E 317 ? 1.0494 0.6647 1.0602 -0.2676 0.0883  0.2721  317 LEU E CD1 
14305 C CD2 . LEU E 317 ? 0.9463 0.6124 1.0554 -0.2250 0.0946  0.1937  317 LEU E CD2 
14306 N N   . CYS E 318 ? 1.2276 0.9187 1.0461 -0.2753 0.1377  0.2576  318 CYS E N   
14307 C CA  . CYS E 318 ? 1.2533 0.9853 1.0245 -0.2927 0.1872  0.2484  318 CYS E CA  
14308 C C   . CYS E 318 ? 1.3008 1.0530 1.0928 -0.3266 0.2164  0.2792  318 CYS E C   
14309 O O   . CYS E 318 ? 1.3403 1.0551 1.1489 -0.3464 0.1924  0.3185  318 CYS E O   
14310 C CB  . CYS E 318 ? 1.3272 1.0437 0.9861 -0.3056 0.1848  0.2589  318 CYS E CB  
14311 S SG  . CYS E 318 ? 1.1782 0.8819 0.8059 -0.2766 0.1582  0.2176  318 CYS E SG  
14312 N N   . TYR E 319 ? 1.2971 1.1083 1.0916 -0.3327 0.2693  0.2615  319 TYR E N   
14313 C CA  . TYR E 319 ? 1.3088 1.1606 1.1346 -0.3679 0.3046  0.2891  319 TYR E CA  
14314 C C   . TYR E 319 ? 1.3972 1.2860 1.1431 -0.3915 0.3575  0.3009  319 TYR E C   
14315 O O   . TYR E 319 ? 1.4418 1.3238 1.1044 -0.3775 0.3705  0.2790  319 TYR E O   
14316 C CB  . TYR E 319 ? 1.2301 1.1413 1.1675 -0.3560 0.3227  0.2626  319 TYR E CB  
14317 C CG  . TYR E 319 ? 1.1842 1.0600 1.1989 -0.3498 0.2761  0.2613  319 TYR E CG  
14318 C CD1 . TYR E 319 ? 1.1346 0.9543 1.1431 -0.3184 0.2318  0.2441  319 TYR E CD1 
14319 C CD2 . TYR E 319 ? 1.1904 1.0891 1.2803 -0.3792 0.2776  0.2776  319 TYR E CD2 
14320 C CE1 . TYR E 319 ? 1.0983 0.8833 1.1675 -0.3111 0.1955  0.2397  319 TYR E CE1 
14321 C CE2 . TYR E 319 ? 1.1714 1.0271 1.3168 -0.3761 0.2358  0.2721  319 TYR E CE2 
14322 C CZ  . TYR E 319 ? 1.1427 0.9401 1.2743 -0.3393 0.1973  0.2514  319 TYR E CZ  
14323 O OH  . TYR E 319 ? 1.1404 0.8936 1.3138 -0.3313 0.1600  0.2394  319 TYR E OH  
14324 N N   . ASP E 320 ? 1.4279 1.3576 1.2110 -0.4153 0.3766  0.3319  320 ASP E N   
14325 C CA  . ASP E 320 ? 1.4936 1.4725 1.2300 -0.4304 0.4233  0.3481  320 ASP E CA  
14326 C C   . ASP E 320 ? 1.4719 1.5344 1.2203 -0.4089 0.4860  0.3082  320 ASP E C   
14327 O O   . ASP E 320 ? 1.3551 1.4422 1.1594 -0.3805 0.4964  0.2667  320 ASP E O   
14328 C CB  . ASP E 320 ? 1.3909 1.3809 1.1894 -0.4602 0.4202  0.3924  320 ASP E CB  
14329 C CG  . ASP E 320 ? 1.4775 1.5287 1.2552 -0.4790 0.4736  0.4139  320 ASP E CG  
14330 O OD1 . ASP E 320 ? 1.5321 1.6100 1.2306 -0.4693 0.5100  0.4000  320 ASP E OD1 
14331 O OD2 . ASP E 320 ? 1.5016 1.5682 1.3400 -0.5047 0.4798  0.4431  320 ASP E OD2 
14332 N N   . SER E 321 ? 1.6020 1.7011 1.2913 -0.4167 0.5282  0.3193  321 SER E N   
14333 C CA  . SER E 321 ? 1.6043 1.7789 1.2977 -0.3886 0.5889  0.2821  321 SER E CA  
14334 C C   . SER E 321 ? 1.5269 1.7952 1.3595 -0.3846 0.6104  0.2860  321 SER E C   
14335 O O   . SER E 321 ? 1.4931 1.8205 1.3788 -0.3485 0.6395  0.2464  321 SER E O   
14336 C CB  . SER E 321 ? 1.7078 1.8982 1.3029 -0.3986 0.6282  0.2966  321 SER E CB  
14337 O OG  . SER E 321 ? 1.7104 1.9841 1.3287 -0.3675 0.6897  0.2646  321 SER E OG  
14338 N N   . ARG E 322 ? 1.5055 1.7801 1.3925 -0.4213 0.5934  0.3351  322 ARG E N   
14339 C CA  . ARG E 322 ? 1.4219 1.7705 1.4457 -0.4299 0.5975  0.3487  322 ARG E CA  
14340 C C   . ARG E 322 ? 1.3019 1.6990 1.3922 -0.3902 0.5974  0.2978  322 ARG E C   
14341 O O   . ARG E 322 ? 1.2229 1.5586 1.3219 -0.3809 0.5557  0.2760  322 ARG E O   
14342 C CB  . ARG E 322 ? 1.3475 1.6190 1.4038 -0.4657 0.5446  0.3822  322 ARG E CB  
14343 C CG  . ARG E 322 ? 1.2545 1.5332 1.4245 -0.4668 0.5111  0.3715  322 ARG E CG  
14344 C CD  . ARG E 322 ? 1.2383 1.6274 1.5158 -0.4651 0.5495  0.3680  322 ARG E CD  
14345 N NE  . ARG E 322 ? 1.1369 1.5603 1.5046 -0.4474 0.5143  0.3404  322 ARG E NE  
14346 C CZ  . ARG E 322 ? 1.1025 1.6610 1.5450 -0.4427 0.5187  0.3323  322 ARG E CZ  
14347 N NH1 . ARG E 322 ? 1.0371 1.6087 1.5149 -0.4537 0.4963  0.2717  322 ARG E NH1 
14348 N NH2 . ARG E 322 ? 1.1783 1.7606 1.6506 -0.4306 0.6022  0.3292  322 ARG E NH2 
14349 N N   . LYS E 323 ? 1.3047 1.8032 1.4324 -0.3623 0.6475  0.2777  323 LYS E N   
14350 C CA  . LYS E 323 ? 1.2339 1.7687 1.4027 -0.3096 0.6618  0.2217  323 LYS E CA  
14351 C C   . LYS E 323 ? 1.1315 1.6081 1.3461 -0.2960 0.6132  0.1978  323 LYS E C   
14352 O O   . LYS E 323 ? 1.1142 1.5079 1.2614 -0.2700 0.6050  0.1666  323 LYS E O   
14353 C CB  . LYS E 323 ? 1.2275 1.9036 1.4960 -0.2965 0.6984  0.2216  323 LYS E CB  
14354 C CG  . LYS E 323 ? 1.1832 1.9327 1.5625 -0.3417 0.6701  0.2572  323 LYS E CG  
14355 C CD  . LYS E 323 ? 1.1985 2.0850 1.6580 -0.3423 0.7027  0.2494  323 LYS E CD  
14356 C CE  . LYS E 323 ? 1.1334 2.0568 1.7036 -0.3668 0.6693  0.2304  323 LYS E CE  
14357 N NZ  . LYS E 323 ? 1.1945 2.0625 1.7772 -0.4445 0.6678  0.2399  323 LYS E NZ  
14358 N N   . ILE E 324 ? 1.0764 1.5882 1.3905 -0.3218 0.5785  0.2176  324 ILE E N   
14359 C CA  . ILE E 324 ? 0.9964 1.4576 1.3641 -0.3207 0.5246  0.2066  324 ILE E CA  
14360 C C   . ILE E 324 ? 1.1355 1.6789 1.6264 -0.3039 0.5103  0.1912  324 ILE E C   
14361 O O   . ILE E 324 ? 1.0682 1.5750 1.6020 -0.3097 0.4623  0.1872  324 ILE E O   
14362 C CB  . ILE E 324 ? 0.9777 1.3350 1.2773 -0.2882 0.5109  0.1754  324 ILE E CB  
14363 C CG1 . ILE E 324 ? 1.0524 1.3134 1.2724 -0.3281 0.4780  0.2057  324 ILE E CG1 
14364 C CG2 . ILE E 324 ? 0.8693 1.2035 1.2334 -0.2610 0.4731  0.1503  324 ILE E CG2 
14365 C CD1 . ILE E 324 ? 1.0686 1.3214 1.3454 -0.3708 0.4326  0.2400  324 ILE E CD1 
14366 N N   . SER E 325 ? 1.1664 1.8231 1.7144 -0.2892 0.5462  0.1862  325 SER E N   
14367 C CA  . SER E 325 ? 1.1365 1.8728 1.7989 -0.2808 0.5249  0.1771  325 SER E CA  
14368 C C   . SER E 325 ? 1.1703 1.9159 1.8725 -0.3501 0.4884  0.2034  325 SER E C   
14369 O O   . SER E 325 ? 1.1901 2.0254 1.9681 -0.3709 0.4960  0.2043  325 SER E O   
14370 C CB  . SER E 325 ? 1.1667 2.0232 1.8832 -0.2482 0.5714  0.1632  325 SER E CB  
14371 O OG  . SER E 325 ? 1.2325 2.1702 1.9764 -0.3021 0.5942  0.1850  325 SER E OG  
14372 N N   . GLY E 326 ? 1.1906 1.8292 1.8373 -0.3844 0.4506  0.2183  326 GLY E N   
14373 C CA  . GLY E 326 ? 1.2186 1.8208 1.8841 -0.4433 0.4131  0.2306  326 GLY E CA  
14374 C C   . GLY E 326 ? 1.1564 1.6793 1.8287 -0.4338 0.3522  0.2186  326 GLY E C   
14375 O O   . GLY E 326 ? 1.1677 1.6804 1.8772 -0.4662 0.3185  0.2170  326 GLY E O   
14376 N N   . GLY E 327 ? 1.0981 1.5593 1.7355 -0.3886 0.3413  0.2040  327 GLY E N   
14377 C CA  . GLY E 327 ? 1.0672 1.4652 1.7188 -0.3772 0.2887  0.1858  327 GLY E CA  
14378 C C   . GLY E 327 ? 1.0530 1.3794 1.6711 -0.3298 0.2797  0.1620  327 GLY E C   
14379 O O   . GLY E 327 ? 1.1019 1.3504 1.7030 -0.3318 0.2354  0.1523  327 GLY E O   
14380 N N   . ALA E 328 ? 0.9900 1.3357 1.5903 -0.2889 0.3223  0.1481  328 ALA E N   
14381 C CA  . ALA E 328 ? 0.8870 1.1645 1.4391 -0.2415 0.3072  0.1167  328 ALA E CA  
14382 C C   . ALA E 328 ? 0.7804 1.0658 1.3900 -0.2214 0.2680  0.0964  328 ALA E C   
14383 O O   . ALA E 328 ? 0.7421 1.1085 1.4219 -0.1989 0.2791  0.0882  328 ALA E O   
14384 C CB  . ALA E 328 ? 0.8778 1.1783 1.3947 -0.1991 0.3520  0.0974  328 ALA E CB  
14385 N N   . PRO E 329 ? 0.7329 0.9355 1.3121 -0.2286 0.2222  0.0901  329 PRO E N   
14386 C CA  . PRO E 329 ? 0.6838 0.8903 1.3083 -0.2205 0.1828  0.0737  329 PRO E CA  
14387 C C   . PRO E 329 ? 0.6482 0.8480 1.2648 -0.1680 0.1742  0.0453  329 PRO E C   
14388 O O   . PRO E 329 ? 0.6107 0.7839 1.1786 -0.1335 0.1930  0.0321  329 PRO E O   
14389 C CB  . PRO E 329 ? 0.6874 0.7984 1.2701 -0.2460 0.1445  0.0756  329 PRO E CB  
14390 C CG  . PRO E 329 ? 0.7185 0.7664 1.2270 -0.2423 0.1580  0.0847  329 PRO E CG  
14391 C CD  . PRO E 329 ? 0.7434 0.8498 1.2496 -0.2473 0.2048  0.1012  329 PRO E CD  
14392 N N   . SER E 330 ? 0.6620 0.8825 1.3249 -0.1690 0.1408  0.0377  330 SER E N   
14393 C CA  . SER E 330 ? 0.6422 0.8417 1.2950 -0.1321 0.1174  0.0157  330 SER E CA  
14394 C C   . SER E 330 ? 0.6311 0.7371 1.2027 -0.1141 0.1093  0.0010  330 SER E C   
14395 O O   . SER E 330 ? 0.7154 0.7626 1.2543 -0.1370 0.0924  0.0034  330 SER E O   
14396 C CB  . SER E 330 ? 0.6514 0.8584 1.3388 -0.1570 0.0731  0.0135  330 SER E CB  
14397 O OG  . SER E 330 ? 0.6334 0.8029 1.2929 -0.1308 0.0450  -0.0060 330 SER E OG  
14398 N N   . VAL E 331 ? 0.5224 0.6143 1.0645 -0.0746 0.1217  -0.0127 331 VAL E N   
14399 C CA  . VAL E 331 ? 0.4704 0.4873 0.9507 -0.0604 0.1054  -0.0261 331 VAL E CA  
14400 C C   . VAL E 331 ? 0.4395 0.4584 0.9242 -0.0286 0.0914  -0.0404 331 VAL E C   
14401 O O   . VAL E 331 ? 0.4464 0.4804 0.9327 0.0002  0.1096  -0.0453 331 VAL E O   
14402 C CB  . VAL E 331 ? 0.4667 0.4443 0.8874 -0.0532 0.1276  -0.0259 331 VAL E CB  
14403 C CG1 . VAL E 331 ? 0.4058 0.3209 0.7769 -0.0410 0.1078  -0.0366 331 VAL E CG1 
14404 C CG2 . VAL E 331 ? 0.4956 0.4646 0.9025 -0.0845 0.1374  -0.0069 331 VAL E CG2 
14405 N N   . ASP E 332 ? 0.4128 0.4091 0.8929 -0.0341 0.0595  -0.0471 332 ASP E N   
14406 C CA  . ASP E 332 ? 0.3896 0.3884 0.8700 -0.0098 0.0425  -0.0555 332 ASP E CA  
14407 C C   . ASP E 332 ? 0.3712 0.3086 0.7968 -0.0060 0.0271  -0.0667 332 ASP E C   
14408 O O   . ASP E 332 ? 0.3579 0.2630 0.7650 -0.0248 0.0157  -0.0708 332 ASP E O   
14409 C CB  . ASP E 332 ? 0.4084 0.4579 0.9397 -0.0214 0.0167  -0.0510 332 ASP E CB  
14410 C CG  . ASP E 332 ? 0.4013 0.5299 1.0030 -0.0270 0.0318  -0.0364 332 ASP E CG  
14411 O OD1 . ASP E 332 ? 0.3841 0.5295 0.9922 -0.0059 0.0661  -0.0336 332 ASP E OD1 
14412 O OD2 . ASP E 332 ? 0.3972 0.5727 1.0468 -0.0537 0.0107  -0.0286 332 ASP E OD2 
14413 N N   . LEU E 333 ? 0.3814 0.3030 0.7836 0.0192  0.0281  -0.0710 333 LEU E N   
14414 C CA  . LEU E 333 ? 0.3723 0.2508 0.7301 0.0228  0.0153  -0.0789 333 LEU E CA  
14415 C C   . LEU E 333 ? 0.3885 0.2796 0.7505 0.0232  -0.0106 -0.0808 333 LEU E C   
14416 O O   . LEU E 333 ? 0.3936 0.3114 0.7757 0.0389  -0.0177 -0.0736 333 LEU E O   
14417 C CB  . LEU E 333 ? 0.4047 0.2589 0.7285 0.0409  0.0279  -0.0785 333 LEU E CB  
14418 C CG  . LEU E 333 ? 0.4094 0.2578 0.7171 0.0383  0.0504  -0.0759 333 LEU E CG  
14419 C CD1 . LEU E 333 ? 0.4574 0.2842 0.7100 0.0462  0.0537  -0.0739 333 LEU E CD1 
14420 C CD2 . LEU E 333 ? 0.3857 0.2240 0.6798 0.0186  0.0500  -0.0727 333 LEU E CD2 
14421 N N   . ILE E 334 ? 0.4520 0.3210 0.7914 0.0075  -0.0254 -0.0906 334 ILE E N   
14422 C CA  . ILE E 334 ? 0.4729 0.3469 0.7981 0.0049  -0.0510 -0.0947 334 ILE E CA  
14423 C C   . ILE E 334 ? 0.4631 0.3066 0.7400 0.0201  -0.0471 -0.0966 334 ILE E C   
14424 O O   . ILE E 334 ? 0.4643 0.2764 0.7122 0.0199  -0.0338 -0.1043 334 ILE E O   
14425 C CB  . ILE E 334 ? 0.4890 0.3455 0.8009 -0.0205 -0.0679 -0.1092 334 ILE E CB  
14426 C CG1 . ILE E 334 ? 0.4662 0.3385 0.8214 -0.0425 -0.0651 -0.1049 334 ILE E CG1 
14427 C CG2 . ILE E 334 ? 0.5169 0.3881 0.8135 -0.0282 -0.0991 -0.1124 334 ILE E CG2 
14428 C CD1 . ILE E 334 ? 0.4276 0.3678 0.8444 -0.0450 -0.0700 -0.0884 334 ILE E CD1 
14429 N N   . LEU E 335 ? 0.4699 0.3258 0.7423 0.0332  -0.0587 -0.0859 335 LEU E N   
14430 C CA  . LEU E 335 ? 0.4828 0.3095 0.7125 0.0445  -0.0517 -0.0813 335 LEU E CA  
14431 C C   . LEU E 335 ? 0.5691 0.3825 0.7489 0.0365  -0.0661 -0.0863 335 LEU E C   
14432 O O   . LEU E 335 ? 0.5918 0.4084 0.7611 0.0218  -0.0807 -0.0994 335 LEU E O   
14433 C CB  . LEU E 335 ? 0.4484 0.2790 0.6916 0.0654  -0.0524 -0.0639 335 LEU E CB  
14434 C CG  . LEU E 335 ? 0.4122 0.2516 0.6943 0.0762  -0.0320 -0.0633 335 LEU E CG  
14435 C CD1 . LEU E 335 ? 0.4246 0.2533 0.7127 0.1021  -0.0298 -0.0506 335 LEU E CD1 
14436 C CD2 . LEU E 335 ? 0.4118 0.2250 0.6701 0.0655  -0.0102 -0.0722 335 LEU E CD2 
14437 N N   . ASP E 336 ? 0.6387 0.4319 0.7818 0.0433  -0.0595 -0.0767 336 ASP E N   
14438 C CA  . ASP E 336 ? 0.7355 0.5157 0.8212 0.0361  -0.0648 -0.0783 336 ASP E CA  
14439 C C   . ASP E 336 ? 0.7974 0.5928 0.8673 0.0273  -0.0962 -0.0805 336 ASP E C   
14440 O O   . ASP E 336 ? 0.8157 0.6329 0.9087 0.0339  -0.1204 -0.0628 336 ASP E O   
14441 C CB  . ASP E 336 ? 0.7682 0.5312 0.8276 0.0427  -0.0606 -0.0560 336 ASP E CB  
14442 C CG  . ASP E 336 ? 0.8311 0.5834 0.8264 0.0324  -0.0587 -0.0532 336 ASP E CG  
14443 O OD1 . ASP E 336 ? 0.9108 0.6661 0.8716 0.0288  -0.0825 -0.0453 336 ASP E OD1 
14444 O OD2 . ASP E 336 ? 0.8230 0.5688 0.8024 0.0271  -0.0333 -0.0564 336 ASP E OD2 
14445 N N   . LYS E 337 ? 0.8406 0.6237 0.8716 0.0132  -0.0964 -0.1033 337 LYS E N   
14446 C CA  . LYS E 337 ? 0.9116 0.6989 0.9063 -0.0029 -0.1276 -0.1119 337 LYS E CA  
14447 C C   . LYS E 337 ? 0.8703 0.6913 0.9219 -0.0123 -0.1572 -0.1089 337 LYS E C   
14448 O O   . LYS E 337 ? 0.9078 0.7478 0.9448 -0.0262 -0.1936 -0.1050 337 LYS E O   
14449 C CB  . LYS E 337 ? 1.0004 0.7869 0.9382 -0.0026 -0.1437 -0.0924 337 LYS E CB  
14450 C CG  . LYS E 337 ? 1.0662 0.8245 0.9324 -0.0055 -0.1154 -0.1044 337 LYS E CG  
14451 C CD  . LYS E 337 ? 1.1825 0.9361 0.9748 -0.0122 -0.1296 -0.0858 337 LYS E CD  
14452 C CE  . LYS E 337 ? 1.2224 0.9916 1.0390 -0.0039 -0.1612 -0.0471 337 LYS E CE  
14453 N NZ  . LYS E 337 ? 1.3183 1.0898 1.0644 -0.0178 -0.1977 -0.0347 337 LYS E NZ  
14454 N N   . ASN E 338 ? 0.8115 0.6446 0.9275 -0.0070 -0.1415 -0.1085 338 ASN E N   
14455 C CA  . ASN E 338 ? 0.8092 0.6846 0.9922 -0.0159 -0.1598 -0.1019 338 ASN E CA  
14456 C C   . ASN E 338 ? 0.8439 0.7684 1.0630 -0.0033 -0.1863 -0.0739 338 ASN E C   
14457 O O   . ASN E 338 ? 0.8666 0.8416 1.1399 -0.0141 -0.2105 -0.0662 338 ASN E O   
14458 C CB  . ASN E 338 ? 0.8712 0.7391 1.0384 -0.0488 -0.1829 -0.1236 338 ASN E CB  
14459 C CG  . ASN E 338 ? 0.8902 0.6965 1.0097 -0.0561 -0.1600 -0.1535 338 ASN E CG  
14460 O OD1 . ASN E 338 ? 0.8639 0.6518 0.9980 -0.0415 -0.1279 -0.1546 338 ASN E OD1 
14461 N ND2 . ASN E 338 ? 0.9420 0.7155 1.0050 -0.0786 -0.1784 -0.1782 338 ASN E ND2 
14462 N N   . ASP E 339 ? 0.8493 0.7611 1.0446 0.0197  -0.1823 -0.0558 339 ASP E N   
14463 C CA  . ASP E 339 ? 0.8693 0.8184 1.0964 0.0383  -0.2091 -0.0259 339 ASP E CA  
14464 C C   . ASP E 339 ? 0.7786 0.7615 1.0885 0.0640  -0.1929 -0.0133 339 ASP E C   
14465 O O   . ASP E 339 ? 0.7964 0.8283 1.1604 0.0816  -0.2143 0.0090  339 ASP E O   
14466 C CB  . ASP E 339 ? 0.9210 0.8319 1.0872 0.0526  -0.2109 -0.0081 339 ASP E CB  
14467 C CG  . ASP E 339 ? 1.0141 0.9063 1.0963 0.0289  -0.2323 -0.0145 339 ASP E CG  
14468 O OD1 . ASP E 339 ? 1.0860 1.0068 1.1646 0.0076  -0.2663 -0.0208 339 ASP E OD1 
14469 O OD2 . ASP E 339 ? 1.0245 0.8742 1.0415 0.0282  -0.2136 -0.0146 339 ASP E OD2 
14470 N N   . ALA E 340 ? 0.6702 0.6292 0.9890 0.0676  -0.1546 -0.0272 340 ALA E N   
14471 C CA  . ALA E 340 ? 0.5923 0.5718 0.9711 0.0929  -0.1319 -0.0195 340 ALA E CA  
14472 C C   . ALA E 340 ? 0.4994 0.4793 0.8966 0.0776  -0.1033 -0.0375 340 ALA E C   
14473 O O   . ALA E 340 ? 0.5084 0.4550 0.8654 0.0555  -0.0969 -0.0542 340 ALA E O   
14474 C CB  . ALA E 340 ? 0.6168 0.5463 0.9660 0.1199  -0.1145 -0.0107 340 ALA E CB  
14475 N N   . VAL E 341 ? 0.4387 0.4542 0.8945 0.0925  -0.0839 -0.0327 341 VAL E N   
14476 C CA  . VAL E 341 ? 0.4120 0.4326 0.8842 0.0758  -0.0579 -0.0442 341 VAL E CA  
14477 C C   . VAL E 341 ? 0.3732 0.3850 0.8567 0.1042  -0.0238 -0.0430 341 VAL E C   
14478 O O   . VAL E 341 ? 0.3880 0.4247 0.9072 0.1351  -0.0219 -0.0320 341 VAL E O   
14479 C CB  . VAL E 341 ? 0.4074 0.4959 0.9428 0.0518  -0.0703 -0.0397 341 VAL E CB  
14480 C CG1 . VAL E 341 ? 0.3829 0.4803 0.9399 0.0388  -0.0382 -0.0437 341 VAL E CG1 
14481 C CG2 . VAL E 341 ? 0.4597 0.5353 0.9657 0.0173  -0.1030 -0.0484 341 VAL E CG2 
14482 N N   . TRP E 342 ? 0.3992 0.3692 0.8462 0.0959  0.0015  -0.0547 342 TRP E N   
14483 C CA  . TRP E 342 ? 0.4113 0.3704 0.8589 0.1154  0.0350  -0.0582 342 TRP E CA  
14484 C C   . TRP E 342 ? 0.4050 0.3986 0.8796 0.0980  0.0576  -0.0601 342 TRP E C   
14485 O O   . TRP E 342 ? 0.4191 0.3843 0.8600 0.0743  0.0638  -0.0655 342 TRP E O   
14486 C CB  . TRP E 342 ? 0.4577 0.3464 0.8311 0.1135  0.0437  -0.0661 342 TRP E CB  
14487 C CG  . TRP E 342 ? 0.5217 0.3893 0.8609 0.1308  0.0660  -0.0681 342 TRP E CG  
14488 C CD1 . TRP E 342 ? 0.5839 0.4820 0.9586 0.1513  0.0899  -0.0701 342 TRP E CD1 
14489 C CD2 . TRP E 342 ? 0.5484 0.3589 0.8122 0.1300  0.0658  -0.0703 342 TRP E CD2 
14490 N NE1 . TRP E 342 ? 0.6206 0.4732 0.9381 0.1652  0.1042  -0.0776 342 TRP E NE1 
14491 C CE2 . TRP E 342 ? 0.5995 0.3964 0.8511 0.1506  0.0868  -0.0777 342 TRP E CE2 
14492 C CE3 . TRP E 342 ? 0.5630 0.3353 0.7730 0.1135  0.0508  -0.0674 342 TRP E CE3 
14493 C CZ2 . TRP E 342 ? 0.6494 0.3867 0.8355 0.1530  0.0871  -0.0848 342 TRP E CZ2 
14494 C CZ3 . TRP E 342 ? 0.6133 0.3352 0.7663 0.1141  0.0526  -0.0704 342 TRP E CZ3 
14495 C CH2 . TRP E 342 ? 0.6458 0.3464 0.7864 0.1326  0.0676  -0.0803 342 TRP E CH2 
14496 N N   . ARG E 343 ? 0.4164 0.4753 0.9547 0.1102  0.0702  -0.0522 343 ARG E N   
14497 C CA  . ARG E 343 ? 0.4416 0.5426 1.0090 0.0910  0.0951  -0.0494 343 ARG E CA  
14498 C C   . ARG E 343 ? 0.4431 0.5071 0.9653 0.1011  0.1336  -0.0598 343 ARG E C   
14499 O O   . ARG E 343 ? 0.4705 0.5122 0.9783 0.1348  0.1506  -0.0680 343 ARG E O   
14500 C CB  . ARG E 343 ? 0.4905 0.6860 1.1478 0.1016  0.0995  -0.0356 343 ARG E CB  
14501 C CG  . ARG E 343 ? 0.5638 0.8027 1.2637 0.0762  0.0568  -0.0244 343 ARG E CG  
14502 C CD  . ARG E 343 ? 0.6309 0.9501 1.4110 0.1030  0.0416  -0.0088 343 ARG E CD  
14503 N NE  . ARG E 343 ? 0.6744 1.0152 1.4691 0.0760  -0.0092 -0.0009 343 ARG E NE  
14504 C CZ  . ARG E 343 ? 0.7088 1.0576 1.5102 0.0963  -0.0439 0.0078  343 ARG E CZ  
14505 N NH1 . ARG E 343 ? 0.7158 1.0490 1.5167 0.1464  -0.0334 0.0123  343 ARG E NH1 
14506 N NH2 . ARG E 343 ? 0.7335 1.0984 1.5347 0.0648  -0.0907 0.0123  343 ARG E NH2 
14507 N N   . ILE E 344 ? 0.4426 0.4936 0.9365 0.0714  0.1458  -0.0592 344 ILE E N   
14508 C CA  . ILE E 344 ? 0.4741 0.4936 0.9172 0.0765  0.1798  -0.0681 344 ILE E CA  
14509 C C   . ILE E 344 ? 0.5388 0.6203 1.0173 0.0685  0.2147  -0.0597 344 ILE E C   
14510 O O   . ILE E 344 ? 0.5522 0.6684 1.0592 0.0349  0.2090  -0.0441 344 ILE E O   
14511 C CB  . ILE E 344 ? 0.4781 0.4365 0.8537 0.0513  0.1692  -0.0699 344 ILE E CB  
14512 C CG1 . ILE E 344 ? 0.4732 0.3825 0.8211 0.0579  0.1391  -0.0764 344 ILE E CG1 
14513 C CG2 . ILE E 344 ? 0.5439 0.4702 0.8595 0.0545  0.1993  -0.0794 344 ILE E CG2 
14514 C CD1 . ILE E 344 ? 0.4596 0.3223 0.7567 0.0363  0.1256  -0.0754 344 ILE E CD1 
14515 N N   . SER E 345 ? 0.5984 0.6895 1.0718 0.0989  0.2531  -0.0706 345 SER E N   
14516 C CA  . SER E 345 ? 0.6393 0.8012 1.1513 0.0983  0.2953  -0.0637 345 SER E CA  
14517 C C   . SER E 345 ? 0.6590 0.8037 1.1185 0.0566  0.3073  -0.0549 345 SER E C   
14518 O O   . SER E 345 ? 0.6693 0.7398 1.0457 0.0460  0.2998  -0.0631 345 SER E O   
14519 C CB  . SER E 345 ? 0.7243 0.8837 1.2250 0.1454  0.3394  -0.0834 345 SER E CB  
14520 O OG  . SER E 345 ? 0.7386 0.8769 1.2468 0.1814  0.3112  -0.0884 345 SER E OG  
14521 N N   . SER E 346 ? 0.6967 0.9147 1.2071 0.0322  0.3262  -0.0351 346 SER E N   
14522 C CA  . SER E 346 ? 0.7604 0.9654 1.2292 -0.0130 0.3325  -0.0177 346 SER E CA  
14523 C C   . SER E 346 ? 0.8429 1.0081 1.2200 -0.0123 0.3693  -0.0269 346 SER E C   
14524 O O   . SER E 346 ? 0.8668 1.0101 1.1958 -0.0491 0.3692  -0.0095 346 SER E O   
14525 C CB  . SER E 346 ? 0.7659 1.0619 1.3149 -0.0436 0.3455  0.0088  346 SER E CB  
14526 O OG  . SER E 346 ? 0.8006 1.1705 1.3808 -0.0236 0.4005  0.0074  346 SER E OG  
14527 N N   . GLU E 347 ? 0.8974 1.0480 1.2443 0.0277  0.3997  -0.0533 347 GLU E N   
14528 C CA  . GLU E 347 ? 0.9991 1.0931 1.2387 0.0232  0.4256  -0.0670 347 GLU E CA  
14529 C C   . GLU E 347 ? 1.0678 1.0752 1.2473 0.0483  0.4037  -0.0954 347 GLU E C   
14530 O O   . GLU E 347 ? 1.1496 1.0936 1.2312 0.0427  0.4119  -0.1113 347 GLU E O   
14531 C CB  . GLU E 347 ? 1.0277 1.1707 1.2579 0.0381  0.4917  -0.0755 347 GLU E CB  
14532 C CG  . GLU E 347 ? 1.0797 1.1580 1.1794 0.0197  0.5122  -0.0863 347 GLU E CG  
14533 C CD  . GLU E 347 ? 1.1480 1.2444 1.2039 0.0444  0.5813  -0.1099 347 GLU E CD  
14534 O OE1 . GLU E 347 ? 1.1523 1.3408 1.2716 0.0483  0.6073  -0.0945 347 GLU E OE1 
14535 O OE2 . GLU E 347 ? 1.2127 1.2298 1.1647 0.0566  0.5851  -0.1405 347 GLU E OE2 
14536 N N   . ASN E 348 ? 1.0399 1.0442 1.2744 0.0726  0.3747  -0.1006 348 ASN E N   
14537 C CA  . ASN E 348 ? 1.0559 0.9769 1.2356 0.0829  0.3455  -0.1185 348 ASN E CA  
14538 C C   . ASN E 348 ? 1.0187 0.9020 1.1454 0.0401  0.3126  -0.1036 348 ASN E C   
14539 O O   . ASN E 348 ? 1.1023 0.9211 1.1489 0.0313  0.3026  -0.1155 348 ASN E O   
14540 C CB  . ASN E 348 ? 1.0301 0.9556 1.2739 0.1085  0.3157  -0.1187 348 ASN E CB  
14541 C CG  . ASN E 348 ? 1.0597 0.8995 1.2455 0.1165  0.2902  -0.1348 348 ASN E CG  
14542 O OD1 . ASN E 348 ? 1.0567 0.8545 1.1934 0.0873  0.2632  -0.1310 348 ASN E OD1 
14543 N ND2 . ASN E 348 ? 1.0911 0.9120 1.2749 0.1502  0.2885  -0.1455 348 ASN E ND2 
14544 N N   . PHE E 349 ? 0.8818 0.8033 1.0553 0.0138  0.2934  -0.0772 349 PHE E N   
14545 C CA  . PHE E 349 ? 0.7915 0.6771 0.9250 -0.0194 0.2618  -0.0601 349 PHE E CA  
14546 C C   . PHE E 349 ? 0.8218 0.7128 0.9093 -0.0509 0.2790  -0.0403 349 PHE E C   
14547 O O   . PHE E 349 ? 0.8447 0.7013 0.8921 -0.0742 0.2526  -0.0240 349 PHE E O   
14548 C CB  . PHE E 349 ? 0.6995 0.5973 0.8950 -0.0282 0.2249  -0.0451 349 PHE E CB  
14549 C CG  . PHE E 349 ? 0.6568 0.6137 0.9216 -0.0429 0.2320  -0.0273 349 PHE E CG  
14550 C CD1 . PHE E 349 ? 0.6697 0.6357 0.9253 -0.0767 0.2387  -0.0027 349 PHE E CD1 
14551 C CD2 . PHE E 349 ? 0.6001 0.6018 0.9388 -0.0272 0.2264  -0.0318 349 PHE E CD2 
14552 C CE1 . PHE E 349 ? 0.6469 0.6644 0.9675 -0.0979 0.2426  0.0153  349 PHE E CE1 
14553 C CE2 . PHE E 349 ? 0.5808 0.6410 0.9864 -0.0476 0.2272  -0.0147 349 PHE E CE2 
14554 C CZ  . PHE E 349 ? 0.6093 0.6764 1.0066 -0.0849 0.2363  0.0081  349 PHE E CZ  
14555 N N   . MET E 350 ? 0.8249 0.7614 0.9180 -0.0514 0.3233  -0.0386 350 MET E N   
14556 C CA  . MET E 350 ? 0.8719 0.8082 0.9042 -0.0833 0.3428  -0.0189 350 MET E CA  
14557 C C   . MET E 350 ? 0.9491 0.8485 0.8823 -0.0763 0.3703  -0.0418 350 MET E C   
14558 O O   . MET E 350 ? 0.9465 0.8618 0.8783 -0.0481 0.4111  -0.0680 350 MET E O   
14559 C CB  . MET E 350 ? 0.8740 0.8857 0.9609 -0.0980 0.3794  0.0016  350 MET E CB  
14560 C CG  . MET E 350 ? 0.8309 0.8750 1.0033 -0.1201 0.3523  0.0286  350 MET E CG  
14561 S SD  . MET E 350 ? 0.9012 0.8782 1.0435 -0.1534 0.2985  0.0572  350 MET E SD  
14562 C CE  . MET E 350 ? 0.8476 0.8054 0.8932 -0.1871 0.3209  0.0845  350 MET E CE  
14563 N N   . VAL E 351 ? 1.0419 0.8914 0.8898 -0.1022 0.3479  -0.0316 351 VAL E N   
14564 C CA  . VAL E 351 ? 1.1741 0.9789 0.9117 -0.1034 0.3664  -0.0551 351 VAL E CA  
14565 C C   . VAL E 351 ? 1.2331 1.0479 0.8977 -0.1375 0.3894  -0.0309 351 VAL E C   
14566 O O   . VAL E 351 ? 1.2266 1.0595 0.9126 -0.1657 0.3716  0.0097  351 VAL E O   
14567 C CB  . VAL E 351 ? 1.3962 1.1343 1.0810 -0.1084 0.3181  -0.0660 351 VAL E CB  
14568 C CG1 . VAL E 351 ? 1.2819 1.0239 1.0544 -0.0954 0.2770  -0.0598 351 VAL E CG1 
14569 C CG2 . VAL E 351 ? 1.4659 1.1782 1.0685 -0.1472 0.2906  -0.0392 351 VAL E CG2 
14570 N N   . GLN E 352 ? 1.3138 1.1132 0.8894 -0.1343 0.4322  -0.0562 352 GLN E N   
14571 C CA  . GLN E 352 ? 1.4280 1.2385 0.9212 -0.1671 0.4610  -0.0348 352 GLN E CA  
14572 C C   . GLN E 352 ? 1.5287 1.2740 0.8924 -0.2000 0.4256  -0.0279 352 GLN E C   
14573 O O   . GLN E 352 ? 1.5358 1.2807 0.8774 -0.2348 0.3951  0.0171  352 GLN E O   
14574 C CB  . GLN E 352 ? 1.5187 1.3601 0.9875 -0.1444 0.5366  -0.0658 352 GLN E CB  
14575 C CG  . GLN E 352 ? 1.6689 1.5230 1.0406 -0.1764 0.5765  -0.0493 352 GLN E CG  
14576 C CD  . GLN E 352 ? 1.6776 1.6014 1.1179 -0.2066 0.5841  0.0046  352 GLN E CD  
14577 O OE1 . GLN E 352 ? 1.7466 1.6696 1.1175 -0.2456 0.5822  0.0401  352 GLN E OE1 
14578 N NE2 . GLN E 352 ? 1.6051 1.5878 1.1866 -0.1892 0.5829  0.0134  352 GLN E NE2 
14579 N N   . ALA E 353 ? 1.6210 1.3094 0.8977 -0.1902 0.4284  -0.0711 353 ALA E N   
14580 C CA  . ALA E 353 ? 1.7113 1.3377 0.8670 -0.2230 0.3863  -0.0699 353 ALA E CA  
14581 C C   . ALA E 353 ? 1.8092 1.4350 0.8491 -0.2626 0.4012  -0.0440 353 ALA E C   
14582 O O   . ALA E 353 ? 1.9017 1.4775 0.8212 -0.2912 0.3735  -0.0481 353 ALA E O   
14583 C CB  . ALA E 353 ? 1.6385 1.2577 0.8513 -0.2344 0.3125  -0.0390 353 ALA E CB  
14584 N N   . GLN E 354 ? 1.7911 1.4742 0.8649 -0.2676 0.4445  -0.0165 354 GLN E N   
14585 C CA  . GLN E 354 ? 1.8824 1.5754 0.8651 -0.3044 0.4576  0.0170  354 GLN E CA  
14586 C C   . GLN E 354 ? 1.9292 1.6889 0.9529 -0.2833 0.5268  0.0075  354 GLN E C   
14587 O O   . GLN E 354 ? 1.8785 1.6734 0.9910 -0.2458 0.5638  -0.0205 354 GLN E O   
14588 C CB  . GLN E 354 ? 1.8251 1.5281 0.8361 -0.3392 0.4114  0.0854  354 GLN E CB  
14589 C CG  . GLN E 354 ? 1.9173 1.5850 0.8163 -0.3742 0.3634  0.1155  354 GLN E CG  
14590 C CD  . GLN E 354 ? 1.8901 1.5586 0.8305 -0.3976 0.3093  0.1829  354 GLN E CD  
14591 O OE1 . GLN E 354 ? 1.8508 1.5523 0.8843 -0.3967 0.3228  0.2134  354 GLN E OE1 
14592 N NE2 . GLN E 354 ? 1.9203 1.5532 0.8004 -0.4164 0.2445  0.2064  354 GLN E NE2 
14593 N N   . ASP E 355 ? 2.0442 1.8221 0.9975 -0.3052 0.5419  0.0297  355 ASP E N   
14594 C CA  . ASP E 355 ? 2.0681 1.9229 1.0581 -0.2943 0.6046  0.0367  355 ASP E CA  
14595 C C   . ASP E 355 ? 1.9057 1.8385 1.0482 -0.2827 0.6289  0.0587  355 ASP E C   
14596 O O   . ASP E 355 ? 1.8409 1.8164 1.0620 -0.2421 0.6667  0.0246  355 ASP E O   
14597 C CB  . ASP E 355 ? 2.1964 2.0588 1.1020 -0.3338 0.6008  0.0830  355 ASP E CB  
14598 C CG  . ASP E 355 ? 2.1814 2.0188 1.0947 -0.3730 0.5384  0.1439  355 ASP E CG  
14599 O OD1 . ASP E 355 ? 2.0758 1.9261 1.0960 -0.3724 0.5189  0.1649  355 ASP E OD1 
14600 O OD2 . ASP E 355 ? 2.2780 2.0809 1.0923 -0.4019 0.5063  0.1704  355 ASP E OD2 
14601 N N   . GLY E 356 ? 1.8464 1.7959 1.0331 -0.3178 0.6016  0.1169  356 GLY E N   
14602 C CA  . GLY E 356 ? 1.7519 1.7716 1.0780 -0.3170 0.6162  0.1421  356 GLY E CA  
14603 C C   . GLY E 356 ? 1.6681 1.6551 1.0608 -0.3350 0.5608  0.1713  356 GLY E C   
14604 O O   . GLY E 356 ? 1.6239 1.6494 1.1072 -0.3526 0.5547  0.2088  356 GLY E O   
14605 N N   . VAL E 357 ? 1.6524 1.5672 1.0023 -0.3303 0.5188  0.1536  357 VAL E N   
14606 C CA  . VAL E 357 ? 1.5483 1.4342 0.9725 -0.3348 0.4601  0.1766  357 VAL E CA  
14607 C C   . VAL E 357 ? 1.4138 1.2982 0.9177 -0.2891 0.4449  0.1302  357 VAL E C   
14608 O O   . VAL E 357 ? 1.4169 1.2643 0.8664 -0.2670 0.4388  0.0905  357 VAL E O   
14609 C CB  . VAL E 357 ? 1.5970 1.4140 0.9421 -0.3562 0.3963  0.2065  357 VAL E CB  
14610 C CG1 . VAL E 357 ? 1.4781 1.2713 0.9181 -0.3425 0.3346  0.2193  357 VAL E CG1 
14611 C CG2 . VAL E 357 ? 1.7005 1.5175 0.9824 -0.3944 0.3951  0.2595  357 VAL E CG2 
14612 N N   . SER E 358 ? 1.3201 1.2392 0.9485 -0.2795 0.4348  0.1380  358 SER E N   
14613 C CA  . SER E 358 ? 1.2471 1.1726 0.9579 -0.2381 0.4222  0.0998  358 SER E CA  
14614 C C   . SER E 358 ? 1.2240 1.1106 0.9854 -0.2382 0.3567  0.1154  358 SER E C   
14615 O O   . SER E 358 ? 1.2416 1.1308 1.0474 -0.2617 0.3375  0.1521  358 SER E O   
14616 C CB  . SER E 358 ? 1.1727 1.1798 0.9859 -0.2240 0.4666  0.0920  358 SER E CB  
14617 O OG  . SER E 358 ? 1.0722 1.0889 0.9722 -0.1871 0.4484  0.0638  358 SER E OG  
14618 N N   . CYS E 359 ? 1.1883 1.0336 0.9348 -0.2141 0.3240  0.0883  359 CYS E N   
14619 C CA  . CYS E 359 ? 1.1109 0.9210 0.8945 -0.2109 0.2662  0.1010  359 CYS E CA  
14620 C C   . CYS E 359 ? 0.9733 0.7919 0.8413 -0.1783 0.2521  0.0723  359 CYS E C   
14621 O O   . CYS E 359 ? 0.9615 0.7945 0.8403 -0.1525 0.2752  0.0372  359 CYS E O   
14622 C CB  . CYS E 359 ? 1.1755 0.9361 0.8747 -0.2179 0.2303  0.1048  359 CYS E CB  
14623 S SG  . CYS E 359 ? 1.4904 1.2314 1.0916 -0.2601 0.2237  0.1538  359 CYS E SG  
14624 N N   . LEU E 360 ? 0.9104 0.7149 0.8337 -0.1791 0.2144  0.0890  360 LEU E N   
14625 C CA  . LEU E 360 ? 0.8448 0.6507 0.8355 -0.1524 0.1949  0.0662  360 LEU E CA  
14626 C C   . LEU E 360 ? 0.8604 0.6355 0.8129 -0.1356 0.1740  0.0452  360 LEU E C   
14627 O O   . LEU E 360 ? 0.8762 0.6226 0.7977 -0.1438 0.1421  0.0619  360 LEU E O   
14628 C CB  . LEU E 360 ? 0.8245 0.6141 0.8684 -0.1590 0.1629  0.0871  360 LEU E CB  
14629 C CG  . LEU E 360 ? 0.7632 0.5521 0.8664 -0.1343 0.1432  0.0640  360 LEU E CG  
14630 C CD1 . LEU E 360 ? 0.7221 0.5582 0.8764 -0.1238 0.1678  0.0432  360 LEU E CD1 
14631 C CD2 . LEU E 360 ? 0.7681 0.5267 0.9057 -0.1399 0.1136  0.0809  360 LEU E CD2 
14632 N N   . GLY E 361 ? 0.8762 0.6586 0.8356 -0.1125 0.1902  0.0116  361 GLY E N   
14633 C CA  . GLY E 361 ? 0.9132 0.6620 0.8256 -0.1032 0.1766  -0.0100 361 GLY E CA  
14634 C C   . GLY E 361 ? 0.8218 0.5579 0.7729 -0.0919 0.1401  -0.0126 361 GLY E C   
14635 O O   . GLY E 361 ? 0.8409 0.5643 0.7933 -0.0761 0.1385  -0.0364 361 GLY E O   
14636 N N   . PHE E 362 ? 0.7471 0.4834 0.7272 -0.0992 0.1130  0.0126  362 PHE E N   
14637 C CA  . PHE E 362 ? 0.6946 0.4239 0.7080 -0.0878 0.0825  0.0119  362 PHE E CA  
14638 C C   . PHE E 362 ? 0.7356 0.4540 0.7235 -0.1003 0.0527  0.0377  362 PHE E C   
14639 O O   . PHE E 362 ? 0.7938 0.5075 0.7683 -0.1137 0.0489  0.0650  362 PHE E O   
14640 C CB  . PHE E 362 ? 0.6429 0.3827 0.7251 -0.0760 0.0780  0.0142  362 PHE E CB  
14641 C CG  . PHE E 362 ? 0.6568 0.4169 0.7738 -0.0641 0.0987  -0.0064 362 PHE E CG  
14642 C CD1 . PHE E 362 ? 0.7137 0.4972 0.8380 -0.0716 0.1253  -0.0041 362 PHE E CD1 
14643 C CD2 . PHE E 362 ? 0.6507 0.4130 0.7966 -0.0457 0.0910  -0.0242 362 PHE E CD2 
14644 C CE1 . PHE E 362 ? 0.7134 0.5277 0.8817 -0.0584 0.1412  -0.0189 362 PHE E CE1 
14645 C CE2 . PHE E 362 ? 0.6514 0.4354 0.8309 -0.0336 0.1046  -0.0381 362 PHE E CE2 
14646 C CZ  . PHE E 362 ? 0.6823 0.4952 0.8775 -0.0385 0.1282  -0.0352 362 PHE E CZ  
14647 N N   . VAL E 363 ? 0.7050 0.4226 0.6905 -0.0972 0.0301  0.0333  363 VAL E N   
14648 C CA  . VAL E 363 ? 0.7318 0.4520 0.7008 -0.1083 -0.0020 0.0605  363 VAL E CA  
14649 C C   . VAL E 363 ? 0.7057 0.4443 0.7376 -0.0902 -0.0258 0.0700  363 VAL E C   
14650 O O   . VAL E 363 ? 0.6876 0.4347 0.7565 -0.0752 -0.0197 0.0500  363 VAL E O   
14651 C CB  . VAL E 363 ? 0.7898 0.5013 0.6865 -0.1312 -0.0115 0.0532  363 VAL E CB  
14652 C CG1 . VAL E 363 ? 0.8702 0.5617 0.6948 -0.1469 0.0153  0.0450  363 VAL E CG1 
14653 C CG2 . VAL E 363 ? 0.7691 0.4770 0.6716 -0.1272 -0.0104 0.0247  363 VAL E CG2 
14654 N N   . ASP E 364 ? 0.7122 0.4577 0.7547 -0.0898 -0.0516 0.1029  364 ASP E N   
14655 C CA  . ASP E 364 ? 0.6461 0.4129 0.7518 -0.0669 -0.0708 0.1162  364 ASP E CA  
14656 C C   . ASP E 364 ? 0.6544 0.4573 0.7654 -0.0743 -0.0894 0.1134  364 ASP E C   
14657 O O   . ASP E 364 ? 0.7141 0.5262 0.7827 -0.0986 -0.1115 0.1278  364 ASP E O   
14658 C CB  . ASP E 364 ? 0.7319 0.4911 0.8463 -0.0613 -0.0931 0.1567  364 ASP E CB  
14659 C CG  . ASP E 364 ? 0.6933 0.4625 0.8810 -0.0260 -0.1029 0.1675  364 ASP E CG  
14660 O OD1 . ASP E 364 ? 0.6091 0.4029 0.8387 -0.0088 -0.0948 0.1464  364 ASP E OD1 
14661 O OD2 . ASP E 364 ? 0.7556 0.5048 0.9560 -0.0142 -0.1179 0.1990  364 ASP E OD2 
14662 N N   . GLY E 365 ? 0.6023 0.4258 0.7605 -0.0582 -0.0816 0.0962  365 GLY E N   
14663 C CA  . GLY E 365 ? 0.6120 0.4747 0.7842 -0.0691 -0.0969 0.0961  365 GLY E CA  
14664 C C   . GLY E 365 ? 0.6698 0.5864 0.8993 -0.0575 -0.1241 0.1279  365 GLY E C   
14665 O O   . GLY E 365 ? 0.6597 0.6227 0.9128 -0.0695 -0.1381 0.1325  365 GLY E O   
14666 N N   . GLY E 366 ? 0.6834 0.5950 0.9393 -0.0339 -0.1319 0.1521  366 GLY E N   
14667 C CA  . GLY E 366 ? 0.7016 0.6642 1.0214 -0.0126 -0.1566 0.1854  366 GLY E CA  
14668 C C   . GLY E 366 ? 0.6739 0.6588 1.0655 0.0265  -0.1344 0.1726  366 GLY E C   
14669 O O   . GLY E 366 ? 0.6454 0.5961 1.0282 0.0352  -0.1041 0.1408  366 GLY E O   
14670 N N   . VAL E 367 ? 0.6987 0.7436 1.1614 0.0516  -0.1489 0.1978  367 VAL E N   
14671 C CA  . VAL E 367 ? 0.6775 0.7418 1.2047 0.0942  -0.1222 0.1844  367 VAL E CA  
14672 C C   . VAL E 367 ? 0.6608 0.7897 1.2162 0.0816  -0.1096 0.1709  367 VAL E C   
14673 O O   . VAL E 367 ? 0.6285 0.7667 1.2135 0.1066  -0.0784 0.1498  367 VAL E O   
14674 C CB  . VAL E 367 ? 0.6838 0.7777 1.2816 0.1388  -0.1363 0.2176  367 VAL E CB  
14675 C CG1 . VAL E 367 ? 0.7284 0.7423 1.2926 0.1501  -0.1459 0.2314  367 VAL E CG1 
14676 C CG2 . VAL E 367 ? 0.6838 0.8676 1.3235 0.1245  -0.1750 0.2576  367 VAL E CG2 
14677 N N   . HIS E 368 ? 0.6911 0.8568 1.2268 0.0379  -0.1336 0.1819  368 HIS E N   
14678 C CA  . HIS E 368 ? 0.6934 0.9131 1.2482 0.0145  -0.1254 0.1730  368 HIS E CA  
14679 C C   . HIS E 368 ? 0.7473 0.9111 1.2196 -0.0293 -0.1213 0.1468  368 HIS E C   
14680 O O   . HIS E 368 ? 0.8022 0.9912 1.2597 -0.0705 -0.1373 0.1505  368 HIS E O   
14681 C CB  . HIS E 368 ? 0.7010 1.0181 1.3146 -0.0026 -0.1592 0.2096  368 HIS E CB  
14682 C CG  . HIS E 368 ? 0.7233 1.1092 1.4342 0.0479  -0.1610 0.2378  368 HIS E CG  
14683 N ND1 . HIS E 368 ? 0.7073 1.1303 1.4825 0.0901  -0.1228 0.2267  368 HIS E ND1 
14684 C CD2 . HIS E 368 ? 0.7608 1.1820 1.5137 0.0667  -0.1952 0.2769  368 HIS E CD2 
14685 C CE1 . HIS E 368 ? 0.7368 1.2097 1.5857 0.1350  -0.1290 0.2528  368 HIS E CE1 
14686 N NE2 . HIS E 368 ? 0.7720 1.2434 1.6094 0.1220  -0.1739 0.2847  368 HIS E NE2 
14687 N N   . ALA E 369 ? 0.7425 0.8285 1.1627 -0.0202 -0.1012 0.1216  369 ALA E N   
14688 C CA  . ALA E 369 ? 0.7247 0.7549 1.0749 -0.0490 -0.0907 0.0946  369 ALA E CA  
14689 C C   . ALA E 369 ? 0.6592 0.7037 1.0220 -0.0527 -0.0692 0.0782  369 ALA E C   
14690 O O   . ALA E 369 ? 0.6228 0.7016 1.0356 -0.0250 -0.0506 0.0777  369 ALA E O   
14691 C CB  . ALA E 369 ? 0.7356 0.6975 1.0453 -0.0346 -0.0742 0.0767  369 ALA E CB  
14692 N N   . ARG E 370 ? 0.6502 0.6622 0.9622 -0.0861 -0.0701 0.0646  370 ARG E N   
14693 C CA  . ARG E 370 ? 0.6384 0.6590 0.9551 -0.0967 -0.0544 0.0559  370 ARG E CA  
14694 C C   . ARG E 370 ? 0.5882 0.5819 0.9044 -0.0651 -0.0242 0.0361  370 ARG E C   
14695 O O   . ARG E 370 ? 0.5773 0.6052 0.9234 -0.0555 -0.0071 0.0367  370 ARG E O   
14696 C CB  . ARG E 370 ? 0.7174 0.6883 0.9708 -0.1381 -0.0645 0.0457  370 ARG E CB  
14697 C CG  . ARG E 370 ? 0.7686 0.7168 1.0055 -0.1513 -0.0487 0.0361  370 ARG E CG  
14698 C CD  . ARG E 370 ? 0.8142 0.8385 1.1067 -0.1659 -0.0474 0.0570  370 ARG E CD  
14699 N NE  . ARG E 370 ? 0.8558 0.8596 1.1299 -0.1815 -0.0316 0.0540  370 ARG E NE  
14700 C CZ  . ARG E 370 ? 0.8396 0.8449 1.1206 -0.1552 -0.0047 0.0478  370 ARG E CZ  
14701 N NH1 . ARG E 370 ? 0.8115 0.8306 1.1154 -0.1120 0.0104  0.0385  370 ARG E NH1 
14702 N NH2 . ARG E 370 ? 0.8520 0.8369 1.1091 -0.1748 0.0053  0.0511  370 ARG E NH2 
14703 N N   . ALA E 371 ? 0.5533 0.4911 0.8351 -0.0510 -0.0179 0.0196  371 ALA E N   
14704 C CA  . ALA E 371 ? 0.4933 0.4062 0.7721 -0.0259 0.0037  0.0013  371 ALA E CA  
14705 C C   . ALA E 371 ? 0.4865 0.3716 0.7648 -0.0047 0.0051  -0.0048 371 ALA E C   
14706 O O   . ALA E 371 ? 0.5153 0.3909 0.7839 -0.0117 -0.0080 0.0050  371 ALA E O   
14707 C CB  . ALA E 371 ? 0.4964 0.3663 0.7311 -0.0389 0.0101  -0.0129 371 ALA E CB  
14708 N N   . GLY E 372 ? 0.4658 0.3353 0.7490 0.0167  0.0197  -0.0197 372 GLY E N   
14709 C CA  . GLY E 372 ? 0.4614 0.3007 0.7452 0.0307  0.0200  -0.0253 372 GLY E CA  
14710 C C   . GLY E 372 ? 0.4741 0.2818 0.7260 0.0156  0.0168  -0.0289 372 GLY E C   
14711 O O   . GLY E 372 ? 0.5009 0.2961 0.7493 0.0140  0.0118  -0.0208 372 GLY E O   
14712 N N   . ILE E 373 ? 0.4880 0.3625 0.6596 0.0457  0.0689  0.0412  373 ILE E N   
14713 C CA  . ILE E 373 ? 0.4493 0.3226 0.5884 0.0314  0.0622  0.0498  373 ILE E CA  
14714 C C   . ILE E 373 ? 0.4200 0.3273 0.5437 0.0268  0.0503  0.0514  373 ILE E C   
14715 O O   . ILE E 373 ? 0.4209 0.3476 0.5493 0.0235  0.0542  0.0370  373 ILE E O   
14716 C CB  . ILE E 373 ? 0.4306 0.2900 0.5569 0.0152  0.0716  0.0304  373 ILE E CB  
14717 C CG1 . ILE E 373 ? 0.4429 0.2665 0.5911 0.0167  0.0826  0.0216  373 ILE E CG1 
14718 C CG2 . ILE E 373 ? 0.4034 0.2652 0.5066 0.0018  0.0677  0.0393  373 ILE E CG2 
14719 C CD1 . ILE E 373 ? 0.4350 0.2494 0.5777 0.0016  0.0863  -0.0052 373 ILE E CD1 
14720 N N   . ALA E 374 ? 0.4302 0.3421 0.5340 0.0273  0.0375  0.0686  374 ALA E N   
14721 C CA  . ALA E 374 ? 0.4202 0.3593 0.5085 0.0205  0.0261  0.0650  374 ALA E CA  
14722 C C   . ALA E 374 ? 0.4271 0.3573 0.4787 0.0101  0.0271  0.0701  374 ALA E C   
14723 O O   . ALA E 374 ? 0.4831 0.4036 0.5127 0.0160  0.0216  0.0873  374 ALA E O   
14724 C CB  . ALA E 374 ? 0.4390 0.3997 0.5397 0.0330  0.0057  0.0740  374 ALA E CB  
14725 N N   . LEU E 375 ? 0.4107 0.3446 0.4550 -0.0033 0.0351  0.0560  375 LEU E N   
14726 C CA  . LEU E 375 ? 0.3936 0.3230 0.4131 -0.0132 0.0392  0.0576  375 LEU E CA  
14727 C C   . LEU E 375 ? 0.4432 0.3895 0.4419 -0.0128 0.0274  0.0581  375 LEU E C   
14728 O O   . LEU E 375 ? 0.4509 0.4154 0.4609 -0.0152 0.0209  0.0469  375 LEU E O   
14729 C CB  . LEU E 375 ? 0.3340 0.2654 0.3594 -0.0243 0.0473  0.0412  375 LEU E CB  
14730 C CG  . LEU E 375 ? 0.3639 0.2810 0.4081 -0.0252 0.0546  0.0314  375 LEU E CG  
14731 C CD1 . LEU E 375 ? 0.3877 0.3129 0.4292 -0.0321 0.0549  0.0136  375 LEU E CD1 
14732 C CD2 . LEU E 375 ? 0.3892 0.2841 0.4412 -0.0292 0.0630  0.0395  375 LEU E CD2 
14733 N N   . GLY E 376 ? 0.4644 0.4022 0.4322 -0.0098 0.0266  0.0705  376 GLY E N   
14734 C CA  . GLY E 376 ? 0.4606 0.4106 0.4011 -0.0066 0.0124  0.0682  376 GLY E CA  
14735 C C   . GLY E 376 ? 0.4314 0.3804 0.3471 -0.0146 0.0219  0.0610  376 GLY E C   
14736 O O   . GLY E 376 ? 0.4371 0.3834 0.3665 -0.0240 0.0367  0.0554  376 GLY E O   
14737 N N   . ALA E 377 ? 0.4770 0.4284 0.3561 -0.0093 0.0121  0.0597  377 ALA E N   
14738 C CA  . ALA E 377 ? 0.4953 0.4460 0.3514 -0.0149 0.0219  0.0486  377 ALA E CA  
14739 C C   . ALA E 377 ? 0.5287 0.4645 0.3746 -0.0183 0.0497  0.0594  377 ALA E C   
14740 O O   . ALA E 377 ? 0.5328 0.4727 0.3917 -0.0262 0.0624  0.0485  377 ALA E O   
14741 C CB  . ALA E 377 ? 0.5048 0.4580 0.3164 -0.0063 0.0050  0.0420  377 ALA E CB  
14742 N N   . HIS E 378 ? 0.5714 0.4900 0.4002 -0.0120 0.0600  0.0819  378 HIS E N   
14743 C CA  . HIS E 378 ? 0.5665 0.4705 0.3943 -0.0167 0.0905  0.0944  378 HIS E CA  
14744 C C   . HIS E 378 ? 0.5278 0.4369 0.4127 -0.0303 0.1006  0.0864  378 HIS E C   
14745 O O   . HIS E 378 ? 0.5289 0.4399 0.4310 -0.0382 0.1209  0.0839  378 HIS E O   
14746 C CB  . HIS E 378 ? 0.6450 0.5246 0.4456 -0.0069 0.1011  0.1239  378 HIS E CB  
14747 C CG  . HIS E 378 ? 0.7548 0.6255 0.4837 0.0076  0.1010  0.1348  378 HIS E CG  
14748 N ND1 . HIS E 378 ? 0.8402 0.6843 0.5279 0.0180  0.1212  0.1659  378 HIS E ND1 
14749 C CD2 . HIS E 378 ? 0.7826 0.6651 0.4697 0.0141  0.0837  0.1174  378 HIS E CD2 
14750 C CE1 . HIS E 378 ? 0.9095 0.7506 0.5244 0.0324  0.1149  0.1678  378 HIS E CE1 
14751 N NE2 . HIS E 378 ? 0.8594 0.7242 0.4744 0.0296  0.0906  0.1358  378 HIS E NE2 
14752 N N   . HIS E 379 ? 0.5124 0.4248 0.4272 -0.0317 0.0860  0.0814  379 HIS E N   
14753 C CA  . HIS E 379 ? 0.4827 0.4009 0.4426 -0.0422 0.0886  0.0689  379 HIS E CA  
14754 C C   . HIS E 379 ? 0.4694 0.4071 0.4390 -0.0474 0.0846  0.0503  379 HIS E C   
14755 O O   . HIS E 379 ? 0.4592 0.4034 0.4572 -0.0549 0.0917  0.0426  379 HIS E O   
14756 C CB  . HIS E 379 ? 0.4725 0.3891 0.4503 -0.0391 0.0748  0.0650  379 HIS E CB  
14757 C CG  . HIS E 379 ? 0.4427 0.3632 0.4547 -0.0473 0.0746  0.0492  379 HIS E CG  
14758 N ND1 . HIS E 379 ? 0.4632 0.3694 0.5032 -0.0536 0.0838  0.0488  379 HIS E ND1 
14759 C CD2 . HIS E 379 ? 0.4098 0.3453 0.4294 -0.0493 0.0652  0.0326  379 HIS E CD2 
14760 C CE1 . HIS E 379 ? 0.4133 0.3280 0.4740 -0.0588 0.0763  0.0290  379 HIS E CE1 
14761 N NE2 . HIS E 379 ? 0.4122 0.3441 0.4566 -0.0550 0.0657  0.0212  379 HIS E NE2 
14762 N N   . LEU E 380 ? 0.4594 0.4061 0.4102 -0.0430 0.0718  0.0428  380 LEU E N   
14763 C CA  . LEU E 380 ? 0.4238 0.3831 0.3853 -0.0462 0.0691  0.0284  380 LEU E CA  
14764 C C   . LEU E 380 ? 0.4069 0.3678 0.3603 -0.0467 0.0833  0.0253  380 LEU E C   
14765 O O   . LEU E 380 ? 0.4006 0.3705 0.3746 -0.0486 0.0851  0.0159  380 LEU E O   
14766 C CB  . LEU E 380 ? 0.4340 0.3993 0.3883 -0.0433 0.0536  0.0208  380 LEU E CB  
14767 C CG  . LEU E 380 ? 0.4001 0.3684 0.3700 -0.0421 0.0437  0.0216  380 LEU E CG  
14768 C CD1 . LEU E 380 ? 0.4184 0.3945 0.3883 -0.0407 0.0318  0.0155  380 LEU E CD1 
14769 C CD2 . LEU E 380 ? 0.3851 0.3565 0.3741 -0.0451 0.0462  0.0160  380 LEU E CD2 
14770 N N   . GLU E 381 ? 0.3992 0.3506 0.3197 -0.0424 0.0937  0.0337  381 GLU E N   
14771 C CA  . GLU E 381 ? 0.4232 0.3748 0.3294 -0.0405 0.1113  0.0290  381 GLU E CA  
14772 C C   . GLU E 381 ? 0.4458 0.4054 0.3944 -0.0467 0.1306  0.0295  381 GLU E C   
14773 O O   . GLU E 381 ? 0.4479 0.4055 0.4226 -0.0526 0.1382  0.0394  381 GLU E O   
14774 C CB  . GLU E 381 ? 0.4477 0.3849 0.3012 -0.0327 0.1225  0.0407  381 GLU E CB  
14775 C CG  . GLU E 381 ? 0.4916 0.4265 0.3034 -0.0250 0.0996  0.0332  381 GLU E CG  
14776 C CD  . GLU E 381 ? 0.6156 0.5354 0.3694 -0.0140 0.1037  0.0495  381 GLU E CD  
14777 O OE1 . GLU E 381 ? 0.6770 0.5848 0.4236 -0.0133 0.1309  0.0691  381 GLU E OE1 
14778 O OE2 . GLU E 381 ? 0.6602 0.5803 0.3783 -0.0056 0.0790  0.0442  381 GLU E OE2 
14779 N N   . GLU E 382 ? 0.4081 0.3769 0.3693 -0.0450 0.1376  0.0171  382 GLU E N   
14780 C CA  . GLU E 382 ? 0.4174 0.4008 0.4286 -0.0488 0.1526  0.0144  382 GLU E CA  
14781 C C   . GLU E 382 ? 0.3901 0.3860 0.4453 -0.0542 0.1334  0.0107  382 GLU E C   
14782 O O   . GLU E 382 ? 0.3923 0.4018 0.4950 -0.0596 0.1399  0.0097  382 GLU E O   
14783 C CB  . GLU E 382 ? 0.4067 0.3862 0.4244 -0.0523 0.1833  0.0280  382 GLU E CB  
14784 C CG  . GLU E 382 ? 0.4702 0.4355 0.4313 -0.0436 0.2053  0.0320  382 GLU E CG  
14785 C CD  . GLU E 382 ? 0.5034 0.4747 0.4585 -0.0360 0.2085  0.0130  382 GLU E CD  
14786 O OE1 . GLU E 382 ? 0.4874 0.4765 0.4972 -0.0372 0.2127  0.0041  382 GLU E OE1 
14787 O OE2 . GLU E 382 ? 0.5376 0.4955 0.4359 -0.0281 0.2036  0.0050  382 GLU E OE2 
14788 N N   . ASN E 383 ? 0.3911 0.3833 0.4309 -0.0524 0.1103  0.0075  383 ASN E N   
14789 C CA  . ASN E 383 ? 0.3722 0.3740 0.4381 -0.0534 0.0914  0.0021  383 ASN E CA  
14790 C C   . ASN E 383 ? 0.3734 0.3749 0.4289 -0.0466 0.0791  -0.0031 383 ASN E C   
14791 O O   . ASN E 383 ? 0.4072 0.3983 0.4354 -0.0446 0.0784  -0.0036 383 ASN E O   
14792 C CB  . ASN E 383 ? 0.3960 0.3893 0.4540 -0.0572 0.0811  0.0058  383 ASN E CB  
14793 C CG  . ASN E 383 ? 0.4606 0.4501 0.5405 -0.0649 0.0926  0.0109  383 ASN E CG  
14794 O OD1 . ASN E 383 ? 0.4993 0.5007 0.6209 -0.0705 0.0921  0.0038  383 ASN E OD1 
14795 N ND2 . ASN E 383 ? 0.4869 0.4593 0.5425 -0.0650 0.1024  0.0236  383 ASN E ND2 
14796 N N   . LEU E 384 ? 0.3556 0.3683 0.4355 -0.0426 0.0685  -0.0068 384 LEU E N   
14797 C CA  . LEU E 384 ? 0.3644 0.3723 0.4350 -0.0350 0.0581  -0.0064 384 LEU E CA  
14798 C C   . LEU E 384 ? 0.3960 0.4001 0.4511 -0.0351 0.0448  -0.0033 384 LEU E C   
14799 O O   . LEU E 384 ? 0.4037 0.4168 0.4691 -0.0345 0.0340  -0.0066 384 LEU E O   
14800 C CB  . LEU E 384 ? 0.4068 0.4267 0.5072 -0.0259 0.0538  -0.0083 384 LEU E CB  
14801 C CG  . LEU E 384 ? 0.4525 0.4628 0.5435 -0.0154 0.0444  -0.0024 384 LEU E CG  
14802 C CD1 . LEU E 384 ? 0.4186 0.4098 0.4982 -0.0150 0.0562  -0.0032 384 LEU E CD1 
14803 C CD2 . LEU E 384 ? 0.4766 0.5021 0.5986 -0.0033 0.0337  -0.0017 384 LEU E CD2 
14804 N N   . VAL E 385 ? 0.3795 0.3713 0.4122 -0.0356 0.0458  0.0005  385 VAL E N   
14805 C CA  . VAL E 385 ? 0.3520 0.3395 0.3696 -0.0352 0.0402  0.0036  385 VAL E CA  
14806 C C   . VAL E 385 ? 0.3573 0.3362 0.3655 -0.0291 0.0408  0.0107  385 VAL E C   
14807 O O   . VAL E 385 ? 0.3569 0.3279 0.3682 -0.0315 0.0473  0.0121  385 VAL E O   
14808 C CB  . VAL E 385 ? 0.3396 0.3225 0.3492 -0.0410 0.0442  0.0041  385 VAL E CB  
14809 C CG1 . VAL E 385 ? 0.3471 0.3270 0.3475 -0.0391 0.0421  0.0055  385 VAL E CG1 
14810 C CG2 . VAL E 385 ? 0.3137 0.2988 0.3302 -0.0458 0.0480  0.0026  385 VAL E CG2 
14811 N N   . VAL E 386 ? 0.3514 0.3300 0.3475 -0.0209 0.0342  0.0149  386 VAL E N   
14812 C CA  . VAL E 386 ? 0.3542 0.3205 0.3368 -0.0126 0.0385  0.0275  386 VAL E CA  
14813 C C   . VAL E 386 ? 0.4153 0.3738 0.3771 -0.0124 0.0474  0.0334  386 VAL E C   
14814 O O   . VAL E 386 ? 0.4363 0.3977 0.3776 -0.0085 0.0427  0.0292  386 VAL E O   
14815 C CB  . VAL E 386 ? 0.3862 0.3554 0.3600 0.0014  0.0255  0.0327  386 VAL E CB  
14816 C CG1 . VAL E 386 ? 0.4103 0.3611 0.3635 0.0125  0.0328  0.0516  386 VAL E CG1 
14817 C CG2 . VAL E 386 ? 0.3961 0.3758 0.4015 0.0027  0.0200  0.0273  386 VAL E CG2 
14818 N N   . PHE E 387 ? 0.4299 0.3788 0.4014 -0.0167 0.0616  0.0409  387 PHE E N   
14819 C CA  . PHE E 387 ? 0.4259 0.3695 0.3884 -0.0165 0.0761  0.0483  387 PHE E CA  
14820 C C   . PHE E 387 ? 0.4730 0.3998 0.4149 -0.0060 0.0879  0.0675  387 PHE E C   
14821 O O   . PHE E 387 ? 0.4703 0.3841 0.4319 -0.0089 0.1001  0.0784  387 PHE E O   
14822 C CB  . PHE E 387 ? 0.3990 0.3460 0.3952 -0.0286 0.0846  0.0447  387 PHE E CB  
14823 C CG  . PHE E 387 ? 0.4106 0.3713 0.4173 -0.0348 0.0737  0.0311  387 PHE E CG  
14824 C CD1 . PHE E 387 ? 0.4305 0.3947 0.4428 -0.0386 0.0627  0.0226  387 PHE E CD1 
14825 C CD2 . PHE E 387 ? 0.4398 0.4078 0.4483 -0.0347 0.0766  0.0282  387 PHE E CD2 
14826 C CE1 . PHE E 387 ? 0.4344 0.4072 0.4488 -0.0422 0.0550  0.0149  387 PHE E CE1 
14827 C CE2 . PHE E 387 ? 0.4086 0.3851 0.4251 -0.0378 0.0665  0.0199  387 PHE E CE2 
14828 C CZ  . PHE E 387 ? 0.4128 0.3907 0.4294 -0.0415 0.0559  0.0149  387 PHE E CZ  
14829 N N   . ASP E 388 ? 0.5204 0.4449 0.4206 0.0068  0.0841  0.0715  388 ASP E N   
14830 C CA  . ASP E 388 ? 0.5731 0.4793 0.4383 0.0215  0.0940  0.0933  388 ASP E CA  
14831 C C   . ASP E 388 ? 0.6012 0.4975 0.4513 0.0222  0.1233  0.1046  388 ASP E C   
14832 O O   . ASP E 388 ? 0.5977 0.4957 0.4097 0.0300  0.1262  0.0993  388 ASP E O   
14833 C CB  . ASP E 388 ? 0.6181 0.5284 0.4398 0.0379  0.0705  0.0900  388 ASP E CB  
14834 C CG  . ASP E 388 ? 0.6984 0.5889 0.4787 0.0576  0.0741  0.1159  388 ASP E CG  
14835 O OD1 . ASP E 388 ? 0.7349 0.6041 0.5179 0.0578  0.1015  0.1391  388 ASP E OD1 
14836 O OD2 . ASP E 388 ? 0.7304 0.6266 0.4778 0.0733  0.0486  0.1134  388 ASP E OD2 
14837 N N   . LEU E 389 ? 0.5961 0.4820 0.4807 0.0135  0.1468  0.1182  389 LEU E N   
14838 C CA  . LEU E 389 ? 0.5673 0.4492 0.4547 0.0114  0.1782  0.1277  389 LEU E CA  
14839 C C   . LEU E 389 ? 0.6210 0.4815 0.4478 0.0302  0.1970  0.1515  389 LEU E C   
14840 O O   . LEU E 389 ? 0.6493 0.5125 0.4626 0.0339  0.2143  0.1504  389 LEU E O   
14841 C CB  . LEU E 389 ? 0.5747 0.4551 0.5290 -0.0057 0.1965  0.1324  389 LEU E CB  
14842 C CG  . LEU E 389 ? 0.5258 0.4248 0.5282 -0.0209 0.1719  0.1082  389 LEU E CG  
14843 C CD1 . LEU E 389 ? 0.5662 0.4597 0.6294 -0.0361 0.1845  0.1103  389 LEU E CD1 
14844 C CD2 . LEU E 389 ? 0.3654 0.2885 0.3771 -0.0252 0.1626  0.0889  389 LEU E CD2 
14845 N N   . GLU E 390 ? 0.6424 0.4860 0.4364 0.0439  0.1861  0.1679  390 GLU E N   
14846 C CA  . GLU E 390 ? 0.7056 0.5336 0.4436 0.0632  0.1934  0.1859  390 GLU E CA  
14847 C C   . GLU E 390 ? 0.7345 0.5685 0.4011 0.0789  0.1811  0.1740  390 GLU E C   
14848 O O   . GLU E 390 ? 0.7751 0.5998 0.3971 0.0913  0.1935  0.1822  390 GLU E O   
14849 C CB  . GLU E 390 ? 0.7434 0.5531 0.4664 0.0767  0.1805  0.2066  390 GLU E CB  
14850 C CG  . GLU E 390 ? 0.7644 0.5617 0.5515 0.0640  0.1939  0.2167  390 GLU E CG  
14851 C CD  . GLU E 390 ? 0.8915 0.6653 0.6584 0.0811  0.1906  0.2418  390 GLU E CD  
14852 O OE1 . GLU E 390 ? 0.9317 0.7044 0.6383 0.1030  0.1686  0.2490  390 GLU E OE1 
14853 O OE2 . GLU E 390 ? 0.9394 0.6968 0.7526 0.0733  0.2077  0.2525  390 GLU E OE2 
14854 N N   . ARG E 391 ? 0.7281 0.5776 0.3867 0.0781  0.1540  0.1514  391 ARG E N   
14855 C CA  . ARG E 391 ? 0.7468 0.6037 0.3472 0.0907  0.1348  0.1304  391 ARG E CA  
14856 C C   . ARG E 391 ? 0.6824 0.5556 0.3121 0.0765  0.1397  0.1017  391 ARG E C   
14857 O O   . ARG E 391 ? 0.7105 0.5875 0.3019 0.0840  0.1268  0.0791  391 ARG E O   
14858 C CB  . ARG E 391 ? 0.7577 0.6284 0.3514 0.0975  0.0876  0.1155  391 ARG E CB  
14859 C CG  . ARG E 391 ? 1.0099 0.8679 0.5760 0.1167  0.0737  0.1422  391 ARG E CG  
14860 C CD  . ARG E 391 ? 1.1140 0.9679 0.5940 0.1435  0.0501  0.1417  391 ARG E CD  
14861 N NE  . ARG E 391 ? 1.1225 1.0020 0.6012 0.1423  0.0095  0.1029  391 ARG E NE  
14862 C CZ  . ARG E 391 ? 1.2099 1.0918 0.6235 0.1587  -0.0139 0.0861  391 ARG E CZ  
14863 N NH1 . ARG E 391 ? 1.3131 1.1792 0.6753 0.1715  0.0002  0.1026  391 ARG E NH1 
14864 N NH2 . ARG E 391 ? 1.1881 1.0926 0.6125 0.1546  -0.0511 0.0477  391 ARG E NH2 
14865 N N   . SER E 392 ? 0.6088 0.4900 0.3069 0.0576  0.1571  0.1022  392 SER E N   
14866 C CA  . SER E 392 ? 0.5636 0.4604 0.3003 0.0454  0.1613  0.0797  392 SER E CA  
14867 C C   . SER E 392 ? 0.5499 0.4599 0.2896 0.0422  0.1265  0.0505  392 SER E C   
14868 O O   . SER E 392 ? 0.5667 0.4775 0.2892 0.0458  0.1257  0.0303  392 SER E O   
14869 C CB  . SER E 392 ? 0.5856 0.4751 0.2932 0.0544  0.1950  0.0806  392 SER E CB  
14870 O OG  . SER E 392 ? 0.5438 0.4488 0.3081 0.0426  0.2045  0.0662  392 SER E OG  
14871 N N   . ARG E 393 ? 0.5340 0.4526 0.3016 0.0348  0.1012  0.0482  393 ARG E N   
14872 C CA  . ARG E 393 ? 0.5256 0.4566 0.3066 0.0297  0.0720  0.0245  393 ARG E CA  
14873 C C   . ARG E 393 ? 0.4856 0.4275 0.3199 0.0158  0.0623  0.0258  393 ARG E C   
14874 O O   . ARG E 393 ? 0.4794 0.4179 0.3297 0.0138  0.0698  0.0422  393 ARG E O   
14875 C CB  . ARG E 393 ? 0.5355 0.4663 0.2723 0.0433  0.0462  0.0171  393 ARG E CB  
14876 C CG  . ARG E 393 ? 0.5373 0.4675 0.2736 0.0500  0.0364  0.0368  393 ARG E CG  
14877 C CD  . ARG E 393 ? 0.5942 0.5258 0.2823 0.0684  0.0088  0.0330  393 ARG E CD  
14878 N NE  . ARG E 393 ? 0.5832 0.5168 0.2851 0.0757  -0.0034 0.0514  393 ARG E NE  
14879 C CZ  . ARG E 393 ? 0.6491 0.5926 0.3339 0.0907  -0.0357 0.0483  393 ARG E CZ  
14880 N NH1 . ARG E 393 ? 0.7280 0.6798 0.3760 0.0991  -0.0610 0.0257  393 ARG E NH1 
14881 N NH2 . ARG E 393 ? 0.6929 0.6378 0.3989 0.0985  -0.0439 0.0663  393 ARG E NH2 
14882 N N   . VAL E 394 ? 0.4515 0.4035 0.3112 0.0070  0.0476  0.0080  394 VAL E N   
14883 C CA  . VAL E 394 ? 0.4220 0.3836 0.3226 -0.0041 0.0396  0.0071  394 VAL E CA  
14884 C C   . VAL E 394 ? 0.4108 0.3821 0.3170 -0.0031 0.0173  -0.0043 394 VAL E C   
14885 O O   . VAL E 394 ? 0.4443 0.4169 0.3369 -0.0002 0.0054  -0.0198 394 VAL E O   
14886 C CB  . VAL E 394 ? 0.4217 0.3860 0.3507 -0.0147 0.0451  0.0005  394 VAL E CB  
14887 C CG1 . VAL E 394 ? 0.4376 0.4088 0.3953 -0.0235 0.0399  0.0017  394 VAL E CG1 
14888 C CG2 . VAL E 394 ? 0.3894 0.3510 0.3253 -0.0156 0.0626  0.0093  394 VAL E CG2 
14889 N N   . GLY E 395 ? 0.4091 0.3880 0.3386 -0.0049 0.0116  0.0012  395 GLY E N   
14890 C CA  . GLY E 395 ? 0.4360 0.4301 0.3878 -0.0052 -0.0073 -0.0095 395 GLY E CA  
14891 C C   . GLY E 395 ? 0.4028 0.4043 0.3957 -0.0179 -0.0003 -0.0125 395 GLY E C   
14892 O O   . GLY E 395 ? 0.3634 0.3582 0.3599 -0.0223 0.0144  -0.0037 395 GLY E O   
14893 N N   . PHE E 396 ? 0.4028 0.4175 0.4264 -0.0240 -0.0099 -0.0254 396 PHE E N   
14894 C CA  . PHE E 396 ? 0.3675 0.3877 0.4275 -0.0350 0.0021  -0.0252 396 PHE E CA  
14895 C C   . PHE E 396 ? 0.3777 0.4195 0.4833 -0.0375 -0.0083 -0.0357 396 PHE E C   
14896 O O   . PHE E 396 ? 0.3798 0.4330 0.4931 -0.0339 -0.0301 -0.0485 396 PHE E O   
14897 C CB  . PHE E 396 ? 0.3580 0.3662 0.4187 -0.0451 0.0136  -0.0266 396 PHE E CB  
14898 C CG  . PHE E 396 ? 0.4171 0.4221 0.4819 -0.0480 0.0029  -0.0419 396 PHE E CG  
14899 C CD1 . PHE E 396 ? 0.4592 0.4736 0.5663 -0.0571 -0.0030 -0.0549 396 PHE E CD1 
14900 C CD2 . PHE E 396 ? 0.4335 0.4259 0.4650 -0.0422 0.0007  -0.0457 396 PHE E CD2 
14901 C CE1 . PHE E 396 ? 0.4821 0.4911 0.5973 -0.0611 -0.0146 -0.0743 396 PHE E CE1 
14902 C CE2 . PHE E 396 ? 0.4558 0.4423 0.4890 -0.0440 -0.0086 -0.0647 396 PHE E CE2 
14903 C CZ  . PHE E 396 ? 0.4653 0.4589 0.5397 -0.0538 -0.0180 -0.0803 396 PHE E CZ  
14904 N N   . ASN E 397 ? 0.3872 0.4358 0.5245 -0.0434 0.0074  -0.0318 397 ASN E N   
14905 C CA  . ASN E 397 ? 0.3511 0.4235 0.5447 -0.0472 0.0034  -0.0408 397 ASN E CA  
14906 C C   . ASN E 397 ? 0.3574 0.4325 0.5803 -0.0599 -0.0021 -0.0545 397 ASN E C   
14907 O O   . ASN E 397 ? 0.3975 0.4535 0.6107 -0.0692 0.0137  -0.0504 397 ASN E O   
14908 C CB  . ASN E 397 ? 0.3690 0.4450 0.5864 -0.0505 0.0300  -0.0329 397 ASN E CB  
14909 C CG  . ASN E 397 ? 0.3787 0.4317 0.5652 -0.0578 0.0539  -0.0225 397 ASN E CG  
14910 O OD1 . ASN E 397 ? 0.4176 0.4536 0.5587 -0.0533 0.0546  -0.0158 397 ASN E OD1 
14911 N ND2 . ASN E 397 ? 0.3787 0.4316 0.5926 -0.0685 0.0731  -0.0202 397 ASN E ND2 
14912 N N   . SER E 398 ? 0.3079 0.4058 0.5692 -0.0596 -0.0263 -0.0716 398 SER E N   
14913 C CA  . SER E 398 ? 0.3432 0.4424 0.6380 -0.0729 -0.0353 -0.0904 398 SER E CA  
14914 C C   . SER E 398 ? 0.4043 0.5158 0.7742 -0.0895 -0.0145 -0.0916 398 SER E C   
14915 O O   . SER E 398 ? 0.4555 0.5603 0.8606 -0.1045 -0.0122 -0.1033 398 SER E O   
14916 C CB  . SER E 398 ? 0.3930 0.5115 0.6933 -0.0653 -0.0760 -0.1136 398 SER E CB  
14917 O OG  . SER E 398 ? 0.3924 0.5450 0.7365 -0.0573 -0.0929 -0.1166 398 SER E OG  
14918 N N   . ASN E 399 ? 0.3866 0.5133 0.7821 -0.0867 0.0041  -0.0793 399 ASN E N   
14919 C CA  . ASN E 399 ? 0.3364 0.4713 0.7937 -0.1004 0.0363  -0.0736 399 ASN E CA  
14920 C C   . ASN E 399 ? 0.3391 0.4553 0.7512 -0.0946 0.0704  -0.0502 399 ASN E C   
14921 O O   . ASN E 399 ? 0.3513 0.4592 0.7084 -0.0807 0.0632  -0.0439 399 ASN E O   
14922 C CB  . ASN E 399 ? 0.3278 0.5034 0.8639 -0.0993 0.0269  -0.0854 399 ASN E CB  
14923 C CG  . ASN E 399 ? 0.3885 0.5813 0.9591 -0.1014 -0.0124 -0.1106 399 ASN E CG  
14924 O OD1 . ASN E 399 ? 0.4368 0.6190 1.0318 -0.1131 -0.0078 -0.1182 399 ASN E OD1 
14925 N ND2 . ASN E 399 ? 0.3973 0.6156 0.9673 -0.0875 -0.0518 -0.1232 399 ASN E ND2 
14926 N N   . SER E 400 ? 0.3393 0.4459 0.7689 -0.1040 0.1071  -0.0374 400 SER E N   
14927 C CA  . SER E 400 ? 0.3335 0.4217 0.7123 -0.0975 0.1378  -0.0182 400 SER E CA  
14928 C C   . SER E 400 ? 0.3422 0.4506 0.7286 -0.0846 0.1409  -0.0211 400 SER E C   
14929 O O   . SER E 400 ? 0.3585 0.4977 0.8090 -0.0835 0.1331  -0.0320 400 SER E O   
14930 C CB  . SER E 400 ? 0.3259 0.3944 0.6973 -0.1005 0.1693  -0.0026 400 SER E CB  
14931 O OG  . SER E 400 ? 0.3434 0.4328 0.7668 -0.0995 0.1827  -0.0065 400 SER E OG  
14932 N N   . LEU E 401 ? 0.3692 0.4592 0.6922 -0.0739 0.1500  -0.0130 401 LEU E N   
14933 C CA  . LEU E 401 ? 0.3462 0.4470 0.6720 -0.0610 0.1575  -0.0166 401 LEU E CA  
14934 C C   . LEU E 401 ? 0.3568 0.4742 0.7356 -0.0634 0.1913  -0.0155 401 LEU E C   
14935 O O   . LEU E 401 ? 0.3586 0.4995 0.7844 -0.0549 0.1908  -0.0237 401 LEU E O   
14936 C CB  . LEU E 401 ? 0.3578 0.4305 0.6057 -0.0525 0.1637  -0.0114 401 LEU E CB  
14937 C CG  . LEU E 401 ? 0.3503 0.4079 0.5519 -0.0486 0.1331  -0.0123 401 LEU E CG  
14938 C CD1 . LEU E 401 ? 0.3371 0.3739 0.4833 -0.0413 0.1386  -0.0124 401 LEU E CD1 
14939 C CD2 . LEU E 401 ? 0.3429 0.4175 0.5748 -0.0414 0.1053  -0.0197 401 LEU E CD2 
14940 N N   . LYS E 402 ? 0.3810 0.4779 0.7378 -0.0705 0.2119  -0.0037 402 LYS E N   
14941 C CA  . LYS E 402 ? 0.3954 0.4947 0.7772 -0.0701 0.2404  0.0010  402 LYS E CA  
14942 C C   . LYS E 402 ? 0.3648 0.4951 0.8357 -0.0752 0.2286  -0.0103 402 LYS E C   
14943 O O   . LYS E 402 ? 0.3789 0.5235 0.8895 -0.0711 0.2469  -0.0124 402 LYS E O   
14944 C CB  . LYS E 402 ? 0.4609 0.5307 0.8018 -0.0760 0.2614  0.0187  402 LYS E CB  
14945 C CG  . LYS E 402 ? 0.6083 0.6827 1.0041 -0.0841 0.2790  0.0231  402 LYS E CG  
14946 C CD  . LYS E 402 ? 0.7596 0.8017 1.1151 -0.0882 0.2992  0.0438  402 LYS E CD  
14947 C CE  . LYS E 402 ? 0.8623 0.9064 1.2837 -0.0992 0.3136  0.0470  402 LYS E CE  
14948 N NZ  . LYS E 402 ? 0.9488 0.9678 1.3434 -0.0978 0.3524  0.0696  402 LYS E NZ  
14949 N N   . SER E 403 ? 0.3225 0.4642 0.8243 -0.0831 0.1961  -0.0198 403 SER E N   
14950 C CA  . SER E 403 ? 0.3095 0.4826 0.8926 -0.0866 0.1768  -0.0346 403 SER E CA  
14951 C C   . SER E 403 ? 0.2916 0.4961 0.9089 -0.0724 0.1589  -0.0453 403 SER E C   
14952 O O   . SER E 403 ? 0.2976 0.5314 0.9831 -0.0711 0.1449  -0.0564 403 SER E O   
14953 C CB  . SER E 403 ? 0.3132 0.4873 0.9108 -0.0972 0.1434  -0.0458 403 SER E CB  
14954 O OG  . SER E 403 ? 0.2836 0.4728 0.8723 -0.0904 0.1058  -0.0573 403 SER E OG  
14955 N N   . TYR E 404 ? 0.3062 0.5039 0.8780 -0.0608 0.1581  -0.0420 404 TYR E N   
14956 C CA  . TYR E 404 ? 0.3166 0.5372 0.9157 -0.0434 0.1459  -0.0485 404 TYR E CA  
14957 C C   . TYR E 404 ? 0.3675 0.5795 0.9575 -0.0338 0.1835  -0.0439 404 TYR E C   
14958 O O   . TYR E 404 ? 0.4070 0.6320 1.0193 -0.0175 0.1799  -0.0486 404 TYR E O   
14959 C CB  . TYR E 404 ? 0.2815 0.4971 0.8414 -0.0339 0.1221  -0.0486 404 TYR E CB  
14960 C CG  . TYR E 404 ? 0.2921 0.5089 0.8398 -0.0387 0.0794  -0.0541 404 TYR E CG  
14961 C CD1 . TYR E 404 ? 0.3036 0.5515 0.8969 -0.0292 0.0396  -0.0648 404 TYR E CD1 
14962 C CD2 . TYR E 404 ? 0.3020 0.4887 0.7900 -0.0504 0.0780  -0.0497 404 TYR E CD2 
14963 C CE1 . TYR E 404 ? 0.3066 0.5531 0.8768 -0.0318 0.0005  -0.0729 404 TYR E CE1 
14964 C CE2 . TYR E 404 ? 0.2921 0.4775 0.7653 -0.0534 0.0426  -0.0577 404 TYR E CE2 
14965 C CZ  . TYR E 404 ? 0.2886 0.5026 0.7983 -0.0443 0.0045  -0.0702 404 TYR E CZ  
14966 O OH  . TYR E 404 ? 0.2919 0.5020 0.7753 -0.0454 -0.0302 -0.0808 404 TYR E OH  
14967 N N   . GLY E 405 ? 0.3744 0.5616 0.9270 -0.0417 0.2188  -0.0344 405 GLY E N   
14968 C CA  . GLY E 405 ? 0.3492 0.5240 0.8770 -0.0317 0.2540  -0.0320 405 GLY E CA  
14969 C C   . GLY E 405 ? 0.4177 0.5690 0.8747 -0.0217 0.2555  -0.0331 405 GLY E C   
14970 O O   . GLY E 405 ? 0.4332 0.5767 0.8740 -0.0091 0.2741  -0.0385 405 GLY E O   
14971 N N   . LYS E 406 ? 0.4036 0.5429 0.8212 -0.0274 0.2358  -0.0302 406 LYS E N   
14972 C CA  . LYS E 406 ? 0.4037 0.5218 0.7620 -0.0192 0.2343  -0.0335 406 LYS E CA  
14973 C C   . LYS E 406 ? 0.4110 0.4965 0.6867 -0.0268 0.2428  -0.0250 406 LYS E C   
14974 O O   . LYS E 406 ? 0.4052 0.4858 0.6741 -0.0385 0.2460  -0.0137 406 LYS E O   
14975 C CB  . LYS E 406 ? 0.4253 0.5458 0.7852 -0.0141 0.1888  -0.0359 406 LYS E CB  
14976 C CG  . LYS E 406 ? 0.4783 0.6315 0.9146 -0.0027 0.1714  -0.0417 406 LYS E CG  
14977 C CD  . LYS E 406 ? 0.5713 0.7217 1.0210 0.0156  0.1880  -0.0483 406 LYS E CD  
14978 C CE  . LYS E 406 ? 0.6199 0.8082 1.1593 0.0294  0.1759  -0.0523 406 LYS E CE  
14979 N NZ  . LYS E 406 ? 0.6370 0.8418 1.1938 0.0311  0.1279  -0.0485 406 LYS E NZ  
14980 N N   . THR E 407 ? 0.4388 0.4991 0.6507 -0.0186 0.2399  -0.0310 407 THR E N   
14981 C CA  . THR E 407 ? 0.4235 0.4559 0.5574 -0.0228 0.2349  -0.0255 407 THR E CA  
14982 C C   . THR E 407 ? 0.4440 0.4628 0.5500 -0.0187 0.2030  -0.0337 407 THR E C   
14983 O O   . THR E 407 ? 0.4337 0.4585 0.5718 -0.0110 0.1929  -0.0417 407 THR E O   
14984 C CB  . THR E 407 ? 0.4420 0.4564 0.5204 -0.0170 0.2685  -0.0273 407 THR E CB  
14985 O OG1 . THR E 407 ? 0.4893 0.4957 0.5554 -0.0048 0.2721  -0.0469 407 THR E OG1 
14986 C CG2 . THR E 407 ? 0.4714 0.4962 0.5795 -0.0184 0.2952  -0.0172 407 THR E CG2 
14987 N N   . CYS E 408 ? 0.4418 0.4421 0.4926 -0.0229 0.1885  -0.0304 408 CYS E N   
14988 C CA  . CYS E 408 ? 0.4312 0.4193 0.4632 -0.0211 0.1629  -0.0383 408 CYS E CA  
14989 C C   . CYS E 408 ? 0.4501 0.4244 0.4656 -0.0122 0.1732  -0.0565 408 CYS E C   
14990 O O   . CYS E 408 ? 0.4610 0.4267 0.4877 -0.0092 0.1594  -0.0650 408 CYS E O   
14991 C CB  . CYS E 408 ? 0.4158 0.3920 0.4026 -0.0272 0.1462  -0.0323 408 CYS E CB  
14992 S SG  . CYS E 408 ? 0.4501 0.4357 0.4614 -0.0349 0.1235  -0.0189 408 CYS E SG  
14993 N N   . SER E 409 ? 0.4164 0.3871 0.4095 -0.0073 0.2013  -0.0625 409 SER E N   
14994 C CA  . SER E 409 ? 0.4561 0.4112 0.4287 0.0023  0.2139  -0.0847 409 SER E CA  
14995 C C   . SER E 409 ? 0.5395 0.5029 0.5719 0.0120  0.2271  -0.0929 409 SER E C   
14996 O O   . SER E 409 ? 0.5502 0.4965 0.5804 0.0196  0.2277  -0.1121 409 SER E O   
14997 C CB  . SER E 409 ? 0.5169 0.4623 0.4308 0.0072  0.2418  -0.0889 409 SER E CB  
14998 O OG  . SER E 409 ? 0.5499 0.4855 0.4050 0.0023  0.2250  -0.0812 409 SER E OG  
14999 N N   . ASN E 410 ? 0.5180 0.5073 0.6091 0.0127  0.2366  -0.0803 410 ASN E N   
15000 C CA  . ASN E 410 ? 0.4948 0.4947 0.6466 0.0254  0.2473  -0.0883 410 ASN E CA  
15001 C C   . ASN E 410 ? 0.4696 0.4856 0.6777 0.0273  0.2183  -0.0769 410 ASN E C   
15002 O O   . ASN E 410 ? 0.5367 0.5670 0.8034 0.0400  0.2220  -0.0789 410 ASN E O   
15003 C CB  . ASN E 410 ? 0.4925 0.5133 0.6797 0.0305  0.2859  -0.0884 410 ASN E CB  
15004 C CG  . ASN E 410 ? 0.4821 0.5317 0.7107 0.0193  0.2837  -0.0691 410 ASN E CG  
15005 O OD1 . ASN E 410 ? 0.4452 0.5093 0.7060 0.0136  0.2548  -0.0602 410 ASN E OD1 
15006 N ND2 . ASN E 410 ? 0.5197 0.5738 0.7440 0.0158  0.3071  -0.0620 410 ASN E ND2 
15007 N N   . LEU E 411 ? 0.3850 0.3994 0.5742 0.0171  0.1898  -0.0648 411 LEU E N   
15008 C CA  . LEU E 411 ? 0.3665 0.3914 0.5910 0.0210  0.1615  -0.0540 411 LEU E CA  
15009 C C   . LEU E 411 ? 0.4502 0.4534 0.6802 0.0334  0.1545  -0.0581 411 LEU E C   
15010 O O   . LEU E 411 ? 0.4967 0.5088 0.7691 0.0462  0.1424  -0.0506 411 LEU E O   
15011 C CB  . LEU E 411 ? 0.3706 0.3928 0.5638 0.0088  0.1377  -0.0427 411 LEU E CB  
15012 C CG  . LEU E 411 ? 0.3749 0.4231 0.5959 0.0028  0.1238  -0.0334 411 LEU E CG  
15013 C CD1 . LEU E 411 ? 0.3743 0.4123 0.5615 -0.0034 0.0987  -0.0250 411 LEU E CD1 
15014 C CD2 . LEU E 411 ? 0.3356 0.4119 0.6221 0.0140  0.1161  -0.0333 411 LEU E CD2 
15015 N N   . PHE E 412 ? 0.4801 0.4532 0.6681 0.0300  0.1606  -0.0702 412 PHE E N   
15016 C CA  . PHE E 412 ? 0.4896 0.4350 0.6853 0.0386  0.1574  -0.0762 412 PHE E CA  
15017 C C   . PHE E 412 ? 0.5671 0.4917 0.7493 0.0430  0.1812  -0.1023 412 PHE E C   
15018 O O   . PHE E 412 ? 0.6077 0.5337 0.7507 0.0367  0.1951  -0.1146 412 PHE E O   
15019 C CB  . PHE E 412 ? 0.4701 0.3955 0.6363 0.0280  0.1373  -0.0688 412 PHE E CB  
15020 C CG  . PHE E 412 ? 0.4305 0.3737 0.5948 0.0233  0.1173  -0.0469 412 PHE E CG  
15021 C CD1 . PHE E 412 ? 0.4084 0.3585 0.6012 0.0353  0.1041  -0.0296 412 PHE E CD1 
15022 C CD2 . PHE E 412 ? 0.4315 0.3831 0.5625 0.0091  0.1109  -0.0445 412 PHE E CD2 
15023 C CE1 . PHE E 412 ? 0.3646 0.3297 0.5477 0.0325  0.0852  -0.0139 412 PHE E CE1 
15024 C CE2 . PHE E 412 ? 0.4216 0.3870 0.5504 0.0058  0.0944  -0.0284 412 PHE E CE2 
15025 C CZ  . PHE E 412 ? 0.3853 0.3574 0.5375 0.0171  0.0816  -0.0149 412 PHE E CZ  
15026 N N   . ASP E 413 ? 0.5939 0.4963 0.8052 0.0555  0.1859  -0.1105 413 ASP E N   
15027 C CA  . ASP E 413 ? 0.6411 0.5175 0.8411 0.0610  0.2071  -0.1405 413 ASP E CA  
15028 C C   . ASP E 413 ? 0.6439 0.4925 0.7970 0.0461  0.1949  -0.1563 413 ASP E C   
15029 O O   . ASP E 413 ? 0.6366 0.4633 0.8046 0.0421  0.1803  -0.1514 413 ASP E O   
15030 C CB  . ASP E 413 ? 0.6753 0.5338 0.9306 0.0801  0.2151  -0.1432 413 ASP E CB  
15031 C CG  . ASP E 413 ? 0.7275 0.5666 0.9713 0.0859  0.2349  -0.1722 413 ASP E CG  
15032 O OD1 . ASP E 413 ? 0.7441 0.5674 0.9339 0.0750  0.2365  -0.1953 413 ASP E OD1 
15033 O OD2 . ASP E 413 ? 0.7604 0.6023 1.0457 0.1015  0.2441  -0.1707 413 ASP E OD2 
15034 N N   . LEU E 414 ? 0.6536 0.5028 0.7524 0.0388  0.2014  -0.1751 414 LEU E N   
15035 C CA  . LEU E 414 ? 0.6880 0.5173 0.7453 0.0254  0.1841  -0.1931 414 LEU E CA  
15036 C C   . LEU E 414 ? 0.8164 0.6169 0.8518 0.0311  0.1972  -0.2338 414 LEU E C   
15037 O O   . LEU E 414 ? 0.8799 0.6686 0.8709 0.0221  0.1829  -0.2570 414 LEU E O   
15038 C CB  . LEU E 414 ? 0.6159 0.4654 0.6212 0.0145  0.1729  -0.1841 414 LEU E CB  
15039 C CG  . LEU E 414 ? 0.5389 0.4132 0.5628 0.0078  0.1588  -0.1491 414 LEU E CG  
15040 C CD1 . LEU E 414 ? 0.5032 0.3930 0.4802 -0.0007 0.1508  -0.1404 414 LEU E CD1 
15041 C CD2 . LEU E 414 ? 0.5348 0.3975 0.5886 0.0007  0.1389  -0.1397 414 LEU E CD2 
15042 N N   . ASN E 415 ? 0.8408 0.6376 0.9074 0.0462  0.2158  -0.2368 415 ASN E N   
15043 C CA  . ASN E 415 ? 0.9012 0.6755 0.9502 0.0523  0.2202  -0.2664 415 ASN E CA  
15044 C C   . ASN E 415 ? 0.8745 0.6189 0.9615 0.0464  0.2038  -0.2730 415 ASN E C   
15045 O O   . ASN E 415 ? 0.8029 0.5441 0.9461 0.0500  0.2035  -0.2495 415 ASN E O   
15046 C CB  . ASN E 415 ? 0.9567 0.7397 1.0271 0.0708  0.2477  -0.2661 415 ASN E CB  
15047 C CG  . ASN E 415 ? 0.9612 0.7753 1.0025 0.0748  0.2678  -0.2552 415 ASN E CG  
15048 O OD1 . ASN E 415 ? 0.9935 0.8100 0.9685 0.0693  0.2662  -0.2631 415 ASN E OD1 
15049 N ND2 . ASN E 415 ? 0.9403 0.7791 1.0335 0.0844  0.2851  -0.2351 415 ASN E ND2 
15050 N N   . ASN E 416 ? 0.9346 0.6579 0.9897 0.0386  0.1897  -0.3034 416 ASN E N   
15051 C CA  . ASN E 416 ? 0.9850 0.6788 1.0747 0.0293  0.1743  -0.3142 416 ASN E CA  
15052 C C   . ASN E 416 ? 1.0019 0.6740 1.1498 0.0407  0.1879  -0.3072 416 ASN E C   
15053 O O   . ASN E 416 ? 0.9937 0.6406 1.1768 0.0326  0.1790  -0.3095 416 ASN E O   
15054 C CB  . ASN E 416 ? 1.0594 0.7374 1.1000 0.0239  0.1597  -0.3541 416 ASN E CB  
15055 C CG  . ASN E 416 ? 1.1224 0.8060 1.1006 0.0399  0.1756  -0.3730 416 ASN E CG  
15056 O OD1 . ASN E 416 ? 1.1462 0.8209 1.1357 0.0561  0.1984  -0.3794 416 ASN E OD1 
15057 N ND2 . ASN E 416 ? 1.1429 0.8423 1.0548 0.0372  0.1652  -0.3787 416 ASN E ND2 
15058 N N   . SER F 10  ? 1.1801 0.7854 1.3129 0.1631  0.1307  0.2279  10  SER F N   
15059 C CA  . SER F 10  ? 1.1698 0.7686 1.3012 0.1494  0.1236  0.1868  10  SER F CA  
15060 C C   . SER F 10  ? 1.0972 0.7312 1.1975 0.1401  0.1031  0.1813  10  SER F C   
15061 O O   . SER F 10  ? 1.0877 0.7226 1.1828 0.1312  0.0954  0.1517  10  SER F O   
15062 C CB  . SER F 10  ? 1.1956 0.7966 1.3421 0.1674  0.1238  0.1752  10  SER F CB  
15063 O OG  . SER F 10  ? 1.1665 0.8116 1.2920 0.1794  0.1048  0.1780  10  SER F OG  
15064 N N   . LYS F 11  ? 1.0281 0.6920 1.1094 0.1413  0.0959  0.2090  11  LYS F N   
15065 C CA  . LYS F 11  ? 0.9355 0.6390 0.9902 0.1345  0.0777  0.2069  11  LYS F CA  
15066 C C   . LYS F 11  ? 0.7945 0.4847 0.8421 0.1091  0.0792  0.2001  11  LYS F C   
15067 O O   . LYS F 11  ? 0.8032 0.4889 0.8521 0.1049  0.0879  0.2200  11  LYS F O   
15068 C CB  . LYS F 11  ? 0.9755 0.7391 1.0140 0.1531  0.0666  0.2372  11  LYS F CB  
15069 C CG  . LYS F 11  ? 1.1054 0.9099 1.1209 0.1401  0.0550  0.2436  11  LYS F CG  
15070 C CD  . LYS F 11  ? 1.0645 0.9184 1.0708 0.1512  0.0540  0.2767  11  LYS F CD  
15071 C CE  . LYS F 11  ? 0.9526 0.8439 0.9407 0.1341  0.0470  0.2812  11  LYS F CE  
15072 N NZ  . LYS F 11  ? 0.9035 0.8561 0.8821 0.1449  0.0451  0.3088  11  LYS F NZ  
15073 N N   . PRO F 12  ? 0.6549 0.3368 0.6973 0.0917  0.0723  0.1705  12  PRO F N   
15074 C CA  . PRO F 12  ? 0.6680 0.3434 0.7062 0.0643  0.0710  0.1532  12  PRO F CA  
15075 C C   . PRO F 12  ? 0.6886 0.4095 0.7078 0.0597  0.0600  0.1710  12  PRO F C   
15076 O O   . PRO F 12  ? 0.6806 0.4497 0.6855 0.0717  0.0472  0.1824  12  PRO F O   
15077 C CB  . PRO F 12  ? 0.5373 0.2217 0.5692 0.0493  0.0570  0.1118  12  PRO F CB  
15078 C CG  . PRO F 12  ? 0.5181 0.2324 0.5400 0.0660  0.0456  0.1134  12  PRO F CG  
15079 C CD  . PRO F 12  ? 0.6080 0.3096 0.6430 0.0922  0.0584  0.1424  12  PRO F CD  
15080 N N   . ASN F 13  ? 0.7080 0.4173 0.7294 0.0406  0.0665  0.1698  13  ASN F N   
15081 C CA  . ASN F 13  ? 0.7016 0.4546 0.7082 0.0334  0.0589  0.1833  13  ASN F CA  
15082 C C   . ASN F 13  ? 0.6301 0.4040 0.6311 0.0101  0.0438  0.1483  13  ASN F C   
15083 O O   . ASN F 13  ? 0.5752 0.3895 0.5675 0.0012  0.0359  0.1501  13  ASN F O   
15084 C CB  . ASN F 13  ? 0.8165 0.5462 0.8302 0.0295  0.0786  0.2111  13  ASN F CB  
15085 C CG  . ASN F 13  ? 0.9444 0.6748 0.9594 0.0551  0.0885  0.2496  13  ASN F CG  
15086 O OD1 . ASN F 13  ? 0.9777 0.7601 0.9778 0.0702  0.0795  0.2734  13  ASN F OD1 
15087 N ND2 . ASN F 13  ? 0.9996 0.6839 1.0339 0.0583  0.1044  0.2475  13  ASN F ND2 
15088 N N   . LEU F 14  ? 0.4890 0.2390 0.4969 0.0011  0.0403  0.1166  14  LEU F N   
15089 C CA  . LEU F 14  ? 0.4548 0.2224 0.4600 -0.0175 0.0261  0.0858  14  LEU F CA  
15090 C C   . LEU F 14  ? 0.4435 0.2007 0.4491 -0.0165 0.0184  0.0603  14  LEU F C   
15091 O O   . LEU F 14  ? 0.4876 0.2112 0.5031 -0.0132 0.0295  0.0541  14  LEU F O   
15092 C CB  . LEU F 14  ? 0.4666 0.2181 0.4826 -0.0386 0.0345  0.0743  14  LEU F CB  
15093 C CG  . LEU F 14  ? 0.4322 0.2109 0.4480 -0.0558 0.0192  0.0468  14  LEU F CG  
15094 C CD1 . LEU F 14  ? 0.4053 0.2294 0.4138 -0.0570 0.0092  0.0553  14  LEU F CD1 
15095 C CD2 . LEU F 14  ? 0.4487 0.2082 0.4788 -0.0757 0.0292  0.0299  14  LEU F CD2 
15096 N N   . LEU F 15  ? 0.4082 0.1964 0.4045 -0.0189 0.0012  0.0467  15  LEU F N   
15097 C CA  . LEU F 15  ? 0.4249 0.2113 0.4174 -0.0185 -0.0073 0.0261  15  LEU F CA  
15098 C C   . LEU F 15  ? 0.4387 0.2397 0.4320 -0.0332 -0.0191 0.0054  15  LEU F C   
15099 O O   . LEU F 15  ? 0.4297 0.2497 0.4259 -0.0405 -0.0237 0.0072  15  LEU F O   
15100 C CB  . LEU F 15  ? 0.4225 0.2317 0.4039 -0.0048 -0.0152 0.0333  15  LEU F CB  
15101 C CG  . LEU F 15  ? 0.4490 0.2593 0.4295 0.0134  -0.0071 0.0562  15  LEU F CG  
15102 C CD1 . LEU F 15  ? 0.4078 0.2521 0.3787 0.0216  -0.0166 0.0566  15  LEU F CD1 
15103 C CD2 . LEU F 15  ? 0.4268 0.1999 0.4166 0.0215  0.0057  0.0547  15  LEU F CD2 
15104 N N   . VAL F 16  ? 0.4584 0.2544 0.4510 -0.0371 -0.0235 -0.0147 16  VAL F N   
15105 C CA  . VAL F 16  ? 0.4663 0.2792 0.4615 -0.0486 -0.0348 -0.0325 16  VAL F CA  
15106 C C   . VAL F 16  ? 0.4373 0.2663 0.4217 -0.0444 -0.0471 -0.0410 16  VAL F C   
15107 O O   . VAL F 16  ? 0.4399 0.2621 0.4185 -0.0415 -0.0442 -0.0492 16  VAL F O   
15108 C CB  . VAL F 16  ? 0.5146 0.3140 0.5229 -0.0628 -0.0267 -0.0526 16  VAL F CB  
15109 C CG1 . VAL F 16  ? 0.4795 0.3054 0.4912 -0.0719 -0.0405 -0.0705 16  VAL F CG1 
15110 C CG2 . VAL F 16  ? 0.4492 0.2286 0.4691 -0.0691 -0.0111 -0.0422 16  VAL F CG2 
15111 N N   . LEU F 17  ? 0.4120 0.2632 0.3959 -0.0448 -0.0595 -0.0393 17  LEU F N   
15112 C CA  . LEU F 17  ? 0.4185 0.2851 0.3928 -0.0402 -0.0703 -0.0416 17  LEU F CA  
15113 C C   . LEU F 17  ? 0.4570 0.3429 0.4387 -0.0460 -0.0814 -0.0525 17  LEU F C   
15114 O O   . LEU F 17  ? 0.4416 0.3379 0.4357 -0.0476 -0.0865 -0.0494 17  LEU F O   
15115 C CB  . LEU F 17  ? 0.4327 0.3075 0.4034 -0.0324 -0.0728 -0.0263 17  LEU F CB  
15116 C CG  . LEU F 17  ? 0.4371 0.3234 0.3983 -0.0274 -0.0806 -0.0236 17  LEU F CG  
15117 C CD1 . LEU F 17  ? 0.4483 0.3291 0.3928 -0.0238 -0.0766 -0.0270 17  LEU F CD1 
15118 C CD2 . LEU F 17  ? 0.4348 0.3277 0.4020 -0.0238 -0.0800 -0.0123 17  LEU F CD2 
15119 N N   . PRO F 18  ? 0.4759 0.3719 0.4523 -0.0491 -0.0848 -0.0675 18  PRO F N   
15120 C CA  . PRO F 18  ? 0.4637 0.3881 0.4456 -0.0515 -0.0973 -0.0769 18  PRO F CA  
15121 C C   . PRO F 18  ? 0.4679 0.4089 0.4439 -0.0400 -0.1091 -0.0594 18  PRO F C   
15122 O O   . PRO F 18  ? 0.4364 0.3746 0.3967 -0.0330 -0.1084 -0.0480 18  PRO F O   
15123 C CB  . PRO F 18  ? 0.4889 0.4265 0.4646 -0.0579 -0.0957 -0.0989 18  PRO F CB  
15124 C CG  . PRO F 18  ? 0.4925 0.3981 0.4695 -0.0623 -0.0784 -0.1047 18  PRO F CG  
15125 C CD  . PRO F 18  ? 0.4955 0.3814 0.4649 -0.0516 -0.0756 -0.0802 18  PRO F CD  
15126 N N   . VAL F 19  ? 0.4803 0.4378 0.4719 -0.0383 -0.1183 -0.0576 19  VAL F N   
15127 C CA  . VAL F 19  ? 0.5103 0.4790 0.5049 -0.0264 -0.1270 -0.0389 19  VAL F CA  
15128 C C   . VAL F 19  ? 0.5259 0.5297 0.5274 -0.0219 -0.1412 -0.0434 19  VAL F C   
15129 O O   . VAL F 19  ? 0.5077 0.5260 0.5198 -0.0305 -0.1435 -0.0640 19  VAL F O   
15130 C CB  A VAL F 19  ? 0.4302 0.3847 0.4463 -0.0261 -0.1220 -0.0309 19  VAL F CB  
15131 C CB  B VAL F 19  ? 0.4304 0.3856 0.4463 -0.0253 -0.1225 -0.0298 19  VAL F CB  
15132 C CG1 A VAL F 19  ? 0.4374 0.4012 0.4695 -0.0152 -0.1284 -0.0160 19  VAL F CG1 
15133 C CG1 B VAL F 19  ? 0.4190 0.3517 0.4277 -0.0287 -0.1099 -0.0261 19  VAL F CG1 
15134 C CG2 A VAL F 19  ? 0.4194 0.3519 0.4265 -0.0276 -0.1100 -0.0242 19  VAL F CG2 
15135 C CG2 B VAL F 19  ? 0.4157 0.3801 0.4558 -0.0326 -0.1245 -0.0438 19  VAL F CG2 
15136 N N   . GLN F 20  ? 0.5158 0.5356 0.5119 -0.0082 -0.1498 -0.0235 20  GLN F N   
15137 C CA  . GLN F 20  ? 0.4879 0.5487 0.4887 0.0009  -0.1649 -0.0215 20  GLN F CA  
15138 C C   . GLN F 20  ? 0.4499 0.5129 0.4704 0.0179  -0.1708 0.0050  20  GLN F C   
15139 O O   . GLN F 20  ? 0.4805 0.5198 0.4986 0.0245  -0.1638 0.0272  20  GLN F O   
15140 C CB  . GLN F 20  ? 0.5189 0.6095 0.4904 0.0033  -0.1704 -0.0208 20  GLN F CB  
15141 C CG  . GLN F 20  ? 0.5593 0.7055 0.5325 0.0113  -0.1868 -0.0234 20  GLN F CG  
15142 C CD  . GLN F 20  ? 0.5960 0.7827 0.5399 0.0099  -0.1913 -0.0299 20  GLN F CD  
15143 O OE1 . GLN F 20  ? 0.6250 0.8422 0.5539 0.0244  -0.2005 -0.0049 20  GLN F OE1 
15144 N NE2 . GLN F 20  ? 0.5935 0.7830 0.5310 -0.0079 -0.1835 -0.0634 20  GLN F NE2 
15145 N N   . GLU F 21  ? 0.4048 0.4971 0.4474 0.0254  -0.1824 0.0022  21  GLU F N   
15146 C CA  . GLU F 21  ? 0.3941 0.4893 0.4613 0.0445  -0.1874 0.0282  21  GLU F CA  
15147 C C   . GLU F 21  ? 0.4235 0.5466 0.4728 0.0636  -0.1972 0.0585  21  GLU F C   
15148 O O   . GLU F 21  ? 0.4422 0.6106 0.4708 0.0650  -0.2090 0.0518  21  GLU F O   
15149 C CB  . GLU F 21  ? 0.3884 0.5073 0.4903 0.0472  -0.1960 0.0135  21  GLU F CB  
15150 C CG  . GLU F 21  ? 0.4333 0.5417 0.5739 0.0642  -0.1953 0.0344  21  GLU F CG  
15151 C CD  . GLU F 21  ? 0.5327 0.6813 0.6806 0.0894  -0.2112 0.0587  21  GLU F CD  
15152 O OE1 . GLU F 21  ? 0.5595 0.7503 0.6785 0.0922  -0.2236 0.0579  21  GLU F OE1 
15153 O OE2 . GLU F 21  ? 0.5628 0.7048 0.7475 0.1070  -0.2108 0.0779  21  GLU F OE2 
15154 N N   . ASP F 22  ? 0.4380 0.5372 0.4966 0.0776  -0.1909 0.0914  22  ASP F N   
15155 C CA  . ASP F 22  ? 0.4668 0.5916 0.5109 0.0981  -0.1989 0.1275  22  ASP F CA  
15156 C C   . ASP F 22  ? 0.4893 0.6335 0.5702 0.1204  -0.2086 0.1462  22  ASP F C   
15157 O O   . ASP F 22  ? 0.4948 0.6032 0.6141 0.1258  -0.1984 0.1549  22  ASP F O   
15158 C CB  . ASP F 22  ? 0.4864 0.5717 0.5191 0.1002  -0.1832 0.1556  22  ASP F CB  
15159 C CG  . ASP F 22  ? 0.5504 0.6588 0.5678 0.1214  -0.1885 0.1987  22  ASP F CG  
15160 O OD1 . ASP F 22  ? 0.5698 0.7238 0.5507 0.1222  -0.1995 0.1982  22  ASP F OD1 
15161 O OD2 . ASP F 22  ? 0.5864 0.6651 0.6275 0.1354  -0.1774 0.2278  22  ASP F OD2 
15162 N N   . ALA F 23  ? 0.5054 0.7102 0.5775 0.1335  -0.2277 0.1502  23  ALA F N   
15163 C CA  . ALA F 23  ? 0.5377 0.7679 0.6444 0.1552  -0.2381 0.1604  23  ALA F CA  
15164 C C   . ALA F 23  ? 0.5821 0.7762 0.7039 0.1773  -0.2257 0.1991  23  ALA F C   
15165 O O   . ALA F 23  ? 0.5715 0.7518 0.7373 0.1901  -0.2219 0.2035  23  ALA F O   
15166 C CB  . ALA F 23  ? 0.6096 0.9004 0.6950 0.1575  -0.2547 0.1484  23  ALA F CB  
15167 N N   . SER F 24  ? 0.6220 0.8022 0.7085 0.1794  -0.2175 0.2246  24  SER F N   
15168 C CA  . SER F 24  ? 0.6694 0.8159 0.7657 0.1964  -0.2036 0.2618  24  SER F CA  
15169 C C   . SER F 24  ? 0.6479 0.7355 0.7886 0.1936  -0.1825 0.2631  24  SER F C   
15170 O O   . SER F 24  ? 0.6634 0.7356 0.8424 0.2089  -0.1761 0.2747  24  SER F O   
15171 C CB  . SER F 24  ? 0.7320 0.8723 0.7833 0.1914  -0.1954 0.2835  24  SER F CB  
15172 O OG  . SER F 24  ? 0.8082 0.9106 0.8707 0.2031  -0.1781 0.3185  24  SER F OG  
15173 N N   . THR F 25  ? 0.6001 0.6577 0.7391 0.1723  -0.1717 0.2474  25  THR F N   
15174 C CA  . THR F 25  ? 0.5743 0.5771 0.7536 0.1635  -0.1492 0.2434  25  THR F CA  
15175 C C   . THR F 25  ? 0.5411 0.5414 0.7632 0.1518  -0.1532 0.2091  25  THR F C   
15176 O O   . THR F 25  ? 0.5222 0.4885 0.7885 0.1473  -0.1360 0.1998  25  THR F O   
15177 C CB  . THR F 25  ? 0.5349 0.5056 0.6897 0.1457  -0.1342 0.2445  25  THR F CB  
15178 O OG1 . THR F 25  ? 0.5217 0.5107 0.6512 0.1282  -0.1470 0.2183  25  THR F OG1 
15179 C CG2 . THR F 25  ? 0.6648 0.6385 0.7786 0.1534  -0.1294 0.2749  25  THR F CG2 
15180 N N   . GLY F 26  ? 0.4689 0.5065 0.6746 0.1429  -0.1725 0.1828  26  GLY F N   
15181 C CA  . GLY F 26  ? 0.4311 0.4661 0.6615 0.1254  -0.1709 0.1411  26  GLY F CA  
15182 C C   . GLY F 26  ? 0.4387 0.4426 0.6535 0.0988  -0.1557 0.1160  26  GLY F C   
15183 O O   . GLY F 26  ? 0.4306 0.4300 0.6646 0.0829  -0.1510 0.0847  26  GLY F O   
15184 N N   . LEU F 27  ? 0.4414 0.4285 0.6204 0.0942  -0.1483 0.1301  27  LEU F N   
15185 C CA  . LEU F 27  ? 0.3874 0.3499 0.5511 0.0723  -0.1347 0.1093  27  LEU F CA  
15186 C C   . LEU F 27  ? 0.4430 0.4251 0.5635 0.0600  -0.1444 0.0907  27  LEU F C   
15187 O O   . LEU F 27  ? 0.4703 0.4850 0.5698 0.0672  -0.1598 0.0945  27  LEU F O   
15188 C CB  . LEU F 27  ? 0.4049 0.3368 0.5617 0.0731  -0.1178 0.1314  27  LEU F CB  
15189 C CG  . LEU F 27  ? 0.4450 0.3514 0.6525 0.0835  -0.1029 0.1478  27  LEU F CG  
15190 C CD1 . LEU F 27  ? 0.4679 0.3439 0.6705 0.0838  -0.0838 0.1711  27  LEU F CD1 
15191 C CD2 . LEU F 27  ? 0.4141 0.3115 0.6649 0.0699  -0.0923 0.1150  27  LEU F CD2 
15192 N N   . HIS F 28  ? 0.3950 0.3598 0.5055 0.0419  -0.1343 0.0698  28  HIS F N   
15193 C CA  . HIS F 28  ? 0.3747 0.3493 0.4515 0.0295  -0.1388 0.0510  28  HIS F CA  
15194 C C   . HIS F 28  ? 0.4003 0.3571 0.4476 0.0241  -0.1287 0.0569  28  HIS F C   
15195 O O   . HIS F 28  ? 0.4086 0.3436 0.4662 0.0230  -0.1154 0.0647  28  HIS F O   
15196 C CB  . HIS F 28  ? 0.3464 0.3194 0.4382 0.0148  -0.1358 0.0230  28  HIS F CB  
15197 C CG  . HIS F 28  ? 0.3104 0.3056 0.4292 0.0173  -0.1457 0.0118  28  HIS F CG  
15198 N ND1 . HIS F 28  ? 0.3450 0.3622 0.4550 0.0098  -0.1544 -0.0080 28  HIS F ND1 
15199 C CD2 . HIS F 28  ? 0.3104 0.3101 0.4686 0.0259  -0.1467 0.0151  28  HIS F CD2 
15200 C CE1 . HIS F 28  ? 0.3420 0.3795 0.4822 0.0136  -0.1616 -0.0164 28  HIS F CE1 
15201 N NE2 . HIS F 28  ? 0.3058 0.3332 0.4762 0.0244  -0.1577 -0.0021 28  HIS F NE2 
15202 N N   . TRP F 29  ? 0.4194 0.3888 0.4330 0.0203  -0.1340 0.0505  29  TRP F N   
15203 C CA  . TRP F 29  ? 0.4226 0.3806 0.4084 0.0162  -0.1256 0.0541  29  TRP F CA  
15204 C C   . TRP F 29  ? 0.4480 0.4120 0.4135 0.0057  -0.1268 0.0310  29  TRP F C   
15205 O O   . TRP F 29  ? 0.4547 0.4349 0.4247 0.0021  -0.1346 0.0154  29  TRP F O   
15206 C CB  . TRP F 29  ? 0.4264 0.3972 0.3923 0.0268  -0.1289 0.0787  29  TRP F CB  
15207 C CG  . TRP F 29  ? 0.4754 0.4845 0.4239 0.0307  -0.1439 0.0752  29  TRP F CG  
15208 C CD1 . TRP F 29  ? 0.5178 0.5551 0.4799 0.0407  -0.1575 0.0801  29  TRP F CD1 
15209 C CD2 . TRP F 29  ? 0.5119 0.5429 0.4288 0.0243  -0.1466 0.0623  29  TRP F CD2 
15210 N NE1 . TRP F 29  ? 0.5336 0.6135 0.4726 0.0400  -0.1689 0.0702  29  TRP F NE1 
15211 C CE2 . TRP F 29  ? 0.5420 0.6180 0.4540 0.0289  -0.1616 0.0578  29  TRP F CE2 
15212 C CE3 . TRP F 29  ? 0.5238 0.5444 0.4190 0.0151  -0.1371 0.0517  29  TRP F CE3 
15213 C CZ2 . TRP F 29  ? 0.5445 0.6567 0.4313 0.0223  -0.1661 0.0403  29  TRP F CZ2 
15214 C CZ3 . TRP F 29  ? 0.5211 0.5723 0.3933 0.0097  -0.1412 0.0356  29  TRP F CZ3 
15215 C CH2 . TRP F 29  ? 0.5443 0.6417 0.4124 0.0122  -0.1549 0.0288  29  TRP F CH2 
15216 N N   . ALA F 30  ? 0.4578 0.4088 0.4049 0.0008  -0.1176 0.0278  30  ALA F N   
15217 C CA  . ALA F 30  ? 0.4236 0.3753 0.3564 -0.0074 -0.1155 0.0072  30  ALA F CA  
15218 C C   . ALA F 30  ? 0.4299 0.3853 0.3367 -0.0071 -0.1110 0.0090  30  ALA F C   
15219 O O   . ALA F 30  ? 0.4657 0.4124 0.3669 -0.0036 -0.1047 0.0239  30  ALA F O   
15220 C CB  . ALA F 30  ? 0.4167 0.3461 0.3624 -0.0139 -0.1061 -0.0028 30  ALA F CB  
15221 N N   . ASN F 31  ? 0.4557 0.4252 0.3496 -0.0124 -0.1122 -0.0091 31  ASN F N   
15222 C CA  . ASN F 31  ? 0.4922 0.4633 0.3664 -0.0142 -0.1049 -0.0139 31  ASN F CA  
15223 C C   . ASN F 31  ? 0.5269 0.4688 0.4087 -0.0164 -0.0928 -0.0217 31  ASN F C   
15224 O O   . ASN F 31  ? 0.5859 0.5163 0.4794 -0.0209 -0.0891 -0.0369 31  ASN F O   
15225 C CB  . ASN F 31  ? 0.4821 0.4828 0.3443 -0.0203 -0.1081 -0.0352 31  ASN F CB  
15226 C CG  . ASN F 31  ? 0.5135 0.5545 0.3564 -0.0161 -0.1182 -0.0234 31  ASN F CG  
15227 O OD1 . ASN F 31  ? 0.5348 0.5770 0.3636 -0.0102 -0.1169 -0.0009 31  ASN F OD1 
15228 N ND2 . ASN F 31  ? 0.5476 0.6256 0.3902 -0.0193 -0.1275 -0.0382 31  ASN F ND2 
15229 N N   . ILE F 32  ? 0.5005 0.4325 0.3771 -0.0128 -0.0856 -0.0103 32  ILE F N   
15230 C CA  . ILE F 32  ? 0.5079 0.4210 0.3910 -0.0119 -0.0751 -0.0155 32  ILE F CA  
15231 C C   . ILE F 32  ? 0.4805 0.3979 0.3503 -0.0119 -0.0680 -0.0265 32  ILE F C   
15232 O O   . ILE F 32  ? 0.4678 0.4015 0.3206 -0.0127 -0.0683 -0.0231 32  ILE F O   
15233 C CB  . ILE F 32  ? 0.5366 0.4427 0.4283 -0.0087 -0.0703 -0.0015 32  ILE F CB  
15234 C CG1 . ILE F 32  ? 0.5335 0.4376 0.4430 -0.0096 -0.0755 0.0060  32  ILE F CG1 
15235 C CG2 . ILE F 32  ? 0.5317 0.4291 0.4303 -0.0058 -0.0615 -0.0063 32  ILE F CG2 
15236 C CD1 . ILE F 32  ? 0.5276 0.4244 0.4510 -0.0120 -0.0761 -0.0021 32  ILE F CD1 
15237 N N   . HIS F 33  ? 0.4746 0.3779 0.3539 -0.0108 -0.0603 -0.0390 33  HIS F N   
15238 C CA  . HIS F 33  ? 0.4685 0.3745 0.3424 -0.0098 -0.0520 -0.0527 33  HIS F CA  
15239 C C   . HIS F 33  ? 0.4434 0.3462 0.3176 -0.0024 -0.0448 -0.0451 33  HIS F C   
15240 O O   . HIS F 33  ? 0.4321 0.3235 0.3190 0.0039  -0.0418 -0.0372 33  HIS F O   
15241 C CB  . HIS F 33  ? 0.5090 0.3995 0.3988 -0.0112 -0.0447 -0.0707 33  HIS F CB  
15242 C CG  . HIS F 33  ? 0.5798 0.4808 0.4712 -0.0213 -0.0493 -0.0864 33  HIS F CG  
15243 N ND1 . HIS F 33  ? 0.6305 0.5304 0.5279 -0.0246 -0.0573 -0.0801 33  HIS F ND1 
15244 C CD2 . HIS F 33  ? 0.5853 0.5055 0.4743 -0.0299 -0.0470 -0.1112 33  HIS F CD2 
15245 C CE1 . HIS F 33  ? 0.6390 0.5570 0.5376 -0.0340 -0.0602 -0.0998 33  HIS F CE1 
15246 N NE2 . HIS F 33  ? 0.6055 0.5378 0.4989 -0.0378 -0.0539 -0.1196 33  HIS F NE2 
15247 N N   . LYS F 34  ? 0.4592 0.3781 0.3186 -0.0039 -0.0419 -0.0482 34  LYS F N   
15248 C CA  . LYS F 34  ? 0.4417 0.3649 0.3009 0.0013  -0.0345 -0.0446 34  LYS F CA  
15249 C C   . LYS F 34  ? 0.4348 0.3712 0.2860 0.0004  -0.0272 -0.0610 34  LYS F C   
15250 O O   . LYS F 34  ? 0.4433 0.3912 0.2847 -0.0065 -0.0283 -0.0737 34  LYS F O   
15251 C CB  . LYS F 34  ? 0.4611 0.3925 0.3125 -0.0022 -0.0357 -0.0286 34  LYS F CB  
15252 C CG  . LYS F 34  ? 0.5153 0.4375 0.3777 -0.0026 -0.0415 -0.0152 34  LYS F CG  
15253 C CD  . LYS F 34  ? 0.5134 0.4346 0.3929 0.0024  -0.0367 -0.0128 34  LYS F CD  
15254 C CE  . LYS F 34  ? 0.4616 0.3974 0.3407 0.0015  -0.0275 -0.0132 34  LYS F CE  
15255 N NZ  . LYS F 34  ? 0.4687 0.4041 0.3476 -0.0064 -0.0257 -0.0030 34  LYS F NZ  
15256 N N   . ARG F 35  ? 0.4422 0.3829 0.2992 0.0070  -0.0196 -0.0627 35  ARG F N   
15257 C CA  . ARG F 35  ? 0.4345 0.3924 0.2855 0.0061  -0.0114 -0.0781 35  ARG F CA  
15258 C C   . ARG F 35  ? 0.4741 0.4270 0.3394 0.0107  -0.0050 -0.1000 35  ARG F C   
15259 O O   . ARG F 35  ? 0.5202 0.4540 0.3992 0.0127  -0.0058 -0.1040 35  ARG F O   
15260 C CB  . ARG F 35  ? 0.4580 0.4358 0.2837 -0.0065 -0.0127 -0.0770 35  ARG F CB  
15261 C CG  . ARG F 35  ? 0.4543 0.4319 0.2716 -0.0103 -0.0148 -0.0542 35  ARG F CG  
15262 C CD  . ARG F 35  ? 0.5327 0.5257 0.3257 -0.0201 -0.0166 -0.0443 35  ARG F CD  
15263 N NE  . ARG F 35  ? 0.5641 0.5460 0.3581 -0.0209 -0.0196 -0.0199 35  ARG F NE  
15264 C CZ  . ARG F 35  ? 0.6643 0.6539 0.4418 -0.0260 -0.0202 -0.0009 35  ARG F CZ  
15265 N NH1 . ARG F 35  ? 0.7213 0.7358 0.4746 -0.0317 -0.0191 -0.0026 35  ARG F NH1 
15266 N NH2 . ARG F 35  ? 0.6982 0.6724 0.4850 -0.0248 -0.0209 0.0204  35  ARG F NH2 
15267 N N   . THR F 36  ? 0.4482 0.4179 0.3137 0.0118  0.0035  -0.1156 36  THR F N   
15268 C CA  . THR F 36  ? 0.4527 0.4221 0.3342 0.0139  0.0124  -0.1417 36  THR F CA  
15269 C C   . THR F 36  ? 0.4682 0.4702 0.3305 0.0002  0.0162  -0.1605 36  THR F C   
15270 O O   . THR F 36  ? 0.5027 0.5240 0.3549 -0.0010 0.0201  -0.1599 36  THR F O   
15271 C CB  . THR F 36  ? 0.4612 0.4234 0.3688 0.0318  0.0209  -0.1450 36  THR F CB  
15272 O OG1 . THR F 36  ? 0.5044 0.4459 0.4243 0.0447  0.0167  -0.1220 36  THR F OG1 
15273 C CG2 . THR F 36  ? 0.4794 0.4327 0.4126 0.0353  0.0325  -0.1717 36  THR F CG2 
15274 N N   . PRO F 37  ? 0.4822 0.4957 0.3390 -0.0116 0.0160  -0.1787 37  PRO F N   
15275 C CA  . PRO F 37  ? 0.4929 0.4892 0.3633 -0.0140 0.0136  -0.1861 37  PRO F CA  
15276 C C   . PRO F 37  ? 0.5150 0.5006 0.3720 -0.0156 0.0000  -0.1593 37  PRO F C   
15277 O O   . PRO F 37  ? 0.5255 0.5238 0.3587 -0.0188 -0.0079 -0.1382 37  PRO F O   
15278 C CB  . PRO F 37  ? 0.5067 0.5378 0.3706 -0.0297 0.0180  -0.2183 37  PRO F CB  
15279 C CG  . PRO F 37  ? 0.5094 0.5770 0.3424 -0.0372 0.0161  -0.2132 37  PRO F CG  
15280 C CD  . PRO F 37  ? 0.5138 0.5673 0.3514 -0.0255 0.0202  -0.1984 37  PRO F CD  
15281 N N   . LEU F 38  ? 0.4993 0.4593 0.3755 -0.0132 -0.0006 -0.1604 38  LEU F N   
15282 C CA  . LEU F 38  ? 0.4625 0.4106 0.3326 -0.0133 -0.0122 -0.1375 38  LEU F CA  
15283 C C   . LEU F 38  ? 0.4953 0.4738 0.3419 -0.0254 -0.0228 -0.1372 38  LEU F C   
15284 O O   . LEU F 38  ? 0.5222 0.5263 0.3660 -0.0355 -0.0208 -0.1618 38  LEU F O   
15285 C CB  . LEU F 38  ? 0.4645 0.3807 0.3615 -0.0098 -0.0078 -0.1417 38  LEU F CB  
15286 C CG  . LEU F 38  ? 0.4940 0.3883 0.3947 -0.0044 -0.0151 -0.1159 38  LEU F CG  
15287 C CD1 . LEU F 38  ? 0.4755 0.3633 0.3757 0.0082  -0.0156 -0.0931 38  LEU F CD1 
15288 C CD2 . LEU F 38  ? 0.5339 0.3988 0.4617 -0.0031 -0.0058 -0.1248 38  LEU F CD2 
15289 N N   . MET F 39  ? 0.4723 0.4516 0.3043 -0.0237 -0.0334 -0.1098 39  MET F N   
15290 C CA  . MET F 39  ? 0.5150 0.5230 0.3272 -0.0308 -0.0445 -0.1029 39  MET F CA  
15291 C C   . MET F 39  ? 0.5396 0.5309 0.3555 -0.0260 -0.0545 -0.0775 39  MET F C   
15292 O O   . MET F 39  ? 0.5617 0.5237 0.3927 -0.0194 -0.0520 -0.0671 39  MET F O   
15293 C CB  . MET F 39  ? 0.4938 0.5328 0.2784 -0.0344 -0.0442 -0.0940 39  MET F CB  
15294 C CG  . MET F 39  ? 0.4809 0.5033 0.2630 -0.0289 -0.0382 -0.0747 39  MET F CG  
15295 S SD  . MET F 39  ? 0.6115 0.6135 0.3949 -0.0233 -0.0448 -0.0382 39  MET F SD  
15296 C CE  . MET F 39  ? 0.5380 0.5741 0.2926 -0.0277 -0.0520 -0.0184 39  MET F CE  
15297 N N   . GLN F 40  ? 0.5484 0.5633 0.3525 -0.0288 -0.0657 -0.0691 40  GLN F N   
15298 C CA  . GLN F 40  ? 0.5357 0.5386 0.3476 -0.0241 -0.0751 -0.0483 40  GLN F CA  
15299 C C   . GLN F 40  ? 0.5456 0.5534 0.3449 -0.0192 -0.0790 -0.0173 40  GLN F C   
15300 O O   . GLN F 40  ? 0.5553 0.5922 0.3328 -0.0204 -0.0811 -0.0086 40  GLN F O   
15301 C CB  . GLN F 40  ? 0.5724 0.5970 0.3881 -0.0283 -0.0848 -0.0602 40  GLN F CB  
15302 C CG  . GLN F 40  ? 0.6119 0.6220 0.4483 -0.0342 -0.0785 -0.0882 40  GLN F CG  
15303 C CD  . GLN F 40  ? 0.6382 0.6737 0.4806 -0.0404 -0.0871 -0.1026 40  GLN F CD  
15304 O OE1 . GLN F 40  ? 0.6439 0.6610 0.5038 -0.0402 -0.0895 -0.1011 40  GLN F OE1 
15305 N NE2 . GLN F 40  ? 0.6451 0.7295 0.4729 -0.0466 -0.0917 -0.1179 40  GLN F NE2 
15306 N N   . VAL F 41  ? 0.5441 0.5250 0.3593 -0.0142 -0.0783 -0.0009 41  VAL F N   
15307 C CA  . VAL F 41  ? 0.5844 0.5617 0.3984 -0.0098 -0.0785 0.0272  41  VAL F CA  
15308 C C   . VAL F 41  ? 0.5658 0.5372 0.3981 -0.0049 -0.0878 0.0386  41  VAL F C   
15309 O O   . VAL F 41  ? 0.5539 0.5068 0.4070 -0.0055 -0.0875 0.0301  41  VAL F O   
15310 C CB  . VAL F 41  ? 0.6280 0.5823 0.4518 -0.0100 -0.0656 0.0324  41  VAL F CB  
15311 C CG1 . VAL F 41  ? 0.6513 0.6021 0.4741 -0.0084 -0.0602 0.0588  41  VAL F CG1 
15312 C CG2 . VAL F 41  ? 0.6697 0.6287 0.4829 -0.0134 -0.0566 0.0159  41  VAL F CG2 
15313 N N   . PRO F 42  ? 0.5431 0.5334 0.3687 0.0007  -0.0960 0.0587  42  PRO F N   
15314 C CA  . PRO F 42  ? 0.5056 0.4894 0.3544 0.0068  -0.1038 0.0683  42  PRO F CA  
15315 C C   . PRO F 42  ? 0.4642 0.4174 0.3366 0.0093  -0.0937 0.0836  42  PRO F C   
15316 O O   . PRO F 42  ? 0.4950 0.4420 0.3636 0.0119  -0.0852 0.1047  42  PRO F O   
15317 C CB  . PRO F 42  ? 0.5217 0.5403 0.3566 0.0151  -0.1154 0.0875  42  PRO F CB  
15318 C CG  . PRO F 42  ? 0.5314 0.5633 0.3383 0.0140  -0.1089 0.1004  42  PRO F CG  
15319 C CD  . PRO F 42  ? 0.5256 0.5481 0.3241 0.0030  -0.0992 0.0739  42  PRO F CD  
15320 N N   . LEU F 43  ? 0.4416 0.3784 0.3398 0.0071  -0.0929 0.0718  43  LEU F N   
15321 C CA  . LEU F 43  ? 0.4520 0.3668 0.3771 0.0065  -0.0817 0.0782  43  LEU F CA  
15322 C C   . LEU F 43  ? 0.4729 0.3844 0.4294 0.0093  -0.0872 0.0770  43  LEU F C   
15323 O O   . LEU F 43  ? 0.4340 0.3548 0.3928 0.0077  -0.0971 0.0626  43  LEU F O   
15324 C CB  . LEU F 43  ? 0.3881 0.2929 0.3161 -0.0014 -0.0710 0.0609  43  LEU F CB  
15325 C CG  . LEU F 43  ? 0.4013 0.3086 0.3065 -0.0047 -0.0630 0.0566  43  LEU F CG  
15326 C CD1 . LEU F 43  ? 0.3597 0.2634 0.2752 -0.0088 -0.0557 0.0399  43  LEU F CD1 
15327 C CD2 . LEU F 43  ? 0.4200 0.3240 0.3192 -0.0049 -0.0521 0.0743  43  LEU F CD2 
15328 N N   . LEU F 44  ? 0.4727 0.3707 0.4565 0.0124  -0.0786 0.0899  44  LEU F N   
15329 C CA  . LEU F 44  ? 0.4375 0.3329 0.4576 0.0146  -0.0810 0.0861  44  LEU F CA  
15330 C C   . LEU F 44  ? 0.4116 0.3064 0.4475 0.0037  -0.0769 0.0606  44  LEU F C   
15331 O O   . LEU F 44  ? 0.4030 0.2935 0.4377 -0.0041 -0.0654 0.0513  44  LEU F O   
15332 C CB  . LEU F 44  ? 0.4450 0.3230 0.4963 0.0199  -0.0682 0.1041  44  LEU F CB  
15333 C CG  . LEU F 44  ? 0.4342 0.3082 0.5316 0.0228  -0.0671 0.0991  44  LEU F CG  
15334 C CD1 . LEU F 44  ? 0.4309 0.3179 0.5334 0.0380  -0.0830 0.1150  44  LEU F CD1 
15335 C CD2 . LEU F 44  ? 0.4391 0.2902 0.5744 0.0206  -0.0452 0.1043  44  LEU F CD2 
15336 N N   . LEU F 45  ? 0.3801 0.2841 0.4312 0.0033  -0.0862 0.0499  45  LEU F N   
15337 C CA  . LEU F 45  ? 0.3476 0.2554 0.4161 -0.0070 -0.0820 0.0288  45  LEU F CA  
15338 C C   . LEU F 45  ? 0.3817 0.2863 0.4913 -0.0103 -0.0696 0.0240  45  LEU F C   
15339 O O   . LEU F 45  ? 0.4056 0.3089 0.5446 -0.0044 -0.0713 0.0282  45  LEU F O   
15340 C CB  . LEU F 45  ? 0.3463 0.2664 0.4165 -0.0084 -0.0943 0.0178  45  LEU F CB  
15341 C CG  . LEU F 45  ? 0.3346 0.2623 0.4226 -0.0194 -0.0903 -0.0012 45  LEU F CG  
15342 C CD1 . LEU F 45  ? 0.3507 0.2773 0.4168 -0.0263 -0.0838 -0.0070 45  LEU F CD1 
15343 C CD2 . LEU F 45  ? 0.3135 0.2529 0.4093 -0.0213 -0.1007 -0.0111 45  LEU F CD2 
15344 N N   . ASP F 46  ? 0.3743 0.2809 0.4887 -0.0194 -0.0561 0.0132  46  ASP F N   
15345 C CA  . ASP F 46  ? 0.3827 0.2918 0.5381 -0.0263 -0.0407 0.0018  46  ASP F CA  
15346 C C   . ASP F 46  ? 0.3574 0.2921 0.5207 -0.0387 -0.0368 -0.0219 46  ASP F C   
15347 O O   . ASP F 46  ? 0.3357 0.2827 0.4849 -0.0442 -0.0304 -0.0285 46  ASP F O   
15348 C CB  . ASP F 46  ? 0.3613 0.2579 0.5199 -0.0275 -0.0245 0.0087  46  ASP F CB  
15349 C CG  . ASP F 46  ? 0.3595 0.2580 0.5669 -0.0366 -0.0048 -0.0071 46  ASP F CG  
15350 O OD1 . ASP F 46  ? 0.3858 0.2950 0.6270 -0.0405 -0.0042 -0.0223 46  ASP F OD1 
15351 O OD2 . ASP F 46  ? 0.3948 0.2862 0.6098 -0.0417 0.0122  -0.0077 46  ASP F OD2 
15352 N N   . LEU F 47  ? 0.3449 0.3159 0.4934 0.0625  -0.1146 -0.0798 47  LEU F N   
15353 C CA  . LEU F 47  ? 0.3066 0.3032 0.4699 0.0554  -0.0946 -0.0829 47  LEU F CA  
15354 C C   . LEU F 47  ? 0.3082 0.3075 0.4583 0.0524  -0.0869 -0.0736 47  LEU F C   
15355 O O   . LEU F 47  ? 0.3342 0.3453 0.4772 0.0458  -0.0692 -0.0646 47  LEU F O   
15356 C CB  . LEU F 47  ? 0.2710 0.2913 0.4710 0.0582  -0.0964 -0.1061 47  LEU F CB  
15357 C CG  . LEU F 47  ? 0.2573 0.3094 0.4719 0.0509  -0.0748 -0.1097 47  LEU F CG  
15358 C CD1 . LEU F 47  ? 0.2344 0.2934 0.4468 0.0410  -0.0551 -0.0972 47  LEU F CD1 
15359 C CD2 . LEU F 47  ? 0.2515 0.3286 0.5021 0.0546  -0.0784 -0.1347 47  LEU F CD2 
15360 N N   . ASN F 48  ? 0.3288 0.3167 0.4776 0.0576  -0.1014 -0.0760 48  ASN F N   
15361 C CA  . ASN F 48  ? 0.2767 0.2699 0.4202 0.0557  -0.0961 -0.0720 48  ASN F CA  
15362 C C   . ASN F 48  ? 0.2896 0.2608 0.4051 0.0521  -0.0959 -0.0514 48  ASN F C   
15363 O O   . ASN F 48  ? 0.3179 0.2917 0.4302 0.0504  -0.0927 -0.0481 48  ASN F O   
15364 C CB  . ASN F 48  ? 0.2837 0.2808 0.4506 0.0632  -0.1117 -0.0902 48  ASN F CB  
15365 C CG  . ASN F 48  ? 0.2942 0.3236 0.4915 0.0660  -0.1073 -0.1136 48  ASN F CG  
15366 O OD1 . ASN F 48  ? 0.3316 0.3879 0.5305 0.0608  -0.0878 -0.1147 48  ASN F OD1 
15367 N ND2 . ASN F 48  ? 0.2620 0.2894 0.4830 0.0740  -0.1249 -0.1315 48  ASN F ND2 
15368 N N   . GLY F 49  ? 0.3235 0.2765 0.4200 0.0510  -0.0985 -0.0392 49  GLY F N   
15369 C CA  . GLY F 49  ? 0.3232 0.2581 0.3933 0.0471  -0.0974 -0.0201 49  GLY F CA  
15370 C C   . GLY F 49  ? 0.3267 0.2721 0.3859 0.0406  -0.0794 -0.0107 49  GLY F C   
15371 O O   . GLY F 49  ? 0.3427 0.3028 0.4041 0.0382  -0.0664 -0.0118 49  GLY F O   
15372 N N   . LYS F 50  ? 0.3136 0.2505 0.3626 0.0375  -0.0794 -0.0007 50  LYS F N   
15373 C CA  . LYS F 50  ? 0.3106 0.2590 0.3526 0.0330  -0.0649 0.0055  50  LYS F CA  
15374 C C   . LYS F 50  ? 0.3364 0.2816 0.3588 0.0292  -0.0549 0.0176  50  LYS F C   
15375 O O   . LYS F 50  ? 0.2992 0.2561 0.3187 0.0269  -0.0427 0.0205  50  LYS F O   
15376 C CB  . LYS F 50  ? 0.2885 0.2311 0.3326 0.0311  -0.0691 0.0088  50  LYS F CB  
15377 C CG  . LYS F 50  ? 0.2822 0.2342 0.3495 0.0356  -0.0772 -0.0069 50  LYS F CG  
15378 C CD  . LYS F 50  ? 0.3637 0.3095 0.4362 0.0332  -0.0812 -0.0040 50  LYS F CD  
15379 C CE  . LYS F 50  ? 0.4573 0.4096 0.5568 0.0388  -0.0933 -0.0217 50  LYS F CE  
15380 N NZ  . LYS F 50  ? 0.5450 0.4865 0.6541 0.0355  -0.0995 -0.0183 50  LYS F NZ  
15381 N N   . HIS F 51  ? 0.3381 0.2689 0.3476 0.0296  -0.0611 0.0234  51  HIS F N   
15382 C CA  . HIS F 51  ? 0.3742 0.3049 0.3670 0.0275  -0.0530 0.0310  51  HIS F CA  
15383 C C   . HIS F 51  ? 0.4195 0.3404 0.4016 0.0312  -0.0619 0.0305  51  HIS F C   
15384 O O   . HIS F 51  ? 0.4365 0.3480 0.4217 0.0353  -0.0755 0.0269  51  HIS F O   
15385 C CB  . HIS F 51  ? 0.3565 0.2849 0.3356 0.0223  -0.0469 0.0425  51  HIS F CB  
15386 C CG  . HIS F 51  ? 0.3678 0.2808 0.3385 0.0200  -0.0559 0.0514  51  HIS F CG  
15387 N ND1 . HIS F 51  ? 0.3722 0.2810 0.3539 0.0172  -0.0595 0.0531  51  HIS F ND1 
15388 C CD2 . HIS F 51  ? 0.3979 0.2983 0.3509 0.0202  -0.0630 0.0598  51  HIS F CD2 
15389 C CE1 . HIS F 51  ? 0.4111 0.3027 0.3845 0.0146  -0.0681 0.0640  51  HIS F CE1 
15390 N NE2 . HIS F 51  ? 0.4102 0.2968 0.3636 0.0164  -0.0701 0.0694  51  HIS F NE2 
15391 N N   . LEU F 52  ? 0.3864 0.3111 0.3574 0.0310  -0.0557 0.0323  52  LEU F N   
15392 C CA  . LEU F 52  ? 0.3595 0.2788 0.3162 0.0355  -0.0638 0.0310  52  LEU F CA  
15393 C C   . LEU F 52  ? 0.3767 0.2888 0.3071 0.0327  -0.0645 0.0449  52  LEU F C   
15394 O O   . LEU F 52  ? 0.3828 0.3002 0.3074 0.0269  -0.0535 0.0524  52  LEU F O   
15395 C CB  . LEU F 52  ? 0.3387 0.2679 0.2997 0.0375  -0.0577 0.0232  52  LEU F CB  
15396 C CG  . LEU F 52  ? 0.3550 0.2843 0.3068 0.0442  -0.0666 0.0153  52  LEU F CG  
15397 C CD1 . LEU F 52  ? 0.3235 0.2612 0.2993 0.0460  -0.0632 0.0022  52  LEU F CD1 
15398 C CD2 . LEU F 52  ? 0.3770 0.3092 0.3009 0.0444  -0.0641 0.0220  52  LEU F CD2 
15399 N N   . TRP F 53  ? 0.3943 0.2951 0.3097 0.0365  -0.0774 0.0490  53  TRP F N   
15400 C CA  . TRP F 53  ? 0.4087 0.3040 0.2961 0.0330  -0.0769 0.0650  53  TRP F CA  
15401 C C   . TRP F 53  ? 0.4406 0.3351 0.3043 0.0404  -0.0867 0.0642  53  TRP F C   
15402 O O   . TRP F 53  ? 0.4470 0.3387 0.3183 0.0488  -0.0994 0.0524  53  TRP F O   
15403 C CB  . TRP F 53  ? 0.4216 0.3000 0.3101 0.0281  -0.0833 0.0787  53  TRP F CB  
15404 C CG  . TRP F 53  ? 0.4608 0.3227 0.3577 0.0344  -0.1024 0.0761  53  TRP F CG  
15405 C CD1 . TRP F 53  ? 0.4244 0.2846 0.3508 0.0372  -0.1089 0.0636  53  TRP F CD1 
15406 C CD2 . TRP F 53  ? 0.5322 0.3780 0.4084 0.0393  -0.1186 0.0859  53  TRP F CD2 
15407 N NE1 . TRP F 53  ? 0.4697 0.3138 0.3986 0.0440  -0.1286 0.0627  53  TRP F NE1 
15408 C CE2 . TRP F 53  ? 0.5041 0.3373 0.4018 0.0457  -0.1358 0.0773  53  TRP F CE2 
15409 C CE3 . TRP F 53  ? 0.4518 0.2946 0.2922 0.0398  -0.1205 0.1006  53  TRP F CE3 
15410 C CZ2 . TRP F 53  ? 0.5087 0.3232 0.3947 0.0531  -0.1565 0.0836  53  TRP F CZ2 
15411 C CZ3 . TRP F 53  ? 0.4866 0.3116 0.3115 0.0466  -0.1399 0.1089  53  TRP F CZ3 
15412 C CH2 . TRP F 53  ? 0.5382 0.3475 0.3863 0.0535  -0.1587 0.1007  53  TRP F CH2 
15413 N N   . VAL F 54  ? 0.4795 0.3797 0.3150 0.0373  -0.0802 0.0756  54  VAL F N   
15414 C CA  . VAL F 54  ? 0.5046 0.4092 0.3109 0.0446  -0.0878 0.0757  54  VAL F CA  
15415 C C   . VAL F 54  ? 0.4660 0.3644 0.2417 0.0380  -0.0855 0.0998  54  VAL F C   
15416 O O   . VAL F 54  ? 0.5049 0.4054 0.2830 0.0270  -0.0719 0.1111  54  VAL F O   
15417 C CB  . VAL F 54  ? 0.4640 0.3927 0.2651 0.0482  -0.0781 0.0616  54  VAL F CB  
15418 C CG1 . VAL F 54  ? 0.5170 0.4525 0.2959 0.0599  -0.0907 0.0529  54  VAL F CG1 
15419 C CG2 . VAL F 54  ? 0.4318 0.3671 0.2664 0.0490  -0.0727 0.0445  54  VAL F CG2 
15420 N N   . THR F 55  ? 0.6351 0.5266 0.3818 0.0442  -0.0985 0.1082  55  THR F N   
15421 C CA  . THR F 55  ? 0.7151 0.6046 0.4275 0.0370  -0.0935 0.1336  55  THR F CA  
15422 C C   . THR F 55  ? 0.7821 0.7026 0.4772 0.0370  -0.0777 0.1254  55  THR F C   
15423 O O   . THR F 55  ? 0.8988 0.8342 0.5868 0.0486  -0.0834 0.1068  55  THR F O   
15424 C CB  . THR F 55  ? 0.7543 0.6267 0.4376 0.0447  -0.1136 0.1476  55  THR F CB  
15425 O OG1 . THR F 55  ? 0.7263 0.6101 0.4008 0.0601  -0.1258 0.1268  55  THR F OG1 
15426 C CG2 . THR F 55  ? 0.5838 0.4309 0.2975 0.0446  -0.1271 0.1514  55  THR F CG2 
15427 N N   . CYS F 56  ? 0.7588 0.6910 0.4501 0.0248  -0.0587 0.1366  56  CYS F N   
15428 C CA  . CYS F 56  ? 0.7227 0.6876 0.4020 0.0256  -0.0436 0.1250  56  CYS F CA  
15429 C C   . CYS F 56  ? 0.7480 0.7240 0.3839 0.0210  -0.0373 0.1461  56  CYS F C   
15430 O O   . CYS F 56  ? 0.7646 0.7267 0.3929 0.0086  -0.0320 0.1719  56  CYS F O   
15431 C CB  . CYS F 56  ? 0.6485 0.6253 0.3562 0.0166  -0.0260 0.1183  56  CYS F CB  
15432 S SG  . CYS F 56  ? 0.6088 0.5790 0.3628 0.0218  -0.0299 0.0950  56  CYS F SG  
15433 N N   . SER F 57  ? 0.7440 0.7446 0.3525 0.0313  -0.0385 0.1343  57  SER F N   
15434 C CA  . SER F 57  ? 0.7579 0.7639 0.3285 0.0256  -0.0334 0.1493  57  SER F CA  
15435 C C   . SER F 57  ? 0.7455 0.7872 0.3074 0.0207  -0.0118 0.1405  57  SER F C   
15436 O O   . SER F 57  ? 0.6664 0.7318 0.2512 0.0215  -0.0008 0.1233  57  SER F O   
15437 C CB  . SER F 57  ? 0.7572 0.7603 0.3036 0.0386  -0.0540 0.1431  57  SER F CB  
15438 O OG  . SER F 57  ? 0.7297 0.7616 0.2801 0.0542  -0.0575 0.1118  57  SER F OG  
15439 N N   . GLN F 58  ? 0.8363 0.8812 0.3645 0.0165  -0.0064 0.1526  58  GLN F N   
15440 C CA  . GLN F 58  ? 0.9041 0.9856 0.4204 0.0136  0.0127  0.1436  58  GLN F CA  
15441 C C   . GLN F 58  ? 0.8531 0.9690 0.3737 0.0297  0.0078  0.1091  58  GLN F C   
15442 O O   . GLN F 58  ? 0.8077 0.9566 0.3406 0.0298  0.0224  0.0912  58  GLN F O   
15443 C CB  . GLN F 58  ? 1.0543 1.1302 0.5291 0.0087  0.0162  0.1642  58  GLN F CB  
15444 C CG  . GLN F 58  ? 1.1586 1.2722 0.6196 0.0041  0.0376  0.1587  58  GLN F CG  
15445 C CD  . GLN F 58  ? 1.2160 1.3372 0.7044 -0.0110 0.0596  0.1657  58  GLN F CD  
15446 O OE1 . GLN F 58  ? 1.2660 1.3601 0.7594 -0.0237 0.0647  0.1915  58  GLN F OE1 
15447 N NE2 . GLN F 58  ? 1.2041 1.3624 0.7146 -0.0089 0.0713  0.1410  58  GLN F NE2 
15448 N N   . HIS F 59  ? 0.8514 0.9583 0.3683 0.0442  -0.0141 0.0977  59  HIS F N   
15449 C CA  . HIS F 59  ? 0.6996 0.8348 0.2238 0.0619  -0.0223 0.0629  59  HIS F CA  
15450 C C   . HIS F 59  ? 0.7130 0.8469 0.2760 0.0718  -0.0299 0.0396  59  HIS F C   
15451 O O   . HIS F 59  ? 0.7200 0.8626 0.2938 0.0878  -0.0442 0.0123  59  HIS F O   
15452 C CB  . HIS F 59  ? 0.7379 0.8667 0.2361 0.0729  -0.0419 0.0615  59  HIS F CB  
15453 C CG  . HIS F 59  ? 0.8182 0.9473 0.2734 0.0645  -0.0356 0.0845  59  HIS F CG  
15454 N ND1 . HIS F 59  ? 0.8588 1.0217 0.2964 0.0627  -0.0189 0.0780  59  HIS F ND1 
15455 C CD2 . HIS F 59  ? 0.8402 0.9383 0.2675 0.0566  -0.0428 0.1150  59  HIS F CD2 
15456 C CE1 . HIS F 59  ? 0.8838 1.0370 0.2814 0.0548  -0.0155 0.1039  59  HIS F CE1 
15457 N NE2 . HIS F 59  ? 0.9097 1.0216 0.2999 0.0509  -0.0303 0.1271  59  HIS F NE2 
15458 N N   . TYR F 60  ? 0.6887 0.8112 0.2737 0.0620  -0.0203 0.0500  60  TYR F N   
15459 C CA  . TYR F 60  ? 0.6378 0.7519 0.2714 0.0647  -0.0225 0.0293  60  TYR F CA  
15460 C C   . TYR F 60  ? 0.6234 0.7724 0.2732 0.0698  -0.0127 0.0013  60  TYR F C   
15461 O O   . TYR F 60  ? 0.6062 0.7764 0.2514 0.0610  0.0054  0.0061  60  TYR F O   
15462 C CB  . TYR F 60  ? 0.5756 0.6637 0.2327 0.0493  -0.0141 0.0497  60  TYR F CB  
15463 C CG  . TYR F 60  ? 0.5278 0.6003 0.2329 0.0495  -0.0167 0.0356  60  TYR F CG  
15464 C CD1 . TYR F 60  ? 0.4863 0.5771 0.2186 0.0525  -0.0096 0.0135  60  TYR F CD1 
15465 C CD2 . TYR F 60  ? 0.5477 0.5878 0.2706 0.0463  -0.0257 0.0459  60  TYR F CD2 
15466 C CE1 . TYR F 60  ? 0.4283 0.5035 0.2005 0.0520  -0.0117 0.0054  60  TYR F CE1 
15467 C CE2 . TYR F 60  ? 0.5152 0.5440 0.2775 0.0458  -0.0263 0.0357  60  TYR F CE2 
15468 C CZ  . TYR F 60  ? 0.4980 0.5433 0.2830 0.0483  -0.0191 0.0173  60  TYR F CZ  
15469 O OH  . TYR F 60  ? 0.5017 0.5343 0.3224 0.0474  -0.0199 0.0112  60  TYR F OH  
15470 N N   . SER F 61  ? 0.6493 0.8050 0.3215 0.0840  -0.0252 -0.0291 61  SER F N   
15471 C CA  . SER F 61  ? 0.6823 0.8700 0.3740 0.0910  -0.0194 -0.0588 61  SER F CA  
15472 C C   . SER F 61  ? 0.5929 0.7644 0.3395 0.0924  -0.0238 -0.0756 61  SER F C   
15473 O O   . SER F 61  ? 0.5527 0.7043 0.3218 0.0990  -0.0388 -0.0851 61  SER F O   
15474 C CB  . SER F 61  ? 0.7763 0.9934 0.4477 0.1081  -0.0307 -0.0841 61  SER F CB  
15475 O OG  . SER F 61  ? 0.7943 1.0438 0.4882 0.1166  -0.0273 -0.1167 61  SER F OG  
15476 N N   . SER F 62  ? 0.5700 0.7500 0.3379 0.0858  -0.0104 -0.0776 62  SER F N   
15477 C CA  . SER F 62  ? 0.5245 0.6896 0.3408 0.0865  -0.0134 -0.0895 62  SER F CA  
15478 C C   . SER F 62  ? 0.5123 0.6978 0.3467 0.0834  -0.0003 -0.0981 62  SER F C   
15479 O O   . SER F 62  ? 0.5316 0.7264 0.3501 0.0728  0.0147  -0.0819 62  SER F O   
15480 C CB  . SER F 62  ? 0.4910 0.6178 0.3198 0.0770  -0.0155 -0.0666 62  SER F CB  
15481 O OG  . SER F 62  ? 0.4880 0.6010 0.3588 0.0771  -0.0174 -0.0742 62  SER F OG  
15482 N N   . SER F 63  ? 0.4636 0.6556 0.3347 0.0928  -0.0069 -0.1241 63  SER F N   
15483 C CA  . SER F 63  ? 0.4392 0.6478 0.3328 0.0920  0.0020  -0.1345 63  SER F CA  
15484 C C   . SER F 63  ? 0.4497 0.6283 0.3715 0.0843  0.0031  -0.1193 63  SER F C   
15485 O O   . SER F 63  ? 0.4762 0.6638 0.4187 0.0835  0.0087  -0.1252 63  SER F O   
15486 C CB  . SER F 63  ? 0.4621 0.6938 0.3836 0.1072  -0.0073 -0.1716 63  SER F CB  
15487 O OG  . SER F 63  ? 0.4517 0.6568 0.4098 0.1137  -0.0234 -0.1813 63  SER F OG  
15488 N N   . THR F 64  ? 0.4139 0.5595 0.3362 0.0792  -0.0025 -0.1006 64  THR F N   
15489 C CA  . THR F 64  ? 0.3924 0.5126 0.3380 0.0729  -0.0015 -0.0865 64  THR F CA  
15490 C C   . THR F 64  ? 0.4298 0.5347 0.3542 0.0603  0.0062  -0.0582 64  THR F C   
15491 O O   . THR F 64  ? 0.3864 0.4701 0.3252 0.0554  0.0060  -0.0454 64  THR F O   
15492 C CB  . THR F 64  ? 0.3635 0.4587 0.3381 0.0775  -0.0144 -0.0907 64  THR F CB  
15493 O OG1 . THR F 64  ? 0.3948 0.4851 0.3558 0.0805  -0.0224 -0.0925 64  THR F OG1 
15494 C CG2 . THR F 64  ? 0.3520 0.4558 0.3612 0.0879  -0.0221 -0.1156 64  THR F CG2 
15495 N N   . TYR F 65  ? 0.4482 0.5642 0.3384 0.0556  0.0123  -0.0486 65  TYR F N   
15496 C CA  . TYR F 65  ? 0.4281 0.5293 0.3004 0.0438  0.0182  -0.0227 65  TYR F CA  
15497 C C   . TYR F 65  ? 0.4295 0.5410 0.3074 0.0350  0.0313  -0.0154 65  TYR F C   
15498 O O   . TYR F 65  ? 0.4221 0.5616 0.2992 0.0357  0.0399  -0.0266 65  TYR F O   
15499 C CB  . TYR F 65  ? 0.4507 0.5566 0.2855 0.0416  0.0185  -0.0119 65  TYR F CB  
15500 C CG  . TYR F 65  ? 0.4540 0.5474 0.2735 0.0283  0.0256  0.0147  65  TYR F CG  
15501 C CD1 . TYR F 65  ? 0.4449 0.5083 0.2691 0.0249  0.0178  0.0290  65  TYR F CD1 
15502 C CD2 . TYR F 65  ? 0.4554 0.5684 0.2589 0.0191  0.0401  0.0243  65  TYR F CD2 
15503 C CE1 . TYR F 65  ? 0.4397 0.4911 0.2552 0.0137  0.0222  0.0508  65  TYR F CE1 
15504 C CE2 . TYR F 65  ? 0.4642 0.5641 0.2594 0.0064  0.0456  0.0483  65  TYR F CE2 
15505 C CZ  . TYR F 65  ? 0.4507 0.5187 0.2527 0.0042  0.0356  0.0609  65  TYR F CZ  
15506 O OH  . TYR F 65  ? 0.4628 0.5172 0.2608 -0.0078 0.0393  0.0829  65  TYR F OH  
15507 N N   . GLN F 66  ? 0.4457 0.5368 0.3306 0.0270  0.0323  0.0014  66  GLN F N   
15508 C CA  . GLN F 66  ? 0.4401 0.5381 0.3324 0.0179  0.0430  0.0094  66  GLN F CA  
15509 C C   . GLN F 66  ? 0.4004 0.4777 0.2859 0.0079  0.0431  0.0310  66  GLN F C   
15510 O O   . GLN F 66  ? 0.3753 0.4300 0.2616 0.0099  0.0334  0.0368  66  GLN F O   
15511 C CB  . GLN F 66  ? 0.4894 0.5867 0.4123 0.0229  0.0408  -0.0015 66  GLN F CB  
15512 C CG  . GLN F 66  ? 0.6162 0.7364 0.5509 0.0317  0.0413  -0.0235 66  GLN F CG  
15513 C CD  . GLN F 66  ? 0.6990 0.8129 0.6638 0.0387  0.0351  -0.0329 66  GLN F CD  
15514 O OE1 . GLN F 66  ? 0.7392 0.8468 0.7149 0.0351  0.0367  -0.0252 66  GLN F OE1 
15515 N NE2 . GLN F 66  ? 0.7322 0.8479 0.7120 0.0494  0.0267  -0.0500 66  GLN F NE2 
15516 N N   . ALA F 67  ? 0.4061 0.4924 0.2889 -0.0029 0.0537  0.0413  67  ALA F N   
15517 C CA  . ALA F 67  ? 0.3935 0.4604 0.2795 -0.0120 0.0526  0.0586  67  ALA F CA  
15518 C C   . ALA F 67  ? 0.4069 0.4777 0.3206 -0.0144 0.0558  0.0540  67  ALA F C   
15519 O O   . ALA F 67  ? 0.4406 0.5320 0.3624 -0.0200 0.0665  0.0508  67  ALA F O   
15520 C CB  . ALA F 67  ? 0.3763 0.4464 0.2418 -0.0239 0.0605  0.0765  67  ALA F CB  
15521 N N   . PRO F 68  ? 0.3810 0.4346 0.3094 -0.0096 0.0466  0.0526  68  PRO F N   
15522 C CA  . PRO F 68  ? 0.3424 0.4018 0.2942 -0.0097 0.0480  0.0471  68  PRO F CA  
15523 C C   . PRO F 68  ? 0.3267 0.3929 0.2870 -0.0216 0.0557  0.0544  68  PRO F C   
15524 O O   . PRO F 68  ? 0.3887 0.4446 0.3396 -0.0304 0.0566  0.0684  68  PRO F O   
15525 C CB  . PRO F 68  ? 0.3042 0.3439 0.2625 -0.0041 0.0373  0.0487  68  PRO F CB  
15526 C CG  . PRO F 68  ? 0.2752 0.3049 0.2208 0.0023  0.0314  0.0475  68  PRO F CG  
15527 C CD  . PRO F 68  ? 0.3254 0.3589 0.2507 -0.0025 0.0352  0.0529  68  PRO F CD  
15528 N N   . PHE F 69  ? 0.3194 0.4029 0.2999 -0.0219 0.0605  0.0448  69  PHE F N   
15529 C CA  . PHE F 69  ? 0.2999 0.3919 0.2953 -0.0339 0.0679  0.0494  69  PHE F CA  
15530 C C   . PHE F 69  ? 0.3106 0.3868 0.3217 -0.0344 0.0589  0.0522  69  PHE F C   
15531 O O   . PHE F 69  ? 0.3771 0.4445 0.3908 -0.0241 0.0491  0.0464  69  PHE F O   
15532 C CB  . PHE F 69  ? 0.3865 0.5077 0.4019 -0.0341 0.0767  0.0349  69  PHE F CB  
15533 C CG  . PHE F 69  ? 0.3723 0.4974 0.4048 -0.0207 0.0679  0.0190  69  PHE F CG  
15534 C CD1 . PHE F 69  ? 0.3245 0.4452 0.3761 -0.0186 0.0607  0.0158  69  PHE F CD1 
15535 C CD2 . PHE F 69  ? 0.4132 0.5486 0.4444 -0.0099 0.0664  0.0063  69  PHE F CD2 
15536 C CE1 . PHE F 69  ? 0.3093 0.4345 0.3729 -0.0058 0.0520  0.0034  69  PHE F CE1 
15537 C CE2 . PHE F 69  ? 0.4021 0.5387 0.4490 0.0024  0.0571  -0.0055 69  PHE F CE2 
15538 C CZ  . PHE F 69  ? 0.3441 0.4754 0.4048 0.0044  0.0501  -0.0056 69  PHE F CZ  
15539 N N   . CYS F 70  ? 0.3219 0.3964 0.3455 -0.0466 0.0626  0.0604  70  CYS F N   
15540 C CA  . CYS F 70  ? 0.3195 0.3810 0.3620 -0.0470 0.0529  0.0599  70  CYS F CA  
15541 C C   . CYS F 70  ? 0.3125 0.3873 0.3758 -0.0373 0.0478  0.0424  70  CYS F C   
15542 O O   . CYS F 70  ? 0.3034 0.3994 0.3795 -0.0373 0.0543  0.0325  70  CYS F O   
15543 C CB  . CYS F 70  ? 0.3334 0.3918 0.3923 -0.0628 0.0578  0.0708  70  CYS F CB  
15544 S SG  . CYS F 70  ? 0.4418 0.4759 0.5194 -0.0631 0.0423  0.0729  70  CYS F SG  
15545 N N   . HIS F 71  ? 0.3044 0.3679 0.3703 -0.0287 0.0358  0.0384  71  HIS F N   
15546 C CA  . HIS F 71  ? 0.2953 0.3694 0.3738 -0.0171 0.0284  0.0241  71  HIS F CA  
15547 C C   . HIS F 71  ? 0.3040 0.3834 0.3686 -0.0054 0.0278  0.0196  71  HIS F C   
15548 O O   . HIS F 71  ? 0.3268 0.4158 0.3995 0.0044  0.0221  0.0097  71  HIS F O   
15549 C CB  . HIS F 71  ? 0.2818 0.3747 0.3897 -0.0210 0.0306  0.0130  71  HIS F CB  
15550 C CG  . HIS F 71  ? 0.3008 0.3885 0.4292 -0.0345 0.0320  0.0177  71  HIS F CG  
15551 N ND1 . HIS F 71  ? 0.3521 0.4263 0.4897 -0.0336 0.0212  0.0172  71  HIS F ND1 
15552 C CD2 . HIS F 71  ? 0.3057 0.4000 0.4492 -0.0497 0.0429  0.0234  71  HIS F CD2 
15553 C CE1 . HIS F 71  ? 0.3367 0.4063 0.4969 -0.0474 0.0237  0.0224  71  HIS F CE1 
15554 N NE2 . HIS F 71  ? 0.3407 0.4219 0.5040 -0.0582 0.0376  0.0279  71  HIS F NE2 
15555 N N   . SER F 72  ? 0.2971 0.3693 0.3417 -0.0057 0.0319  0.0268  72  SER F N   
15556 C CA  . SER F 72  ? 0.2828 0.3556 0.3179 0.0051  0.0295  0.0231  72  SER F CA  
15557 C C   . SER F 72  ? 0.2835 0.3434 0.3105 0.0136  0.0206  0.0262  72  SER F C   
15558 O O   . SER F 72  ? 0.2810 0.3323 0.3067 0.0113  0.0168  0.0300  72  SER F O   
15559 C CB  . SER F 72  ? 0.2817 0.3518 0.3013 0.0025  0.0354  0.0272  72  SER F CB  
15560 O OG  . SER F 72  ? 0.2982 0.3510 0.3031 -0.0016 0.0335  0.0379  72  SER F OG  
15561 N N   . THR F 73  ? 0.2956 0.3551 0.3188 0.0231  0.0173  0.0245  73  THR F N   
15562 C CA  . THR F 73  ? 0.3094 0.3580 0.3235 0.0298  0.0115  0.0301  73  THR F CA  
15563 C C   . THR F 73  ? 0.3155 0.3496 0.3178 0.0255  0.0126  0.0376  73  THR F C   
15564 O O   . THR F 73  ? 0.3174 0.3454 0.3153 0.0273  0.0093  0.0414  73  THR F O   
15565 C CB  . THR F 73  ? 0.2970 0.3451 0.3115 0.0390  0.0083  0.0297  73  THR F CB  
15566 O OG1 . THR F 73  ? 0.2871 0.3346 0.3029 0.0376  0.0119  0.0266  73  THR F OG1 
15567 C CG2 . THR F 73  ? 0.2690 0.3307 0.2947 0.0462  0.0036  0.0222  73  THR F CG2 
15568 N N   . GLN F 74  ? 0.3073 0.3384 0.3046 0.0206  0.0169  0.0384  74  GLN F N   
15569 C CA  . GLN F 74  ? 0.3061 0.3244 0.2928 0.0172  0.0161  0.0440  74  GLN F CA  
15570 C C   . GLN F 74  ? 0.3106 0.3230 0.2971 0.0114  0.0139  0.0479  74  GLN F C   
15571 O O   . GLN F 74  ? 0.3135 0.3163 0.2969 0.0122  0.0094  0.0503  74  GLN F O   
15572 C CB  . GLN F 74  ? 0.3067 0.3263 0.2855 0.0143  0.0202  0.0430  74  GLN F CB  
15573 C CG  . GLN F 74  ? 0.2959 0.3193 0.2781 0.0212  0.0199  0.0364  74  GLN F CG  
15574 C CD  . GLN F 74  ? 0.3160 0.3561 0.3059 0.0219  0.0244  0.0283  74  GLN F CD  
15575 O OE1 . GLN F 74  ? 0.3591 0.4080 0.3560 0.0189  0.0269  0.0275  74  GLN F OE1 
15576 N NE2 . GLN F 74  ? 0.3675 0.4141 0.3591 0.0260  0.0251  0.0198  74  GLN F NE2 
15577 N N   . CYS F 75  ? 0.3140 0.3328 0.3078 0.0054  0.0165  0.0473  75  CYS F N   
15578 C CA  . CYS F 75  ? 0.3081 0.3197 0.3077 -0.0002 0.0127  0.0503  75  CYS F CA  
15579 C C   . CYS F 75  ? 0.2932 0.3075 0.3023 0.0059  0.0060  0.0441  75  CYS F C   
15580 O O   . CYS F 75  ? 0.3448 0.3512 0.3568 0.0056  0.0000  0.0441  75  CYS F O   
15581 C CB  . CYS F 75  ? 0.3432 0.3613 0.3532 -0.0095 0.0178  0.0518  75  CYS F CB  
15582 S SG  . CYS F 75  ? 0.4142 0.4326 0.4069 -0.0173 0.0271  0.0610  75  CYS F SG  
15583 N N   . SER F 76  ? 0.2906 0.3174 0.3041 0.0127  0.0061  0.0381  76  SER F N   
15584 C CA  . SER F 76  ? 0.3111 0.3444 0.3279 0.0202  0.0002  0.0325  76  SER F CA  
15585 C C   . SER F 76  ? 0.3283 0.3551 0.3343 0.0238  -0.0011 0.0363  76  SER F C   
15586 O O   . SER F 76  ? 0.3583 0.3869 0.3678 0.0256  -0.0056 0.0321  76  SER F O   
15587 C CB  . SER F 76  ? 0.3071 0.3546 0.3259 0.0282  -0.0004 0.0277  76  SER F CB  
15588 O OG  . SER F 76  ? 0.3417 0.3980 0.3591 0.0359  -0.0059 0.0233  76  SER F OG  
15589 N N   . ARG F 77  ? 0.3249 0.3458 0.3213 0.0249  0.0026  0.0423  77  ARG F N   
15590 C CA  . ARG F 77  ? 0.3101 0.3258 0.3007 0.0269  0.0025  0.0458  77  ARG F CA  
15591 C C   . ARG F 77  ? 0.3393 0.3458 0.3314 0.0227  -0.0008 0.0447  77  ARG F C   
15592 O O   . ARG F 77  ? 0.3518 0.3605 0.3460 0.0248  -0.0030 0.0420  77  ARG F O   
15593 C CB  . ARG F 77  ? 0.3311 0.3403 0.3173 0.0278  0.0059  0.0509  77  ARG F CB  
15594 C CG  . ARG F 77  ? 0.3638 0.3696 0.3491 0.0292  0.0067  0.0548  77  ARG F CG  
15595 C CD  . ARG F 77  ? 0.3754 0.3735 0.3625 0.0301  0.0086  0.0589  77  ARG F CD  
15596 N NE  . ARG F 77  ? 0.3775 0.3731 0.3683 0.0294  0.0103  0.0630  77  ARG F NE  
15597 C CZ  . ARG F 77  ? 0.4034 0.3904 0.4019 0.0286  0.0110  0.0650  77  ARG F CZ  
15598 N NH1 . ARG F 77  ? 0.4376 0.4244 0.4430 0.0265  0.0137  0.0685  77  ARG F NH1 
15599 N NH2 . ARG F 77  ? 0.4069 0.3877 0.4085 0.0297  0.0090  0.0617  77  ARG F NH2 
15600 N N   . ALA F 78  ? 0.3322 0.3296 0.3233 0.0171  -0.0014 0.0468  78  ALA F N   
15601 C CA  . ALA F 78  ? 0.3278 0.3133 0.3191 0.0139  -0.0068 0.0477  78  ALA F CA  
15602 C C   . ALA F 78  ? 0.3670 0.3537 0.3711 0.0134  -0.0133 0.0422  78  ALA F C   
15603 O O   . ALA F 78  ? 0.3865 0.3631 0.3946 0.0124  -0.0203 0.0415  78  ALA F O   
15604 C CB  . ALA F 78  ? 0.3153 0.2913 0.2978 0.0082  -0.0056 0.0544  78  ALA F CB  
15605 N N   . ASN F 79  ? 0.4181 0.4175 0.4305 0.0153  -0.0127 0.0368  79  ASN F N   
15606 C CA  . ASN F 79  ? 0.4869 0.4906 0.5162 0.0161  -0.0200 0.0277  79  ASN F CA  
15607 C C   . ASN F 79  ? 0.4894 0.4788 0.5292 0.0076  -0.0241 0.0322  79  ASN F C   
15608 O O   . ASN F 79  ? 0.4621 0.4439 0.5160 0.0071  -0.0333 0.0277  79  ASN F O   
15609 C CB  . ASN F 79  ? 0.5595 0.5668 0.5931 0.0216  -0.0258 0.0194  79  ASN F CB  
15610 C CG  . ASN F 79  ? 0.5880 0.6071 0.6404 0.0258  -0.0338 0.0049  79  ASN F CG  
15611 O OD1 . ASN F 79  ? 0.6021 0.6321 0.6618 0.0271  -0.0339 -0.0004 79  ASN F OD1 
15612 N ND2 . ASN F 79  ? 0.5919 0.6100 0.6552 0.0287  -0.0418 -0.0042 79  ASN F ND2 
15613 N N   . THR F 80  ? 0.5187 0.5050 0.5528 0.0008  -0.0171 0.0412  80  THR F N   
15614 C CA  . THR F 80  ? 0.5736 0.5489 0.6180 -0.0090 -0.0186 0.0483  80  THR F CA  
15615 C C   . THR F 80  ? 0.6353 0.6229 0.6905 -0.0142 -0.0115 0.0471  80  THR F C   
15616 O O   . THR F 80  ? 0.6631 0.6610 0.7074 -0.0137 -0.0026 0.0485  80  THR F O   
15617 C CB  . THR F 80  ? 0.5571 0.5167 0.5831 -0.0150 -0.0163 0.0633  80  THR F CB  
15618 O OG1 . THR F 80  ? 0.6519 0.6027 0.6865 -0.0261 -0.0154 0.0736  80  THR F OG1 
15619 C CG2 . THR F 80  ? 0.4475 0.4155 0.4528 -0.0134 -0.0062 0.0664  80  THR F CG2 
15620 N N   . HIS F 81  ? 0.6450 0.6326 0.7258 -0.0189 -0.0163 0.0425  81  HIS F N   
15621 C CA  . HIS F 81  ? 0.6586 0.6596 0.7547 -0.0248 -0.0094 0.0399  81  HIS F CA  
15622 C C   . HIS F 81  ? 0.6932 0.6826 0.8051 -0.0397 -0.0072 0.0515  81  HIS F C   
15623 O O   . HIS F 81  ? 0.7006 0.7007 0.8351 -0.0468 -0.0026 0.0481  81  HIS F O   
15624 C CB  . HIS F 81  ? 0.6544 0.6728 0.7715 -0.0164 -0.0159 0.0208  81  HIS F CB  
15625 C CG  . HIS F 81  ? 0.6815 0.7138 0.7806 -0.0033 -0.0155 0.0135  81  HIS F CG  
15626 N ND1 . HIS F 81  ? 0.6697 0.7169 0.7633 0.0003  -0.0091 0.0110  81  HIS F ND1 
15627 C CD2 . HIS F 81  ? 0.7123 0.7455 0.7985 0.0066  -0.0204 0.0096  81  HIS F CD2 
15628 C CE1 . HIS F 81  ? 0.6920 0.7457 0.7695 0.0117  -0.0111 0.0079  81  HIS F CE1 
15629 N NE2 . HIS F 81  ? 0.7176 0.7642 0.7897 0.0149  -0.0167 0.0076  81  HIS F NE2 
15630 N N   . GLN F 82  ? 0.6782 0.6459 0.7775 -0.0443 -0.0104 0.0663  82  GLN F N   
15631 C CA  . GLN F 82  ? 0.6496 0.6014 0.7560 -0.0590 -0.0084 0.0841  82  GLN F CA  
15632 C C   . GLN F 82  ? 0.5830 0.5402 0.6613 -0.0662 0.0068  0.0997  82  GLN F C   
15633 O O   . GLN F 82  ? 0.5734 0.5298 0.6219 -0.0595 0.0082  0.1025  82  GLN F O   
15634 C CB  . GLN F 82  ? 0.7236 0.6487 0.8296 -0.0581 -0.0224 0.0921  82  GLN F CB  
15635 C CG  . GLN F 82  ? 0.8563 0.7615 0.9512 -0.0712 -0.0195 0.1179  82  GLN F CG  
15636 C CD  . GLN F 82  ? 0.9798 0.8559 1.0753 -0.0688 -0.0365 0.1260  82  GLN F CD  
15637 O OE1 . GLN F 82  ? 1.0256 0.8983 1.1342 -0.0577 -0.0502 0.1097  82  GLN F OE1 
15638 N NE2 . GLN F 82  ? 1.0288 0.8853 1.1100 -0.0790 -0.0359 0.1512  82  GLN F NE2 
15639 N N   . CYS F 83  ? 0.5506 0.5175 0.6409 -0.0793 0.0185  0.1070  83  CYS F N   
15640 C CA  . CYS F 83  ? 0.5406 0.5200 0.6059 -0.0862 0.0347  0.1186  83  CYS F CA  
15641 C C   . CYS F 83  ? 0.5520 0.5119 0.5933 -0.0949 0.0355  0.1439  83  CYS F C   
15642 O O   . CYS F 83  ? 0.5721 0.5092 0.6266 -0.1021 0.0270  0.1566  83  CYS F O   
15643 C CB  . CYS F 83  ? 0.5566 0.5591 0.6455 -0.0973 0.0487  0.1153  83  CYS F CB  
15644 S SG  . CYS F 83  ? 0.5114 0.5417 0.6227 -0.0851 0.0482  0.0855  83  CYS F SG  
15645 N N   . PHE F 84  ? 0.5073 0.4775 0.5144 -0.0938 0.0451  0.1505  84  PHE F N   
15646 C CA  . PHE F 84  ? 0.4626 0.4179 0.4381 -0.0982 0.0447  0.1728  84  PHE F CA  
15647 C C   . PHE F 84  ? 0.5302 0.5008 0.4961 -0.1140 0.0631  0.1902  84  PHE F C   
15648 O O   . PHE F 84  ? 0.5162 0.5174 0.4827 -0.1158 0.0784  0.1800  84  PHE F O   
15649 C CB  . PHE F 84  ? 0.4697 0.4285 0.4124 -0.0838 0.0410  0.1653  84  PHE F CB  
15650 C CG  . PHE F 84  ? 0.4882 0.4325 0.3963 -0.0843 0.0368  0.1844  84  PHE F CG  
15651 C CD1 . PHE F 84  ? 0.4952 0.4106 0.4001 -0.0781 0.0184  0.1898  84  PHE F CD1 
15652 C CD2 . PHE F 84  ? 0.5118 0.4737 0.3899 -0.0896 0.0505  0.1954  84  PHE F CD2 
15653 C CE1 . PHE F 84  ? 0.5377 0.4396 0.4100 -0.0768 0.0122  0.2070  84  PHE F CE1 
15654 C CE2 . PHE F 84  ? 0.5031 0.4533 0.3464 -0.0877 0.0454  0.2113  84  PHE F CE2 
15655 C CZ  . PHE F 84  ? 0.5982 0.5172 0.4389 -0.0801 0.0258  0.2157  84  PHE F CZ  
15656 N N   . THR F 85  ? 0.5622 0.5122 0.5190 -0.1254 0.0614  0.2169  85  THR F N   
15657 C CA  . THR F 85  ? 0.6395 0.6007 0.5803 -0.1362 0.0787  0.2292  85  THR F CA  
15658 C C   . THR F 85  ? 0.6997 0.6441 0.5972 -0.1295 0.0734  0.2426  85  THR F C   
15659 O O   . THR F 85  ? 0.7371 0.6499 0.6329 -0.1249 0.0564  0.2508  85  THR F O   
15660 C CB  . THR F 85  ? 0.6680 0.6195 0.6436 -0.1523 0.0833  0.2383  85  THR F CB  
15661 O OG1 . THR F 85  ? 0.6538 0.6261 0.6718 -0.1572 0.0880  0.2226  85  THR F OG1 
15662 C CG2 . THR F 85  ? 0.7117 0.6740 0.6687 -0.1640 0.1026  0.2525  85  THR F CG2 
15663 N N   . CYS F 86  ? 0.7141 0.6820 0.5784 -0.1273 0.0867  0.2424  86  CYS F N   
15664 C CA  . CYS F 86  ? 0.8232 0.7794 0.6453 -0.1198 0.0817  0.2538  86  CYS F CA  
15665 C C   . CYS F 86  ? 0.9370 0.8788 0.7544 -0.1326 0.0893  0.2769  86  CYS F C   
15666 O O   . CYS F 86  ? 0.9782 0.9408 0.7959 -0.1445 0.1094  0.2816  86  CYS F O   
15667 C CB  . CYS F 86  ? 0.8267 0.8151 0.6164 -0.1116 0.0917  0.2424  86  CYS F CB  
15668 S SG  . CYS F 86  ? 0.8941 0.8694 0.6328 -0.0975 0.0797  0.2502  86  CYS F SG  
15669 N N   . THR F 87  ? 0.9900 0.8964 0.8024 -0.1295 0.0727  0.2911  87  THR F N   
15670 C CA  . THR F 87  ? 1.0670 0.9522 0.8780 -0.1409 0.0757  0.3152  87  THR F CA  
15671 C C   . THR F 87  ? 1.1346 1.0128 0.8965 -0.1328 0.0732  0.3296  87  THR F C   
15672 O O   . THR F 87  ? 1.2069 1.0623 0.9573 -0.1380 0.0713  0.3523  87  THR F O   
15673 C CB  . THR F 87  ? 1.0702 0.9194 0.9149 -0.1417 0.0559  0.3196  87  THR F CB  
15674 O OG1 . THR F 87  ? 1.0774 0.9104 0.9107 -0.1242 0.0342  0.3121  87  THR F OG1 
15675 C CG2 . THR F 87  ? 1.0080 0.8639 0.9030 -0.1490 0.0564  0.3041  87  THR F CG2 
15676 N N   . ASP F 88  ? 1.1302 1.0293 0.8634 -0.1197 0.0730  0.3156  88  ASP F N   
15677 C CA  . ASP F 88  ? 1.1962 1.0934 0.8811 -0.1093 0.0691  0.3243  88  ASP F CA  
15678 C C   . ASP F 88  ? 1.2327 1.1632 0.8853 -0.1138 0.0909  0.3260  88  ASP F C   
15679 O O   . ASP F 88  ? 1.3008 1.2318 0.9464 -0.1273 0.1060  0.3453  88  ASP F O   
15680 C CB  . ASP F 88  ? 1.1997 1.0952 0.8764 -0.0902 0.0501  0.3055  88  ASP F CB  
15681 C CG  . ASP F 88  ? 1.2898 1.1906 0.9178 -0.0768 0.0448  0.3068  88  ASP F CG  
15682 O OD1 . ASP F 88  ? 1.3697 1.2667 0.9665 -0.0805 0.0515  0.3262  88  ASP F OD1 
15683 O OD2 . ASP F 88  ? 1.2813 1.1904 0.9022 -0.0626 0.0338  0.2877  88  ASP F OD2 
15684 N N   . SER F 89  ? 1.1897 1.1496 0.8266 -0.1031 0.0929  0.3044  89  SER F N   
15685 C CA  . SER F 89  ? 1.2098 1.2049 0.8152 -0.1031 0.1098  0.2998  89  SER F CA  
15686 C C   . SER F 89  ? 1.1763 1.1985 0.8035 -0.1198 0.1351  0.3000  89  SER F C   
15687 O O   . SER F 89  ? 1.1669 1.1848 0.8365 -0.1299 0.1387  0.2980  89  SER F O   
15688 C CB  . SER F 89  ? 1.1993 1.2188 0.7938 -0.0868 0.1026  0.2715  89  SER F CB  
15689 O OG  . SER F 89  ? 1.2260 1.2885 0.8087 -0.0872 0.1200  0.2568  89  SER F OG  
15690 N N   . THR F 90  ? 1.1577 1.2090 0.7567 -0.1224 0.1522  0.3014  90  THR F N   
15691 C CA  . THR F 90  ? 1.1282 1.2112 0.7480 -0.1365 0.1770  0.2979  90  THR F CA  
15692 C C   . THR F 90  ? 1.0491 1.1754 0.6773 -0.1275 0.1832  0.2654  90  THR F C   
15693 O O   . THR F 90  ? 1.0350 1.1919 0.6882 -0.1359 0.2013  0.2548  90  THR F O   
15694 C CB  . THR F 90  ? 1.2012 1.2937 0.7877 -0.1460 0.1947  0.3192  90  THR F CB  
15695 O OG1 . THR F 90  ? 1.2278 1.3364 0.7669 -0.1318 0.1903  0.3124  90  THR F OG1 
15696 C CG2 . THR F 90  ? 1.2485 1.2974 0.8300 -0.1563 0.1898  0.3531  90  THR F CG2 
15697 N N   . THR F 91  ? 1.0031 1.1302 0.6154 -0.1101 0.1663  0.2484  91  THR F N   
15698 C CA  . THR F 91  ? 0.9640 1.1254 0.5889 -0.0993 0.1668  0.2158  91  THR F CA  
15699 C C   . THR F 91  ? 0.9324 1.0749 0.5758 -0.0886 0.1466  0.2029  91  THR F C   
15700 O O   . THR F 91  ? 0.9288 1.0352 0.5634 -0.0848 0.1294  0.2160  91  THR F O   
15701 C CB  . THR F 91  ? 1.0002 1.1894 0.5871 -0.0869 0.1670  0.2024  91  THR F CB  
15702 O OG1 . THR F 91  ? 1.0460 1.2066 0.5986 -0.0770 0.1480  0.2133  91  THR F OG1 
15703 C CG2 . THR F 91  ? 1.0332 1.2512 0.6035 -0.0967 0.1896  0.2102  91  THR F CG2 
15704 N N   . THR F 92  ? 0.8904 1.0586 0.5583 -0.0825 0.1482  0.1763  92  THR F N   
15705 C CA  . THR F 92  ? 0.8447 0.9976 0.5305 -0.0733 0.1315  0.1647  92  THR F CA  
15706 C C   . THR F 92  ? 0.8207 0.9749 0.4795 -0.0556 0.1160  0.1515  92  THR F C   
15707 O O   . THR F 92  ? 0.8401 1.0164 0.4724 -0.0493 0.1194  0.1435  92  THR F O   
15708 C CB  . THR F 92  ? 0.8154 0.9927 0.5391 -0.0730 0.1381  0.1422  92  THR F CB  
15709 O OG1 . THR F 92  ? 0.8348 1.0505 0.5532 -0.0627 0.1436  0.1161  92  THR F OG1 
15710 C CG2 . THR F 92  ? 0.8112 0.9939 0.5640 -0.0897 0.1538  0.1507  92  THR F CG2 
15711 N N   . ARG F 93  ? 0.7548 0.8845 0.4212 -0.0480 0.0982  0.1500  93  ARG F N   
15712 C CA  . ARG F 93  ? 0.7111 0.8392 0.3601 -0.0312 0.0813  0.1365  93  ARG F CA  
15713 C C   . ARG F 93  ? 0.6440 0.7515 0.3191 -0.0277 0.0687  0.1338  93  ARG F C   
15714 O O   . ARG F 93  ? 0.6376 0.7289 0.3366 -0.0387 0.0718  0.1458  93  ARG F O   
15715 C CB  . ARG F 93  ? 0.7405 0.8472 0.3524 -0.0278 0.0703  0.1529  93  ARG F CB  
15716 C CG  . ARG F 93  ? 0.7625 0.8272 0.3786 -0.0362 0.0625  0.1794  93  ARG F CG  
15717 C CD  . ARG F 93  ? 0.8561 0.8955 0.4386 -0.0305 0.0481  0.1946  93  ARG F CD  
15718 N NE  . ARG F 93  ? 0.9229 0.9234 0.5189 -0.0376 0.0410  0.2171  93  ARG F NE  
15719 C CZ  . ARG F 93  ? 0.9428 0.9178 0.5587 -0.0320 0.0236  0.2158  93  ARG F CZ  
15720 N NH1 . ARG F 93  ? 0.9154 0.8984 0.5382 -0.0204 0.0122  0.1956  93  ARG F NH1 
15721 N NH2 . ARG F 93  ? 0.9672 0.9108 0.5997 -0.0379 0.0175  0.2335  93  ARG F NH2 
15722 N N   . PRO F 94  ? 0.6022 0.7067 0.2799 -0.0119 0.0537  0.1143  94  PRO F N   
15723 C CA  . PRO F 94  ? 0.5686 0.6419 0.2784 -0.0083 0.0405  0.1090  94  PRO F CA  
15724 C C   . PRO F 94  ? 0.6098 0.6492 0.3157 -0.0163 0.0323  0.1350  94  PRO F C   
15725 O O   . PRO F 94  ? 0.6348 0.6654 0.3093 -0.0152 0.0249  0.1509  94  PRO F O   
15726 C CB  . PRO F 94  ? 0.5442 0.6164 0.2521 0.0087  0.0249  0.0878  94  PRO F CB  
15727 C CG  . PRO F 94  ? 0.5664 0.6749 0.2579 0.0151  0.0324  0.0714  94  PRO F CG  
15728 C CD  . PRO F 94  ? 0.6236 0.7494 0.2822 0.0036  0.0471  0.0933  94  PRO F CD  
15729 N N   . GLY F 95  ? 0.5921 0.6141 0.3293 -0.0236 0.0327  0.1389  95  GLY F N   
15730 C CA  . GLY F 95  ? 0.6261 0.6165 0.3668 -0.0303 0.0234  0.1599  95  GLY F CA  
15731 C C   . GLY F 95  ? 0.6677 0.6589 0.4059 -0.0475 0.0363  0.1836  95  GLY F C   
15732 O O   . GLY F 95  ? 0.6973 0.6609 0.4485 -0.0541 0.0296  0.1985  95  GLY F O   
15733 N N   . CYS F 96  ? 0.6734 0.6945 0.4015 -0.0531 0.0546  0.1816  96  CYS F N   
15734 C CA  . CYS F 96  ? 0.7044 0.7256 0.4381 -0.0680 0.0690  0.1967  96  CYS F CA  
15735 C C   . CYS F 96  ? 0.6673 0.7234 0.4195 -0.0756 0.0888  0.1851  96  CYS F C   
15736 O O   . CYS F 96  ? 0.6634 0.7487 0.3991 -0.0746 0.1015  0.1774  96  CYS F O   
15737 C CB  . CYS F 96  ? 0.7863 0.8043 0.4832 -0.0680 0.0715  0.2108  96  CYS F CB  
15738 S SG  . CYS F 96  ? 1.1822 1.2039 0.8825 -0.0870 0.0921  0.2312  96  CYS F SG  
15739 N N   . HIS F 97  ? 0.6466 0.7005 0.4348 -0.0826 0.0907  0.1826  97  HIS F N   
15740 C CA  . HIS F 97  ? 0.6298 0.7144 0.4414 -0.0909 0.1083  0.1726  97  HIS F CA  
15741 C C   . HIS F 97  ? 0.6498 0.7193 0.4961 -0.1047 0.1100  0.1834  97  HIS F C   
15742 O O   . HIS F 97  ? 0.6315 0.6675 0.4856 -0.1059 0.0960  0.1953  97  HIS F O   
15743 C CB  . HIS F 97  ? 0.5703 0.6719 0.4003 -0.0772 0.1058  0.1420  97  HIS F CB  
15744 C CG  . HIS F 97  ? 0.5441 0.6544 0.3497 -0.0615 0.0992  0.1274  97  HIS F CG  
15745 N ND1 . HIS F 97  ? 0.4914 0.5762 0.2908 -0.0494 0.0810  0.1238  97  HIS F ND1 
15746 C CD2 . HIS F 97  ? 0.5675 0.7110 0.3565 -0.0559 0.1079  0.1136  97  HIS F CD2 
15747 C CE1 . HIS F 97  ? 0.4663 0.5666 0.2482 -0.0373 0.0782  0.1087  97  HIS F CE1 
15748 N NE2 . HIS F 97  ? 0.4621 0.5979 0.2369 -0.0403 0.0937  0.1016  97  HIS F NE2 
15749 N N   . ASN F 98  ? 0.6379 0.7343 0.5088 -0.1140 0.1259  0.1758  98  ASN F N   
15750 C CA  . ASN F 98  ? 0.6305 0.7191 0.5421 -0.1254 0.1270  0.1785  98  ASN F CA  
15751 C C   . ASN F 98  ? 0.5180 0.6157 0.4600 -0.1133 0.1212  0.1490  98  ASN F C   
15752 O O   . ASN F 98  ? 0.4802 0.5974 0.4142 -0.1011 0.1223  0.1297  98  ASN F O   
15753 C CB  . ASN F 98  ? 0.7529 0.8594 0.6753 -0.1412 0.1468  0.1857  98  ASN F CB  
15754 C CG  . ASN F 98  ? 0.8638 0.9439 0.7647 -0.1488 0.1475  0.2105  98  ASN F CG  
15755 O OD1 . ASN F 98  ? 0.7960 0.8410 0.6875 -0.1453 0.1310  0.2230  98  ASN F OD1 
15756 N ND2 . ASN F 98  ? 1.0715 1.1694 0.9639 -0.1582 0.1662  0.2172  98  ASN F ND2 
15757 N N   . ASN F 99  ? 0.5015 0.5848 0.4785 -0.1158 0.1135  0.1452  99  ASN F N   
15758 C CA  . ASN F 99  ? 0.4747 0.5658 0.4780 -0.1038 0.1065  0.1195  99  ASN F CA  
15759 C C   . ASN F 99  ? 0.4359 0.5159 0.4234 -0.0846 0.0922  0.1069  99  ASN F C   
15760 O O   . ASN F 99  ? 0.4382 0.5319 0.4360 -0.0738 0.0904  0.0872  99  ASN F O   
15761 C CB  . ASN F 99  ? 0.4756 0.6055 0.4939 -0.1057 0.1217  0.1031  99  ASN F CB  
15762 C CG  . ASN F 99  ? 0.8804 1.0272 0.9201 -0.1264 0.1388  0.1137  99  ASN F CG  
15763 O OD1 . ASN F 99  ? 0.8817 1.0135 0.9490 -0.1362 0.1351  0.1212  99  ASN F OD1 
15764 N ND2 . ASN F 99  ? 0.8689 1.0487 0.8978 -0.1333 0.1576  0.1134  99  ASN F ND2 
15765 N N   . THR F 100 ? 0.4356 0.4900 0.4010 -0.0807 0.0814  0.1185  100 THR F N   
15766 C CA  . THR F 100 ? 0.3856 0.4263 0.3416 -0.0650 0.0676  0.1085  100 THR F CA  
15767 C C   . THR F 100 ? 0.3995 0.4157 0.3730 -0.0639 0.0538  0.1106  100 THR F C   
15768 O O   . THR F 100 ? 0.3961 0.4099 0.3936 -0.0731 0.0547  0.1142  100 THR F O   
15769 C CB  . THR F 100 ? 0.4161 0.4501 0.3375 -0.0604 0.0649  0.1162  100 THR F CB  
15770 O OG1 . THR F 100 ? 0.4650 0.4879 0.3717 -0.0721 0.0673  0.1388  100 THR F OG1 
15771 C CG2 . THR F 100 ? 0.4325 0.4939 0.3399 -0.0561 0.0751  0.1055  100 THR F CG2 
15772 N N   . CYS F 101 ? 0.4250 0.4255 0.3905 -0.0528 0.0411  0.1063  101 CYS F N   
15773 C CA  . CYS F 101 ? 0.4635 0.4444 0.4459 -0.0511 0.0281  0.1061  101 CYS F CA  
15774 C C   . CYS F 101 ? 0.4402 0.3970 0.4073 -0.0489 0.0165  0.1164  101 CYS F C   
15775 O O   . CYS F 101 ? 0.4232 0.3780 0.3666 -0.0427 0.0148  0.1175  101 CYS F O   
15776 C CB  A CYS F 101 ? 0.4499 0.4371 0.4443 -0.0391 0.0224  0.0884  101 CYS F CB  
15777 C CB  B CYS F 101 ? 0.4506 0.4381 0.4472 -0.0395 0.0223  0.0881  101 CYS F CB  
15778 S SG  A CYS F 101 ? 0.4279 0.4408 0.4213 -0.0340 0.0327  0.0762  101 CYS F SG  
15779 S SG  B CYS F 101 ? 0.3699 0.3651 0.3493 -0.0263 0.0225  0.0780  101 CYS F SG  
15780 N N   . GLY F 102 ? 0.4523 0.3914 0.4372 -0.0529 0.0069  0.1215  102 GLY F N   
15781 C CA  . GLY F 102 ? 0.4825 0.3972 0.4584 -0.0517 -0.0059 0.1321  102 GLY F CA  
15782 C C   . GLY F 102 ? 0.4955 0.4041 0.4805 -0.0394 -0.0189 0.1169  102 GLY F C   
15783 O O   . GLY F 102 ? 0.4757 0.3929 0.4828 -0.0353 -0.0210 0.1022  102 GLY F O   
15784 N N   . LEU F 103 ? 0.5494 0.4454 0.5169 -0.0333 -0.0276 0.1203  103 LEU F N   
15785 C CA  . LEU F 103 ? 0.5354 0.4282 0.5096 -0.0220 -0.0386 0.1061  103 LEU F CA  
15786 C C   . LEU F 103 ? 0.4939 0.3632 0.4648 -0.0200 -0.0542 0.1139  103 LEU F C   
15787 O O   . LEU F 103 ? 0.4784 0.3387 0.4251 -0.0218 -0.0552 0.1280  103 LEU F O   
15788 C CB  . LEU F 103 ? 0.5994 0.5064 0.5576 -0.0145 -0.0323 0.0975  103 LEU F CB  
15789 C CG  . LEU F 103 ? 0.6504 0.5611 0.6199 -0.0049 -0.0384 0.0820  103 LEU F CG  
15790 C CD1 . LEU F 103 ? 0.7037 0.6225 0.6974 -0.0044 -0.0390 0.0720  103 LEU F CD1 
15791 C CD2 . LEU F 103 ? 0.6420 0.5666 0.6007 -0.0002 -0.0299 0.0759  103 LEU F CD2 
15792 N N   . LEU F 104 ? 0.4862 0.3470 0.4813 -0.0154 -0.0673 0.1039  104 LEU F N   
15793 C CA  . LEU F 104 ? 0.5268 0.3642 0.5239 -0.0121 -0.0851 0.1092  104 LEU F CA  
15794 C C   . LEU F 104 ? 0.5002 0.3395 0.4869 -0.0009 -0.0921 0.0986  104 LEU F C   
15795 O O   . LEU F 104 ? 0.4764 0.3312 0.4763 0.0058  -0.0906 0.0801  104 LEU F O   
15796 C CB  . LEU F 104 ? 0.5782 0.4072 0.6113 -0.0114 -0.0976 0.0997  104 LEU F CB  
15797 C CG  . LEU F 104 ? 0.6532 0.4524 0.6973 -0.0119 -0.1170 0.1100  104 LEU F CG  
15798 C CD1 . LEU F 104 ? 0.7081 0.4913 0.7389 -0.0252 -0.1120 0.1380  104 LEU F CD1 
15799 C CD2 . LEU F 104 ? 0.6771 0.4753 0.7630 -0.0093 -0.1283 0.0927  104 LEU F CD2 
15800 N N   . SER F 105 ? 0.5012 0.3270 0.4644 0.0011  -0.0991 0.1105  105 SER F N   
15801 C CA  . SER F 105 ? 0.4714 0.2988 0.4274 0.0120  -0.1075 0.0993  105 SER F CA  
15802 C C   . SER F 105 ? 0.4908 0.2955 0.4566 0.0182  -0.1301 0.0999  105 SER F C   
15803 O O   . SER F 105 ? 0.5432 0.3262 0.5067 0.0134  -0.1389 0.1175  105 SER F O   
15804 C CB  . SER F 105 ? 0.4375 0.2712 0.3600 0.0130  -0.1007 0.1068  105 SER F CB  
15805 O OG  . SER F 105 ? 0.4297 0.2847 0.3461 0.0092  -0.0820 0.1032  105 SER F OG  
15806 N N   . SER F 106 ? 0.4951 0.3051 0.4742 0.0286  -0.1397 0.0809  106 SER F N   
15807 C CA  . SER F 106 ? 0.5523 0.3435 0.5460 0.0370  -0.1632 0.0760  106 SER F CA  
15808 C C   . SER F 106 ? 0.5473 0.3382 0.5265 0.0464  -0.1726 0.0704  106 SER F C   
15809 O O   . SER F 106 ? 0.5668 0.3768 0.5436 0.0498  -0.1639 0.0579  106 SER F O   
15810 C CB  . SER F 106 ? 0.5421 0.3442 0.5747 0.0422  -0.1685 0.0517  106 SER F CB  
15811 O OG  . SER F 106 ? 0.5962 0.3939 0.6488 0.0363  -0.1683 0.0537  106 SER F OG  
15812 N N   . ASN F 107 ? 0.4528 0.3106 0.5400 0.0309  -0.0578 0.1264  107 ASN F N   
15813 C CA  . ASN F 107 ? 0.4417 0.3064 0.5350 0.0403  -0.0730 0.1392  107 ASN F CA  
15814 C C   . ASN F 107 ? 0.4275 0.2836 0.5655 0.0508  -0.0719 0.1293  107 ASN F C   
15815 O O   . ASN F 107 ? 0.4195 0.2567 0.5859 0.0532  -0.0683 0.1345  107 ASN F O   
15816 C CB  . ASN F 107 ? 0.4585 0.3164 0.5435 0.0392  -0.0844 0.1714  107 ASN F CB  
15817 C CG  . ASN F 107 ? 0.4836 0.3557 0.5709 0.0470  -0.0994 0.1798  107 ASN F CG  
15818 O OD1 . ASN F 107 ? 0.4845 0.3608 0.6015 0.0557  -0.1018 0.1694  107 ASN F OD1 
15819 N ND2 . ASN F 107 ? 0.4957 0.3758 0.5524 0.0431  -0.1084 0.1984  107 ASN F ND2 
15820 N N   . PRO F 108 ? 0.4642 0.3357 0.6081 0.0563  -0.0724 0.1128  108 PRO F N   
15821 C CA  . PRO F 108 ? 0.4844 0.3508 0.6696 0.0653  -0.0660 0.0985  108 PRO F CA  
15822 C C   . PRO F 108 ? 0.5028 0.3712 0.7154 0.0734  -0.0742 0.1113  108 PRO F C   
15823 O O   . PRO F 108 ? 0.5113 0.3751 0.7575 0.0795  -0.0661 0.1008  108 PRO F O   
15824 C CB  . PRO F 108 ? 0.4539 0.3417 0.6281 0.0655  -0.0633 0.0799  108 PRO F CB  
15825 C CG  . PRO F 108 ? 0.4214 0.3246 0.5627 0.0617  -0.0767 0.0919  108 PRO F CG  
15826 C CD  . PRO F 108 ? 0.4164 0.3103 0.5305 0.0539  -0.0775 0.1062  108 PRO F CD  
15827 N N   . VAL F 109 ? 0.5080 0.3855 0.7029 0.0725  -0.0896 0.1329  109 VAL F N   
15828 C CA  . VAL F 109 ? 0.4769 0.3588 0.6938 0.0791  -0.0992 0.1469  109 VAL F CA  
15829 C C   . VAL F 109 ? 0.4870 0.3468 0.7144 0.0783  -0.0953 0.1600  109 VAL F C   
15830 O O   . VAL F 109 ? 0.5183 0.3702 0.7820 0.0853  -0.0917 0.1589  109 VAL F O   
15831 C CB  . VAL F 109 ? 0.4806 0.3821 0.6723 0.0776  -0.1180 0.1634  109 VAL F CB  
15832 C CG1 . VAL F 109 ? 0.5005 0.4051 0.7154 0.0842  -0.1292 0.1807  109 VAL F CG1 
15833 C CG2 . VAL F 109 ? 0.4683 0.3911 0.6557 0.0779  -0.1225 0.1492  109 VAL F CG2 
15834 N N   . THR F 110 ? 0.4757 0.3259 0.6731 0.0695  -0.0950 0.1722  110 THR F N   
15835 C CA  . THR F 110 ? 0.5342 0.3632 0.7414 0.0672  -0.0912 0.1866  110 THR F CA  
15836 C C   . THR F 110 ? 0.5736 0.3807 0.7962 0.0625  -0.0738 0.1698  110 THR F C   
15837 O O   . THR F 110 ? 0.6080 0.3953 0.8487 0.0613  -0.0689 0.1766  110 THR F O   
15838 C CB  . THR F 110 ? 0.5425 0.3721 0.7106 0.0585  -0.0980 0.2104  110 THR F CB  
15839 O OG1 . THR F 110 ? 0.5500 0.3794 0.6889 0.0483  -0.0898 0.2032  110 THR F OG1 
15840 C CG2 . THR F 110 ? 0.5599 0.4119 0.7054 0.0611  -0.1152 0.2239  110 THR F CG2 
15841 N N   . GLN F 111 ? 0.5661 0.3766 0.7815 0.0592  -0.0652 0.1478  111 GLN F N   
15842 C CA  . GLN F 111 ? 0.5993 0.3918 0.8249 0.0527  -0.0495 0.1283  111 GLN F CA  
15843 C C   . GLN F 111 ? 0.6110 0.3901 0.8191 0.0400  -0.0460 0.1408  111 GLN F C   
15844 O O   . GLN F 111 ? 0.6484 0.4109 0.8682 0.0325  -0.0345 0.1277  111 GLN F O   
15845 C CB  . GLN F 111 ? 0.6609 0.4394 0.9256 0.0587  -0.0405 0.1141  111 GLN F CB  
15846 C CG  . GLN F 111 ? 0.7535 0.5466 1.0354 0.0684  -0.0374 0.0945  111 GLN F CG  
15847 C CD  . GLN F 111 ? 0.8972 0.6801 1.2185 0.0759  -0.0293 0.0842  111 GLN F CD  
15848 O OE1 . GLN F 111 ? 0.9293 0.7159 1.2722 0.0846  -0.0371 0.0990  111 GLN F OE1 
15849 N NE2 . GLN F 111 ? 0.9702 0.7411 1.3004 0.0720  -0.0136 0.0580  111 GLN F NE2 
15850 N N   . GLU F 112 ? 0.6036 0.3919 0.7829 0.0364  -0.0554 0.1651  112 GLU F N   
15851 C CA  . GLU F 112 ? 0.6125 0.3957 0.7685 0.0230  -0.0508 0.1777  112 GLU F CA  
15852 C C   . GLU F 112 ? 0.5506 0.3431 0.6904 0.0154  -0.0432 0.1594  112 GLU F C   
15853 O O   . GLU F 112 ? 0.4685 0.2810 0.5949 0.0206  -0.0456 0.1436  112 GLU F O   
15854 C CB  . GLU F 112 ? 0.6830 0.4806 0.8038 0.0213  -0.0611 0.2037  112 GLU F CB  
15855 C CG  . GLU F 112 ? 0.7644 0.5551 0.8914 0.0252  -0.0687 0.2265  112 GLU F CG  
15856 C CD  . GLU F 112 ? 0.8207 0.6317 0.9089 0.0255  -0.0812 0.2451  112 GLU F CD  
15857 O OE1 . GLU F 112 ? 0.8668 0.6738 0.9394 0.0211  -0.0833 0.2676  112 GLU F OE1 
15858 O OE2 . GLU F 112 ? 0.8157 0.6466 0.8866 0.0291  -0.0884 0.2358  112 GLU F OE2 
15859 N N   . SER F 113 ? 0.5921 0.3797 0.7265 0.0020  -0.0325 0.1559  113 SER F N   
15860 C CA  . SER F 113 ? 0.5987 0.4087 0.7076 -0.0058 -0.0251 0.1358  113 SER F CA  
15861 C C   . SER F 113 ? 0.5534 0.3702 0.6405 -0.0184 -0.0199 0.1517  113 SER F C   
15862 O O   . SER F 113 ? 0.5630 0.3629 0.6593 -0.0241 -0.0190 0.1744  113 SER F O   
15863 C CB  . SER F 113 ? 0.6554 0.4600 0.7840 -0.0102 -0.0157 0.1063  113 SER F CB  
15864 O OG  . SER F 113 ? 0.7236 0.5061 0.8751 -0.0208 -0.0089 0.1091  113 SER F OG  
15865 N N   . GLY F 114 ? 0.5152 0.3571 0.5753 -0.0225 -0.0156 0.1410  114 GLY F N   
15866 C CA  . GLY F 114 ? 0.5375 0.3901 0.5789 -0.0340 -0.0079 0.1536  114 GLY F CA  
15867 C C   . GLY F 114 ? 0.4739 0.3503 0.5055 -0.0388 0.0001  0.1323  114 GLY F C   
15868 O O   . GLY F 114 ? 0.4309 0.3189 0.4569 -0.0311 -0.0030 0.1135  114 GLY F O   
15869 N N   . LEU F 115 ? 0.4742 0.3590 0.5068 -0.0514 0.0102  0.1366  115 LEU F N   
15870 C CA  . LEU F 115 ? 0.4785 0.3888 0.5074 -0.0552 0.0168  0.1184  115 LEU F CA  
15871 C C   . LEU F 115 ? 0.4831 0.4170 0.4802 -0.0513 0.0206  0.1228  115 LEU F C   
15872 O O   . LEU F 115 ? 0.5289 0.4678 0.5109 -0.0571 0.0275  0.1407  115 LEU F O   
15873 C CB  . LEU F 115 ? 0.4873 0.3994 0.5396 -0.0709 0.0257  0.1175  115 LEU F CB  
15874 C CG  . LEU F 115 ? 0.4243 0.3629 0.4830 -0.0747 0.0291  0.0969  115 LEU F CG  
15875 C CD1 . LEU F 115 ? 0.3750 0.3073 0.4476 -0.0720 0.0219  0.0738  115 LEU F CD1 
15876 C CD2 . LEU F 115 ? 0.4957 0.4423 0.5747 -0.0916 0.0386  0.1030  115 LEU F CD2 
15877 N N   . GLY F 116 ? 0.4826 0.4297 0.4694 -0.0418 0.0169  0.1057  116 GLY F N   
15878 C CA  . GLY F 116 ? 0.4956 0.4624 0.4559 -0.0371 0.0209  0.1044  116 GLY F CA  
15879 C C   . GLY F 116 ? 0.4424 0.4323 0.4118 -0.0394 0.0292  0.0908  116 GLY F C   
15880 O O   . GLY F 116 ? 0.4349 0.4275 0.4289 -0.0457 0.0299  0.0829  116 GLY F O   
15881 N N   . GLU F 117 ? 0.4373 0.4442 0.3875 -0.0341 0.0349  0.0874  117 GLU F N   
15882 C CA  . GLU F 117 ? 0.3676 0.3984 0.3280 -0.0333 0.0429  0.0763  117 GLU F CA  
15883 C C   . GLU F 117 ? 0.3551 0.3897 0.3103 -0.0209 0.0365  0.0609  117 GLU F C   
15884 O O   . GLU F 117 ? 0.3580 0.3840 0.2919 -0.0135 0.0322  0.0597  117 GLU F O   
15885 C CB  . GLU F 117 ? 0.3456 0.3925 0.2921 -0.0364 0.0579  0.0841  117 GLU F CB  
15886 C CG  . GLU F 117 ? 0.3364 0.4112 0.3018 -0.0364 0.0691  0.0759  117 GLU F CG  
15887 C CD  . GLU F 117 ? 0.3748 0.4659 0.3247 -0.0371 0.0868  0.0807  117 GLU F CD  
15888 O OE1 . GLU F 117 ? 0.4361 0.5219 0.3551 -0.0301 0.0883  0.0780  117 GLU F OE1 
15889 O OE2 . GLU F 117 ? 0.3801 0.4901 0.3486 -0.0454 0.0998  0.0858  117 GLU F OE2 
15890 N N   . LEU F 118 ? 0.3621 0.4092 0.3371 -0.0194 0.0347  0.0500  118 LEU F N   
15891 C CA  . LEU F 118 ? 0.3383 0.3894 0.3093 -0.0081 0.0301  0.0387  118 LEU F CA  
15892 C C   . LEU F 118 ? 0.3462 0.4074 0.3031 -0.0007 0.0393  0.0369  118 LEU F C   
15893 O O   . LEU F 118 ? 0.3630 0.4408 0.3253 -0.0034 0.0511  0.0397  118 LEU F O   
15894 C CB  . LEU F 118 ? 0.3090 0.3750 0.3024 -0.0086 0.0261  0.0308  118 LEU F CB  
15895 C CG  . LEU F 118 ? 0.3020 0.3704 0.2928 0.0023  0.0202  0.0224  118 LEU F CG  
15896 C CD1 . LEU F 118 ? 0.3135 0.3610 0.2928 0.0051  0.0119  0.0192  118 LEU F CD1 
15897 C CD2 . LEU F 118 ? 0.2712 0.3597 0.2817 0.0017  0.0163  0.0183  118 LEU F CD2 
15898 N N   . ALA F 119 ? 0.3386 0.3897 0.2795 0.0081  0.0347  0.0308  119 ALA F N   
15899 C CA  . ALA F 119 ? 0.3171 0.3720 0.2423 0.0149  0.0426  0.0254  119 ALA F CA  
15900 C C   . ALA F 119 ? 0.3345 0.3875 0.2654 0.0252  0.0385  0.0149  119 ALA F C   
15901 O O   . ALA F 119 ? 0.3434 0.3893 0.2818 0.0265  0.0283  0.0137  119 ALA F O   
15902 C CB  . ALA F 119 ? 0.3271 0.3685 0.2231 0.0128  0.0406  0.0291  119 ALA F CB  
15903 N N   . GLN F 120 ? 0.3318 0.3903 0.2591 0.0322  0.0478  0.0074  120 GLN F N   
15904 C CA  . GLN F 120 ? 0.3374 0.3915 0.2723 0.0424  0.0456  -0.0013 120 GLN F CA  
15905 C C   . GLN F 120 ? 0.3660 0.4110 0.2808 0.0465  0.0525  -0.0115 120 GLN F C   
15906 O O   . GLN F 120 ? 0.3784 0.4321 0.2849 0.0458  0.0655  -0.0143 120 GLN F O   
15907 C CB  . GLN F 120 ? 0.3468 0.4200 0.3109 0.0485  0.0507  -0.0010 120 GLN F CB  
15908 C CG  . GLN F 120 ? 0.3624 0.4308 0.3379 0.0598  0.0491  -0.0063 120 GLN F CG  
15909 C CD  . GLN F 120 ? 0.3607 0.4504 0.3673 0.0671  0.0535  -0.0033 120 GLN F CD  
15910 O OE1 . GLN F 120 ? 0.3639 0.4669 0.3863 0.0642  0.0451  0.0043  120 GLN F OE1 
15911 N NE2 . GLN F 120 ? 0.3582 0.4522 0.3748 0.0766  0.0662  -0.0100 120 GLN F NE2 
15912 N N   . ASP F 121 ? 0.3901 0.4184 0.2967 0.0495  0.0447  -0.0181 121 ASP F N   
15913 C CA  . ASP F 121 ? 0.4265 0.4450 0.3143 0.0521  0.0503  -0.0312 121 ASP F CA  
15914 C C   . ASP F 121 ? 0.4197 0.4218 0.3135 0.0563  0.0418  -0.0380 121 ASP F C   
15915 O O   . ASP F 121 ? 0.3853 0.3862 0.2965 0.0578  0.0338  -0.0310 121 ASP F O   
15916 C CB  . ASP F 121 ? 0.4272 0.4417 0.2814 0.0432  0.0480  -0.0304 121 ASP F CB  
15917 C CG  . ASP F 121 ? 0.4424 0.4564 0.2733 0.0439  0.0603  -0.0445 121 ASP F CG  
15918 O OD1 . ASP F 121 ? 0.4439 0.4520 0.2832 0.0513  0.0673  -0.0590 121 ASP F OD1 
15919 O OD2 . ASP F 121 ? 0.4883 0.5075 0.2917 0.0367  0.0642  -0.0413 121 ASP F OD2 
15920 N N   . VAL F 122 ? 0.4509 0.4409 0.3308 0.0575  0.0448  -0.0522 122 VAL F N   
15921 C CA  . VAL F 122 ? 0.4365 0.4091 0.3221 0.0590  0.0368  -0.0592 122 VAL F CA  
15922 C C   . VAL F 122 ? 0.4638 0.4304 0.3383 0.0506  0.0210  -0.0542 122 VAL F C   
15923 O O   . VAL F 122 ? 0.4720 0.4412 0.3229 0.0437  0.0165  -0.0534 122 VAL F O   
15924 C CB  . VAL F 122 ? 0.4600 0.4199 0.3342 0.0608  0.0444  -0.0790 122 VAL F CB  
15925 C CG1 . VAL F 122 ? 0.4531 0.3940 0.3321 0.0585  0.0344  -0.0862 122 VAL F CG1 
15926 C CG2 . VAL F 122 ? 0.4342 0.3973 0.3277 0.0717  0.0611  -0.0854 122 VAL F CG2 
15927 N N   . LEU F 123 ? 0.4333 0.3934 0.3261 0.0516  0.0130  -0.0497 123 LEU F N   
15928 C CA  . LEU F 123 ? 0.4205 0.3739 0.3100 0.0452  -0.0001 -0.0489 123 LEU F CA  
15929 C C   . LEU F 123 ? 0.4604 0.3989 0.3619 0.0462  -0.0011 -0.0586 123 LEU F C   
15930 O O   . LEU F 123 ? 0.4631 0.3972 0.3835 0.0527  0.0055  -0.0571 123 LEU F O   
15931 C CB  . LEU F 123 ? 0.3599 0.3198 0.2625 0.0440  -0.0066 -0.0350 123 LEU F CB  
15932 C CG  . LEU F 123 ? 0.3574 0.3136 0.2642 0.0389  -0.0186 -0.0329 123 LEU F CG  
15933 C CD1 . LEU F 123 ? 0.3522 0.3162 0.2620 0.0371  -0.0228 -0.0215 123 LEU F CD1 
15934 C CD2 . LEU F 123 ? 0.3628 0.3124 0.2901 0.0401  -0.0190 -0.0336 123 LEU F CD2 
15935 N N   . ALA F 124 ? 0.4676 0.3990 0.3598 0.0391  -0.0102 -0.0673 124 ALA F N   
15936 C CA  . ALA F 124 ? 0.4143 0.3310 0.3204 0.0369  -0.0128 -0.0765 124 ALA F CA  
15937 C C   . ALA F 124 ? 0.4255 0.3447 0.3410 0.0295  -0.0266 -0.0714 124 ALA F C   
15938 O O   . ALA F 124 ? 0.4046 0.3346 0.3100 0.0255  -0.0361 -0.0656 124 ALA F O   
15939 C CB  . ALA F 124 ? 0.4537 0.3592 0.3435 0.0341  -0.0098 -0.0970 124 ALA F CB  
15940 N N   . ILE F 125 ? 0.4188 0.3286 0.3568 0.0279  -0.0269 -0.0720 125 ILE F N   
15941 C CA  . ILE F 125 ? 0.4002 0.3148 0.3539 0.0213  -0.0372 -0.0670 125 ILE F CA  
15942 C C   . ILE F 125 ? 0.4299 0.3297 0.4034 0.0161  -0.0368 -0.0751 125 ILE F C   
15943 O O   . ILE F 125 ? 0.4370 0.3220 0.4172 0.0202  -0.0269 -0.0786 125 ILE F O   
15944 C CB  . ILE F 125 ? 0.3511 0.2763 0.3180 0.0254  -0.0344 -0.0504 125 ILE F CB  
15945 C CG1 . ILE F 125 ? 0.3222 0.2550 0.3080 0.0196  -0.0426 -0.0460 125 ILE F CG1 
15946 C CG2 . ILE F 125 ? 0.3547 0.2734 0.3336 0.0314  -0.0229 -0.0441 125 ILE F CG2 
15947 C CD1 . ILE F 125 ? 0.3215 0.2638 0.3187 0.0233  -0.0377 -0.0334 125 ILE F CD1 
15948 N N   . HIS F 126 ? 0.4109 0.3145 0.3971 0.0069  -0.0477 -0.0778 126 HIS F N   
15949 C CA  . HIS F 126 ? 0.4298 0.3190 0.4381 0.0000  -0.0468 -0.0852 126 HIS F CA  
15950 C C   . HIS F 126 ? 0.3976 0.2812 0.4298 0.0035  -0.0356 -0.0714 126 HIS F C   
15951 O O   . HIS F 126 ? 0.4037 0.3010 0.4434 0.0060  -0.0339 -0.0571 126 HIS F O   
15952 C CB  . HIS F 126 ? 0.4491 0.3482 0.4710 -0.0118 -0.0618 -0.0896 126 HIS F CB  
15953 C CG  . HIS F 126 ? 0.4841 0.3834 0.4847 -0.0195 -0.0747 -0.1071 126 HIS F CG  
15954 N ND1 . HIS F 126 ? 0.5628 0.4434 0.5600 -0.0262 -0.0740 -0.1271 126 HIS F ND1 
15955 C CD2 . HIS F 126 ? 0.5082 0.4238 0.4878 -0.0218 -0.0886 -0.1076 126 HIS F CD2 
15956 C CE1 . HIS F 126 ? 0.5774 0.4644 0.5494 -0.0335 -0.0874 -0.1411 126 HIS F CE1 
15957 N NE2 . HIS F 126 ? 0.5449 0.4539 0.5053 -0.0309 -0.0970 -0.1279 126 HIS F NE2 
15958 N N   . SER F 127 ? 0.4284 0.2910 0.4726 0.0032  -0.0278 -0.0757 127 SER F N   
15959 C CA  . SER F 127 ? 0.4319 0.2881 0.5010 0.0029  -0.0194 -0.0614 127 SER F CA  
15960 C C   . SER F 127 ? 0.4402 0.2938 0.5335 -0.0109 -0.0254 -0.0668 127 SER F C   
15961 O O   . SER F 127 ? 0.4602 0.3218 0.5503 -0.0190 -0.0378 -0.0797 127 SER F O   
15962 C CB  . SER F 127 ? 0.4816 0.3157 0.5557 0.0106  -0.0081 -0.0588 127 SER F CB  
15963 O OG  . SER F 127 ? 0.5238 0.3367 0.5987 0.0074  -0.0084 -0.0789 127 SER F OG  
15964 N N   . THR F 128 ? 0.4836 0.3273 0.6020 -0.0147 -0.0171 -0.0561 128 THR F N   
15965 C CA  . THR F 128 ? 0.4741 0.3141 0.6205 -0.0296 -0.0215 -0.0619 128 THR F CA  
15966 C C   . THR F 128 ? 0.4805 0.2885 0.6447 -0.0337 -0.0141 -0.0662 128 THR F C   
15967 O O   . THR F 128 ? 0.4412 0.2328 0.6030 -0.0237 -0.0032 -0.0561 128 THR F O   
15968 C CB  . THR F 128 ? 0.4558 0.3157 0.6239 -0.0344 -0.0175 -0.0450 128 THR F CB  
15969 O OG1 . THR F 128 ? 0.4918 0.3448 0.6628 -0.0286 -0.0027 -0.0251 128 THR F OG1 
15970 C CG2 . THR F 128 ? 0.3921 0.2797 0.5469 -0.0291 -0.0234 -0.0419 128 THR F CG2 
15971 N N   . HIS F 129 ? 0.4820 0.2814 0.6665 -0.0486 -0.0211 -0.0813 129 HIS F N   
15972 C CA  . HIS F 129 ? 0.5390 0.3053 0.7448 -0.0554 -0.0153 -0.0891 129 HIS F CA  
15973 C C   . HIS F 129 ? 0.5594 0.3270 0.8024 -0.0734 -0.0173 -0.0871 129 HIS F C   
15974 O O   . HIS F 129 ? 0.5719 0.3494 0.8226 -0.0867 -0.0311 -0.1049 129 HIS F O   
15975 C CB  . HIS F 129 ? 0.5821 0.3309 0.7716 -0.0574 -0.0222 -0.1191 129 HIS F CB  
15976 C CG  . HIS F 129 ? 0.6315 0.3500 0.8344 -0.0613 -0.0144 -0.1260 129 HIS F CG  
15977 N ND1 . HIS F 129 ? 0.6753 0.3884 0.8858 -0.0771 -0.0221 -0.1440 129 HIS F ND1 
15978 C CD2 . HIS F 129 ? 0.6537 0.3489 0.8619 -0.0507 -0.0004 -0.1151 129 HIS F CD2 
15979 C CE1 . HIS F 129 ? 0.7225 0.4074 0.9428 -0.0763 -0.0123 -0.1453 129 HIS F CE1 
15980 N NE2 . HIS F 129 ? 0.7205 0.3946 0.9404 -0.0599 0.0006  -0.1274 129 HIS F NE2 
15981 N N   . GLY F 130 ? 0.5608 0.3202 0.8274 -0.0747 -0.0038 -0.0645 130 GLY F N   
15982 C CA  . GLY F 130 ? 0.5417 0.3101 0.8425 -0.0911 -0.0027 -0.0577 130 GLY F CA  
15983 C C   . GLY F 130 ? 0.5086 0.3154 0.8136 -0.0947 -0.0105 -0.0554 130 GLY F C   
15984 O O   . GLY F 130 ? 0.4798 0.3061 0.7672 -0.0830 -0.0051 -0.0400 130 GLY F O   
15985 N N   . SER F 131 ? 0.5214 0.3414 0.8492 -0.1103 -0.0238 -0.0706 131 SER F N   
15986 C CA  . SER F 131 ? 0.5283 0.3881 0.8639 -0.1124 -0.0334 -0.0688 131 SER F CA  
15987 C C   . SER F 131 ? 0.5237 0.3979 0.8287 -0.1065 -0.0526 -0.0856 131 SER F C   
15988 O O   . SER F 131 ? 0.5031 0.4088 0.8148 -0.1067 -0.0630 -0.0841 131 SER F O   
15989 C CB  . SER F 131 ? 0.5527 0.4271 0.9317 -0.1312 -0.0382 -0.0717 131 SER F CB  
15990 O OG  . SER F 131 ? 0.5518 0.4234 0.9248 -0.1405 -0.0559 -0.0948 131 SER F OG  
15991 N N   . LYS F 132 ? 0.5557 0.4070 0.8287 -0.1009 -0.0562 -0.1005 132 LYS F N   
15992 C CA  . LYS F 132 ? 0.5402 0.4025 0.7807 -0.0976 -0.0734 -0.1170 132 LYS F CA  
15993 C C   . LYS F 132 ? 0.4819 0.3439 0.6823 -0.0784 -0.0670 -0.1097 132 LYS F C   
15994 O O   . LYS F 132 ? 0.4502 0.3015 0.6474 -0.0679 -0.0506 -0.0944 132 LYS F O   
15995 C CB  . LYS F 132 ? 0.5666 0.4059 0.7994 -0.1087 -0.0828 -0.1447 132 LYS F CB  
15996 C CG  . LYS F 132 ? 0.6004 0.4450 0.8619 -0.1269 -0.0898 -0.1514 132 LYS F CG  
15997 C CD  . LYS F 132 ? 0.6932 0.5362 0.9277 -0.1359 -0.1056 -0.1766 132 LYS F CD  
15998 C CE  . LYS F 132 ? 0.7954 0.6360 1.0558 -0.1544 -0.1098 -0.1844 132 LYS F CE  
15999 N NZ  . LYS F 132 ? 0.8700 0.6868 1.1035 -0.1622 -0.1135 -0.2094 132 LYS F NZ  
16000 N N   . LEU F 133 ? 0.4701 0.3453 0.6404 -0.0749 -0.0806 -0.1194 133 LEU F N   
16001 C CA  . LEU F 133 ? 0.4569 0.3279 0.5885 -0.0595 -0.0748 -0.1170 133 LEU F CA  
16002 C C   . LEU F 133 ? 0.4975 0.3366 0.6159 -0.0566 -0.0646 -0.1302 133 LEU F C   
16003 O O   . LEU F 133 ? 0.5408 0.3636 0.6630 -0.0675 -0.0698 -0.1510 133 LEU F O   
16004 C CB  . LEU F 133 ? 0.4565 0.3465 0.5584 -0.0585 -0.0912 -0.1243 133 LEU F CB  
16005 C CG  . LEU F 133 ? 0.4382 0.3593 0.5482 -0.0564 -0.1017 -0.1098 133 LEU F CG  
16006 C CD1 . LEU F 133 ? 0.4710 0.4040 0.5473 -0.0558 -0.1177 -0.1167 133 LEU F CD1 
16007 C CD2 . LEU F 133 ? 0.3852 0.3117 0.4977 -0.0432 -0.0870 -0.0896 133 LEU F CD2 
16008 N N   . GLY F 134 ? 0.4881 0.3190 0.5932 -0.0418 -0.0504 -0.1192 134 GLY F N   
16009 C CA  . GLY F 134 ? 0.5193 0.3219 0.6163 -0.0357 -0.0394 -0.1296 134 GLY F CA  
16010 C C   . GLY F 134 ? 0.5641 0.3701 0.6237 -0.0256 -0.0385 -0.1388 134 GLY F C   
16011 O O   . GLY F 134 ? 0.5579 0.3858 0.5948 -0.0261 -0.0488 -0.1393 134 GLY F O   
16012 N N   . PRO F 135 ? 0.6138 0.3983 0.6692 -0.0160 -0.0252 -0.1450 135 PRO F N   
16013 C CA  . PRO F 135 ? 0.6121 0.4010 0.6348 -0.0067 -0.0213 -0.1545 135 PRO F CA  
16014 C C   . PRO F 135 ? 0.5268 0.3401 0.5356 0.0035  -0.0204 -0.1340 135 PRO F C   
16015 O O   . PRO F 135 ? 0.4706 0.2915 0.4958 0.0076  -0.0178 -0.1126 135 PRO F O   
16016 C CB  . PRO F 135 ? 0.6441 0.4052 0.6784 0.0031  -0.0050 -0.1617 135 PRO F CB  
16017 C CG  . PRO F 135 ? 0.6380 0.3850 0.7091 0.0031  -0.0002 -0.1441 135 PRO F CG  
16018 C CD  . PRO F 135 ? 0.6225 0.3776 0.7060 -0.0133 -0.0128 -0.1432 135 PRO F CD  
16019 N N   . MET F 136 ? 0.5372 0.3624 0.5145 0.0064  -0.0220 -0.1415 136 MET F N   
16020 C CA  . MET F 136 ? 0.5195 0.3647 0.4831 0.0156  -0.0195 -0.1250 136 MET F CA  
16021 C C   . MET F 136 ? 0.4661 0.3051 0.4428 0.0290  -0.0048 -0.1144 136 MET F C   
16022 O O   . MET F 136 ? 0.5180 0.3393 0.5003 0.0345  0.0056  -0.1257 136 MET F O   
16023 C CB  . MET F 136 ? 0.5912 0.4467 0.5189 0.0148  -0.0216 -0.1361 136 MET F CB  
16024 C CG  . MET F 136 ? 0.6409 0.5024 0.5516 0.0014  -0.0379 -0.1481 136 MET F CG  
16025 S SD  . MET F 136 ? 0.6559 0.5429 0.5702 -0.0017 -0.0535 -0.1260 136 MET F SD  
16026 C CE  . MET F 136 ? 0.5853 0.4857 0.4692 0.0067  -0.0470 -0.1169 136 MET F CE  
16027 N N   . VAL F 137 ? 0.4216 0.2757 0.4038 0.0345  -0.0042 -0.0935 137 VAL F N   
16028 C CA  . VAL F 137 ? 0.4351 0.2896 0.4266 0.0471  0.0067  -0.0821 137 VAL F CA  
16029 C C   . VAL F 137 ? 0.4592 0.3360 0.4326 0.0515  0.0069  -0.0744 137 VAL F C   
16030 O O   . VAL F 137 ? 0.4499 0.3403 0.4099 0.0454  -0.0017 -0.0713 137 VAL F O   
16031 C CB  . VAL F 137 ? 0.3992 0.2500 0.4151 0.0490  0.0082  -0.0633 137 VAL F CB  
16032 C CG1 . VAL F 137 ? 0.3970 0.2213 0.4345 0.0462  0.0117  -0.0696 137 VAL F CG1 
16033 C CG2 . VAL F 137 ? 0.3774 0.2436 0.3924 0.0415  0.0000  -0.0522 137 VAL F CG2 
16034 N N   . LYS F 138 ? 0.4721 0.3524 0.4490 0.0620  0.0166  -0.0713 138 LYS F N   
16035 C CA  . LYS F 138 ? 0.4847 0.3848 0.4466 0.0649  0.0186  -0.0672 138 LYS F CA  
16036 C C   . LYS F 138 ? 0.4657 0.3812 0.4393 0.0707  0.0191  -0.0485 138 LYS F C   
16037 O O   . LYS F 138 ? 0.4699 0.3815 0.4631 0.0770  0.0216  -0.0390 138 LYS F O   
16038 C CB  . LYS F 138 ? 0.5254 0.4235 0.4809 0.0711  0.0305  -0.0814 138 LYS F CB  
16039 C CG  . LYS F 138 ? 0.5882 0.4735 0.5238 0.0643  0.0310  -0.1038 138 LYS F CG  
16040 C CD  . LYS F 138 ? 0.6652 0.5503 0.5936 0.0712  0.0464  -0.1187 138 LYS F CD  
16041 C CE  . LYS F 138 ? 0.7943 0.6669 0.6976 0.0635  0.0478  -0.1441 138 LYS F CE  
16042 N NZ  . LYS F 138 ? 0.9012 0.7465 0.8232 0.0646  0.0512  -0.1597 138 LYS F NZ  
16043 N N   . VAL F 139 ? 0.4585 0.3913 0.4193 0.0675  0.0158  -0.0428 139 VAL F N   
16044 C CA  . VAL F 139 ? 0.3970 0.3472 0.3653 0.0720  0.0174  -0.0301 139 VAL F CA  
16045 C C   . VAL F 139 ? 0.3861 0.3467 0.3479 0.0751  0.0257  -0.0358 139 VAL F C   
16046 O O   . VAL F 139 ? 0.4001 0.3658 0.3432 0.0689  0.0247  -0.0392 139 VAL F O   
16047 C CB  . VAL F 139 ? 0.3563 0.3167 0.3184 0.0651  0.0093  -0.0210 139 VAL F CB  
16048 C CG1 . VAL F 139 ? 0.3383 0.3165 0.3071 0.0675  0.0099  -0.0107 139 VAL F CG1 
16049 C CG2 . VAL F 139 ? 0.3428 0.2944 0.3113 0.0614  0.0040  -0.0173 139 VAL F CG2 
16050 N N   . PRO F 140 ? 0.3956 0.3593 0.3745 0.0851  0.0348  -0.0363 140 PRO F N   
16051 C CA  . PRO F 140 ? 0.4058 0.3790 0.3802 0.0882  0.0463  -0.0448 140 PRO F CA  
16052 C C   . PRO F 140 ? 0.3785 0.3749 0.3493 0.0843  0.0465  -0.0361 140 PRO F C   
16053 O O   . PRO F 140 ? 0.4014 0.4049 0.3588 0.0816  0.0547  -0.0423 140 PRO F O   
16054 C CB  . PRO F 140 ? 0.3843 0.3560 0.3873 0.1017  0.0557  -0.0457 140 PRO F CB  
16055 C CG  . PRO F 140 ? 0.3823 0.3362 0.3987 0.1042  0.0488  -0.0397 140 PRO F CG  
16056 C CD  . PRO F 140 ? 0.3693 0.3276 0.3736 0.0944  0.0359  -0.0287 140 PRO F CD  
16057 N N   . GLN F 141 ? 0.3770 0.3845 0.3586 0.0828  0.0381  -0.0225 141 GLN F N   
16058 C CA  . GLN F 141 ? 0.3678 0.3950 0.3490 0.0771  0.0367  -0.0150 141 GLN F CA  
16059 C C   . GLN F 141 ? 0.3390 0.3626 0.3080 0.0675  0.0255  -0.0095 141 GLN F C   
16060 O O   . GLN F 141 ? 0.3444 0.3779 0.3224 0.0654  0.0194  -0.0017 141 GLN F O   
16061 C CB  . GLN F 141 ? 0.4230 0.4712 0.4312 0.0830  0.0368  -0.0057 141 GLN F CB  
16062 C CG  . GLN F 141 ? 0.4895 0.5486 0.5189 0.0937  0.0494  -0.0092 141 GLN F CG  
16063 C CD  . GLN F 141 ? 0.5584 0.6062 0.6067 0.1063  0.0508  -0.0093 141 GLN F CD  
16064 O OE1 . GLN F 141 ? 0.5398 0.5779 0.5902 0.1072  0.0410  -0.0016 141 GLN F OE1 
16065 N NE2 . GLN F 141 ? 0.6298 0.6776 0.6923 0.1161  0.0647  -0.0182 141 GLN F NE2 
16066 N N   . PHE F 142 ? 0.3522 0.3620 0.3018 0.0619  0.0225  -0.0145 142 PHE F N   
16067 C CA  . PHE F 142 ? 0.3474 0.3534 0.2897 0.0543  0.0131  -0.0098 142 PHE F CA  
16068 C C   . PHE F 142 ? 0.3159 0.3325 0.2552 0.0478  0.0139  -0.0044 142 PHE F C   
16069 O O   . PHE F 142 ? 0.3115 0.3318 0.2411 0.0458  0.0202  -0.0052 142 PHE F O   
16070 C CB  . PHE F 142 ? 0.3637 0.3544 0.2913 0.0511  0.0080  -0.0153 142 PHE F CB  
16071 C CG  . PHE F 142 ? 0.4065 0.3936 0.3338 0.0457  -0.0011 -0.0105 142 PHE F CG  
16072 C CD1 . PHE F 142 ? 0.3829 0.3666 0.3215 0.0465  -0.0049 -0.0089 142 PHE F CD1 
16073 C CD2 . PHE F 142 ? 0.4007 0.3877 0.3178 0.0402  -0.0049 -0.0066 142 PHE F CD2 
16074 C CE1 . PHE F 142 ? 0.3552 0.3367 0.2969 0.0424  -0.0108 -0.0064 142 PHE F CE1 
16075 C CE2 . PHE F 142 ? 0.3434 0.3264 0.2660 0.0371  -0.0125 -0.0024 142 PHE F CE2 
16076 C CZ  . PHE F 142 ? 0.3389 0.3196 0.2748 0.0385  -0.0146 -0.0037 142 PHE F CZ  
16077 N N   . LEU F 143 ? 0.2850 0.3060 0.2325 0.0438  0.0086  0.0007  143 LEU F N   
16078 C CA  . LEU F 143 ? 0.3010 0.3290 0.2501 0.0364  0.0090  0.0053  143 LEU F CA  
16079 C C   . LEU F 143 ? 0.3173 0.3323 0.2574 0.0309  0.0035  0.0077  143 LEU F C   
16080 O O   . LEU F 143 ? 0.3366 0.3423 0.2780 0.0315  -0.0026 0.0061  143 LEU F O   
16081 C CB  . LEU F 143 ? 0.2970 0.3375 0.2614 0.0339  0.0061  0.0071  143 LEU F CB  
16082 C CG  . LEU F 143 ? 0.3066 0.3652 0.2856 0.0391  0.0087  0.0083  143 LEU F CG  
16083 C CD1 . LEU F 143 ? 0.2832 0.3537 0.2720 0.0346  0.0016  0.0098  143 LEU F CD1 
16084 C CD2 . LEU F 143 ? 0.3153 0.3871 0.3011 0.0386  0.0178  0.0096  143 LEU F CD2 
16085 N N   . PHE F 144 ? 0.3237 0.3390 0.2573 0.0257  0.0064  0.0131  144 PHE F N   
16086 C CA  . PHE F 144 ? 0.3266 0.3294 0.2536 0.0217  0.0005  0.0186  144 PHE F CA  
16087 C C   . PHE F 144 ? 0.3537 0.3585 0.2811 0.0142  0.0046  0.0278  144 PHE F C   
16088 O O   . PHE F 144 ? 0.3760 0.3934 0.3104 0.0112  0.0121  0.0285  144 PHE F O   
16089 C CB  . PHE F 144 ? 0.3412 0.3365 0.2502 0.0244  -0.0034 0.0177  144 PHE F CB  
16090 C CG  . PHE F 144 ? 0.3415 0.3425 0.2314 0.0237  0.0041  0.0177  144 PHE F CG  
16091 C CD1 . PHE F 144 ? 0.3438 0.3511 0.2323 0.0288  0.0119  0.0082  144 PHE F CD1 
16092 C CD2 . PHE F 144 ? 0.3273 0.3267 0.2003 0.0181  0.0039  0.0275  144 PHE F CD2 
16093 C CE1 . PHE F 144 ? 0.3477 0.3601 0.2186 0.0284  0.0212  0.0053  144 PHE F CE1 
16094 C CE2 . PHE F 144 ? 0.3381 0.3439 0.1895 0.0165  0.0125  0.0266  144 PHE F CE2 
16095 C CZ  . PHE F 144 ? 0.3513 0.3639 0.2014 0.0217  0.0220  0.0138  144 PHE F CZ  
16096 N N   . SER F 145 ? 0.3650 0.3579 0.2882 0.0110  -0.0007 0.0365  145 SER F N   
16097 C CA  . SER F 145 ? 0.3782 0.3697 0.3029 0.0031  0.0033  0.0482  145 SER F CA  
16098 C C   . SER F 145 ? 0.3866 0.3765 0.2867 0.0013  0.0040  0.0593  145 SER F C   
16099 O O   . SER F 145 ? 0.3900 0.3723 0.2774 0.0047  -0.0052 0.0616  145 SER F O   
16100 C CB  . SER F 145 ? 0.3642 0.3412 0.3070 0.0000  -0.0026 0.0521  145 SER F CB  
16101 O OG  . SER F 145 ? 0.4050 0.3763 0.3512 -0.0080 0.0008  0.0656  145 SER F OG  
16102 N N   . CYS F 146 ? 0.3892 0.3884 0.2822 -0.0047 0.0148  0.0661  146 CYS F N   
16103 C CA  . CYS F 146 ? 0.4165 0.4140 0.2839 -0.0093 0.0167  0.0804  146 CYS F CA  
16104 C C   . CYS F 146 ? 0.4204 0.4046 0.2979 -0.0161 0.0128  0.0987  146 CYS F C   
16105 O O   . CYS F 146 ? 0.4552 0.4421 0.3473 -0.0239 0.0216  0.1050  146 CYS F O   
16106 C CB  . CYS F 146 ? 0.4164 0.4310 0.2704 -0.0129 0.0332  0.0798  146 CYS F CB  
16107 S SG  . CYS F 146 ? 0.5180 0.5419 0.3477 -0.0047 0.0381  0.0617  146 CYS F SG  
16108 N N   . ALA F 147 ? 0.3967 0.3672 0.2696 -0.0132 -0.0005 0.1077  147 ALA F N   
16109 C CA  . ALA F 147 ? 0.3973 0.3512 0.2870 -0.0170 -0.0056 0.1246  147 ALA F CA  
16110 C C   . ALA F 147 ? 0.4790 0.4306 0.3467 -0.0238 -0.0043 0.1489  147 ALA F C   
16111 O O   . ALA F 147 ? 0.5255 0.4872 0.3587 -0.0240 -0.0042 0.1520  147 ALA F O   
16112 C CB  . ALA F 147 ? 0.4028 0.3441 0.3067 -0.0090 -0.0203 0.1228  147 ALA F CB  
16113 N N   . PRO F 148 ? 0.5310 0.4681 0.4178 -0.0302 -0.0030 0.1664  148 PRO F N   
16114 C CA  . PRO F 148 ? 0.5480 0.4796 0.4159 -0.0371 -0.0027 0.1949  148 PRO F CA  
16115 C C   . PRO F 148 ? 0.5652 0.4922 0.4131 -0.0305 -0.0204 0.2082  148 PRO F C   
16116 O O   . PRO F 148 ? 0.5540 0.4717 0.4222 -0.0215 -0.0339 0.2029  148 PRO F O   
16117 C CB  . PRO F 148 ? 0.5460 0.4572 0.4501 -0.0433 -0.0002 0.2075  148 PRO F CB  
16118 C CG  . PRO F 148 ? 0.5014 0.4052 0.4405 -0.0373 -0.0036 0.1839  148 PRO F CG  
16119 C CD  . PRO F 148 ? 0.4926 0.4175 0.4189 -0.0327 -0.0002 0.1593  148 PRO F CD  
16120 N N   . SER F 149 ? 0.5976 0.5328 0.4061 -0.0355 -0.0202 0.2257  149 SER F N   
16121 C CA  . SER F 149 ? 0.6558 0.5921 0.4413 -0.0289 -0.0366 0.2299  149 SER F CA  
16122 C C   . SER F 149 ? 0.6611 0.5799 0.4745 -0.0215 -0.0535 0.2438  149 SER F C   
16123 O O   . SER F 149 ? 0.6376 0.5601 0.4502 -0.0132 -0.0698 0.2393  149 SER F O   
16124 C CB  . SER F 149 ? 0.7612 0.7065 0.5044 -0.0350 -0.0286 0.2378  149 SER F CB  
16125 O OG  . SER F 149 ? 0.8465 0.7796 0.5987 -0.0416 -0.0211 0.2597  149 SER F OG  
16126 N N   . PHE F 150 ? 0.5705 0.4713 0.4119 -0.0243 -0.0491 0.2589  150 PHE F N   
16127 C CA  . PHE F 150 ? 0.5860 0.4704 0.4553 -0.0165 -0.0626 0.2716  150 PHE F CA  
16128 C C   . PHE F 150 ? 0.6011 0.4822 0.5041 -0.0059 -0.0729 0.2561  150 PHE F C   
16129 O O   . PHE F 150 ? 0.6362 0.5105 0.5623 0.0032  -0.0854 0.2616  150 PHE F O   
16130 C CB  . PHE F 150 ? 0.6058 0.4684 0.5031 -0.0220 -0.0537 0.2869  150 PHE F CB  
16131 C CG  . PHE F 150 ? 0.6769 0.5257 0.6170 -0.0227 -0.0464 0.2734  150 PHE F CG  
16132 C CD1 . PHE F 150 ? 0.6374 0.4713 0.6175 -0.0126 -0.0548 0.2665  150 PHE F CD1 
16133 C CD2 . PHE F 150 ? 0.6401 0.4927 0.5812 -0.0337 -0.0305 0.2654  150 PHE F CD2 
16134 C CE1 . PHE F 150 ? 0.5940 0.4145 0.6105 -0.0137 -0.0470 0.2500  150 PHE F CE1 
16135 C CE2 . PHE F 150 ? 0.5890 0.4293 0.5686 -0.0356 -0.0247 0.2513  150 PHE F CE2 
16136 C CZ  . PHE F 150 ? 0.5680 0.3909 0.5833 -0.0256 -0.0329 0.2425  150 PHE F CZ  
16137 N N   . LEU F 151 ? 0.5112 0.3971 0.4208 -0.0069 -0.0664 0.2375  151 LEU F N   
16138 C CA  . LEU F 151 ? 0.5453 0.4245 0.4913 0.0020  -0.0722 0.2225  151 LEU F CA  
16139 C C   . LEU F 151 ? 0.5717 0.4640 0.5123 0.0116  -0.0883 0.2157  151 LEU F C   
16140 O O   . LEU F 151 ? 0.5701 0.4576 0.5444 0.0206  -0.0944 0.2074  151 LEU F O   
16141 C CB  . LEU F 151 ? 0.4921 0.3774 0.4436 -0.0010 -0.0570 0.1933  151 LEU F CB  
16142 C CG  . LEU F 151 ? 0.4495 0.3251 0.4402 0.0056  -0.0553 0.1730  151 LEU F CG  
16143 C CD1 . LEU F 151 ? 0.4337 0.2843 0.4606 0.0057  -0.0544 0.1847  151 LEU F CD1 
16144 C CD2 . LEU F 151 ? 0.4367 0.3216 0.4253 0.0006  -0.0416 0.1482  151 LEU F CD2 
16145 N N   . ALA F 152 ? 0.5786 0.4886 0.4782 0.0089  -0.0934 0.2162  152 ALA F N   
16146 C CA  . ALA F 152 ? 0.5737 0.4972 0.4691 0.0155  -0.1092 0.2090  152 ALA F CA  
16147 C C   . ALA F 152 ? 0.6702 0.5971 0.5583 0.0181  -0.1223 0.2265  152 ALA F C   
16148 O O   . ALA F 152 ? 0.7207 0.6612 0.6044 0.0221  -0.1366 0.2223  152 ALA F O   
16149 C CB  . ALA F 152 ? 0.5516 0.4917 0.4096 0.0110  -0.1080 0.1931  152 ALA F CB  
16150 N N   . GLN F 153 ? 0.6917 0.6063 0.5802 0.0155  -0.1183 0.2467  153 GLN F N   
16151 C CA  . GLN F 153 ? 0.7085 0.6271 0.5813 0.0165  -0.1304 0.2661  153 GLN F CA  
16152 C C   . GLN F 153 ? 0.6586 0.5744 0.5721 0.0272  -0.1447 0.2726  153 GLN F C   
16153 O O   . GLN F 153 ? 0.6357 0.5595 0.5408 0.0299  -0.1591 0.2862  153 GLN F O   
16154 C CB  . GLN F 153 ? 0.8220 0.7276 0.6819 0.0096  -0.1204 0.2871  153 GLN F CB  
16155 C CG  . GLN F 153 ? 0.9517 0.8665 0.7622 -0.0011 -0.1082 0.2853  153 GLN F CG  
16156 C CD  . GLN F 153 ? 1.0816 0.9833 0.8852 -0.0091 -0.0956 0.3057  153 GLN F CD  
16157 O OE1 . GLN F 153 ? 1.1372 1.0203 0.9751 -0.0070 -0.0956 0.3197  153 GLN F OE1 
16158 N NE2 . GLN F 153 ? 1.1179 1.0286 0.8797 -0.0185 -0.0827 0.3055  153 GLN F NE2 
16159 N N   . LYS F 154 ? 0.6358 0.5418 0.5937 0.0333  -0.1403 0.2615  154 LYS F N   
16160 C CA  . LYS F 154 ? 0.6655 0.5682 0.6674 0.0440  -0.1499 0.2659  154 LYS F CA  
16161 C C   . LYS F 154 ? 0.6352 0.5432 0.6722 0.0512  -0.1498 0.2441  154 LYS F C   
16162 O O   . LYS F 154 ? 0.5805 0.4818 0.6256 0.0497  -0.1373 0.2272  154 LYS F O   
16163 C CB  . LYS F 154 ? 0.7321 0.6104 0.7640 0.0456  -0.1419 0.2796  154 LYS F CB  
16164 C CG  . LYS F 154 ? 0.8525 0.7289 0.8859 0.0488  -0.1539 0.3056  154 LYS F CG  
16165 C CD  . LYS F 154 ? 0.9320 0.7824 1.0042 0.0521  -0.1465 0.3169  154 LYS F CD  
16166 C CE  . LYS F 154 ? 0.9468 0.7776 1.0153 0.0426  -0.1275 0.3128  154 LYS F CE  
16167 N NZ  . LYS F 154 ? 1.0001 0.8281 1.0295 0.0324  -0.1253 0.3350  154 LYS F NZ  
16168 N N   . GLY F 155 ? 0.6481 0.5693 0.7062 0.0588  -0.1638 0.2455  155 GLY F N   
16169 C CA  . GLY F 155 ? 0.6304 0.5559 0.7309 0.0668  -0.1626 0.2286  155 GLY F CA  
16170 C C   . GLY F 155 ? 0.6252 0.5709 0.7124 0.0646  -0.1675 0.2109  155 GLY F C   
16171 O O   . GLY F 155 ? 0.6251 0.5800 0.7449 0.0704  -0.1691 0.1988  155 GLY F O   
16172 N N   . LEU F 156 ? 0.6218 0.5746 0.6616 0.0557  -0.1688 0.2087  156 LEU F N   
16173 C CA  . LEU F 156 ? 0.5454 0.5137 0.5714 0.0524  -0.1715 0.1897  156 LEU F CA  
16174 C C   . LEU F 156 ? 0.5450 0.5351 0.5547 0.0502  -0.1901 0.1920  156 LEU F C   
16175 O O   . LEU F 156 ? 0.5698 0.5635 0.5652 0.0498  -0.2005 0.2096  156 LEU F O   
16176 C CB  . LEU F 156 ? 0.5309 0.4938 0.5173 0.0439  -0.1603 0.1814  156 LEU F CB  
16177 C CG  . LEU F 156 ? 0.5566 0.4988 0.5591 0.0446  -0.1435 0.1809  156 LEU F CG  
16178 C CD1 . LEU F 156 ? 0.5495 0.4893 0.5176 0.0363  -0.1326 0.1726  156 LEU F CD1 
16179 C CD2 . LEU F 156 ? 0.5075 0.4444 0.5583 0.0529  -0.1381 0.1678  156 LEU F CD2 
16180 N N   . PRO F 157 ? 0.5318 0.5364 0.5445 0.0483  -0.1948 0.1742  157 PRO F N   
16181 C CA  . PRO F 157 ? 0.5649 0.5904 0.5588 0.0438  -0.2125 0.1733  157 PRO F CA  
16182 C C   . PRO F 157 ? 0.6028 0.6297 0.5387 0.0354  -0.2147 0.1783  157 PRO F C   
16183 O O   . PRO F 157 ? 0.6267 0.6406 0.5360 0.0318  -0.2007 0.1786  157 PRO F O   
16184 C CB  . PRO F 157 ? 0.5414 0.5763 0.5451 0.0407  -0.2121 0.1505  157 PRO F CB  
16185 C CG  . PRO F 157 ? 0.4927 0.5158 0.5390 0.0481  -0.1978 0.1442  157 PRO F CG  
16186 C CD  . PRO F 157 ? 0.4847 0.4872 0.5220 0.0502  -0.1849 0.1546  157 PRO F CD  
16187 N N   . ASN F 158 ? 0.6090 0.6526 0.5258 0.0321  -0.2315 0.1821  158 ASN F N   
16188 C CA  . ASN F 158 ? 0.6461 0.6913 0.5085 0.0252  -0.2330 0.1880  158 ASN F CA  
16189 C C   . ASN F 158 ? 0.6113 0.6546 0.4365 0.0169  -0.2205 0.1663  158 ASN F C   
16190 O O   . ASN F 158 ? 0.5630 0.6126 0.3965 0.0142  -0.2215 0.1457  158 ASN F O   
16191 C CB  . ASN F 158 ? 0.7618 0.8270 0.6123 0.0234  -0.2552 0.1938  158 ASN F CB  
16192 C CG  . ASN F 158 ? 0.9025 0.9675 0.7019 0.0188  -0.2578 0.2070  158 ASN F CG  
16193 O OD1 . ASN F 158 ? 0.9583 1.0267 0.7112 0.0107  -0.2534 0.1933  158 ASN F OD1 
16194 N ND2 . ASN F 158 ? 0.9671 1.0270 0.7751 0.0240  -0.2638 0.2338  158 ASN F ND2 
16195 N N   . ASN F 159 ? 0.6997 0.7331 0.4873 0.0130  -0.2074 0.1716  159 ASN F N   
16196 C CA  . ASN F 159 ? 0.7862 0.8167 0.5371 0.0060  -0.1921 0.1526  159 ASN F CA  
16197 C C   . ASN F 159 ? 0.6874 0.7070 0.4593 0.0071  -0.1771 0.1392  159 ASN F C   
16198 O O   . ASN F 159 ? 0.6655 0.6831 0.4116 0.0021  -0.1646 0.1224  159 ASN F O   
16199 C CB  . ASN F 159 ? 0.9509 0.9959 0.6731 -0.0006 -0.2007 0.1315  159 ASN F CB  
16200 C CG  . ASN F 159 ? 1.0859 1.1272 0.7611 -0.0073 -0.1837 0.1154  159 ASN F CG  
16201 O OD1 . ASN F 159 ? 1.1234 1.1569 0.7758 -0.0082 -0.1698 0.1265  159 ASN F OD1 
16202 N ND2 . ASN F 159 ? 1.1286 1.1742 0.7935 -0.0120 -0.1827 0.0886  159 ASN F ND2 
16203 N N   . VAL F 160 ? 0.6156 0.6281 0.4342 0.0142  -0.1779 0.1454  160 VAL F N   
16204 C CA  . VAL F 160 ? 0.5530 0.5545 0.3907 0.0158  -0.1650 0.1341  160 VAL F CA  
16205 C C   . VAL F 160 ? 0.5938 0.5818 0.4179 0.0140  -0.1475 0.1432  160 VAL F C   
16206 O O   . VAL F 160 ? 0.6136 0.5953 0.4411 0.0153  -0.1463 0.1630  160 VAL F O   
16207 C CB  . VAL F 160 ? 0.4898 0.4889 0.3823 0.0243  -0.1703 0.1353  160 VAL F CB  
16208 C CG1 . VAL F 160 ? 0.4347 0.4192 0.3478 0.0276  -0.1556 0.1291  160 VAL F CG1 
16209 C CG2 . VAL F 160 ? 0.4810 0.4943 0.3872 0.0235  -0.1829 0.1206  160 VAL F CG2 
16210 N N   . GLN F 161 ? 0.5812 0.5651 0.3911 0.0104  -0.1332 0.1278  161 GLN F N   
16211 C CA  . GLN F 161 ? 0.5763 0.5540 0.3691 0.0066  -0.1137 0.1311  161 GLN F CA  
16212 C C   . GLN F 161 ? 0.5421 0.5106 0.3676 0.0105  -0.0965 0.1202  161 GLN F C   
16213 O O   . GLN F 161 ? 0.5443 0.5119 0.3598 0.0072  -0.0794 0.1154  161 GLN F O   
16214 C CB  . GLN F 161 ? 0.6222 0.6086 0.3705 0.0000  -0.1048 0.1166  161 GLN F CB  
16215 C CG  . GLN F 161 ? 0.7256 0.7212 0.4375 -0.0041 -0.1132 0.1245  161 GLN F CG  
16216 C CD  . GLN F 161 ? 0.8112 0.8155 0.4862 -0.0088 -0.1079 0.1014  161 GLN F CD  
16217 O OE1 . GLN F 161 ? 0.8499 0.8533 0.5084 -0.0115 -0.0892 0.0895  161 GLN F OE1 
16218 N NE2 . GLN F 161 ? 0.8370 0.8499 0.5024 -0.0095 -0.1240 0.0935  161 GLN F NE2 
16219 N N   . GLY F 162 ? 0.4626 0.4267 0.3270 0.0172  -0.1008 0.1151  162 GLY F N   
16220 C CA  . GLY F 162 ? 0.4127 0.3695 0.3037 0.0199  -0.0861 0.1038  162 GLY F CA  
16221 C C   . GLY F 162 ? 0.3730 0.3297 0.2969 0.0264  -0.0904 0.0926  162 GLY F C   
16222 O O   . GLY F 162 ? 0.3966 0.3575 0.3322 0.0296  -0.1051 0.0981  162 GLY F O   
16223 N N   . ALA F 163 ? 0.3614 0.3155 0.3009 0.0280  -0.0777 0.0778  163 ALA F N   
16224 C CA  . ALA F 163 ? 0.3821 0.3372 0.3509 0.0332  -0.0785 0.0671  163 ALA F CA  
16225 C C   . ALA F 163 ? 0.3916 0.3499 0.3568 0.0325  -0.0665 0.0493  163 ALA F C   
16226 O O   . ALA F 163 ? 0.3764 0.3341 0.3291 0.0296  -0.0563 0.0459  163 ALA F O   
16227 C CB  . ALA F 163 ? 0.3697 0.3148 0.3715 0.0375  -0.0763 0.0722  163 ALA F CB  
16228 N N   . LEU F 164 ? 0.4053 0.3683 0.3842 0.0350  -0.0681 0.0396  164 LEU F N   
16229 C CA  . LEU F 164 ? 0.3630 0.3278 0.3428 0.0350  -0.0570 0.0261  164 LEU F CA  
16230 C C   . LEU F 164 ? 0.3473 0.3101 0.3539 0.0381  -0.0504 0.0213  164 LEU F C   
16231 O O   . LEU F 164 ? 0.3771 0.3413 0.4067 0.0414  -0.0548 0.0225  164 LEU F O   
16232 C CB  . LEU F 164 ? 0.3765 0.3465 0.3494 0.0340  -0.0609 0.0185  164 LEU F CB  
16233 C CG  . LEU F 164 ? 0.4160 0.3912 0.4094 0.0349  -0.0715 0.0185  164 LEU F CG  
16234 C CD1 . LEU F 164 ? 0.4124 0.3900 0.4226 0.0353  -0.0641 0.0088  164 LEU F CD1 
16235 C CD2 . LEU F 164 ? 0.4194 0.3991 0.3973 0.0313  -0.0859 0.0206  164 LEU F CD2 
16236 N N   . GLY F 165 ? 0.3347 0.2957 0.3385 0.0367  -0.0396 0.0152  165 GLY F N   
16237 C CA  . GLY F 165 ? 0.3298 0.2888 0.3527 0.0381  -0.0321 0.0083  165 GLY F CA  
16238 C C   . GLY F 165 ? 0.3144 0.2803 0.3359 0.0379  -0.0248 -0.0012 165 GLY F C   
16239 O O   . GLY F 165 ? 0.3363 0.3059 0.3407 0.0361  -0.0225 -0.0028 165 GLY F O   
16240 N N   . LEU F 166 ? 0.2726 0.2404 0.3137 0.0401  -0.0202 -0.0065 166 LEU F N   
16241 C CA  . LEU F 166 ? 0.2847 0.2593 0.3258 0.0393  -0.0117 -0.0134 166 LEU F CA  
16242 C C   . LEU F 166 ? 0.2810 0.2557 0.3262 0.0383  -0.0004 -0.0229 166 LEU F C   
16243 O O   . LEU F 166 ? 0.2913 0.2721 0.3422 0.0381  0.0084  -0.0284 166 LEU F O   
16244 C CB  . LEU F 166 ? 0.3127 0.2931 0.3732 0.0411  -0.0139 -0.0124 166 LEU F CB  
16245 C CG  . LEU F 166 ? 0.3515 0.3327 0.4055 0.0400  -0.0252 -0.0068 166 LEU F CG  
16246 C CD1 . LEU F 166 ? 0.3460 0.3345 0.4243 0.0402  -0.0291 -0.0065 166 LEU F CD1 
16247 C CD2 . LEU F 166 ? 0.3797 0.3601 0.4129 0.0373  -0.0219 -0.0082 166 LEU F CD2 
16248 N N   . GLY F 167 ? 0.2962 0.2638 0.3381 0.0366  0.0001  -0.0253 167 GLY F N   
16249 C CA  . GLY F 167 ? 0.2903 0.2556 0.3348 0.0342  0.0099  -0.0375 167 GLY F CA  
16250 C C   . GLY F 167 ? 0.3006 0.2747 0.3213 0.0287  0.0146  -0.0432 167 GLY F C   
16251 O O   . GLY F 167 ? 0.3020 0.2826 0.3069 0.0277  0.0101  -0.0360 167 GLY F O   
16252 N N   . GLN F 168 ? 0.3252 0.2996 0.3438 0.0253  0.0236  -0.0564 168 GLN F N   
16253 C CA  . GLN F 168 ? 0.3236 0.3084 0.3176 0.0190  0.0263  -0.0617 168 GLN F CA  
16254 C C   . GLN F 168 ? 0.3097 0.2939 0.2942 0.0132  0.0194  -0.0625 168 GLN F C   
16255 O O   . GLN F 168 ? 0.3293 0.3089 0.3147 0.0077  0.0224  -0.0751 168 GLN F O   
16256 C CB  . GLN F 168 ? 0.3621 0.3491 0.3539 0.0163  0.0391  -0.0775 168 GLN F CB  
16257 C CG  . GLN F 168 ? 0.3543 0.3482 0.3514 0.0201  0.0476  -0.0749 168 GLN F CG  
16258 C CD  . GLN F 168 ? 0.3791 0.3843 0.3551 0.0182  0.0440  -0.0628 168 GLN F CD  
16259 O OE1 . GLN F 168 ? 0.4190 0.4332 0.3700 0.0126  0.0448  -0.0649 168 GLN F OE1 
16260 N NE2 . GLN F 168 ? 0.3557 0.3602 0.3420 0.0226  0.0389  -0.0499 168 GLN F NE2 
16261 N N   . ALA F 169 ? 0.3236 0.3129 0.3014 0.0142  0.0110  -0.0499 169 ALA F N   
16262 C CA  . ALA F 169 ? 0.3258 0.3179 0.2999 0.0092  0.0048  -0.0479 169 ALA F CA  
16263 C C   . ALA F 169 ? 0.3310 0.3355 0.2948 0.0116  -0.0008 -0.0360 169 ALA F C   
16264 O O   . ALA F 169 ? 0.3560 0.3595 0.3198 0.0178  -0.0009 -0.0284 169 ALA F O   
16265 C CB  . ALA F 169 ? 0.3010 0.2790 0.2912 0.0098  0.0028  -0.0442 169 ALA F CB  
16266 N N   . PRO F 170 ? 0.3309 0.3472 0.2895 0.0067  -0.0053 -0.0352 170 PRO F N   
16267 C CA  . PRO F 170 ? 0.2912 0.3220 0.2434 0.0101  -0.0096 -0.0253 170 PRO F CA  
16268 C C   . PRO F 170 ? 0.3364 0.3627 0.2941 0.0172  -0.0100 -0.0155 170 PRO F C   
16269 O O   . PRO F 170 ? 0.3611 0.3929 0.3157 0.0226  -0.0109 -0.0088 170 PRO F O   
16270 C CB  . PRO F 170 ? 0.3126 0.3579 0.2659 0.0027  -0.0148 -0.0276 170 PRO F CB  
16271 C CG  . PRO F 170 ? 0.3222 0.3562 0.2845 -0.0045 -0.0128 -0.0366 170 PRO F CG  
16272 C CD  . PRO F 170 ? 0.3530 0.3711 0.3145 -0.0027 -0.0067 -0.0446 170 PRO F CD  
16273 N N   . ILE F 171 ? 0.3633 0.3794 0.3278 0.0172  -0.0093 -0.0143 171 ILE F N   
16274 C CA  . ILE F 171 ? 0.2822 0.2949 0.2459 0.0234  -0.0093 -0.0072 171 ILE F CA  
16275 C C   . ILE F 171 ? 0.2942 0.2926 0.2596 0.0262  -0.0095 -0.0068 171 ILE F C   
16276 O O   . ILE F 171 ? 0.3015 0.2954 0.2644 0.0282  -0.0108 -0.0025 171 ILE F O   
16277 C CB  . ILE F 171 ? 0.3007 0.3191 0.2667 0.0217  -0.0087 -0.0029 171 ILE F CB  
16278 C CG1 . ILE F 171 ? 0.2999 0.3102 0.2710 0.0152  -0.0082 -0.0029 171 ILE F CG1 
16279 C CG2 . ILE F 171 ? 0.3006 0.3377 0.2703 0.0207  -0.0097 -0.0020 171 ILE F CG2 
16280 C CD1 . ILE F 171 ? 0.2894 0.3017 0.2594 0.0141  -0.0057 0.0041  171 ILE F CD1 
16281 N N   . SER F 172 ? 0.3565 0.3502 0.3259 0.0263  -0.0082 -0.0114 172 SER F N   
16282 C CA  . SER F 172 ? 0.3444 0.3292 0.3206 0.0296  -0.0094 -0.0104 172 SER F CA  
16283 C C   . SER F 172 ? 0.3539 0.3395 0.3254 0.0334  -0.0110 -0.0069 172 SER F C   
16284 O O   . SER F 172 ? 0.3619 0.3532 0.3273 0.0347  -0.0094 -0.0054 172 SER F O   
16285 C CB  . SER F 172 ? 0.3274 0.3109 0.3125 0.0294  -0.0050 -0.0167 172 SER F CB  
16286 O OG  . SER F 172 ? 0.3424 0.3337 0.3198 0.0291  -0.0010 -0.0180 172 SER F OG  
16287 N N   . LEU F 173 ? 0.3689 0.3485 0.3452 0.0350  -0.0151 -0.0056 173 LEU F N   
16288 C CA  . LEU F 173 ? 0.3443 0.3223 0.3168 0.0368  -0.0171 -0.0050 173 LEU F CA  
16289 C C   . LEU F 173 ? 0.3345 0.3140 0.3111 0.0376  -0.0127 -0.0058 173 LEU F C   
16290 O O   . LEU F 173 ? 0.3482 0.3273 0.3198 0.0395  -0.0111 -0.0044 173 LEU F O   
16291 C CB  . LEU F 173 ? 0.3366 0.3103 0.3143 0.0365  -0.0245 -0.0046 173 LEU F CB  
16292 C CG  . LEU F 173 ? 0.3381 0.3090 0.3148 0.0363  -0.0271 -0.0075 173 LEU F CG  
16293 C CD1 . LEU F 173 ? 0.3405 0.3090 0.3011 0.0374  -0.0254 -0.0095 173 LEU F CD1 
16294 C CD2 . LEU F 173 ? 0.3266 0.2972 0.3100 0.0344  -0.0370 -0.0074 173 LEU F CD2 
16295 N N   . GLN F 174 ? 0.3443 0.3257 0.3310 0.0363  -0.0094 -0.0072 174 GLN F N   
16296 C CA  . GLN F 174 ? 0.3149 0.2980 0.3044 0.0358  -0.0039 -0.0054 174 GLN F CA  
16297 C C   . GLN F 174 ? 0.3527 0.3413 0.3297 0.0363  -0.0004 -0.0017 174 GLN F C   
16298 O O   . GLN F 174 ? 0.3834 0.3711 0.3589 0.0375  0.0015  0.0040  174 GLN F O   
16299 C CB  . GLN F 174 ? 0.3245 0.3111 0.3275 0.0339  0.0015  -0.0080 174 GLN F CB  
16300 C CG  . GLN F 174 ? 0.2923 0.2850 0.2901 0.0324  0.0088  -0.0121 174 GLN F CG  
16301 C CD  . GLN F 174 ? 0.3213 0.3114 0.3228 0.0328  0.0063  -0.0176 174 GLN F CD  
16302 O OE1 . GLN F 174 ? 0.3354 0.3202 0.3426 0.0346  -0.0011 -0.0155 174 GLN F OE1 
16303 N NE2 . GLN F 174 ? 0.3248 0.3177 0.3224 0.0306  0.0127  -0.0245 174 GLN F NE2 
16304 N N   . ASN F 175 ? 0.3730 0.3674 0.3429 0.0350  -0.0005 -0.0041 175 ASN F N   
16305 C CA  . ASN F 175 ? 0.3813 0.3852 0.3403 0.0343  0.0001  -0.0010 175 ASN F CA  
16306 C C   . ASN F 175 ? 0.3347 0.3392 0.2929 0.0389  -0.0031 0.0056  175 ASN F C   
16307 O O   . ASN F 175 ? 0.3261 0.3356 0.2815 0.0411  -0.0030 0.0132  175 ASN F O   
16308 C CB  . ASN F 175 ? 0.4989 0.5079 0.4544 0.0302  -0.0008 -0.0078 175 ASN F CB  
16309 C CG  . ASN F 175 ? 0.6419 0.6643 0.5864 0.0273  -0.0026 -0.0065 175 ASN F CG  
16310 O OD1 . ASN F 175 ? 0.6801 0.7097 0.6248 0.0290  -0.0072 -0.0014 175 ASN F OD1 
16311 N ND2 . ASN F 175 ? 0.7078 0.7355 0.6433 0.0223  0.0009  -0.0121 175 ASN F ND2 
16312 N N   . GLN F 176 ? 0.3044 0.3037 0.2655 0.0410  -0.0054 0.0034  176 GLN F N   
16313 C CA  . GLN F 176 ? 0.3209 0.3203 0.2832 0.0462  -0.0057 0.0066  176 GLN F CA  
16314 C C   . GLN F 176 ? 0.3404 0.3284 0.3081 0.0497  -0.0040 0.0085  176 GLN F C   
16315 O O   . GLN F 176 ? 0.3714 0.3587 0.3436 0.0550  -0.0026 0.0132  176 GLN F O   
16316 C CB  . GLN F 176 ? 0.3035 0.3017 0.2637 0.0460  -0.0063 0.0024  176 GLN F CB  
16317 C CG  . GLN F 176 ? 0.2864 0.2954 0.2455 0.0425  -0.0069 0.0025  176 GLN F CG  
16318 C CD  . GLN F 176 ? 0.2924 0.3020 0.2491 0.0423  -0.0052 0.0016  176 GLN F CD  
16319 O OE1 . GLN F 176 ? 0.2957 0.3105 0.2545 0.0466  -0.0017 0.0023  176 GLN F OE1 
16320 N NE2 . GLN F 176 ? 0.2939 0.2982 0.2470 0.0376  -0.0067 0.0007  176 GLN F NE2 
16321 N N   . LEU F 177 ? 0.3285 0.3075 0.2993 0.0467  -0.0043 0.0048  177 LEU F N   
16322 C CA  . LEU F 177 ? 0.3015 0.2694 0.2801 0.0475  -0.0029 0.0058  177 LEU F CA  
16323 C C   . LEU F 177 ? 0.2859 0.2555 0.2679 0.0475  0.0009  0.0158  177 LEU F C   
16324 O O   . LEU F 177 ? 0.3105 0.2716 0.2992 0.0508  0.0029  0.0215  177 LEU F O   
16325 C CB  . LEU F 177 ? 0.3258 0.2879 0.3101 0.0426  -0.0057 -0.0005 177 LEU F CB  
16326 C CG  . LEU F 177 ? 0.2936 0.2530 0.2727 0.0414  -0.0117 -0.0083 177 LEU F CG  
16327 C CD1 . LEU F 177 ? 0.3069 0.2653 0.2966 0.0365  -0.0164 -0.0111 177 LEU F CD1 
16328 C CD2 . LEU F 177 ? 0.3044 0.2549 0.2784 0.0437  -0.0114 -0.0141 177 LEU F CD2 
16329 N N   . PHE F 178 ? 0.2801 0.2592 0.2572 0.0437  0.0027  0.0181  178 PHE F N   
16330 C CA  . PHE F 178 ? 0.3068 0.2901 0.2808 0.0426  0.0069  0.0288  178 PHE F CA  
16331 C C   . PHE F 178 ? 0.3456 0.3331 0.3163 0.0484  0.0042  0.0392  178 PHE F C   
16332 O O   . PHE F 178 ? 0.4242 0.4060 0.3998 0.0508  0.0060  0.0510  178 PHE F O   
16333 C CB  . PHE F 178 ? 0.2846 0.2805 0.2479 0.0376  0.0101  0.0267  178 PHE F CB  
16334 C CG  . PHE F 178 ? 0.3045 0.2988 0.2763 0.0332  0.0148  0.0184  178 PHE F CG  
16335 C CD1 . PHE F 178 ? 0.2846 0.2700 0.2728 0.0321  0.0158  0.0175  178 PHE F CD1 
16336 C CD2 . PHE F 178 ? 0.2930 0.2958 0.2590 0.0300  0.0184  0.0107  178 PHE F CD2 
16337 C CE1 . PHE F 178 ? 0.2949 0.2829 0.2961 0.0288  0.0192  0.0110  178 PHE F CE1 
16338 C CE2 . PHE F 178 ? 0.3053 0.3079 0.2846 0.0278  0.0237  0.0033  178 PHE F CE2 
16339 C CZ  . PHE F 178 ? 0.2921 0.2888 0.2902 0.0276  0.0237  0.0045  178 PHE F CZ  
16340 N N   . SER F 179 ? 0.3340 0.3323 0.2995 0.0505  -0.0002 0.0362  179 SER F N   
16341 C CA  . SER F 179 ? 0.3567 0.3655 0.3226 0.0558  -0.0041 0.0468  179 SER F CA  
16342 C C   . SER F 179 ? 0.3317 0.3305 0.3133 0.0648  -0.0035 0.0495  179 SER F C   
16343 O O   . SER F 179 ? 0.3541 0.3554 0.3433 0.0710  -0.0052 0.0623  179 SER F O   
16344 C CB  . SER F 179 ? 0.4062 0.4327 0.3652 0.0535  -0.0090 0.0420  179 SER F CB  
16345 O OG  . SER F 179 ? 0.4793 0.5039 0.4457 0.0556  -0.0089 0.0334  179 SER F OG  
16346 N N   . HIS F 180 ? 0.2897 0.2773 0.2762 0.0656  -0.0011 0.0375  180 HIS F N   
16347 C CA  . HIS F 180 ? 0.2942 0.2714 0.2941 0.0736  0.0017  0.0363  180 HIS F CA  
16348 C C   . HIS F 180 ? 0.3517 0.3110 0.3624 0.0758  0.0046  0.0433  180 HIS F C   
16349 O O   . HIS F 180 ? 0.4049 0.3582 0.4302 0.0844  0.0062  0.0504  180 HIS F O   
16350 C CB  . HIS F 180 ? 0.3256 0.2946 0.3227 0.0724  0.0041  0.0204  180 HIS F CB  
16351 C CG  . HIS F 180 ? 0.3527 0.3125 0.3613 0.0808  0.0093  0.0154  180 HIS F CG  
16352 N ND1 . HIS F 180 ? 0.3925 0.3651 0.4098 0.0885  0.0117  0.0174  180 HIS F ND1 
16353 C CD2 . HIS F 180 ? 0.3666 0.3059 0.3819 0.0825  0.0134  0.0072  180 HIS F CD2 
16354 C CE1 . HIS F 180 ? 0.3800 0.3401 0.4087 0.0958  0.0187  0.0100  180 HIS F CE1 
16355 N NE2 . HIS F 180 ? 0.3911 0.3294 0.4174 0.0920  0.0196  0.0029  180 HIS F NE2 
16356 N N   . PHE F 181 ? 0.3205 0.2709 0.3278 0.0681  0.0058  0.0418  181 PHE F N   
16357 C CA  . PHE F 181 ? 0.3260 0.2570 0.3465 0.0678  0.0094  0.0469  181 PHE F CA  
16358 C C   . PHE F 181 ? 0.3617 0.2968 0.3803 0.0651  0.0105  0.0652  181 PHE F C   
16359 O O   . PHE F 181 ? 0.4293 0.3490 0.4596 0.0638  0.0143  0.0734  181 PHE F O   
16360 C CB  . PHE F 181 ? 0.3075 0.2261 0.3306 0.0598  0.0103  0.0328  181 PHE F CB  
16361 C CG  . PHE F 181 ? 0.3203 0.2319 0.3420 0.0613  0.0091  0.0151  181 PHE F CG  
16362 C CD1 . PHE F 181 ? 0.3559 0.2500 0.3890 0.0667  0.0127  0.0092  181 PHE F CD1 
16363 C CD2 . PHE F 181 ? 0.3399 0.2617 0.3483 0.0573  0.0051  0.0046  181 PHE F CD2 
16364 C CE1 . PHE F 181 ? 0.3702 0.2588 0.3973 0.0671  0.0131  -0.0090 181 PHE F CE1 
16365 C CE2 . PHE F 181 ? 0.3405 0.2574 0.3425 0.0577  0.0042  -0.0099 181 PHE F CE2 
16366 C CZ  . PHE F 181 ? 0.3556 0.2567 0.3650 0.0621  0.0086  -0.0178 181 PHE F CZ  
16367 N N   . GLY F 182 ? 0.3645 0.3200 0.3671 0.0629  0.0078  0.0710  182 GLY F N   
16368 C CA  . GLY F 182 ? 0.3481 0.3104 0.3417 0.0589  0.0096  0.0876  182 GLY F CA  
16369 C C   . GLY F 182 ? 0.3525 0.3094 0.3458 0.0491  0.0167  0.0850  182 GLY F C   
16370 O O   . GLY F 182 ? 0.3776 0.3298 0.3726 0.0460  0.0217  0.1000  182 GLY F O   
16371 N N   . LEU F 183 ? 0.3442 0.3029 0.3374 0.0444  0.0173  0.0676  183 LEU F N   
16372 C CA  . LEU F 183 ? 0.3611 0.3178 0.3611 0.0359  0.0238  0.0637  183 LEU F CA  
16373 C C   . LEU F 183 ? 0.4299 0.4030 0.4146 0.0303  0.0302  0.0681  183 LEU F C   
16374 O O   . LEU F 183 ? 0.4805 0.4675 0.4465 0.0317  0.0274  0.0674  183 LEU F O   
16375 C CB  . LEU F 183 ? 0.3124 0.2673 0.3203 0.0340  0.0203  0.0451  183 LEU F CB  
16376 C CG  . LEU F 183 ? 0.3266 0.2672 0.3444 0.0372  0.0147  0.0358  183 LEU F CG  
16377 C CD1 . LEU F 183 ? 0.3061 0.2505 0.3241 0.0350  0.0093  0.0207  183 LEU F CD1 
16378 C CD2 . LEU F 183 ? 0.3587 0.2821 0.3949 0.0335  0.0178  0.0391  183 LEU F CD2 
16379 N N   . LYS F 184 ? 0.4048 0.3774 0.3984 0.0232  0.0395  0.0706  184 LYS F N   
16380 C CA  . LYS F 184 ? 0.3759 0.3648 0.3568 0.0175  0.0488  0.0694  184 LYS F CA  
16381 C C   . LYS F 184 ? 0.3470 0.3436 0.3271 0.0187  0.0456  0.0501  184 LYS F C   
16382 O O   . LYS F 184 ? 0.3479 0.3377 0.3452 0.0204  0.0401  0.0399  184 LYS F O   
16383 C CB  . LYS F 184 ? 0.3764 0.3643 0.3737 0.0096  0.0612  0.0743  184 LYS F CB  
16384 C CG  . LYS F 184 ? 0.7332 0.7392 0.7210 0.0038  0.0746  0.0696  184 LYS F CG  
16385 C CD  . LYS F 184 ? 0.7866 0.7950 0.7876 -0.0048 0.0901  0.0805  184 LYS F CD  
16386 C CE  . LYS F 184 ? 0.8063 0.8341 0.7977 -0.0100 0.1068  0.0739  184 LYS F CE  
16387 N NZ  . LYS F 184 ? 0.7987 0.8347 0.7995 -0.0065 0.1063  0.0512  184 LYS F NZ  
16388 N N   . ARG F 185 ? 0.3410 0.3513 0.3011 0.0173  0.0489  0.0452  185 ARG F N   
16389 C CA  . ARG F 185 ? 0.2960 0.3107 0.2565 0.0186  0.0464  0.0279  185 ARG F CA  
16390 C C   . ARG F 185 ? 0.2998 0.3177 0.2796 0.0158  0.0560  0.0179  185 ARG F C   
16391 O O   . ARG F 185 ? 0.3130 0.3408 0.2863 0.0125  0.0674  0.0121  185 ARG F O   
16392 C CB  . ARG F 185 ? 0.3284 0.3547 0.2622 0.0171  0.0459  0.0245  185 ARG F CB  
16393 C CG  . ARG F 185 ? 0.3493 0.3769 0.2694 0.0204  0.0348  0.0361  185 ARG F CG  
16394 C CD  . ARG F 185 ? 0.3846 0.4259 0.2811 0.0179  0.0300  0.0314  185 ARG F CD  
16395 N NE  . ARG F 185 ? 0.3790 0.4186 0.2823 0.0188  0.0248  0.0157  185 ARG F NE  
16396 C CZ  . ARG F 185 ? 0.3609 0.3980 0.2719 0.0231  0.0147  0.0166  185 ARG F CZ  
16397 N NH1 . ARG F 185 ? 0.3648 0.3999 0.2816 0.0223  0.0120  0.0039  185 ARG F NH1 
16398 N NH2 . ARG F 185 ? 0.3841 0.4201 0.2988 0.0284  0.0086  0.0303  185 ARG F NH2 
16399 N N   . GLN F 186 ? 0.2853 0.2956 0.2902 0.0174  0.0511  0.0154  186 GLN F N   
16400 C CA  . GLN F 186 ? 0.2910 0.3062 0.3222 0.0155  0.0575  0.0086  186 GLN F CA  
16401 C C   . GLN F 186 ? 0.2845 0.2920 0.3356 0.0182  0.0443  0.0047  186 GLN F C   
16402 O O   . GLN F 186 ? 0.2923 0.2896 0.3411 0.0185  0.0359  0.0098  186 GLN F O   
16403 C CB  . GLN F 186 ? 0.3108 0.3301 0.3519 0.0093  0.0697  0.0181  186 GLN F CB  
16404 C CG  . GLN F 186 ? 0.3673 0.3961 0.4415 0.0065  0.0783  0.0124  186 GLN F CG  
16405 C CD  . GLN F 186 ? 0.4337 0.4638 0.5216 -0.0012 0.0880  0.0242  186 GLN F CD  
16406 O OE1 . GLN F 186 ? 0.5007 0.5369 0.5734 -0.0056 0.1022  0.0325  186 GLN F OE1 
16407 N NE2 . GLN F 186 ? 0.4262 0.4500 0.5409 -0.0038 0.0798  0.0257  186 GLN F NE2 
16408 N N   . PHE F 187 ? 0.2998 0.3118 0.3697 0.0205  0.0421  -0.0041 187 PHE F N   
16409 C CA  . PHE F 187 ? 0.3129 0.3212 0.4024 0.0213  0.0289  -0.0056 187 PHE F CA  
16410 C C   . PHE F 187 ? 0.2720 0.2920 0.3965 0.0208  0.0320  -0.0095 187 PHE F C   
16411 O O   . PHE F 187 ? 0.2337 0.2630 0.3669 0.0220  0.0448  -0.0137 187 PHE F O   
16412 C CB  . PHE F 187 ? 0.3254 0.3265 0.4016 0.0261  0.0159  -0.0087 187 PHE F CB  
16413 C CG  . PHE F 187 ? 0.3128 0.3172 0.3925 0.0302  0.0173  -0.0145 187 PHE F CG  
16414 C CD1 . PHE F 187 ? 0.3394 0.3431 0.3991 0.0309  0.0239  -0.0177 187 PHE F CD1 
16415 C CD2 . PHE F 187 ? 0.2774 0.2854 0.3823 0.0330  0.0110  -0.0165 187 PHE F CD2 
16416 C CE1 . PHE F 187 ? 0.3462 0.3495 0.4119 0.0338  0.0258  -0.0249 187 PHE F CE1 
16417 C CE2 . PHE F 187 ? 0.2549 0.2626 0.3674 0.0376  0.0128  -0.0210 187 PHE F CE2 
16418 C CZ  . PHE F 187 ? 0.2965 0.3002 0.3898 0.0378  0.0209  -0.0261 187 PHE F CZ  
16419 N N   . SER F 188 ? 0.2520 0.2729 0.3978 0.0185  0.0208  -0.0087 188 SER F N   
16420 C CA  . SER F 188 ? 0.2734 0.3089 0.4586 0.0174  0.0212  -0.0106 188 SER F CA  
16421 C C   . SER F 188 ? 0.2959 0.3335 0.4954 0.0203  0.0016  -0.0119 188 SER F C   
16422 O O   . SER F 188 ? 0.3043 0.3330 0.4887 0.0181  -0.0127 -0.0114 188 SER F O   
16423 C CB  . SER F 188 ? 0.3146 0.3550 0.5194 0.0085  0.0268  -0.0067 188 SER F CB  
16424 O OG  . SER F 188 ? 0.3881 0.4273 0.5777 0.0056  0.0452  -0.0022 188 SER F OG  
16425 N N   . VAL F 189 ? 0.2844 0.3347 0.5143 0.0252  0.0015  -0.0134 189 VAL F N   
16426 C CA  . VAL F 189 ? 0.2797 0.3343 0.5250 0.0291  -0.0179 -0.0112 189 VAL F CA  
16427 C C   . VAL F 189 ? 0.2598 0.3347 0.5524 0.0266  -0.0251 -0.0098 189 VAL F C   
16428 O O   . VAL F 189 ? 0.2908 0.3803 0.6181 0.0288  -0.0119 -0.0113 189 VAL F O   
16429 C CB  . VAL F 189 ? 0.2919 0.3430 0.5372 0.0388  -0.0158 -0.0116 189 VAL F CB  
16430 C CG1 . VAL F 189 ? 0.2895 0.3438 0.5487 0.0433  -0.0368 -0.0052 189 VAL F CG1 
16431 C CG2 . VAL F 189 ? 0.3036 0.3375 0.5056 0.0394  -0.0096 -0.0137 189 VAL F CG2 
16432 N N   . CYS F 190 ? 0.2352 0.3127 0.5299 0.0213  -0.0457 -0.0079 190 CYS F N   
16433 C CA  . CYS F 190 ? 0.2488 0.3487 0.5902 0.0186  -0.0572 -0.0061 190 CYS F CA  
16434 C C   . CYS F 190 ? 0.2871 0.3911 0.6266 0.0211  -0.0843 -0.0009 190 CYS F C   
16435 O O   . CYS F 190 ? 0.2864 0.3890 0.6108 0.0127  -0.1016 -0.0026 190 CYS F O   
16436 C CB  . CYS F 190 ? 0.2614 0.3656 0.6142 0.0053  -0.0564 -0.0095 190 CYS F CB  
16437 S SG  . CYS F 190 ? 0.3317 0.4691 0.7553 0.0001  -0.0566 -0.0084 190 CYS F SG  
16438 N N   . LEU F 191 ? 0.3280 0.4371 0.6838 0.0323  -0.0879 0.0056  191 LEU F N   
16439 C CA  . LEU F 191 ? 0.2778 0.3907 0.6303 0.0355  -0.1136 0.0147  191 LEU F CA  
16440 C C   . LEU F 191 ? 0.2552 0.3949 0.6509 0.0319  -0.1335 0.0188  191 LEU F C   
16441 O O   . LEU F 191 ? 0.2643 0.4220 0.7075 0.0333  -0.1245 0.0179  191 LEU F O   
16442 C CB  . LEU F 191 ? 0.2100 0.3171 0.5696 0.0490  -0.1107 0.0225  191 LEU F CB  
16443 C CG  . LEU F 191 ? 0.2049 0.2879 0.5271 0.0523  -0.0921 0.0181  191 LEU F CG  
16444 C CD1 . LEU F 191 ? 0.2288 0.3052 0.5645 0.0645  -0.0924 0.0261  191 LEU F CD1 
16445 C CD2 . LEU F 191 ? 0.2608 0.3285 0.5291 0.0447  -0.0994 0.0168  191 LEU F CD2 
16446 N N   . SER F 192 ? 0.2796 0.4225 0.6557 0.0264  -0.1597 0.0231  192 SER F N   
16447 C CA  . SER F 192 ? 0.2821 0.4456 0.6813 0.0209  -0.1773 0.0268  192 SER F CA  
16448 C C   . SER F 192 ? 0.3272 0.4956 0.7323 0.0310  -0.1875 0.0418  192 SER F C   
16449 O O   . SER F 192 ? 0.3412 0.4956 0.7131 0.0364  -0.1931 0.0500  192 SER F O   
16450 C CB  . SER F 192 ? 0.2665 0.4299 0.6344 0.0065  -0.1970 0.0197  192 SER F CB  
16451 O OG  . SER F 192 ? 0.2889 0.4729 0.6743 0.0006  -0.2146 0.0227  192 SER F OG  
16452 N N   . ARG F 193 ? 0.3583 0.5467 0.8081 0.0337  -0.1886 0.0460  193 ARG F N   
16453 C CA  . ARG F 193 ? 0.3913 0.5876 0.8565 0.0432  -0.1996 0.0608  193 ARG F CA  
16454 C C   . ARG F 193 ? 0.4017 0.6044 0.8373 0.0388  -0.2277 0.0707  193 ARG F C   
16455 O O   . ARG F 193 ? 0.3996 0.6022 0.8345 0.0474  -0.2365 0.0856  193 ARG F O   
16456 C CB  . ARG F 193 ? 0.4698 0.6895 0.9921 0.0454  -0.1960 0.0612  193 ARG F CB  
16457 C CG  . ARG F 193 ? 0.5919 0.8099 1.1446 0.0602  -0.1854 0.0694  193 ARG F CG  
16458 C CD  . ARG F 193 ? 0.7226 0.9668 1.3302 0.0613  -0.1853 0.0702  193 ARG F CD  
16459 N NE  . ARG F 193 ? 0.8380 1.0781 1.4791 0.0713  -0.1580 0.0651  193 ARG F NE  
16460 C CZ  . ARG F 193 ? 0.9409 1.2002 1.6280 0.0709  -0.1454 0.0594  193 ARG F CZ  
16461 N NH1 . ARG F 193 ? 0.9667 1.2508 1.6747 0.0608  -0.1587 0.0591  193 ARG F NH1 
16462 N NH2 . ARG F 193 ? 0.9901 1.2442 1.7012 0.0798  -0.1188 0.0532  193 ARG F NH2 
16463 N N   . TYR F 194 ? 0.4209 0.6294 0.8327 0.0246  -0.2407 0.0617  194 TYR F N   
16464 C CA  . TYR F 194 ? 0.4805 0.7004 0.8640 0.0173  -0.2668 0.0666  194 TYR F CA  
16465 C C   . TYR F 194 ? 0.4524 0.6533 0.7721 0.0129  -0.2720 0.0652  194 TYR F C   
16466 O O   . TYR F 194 ? 0.4219 0.6070 0.7177 0.0066  -0.2623 0.0519  194 TYR F O   
16467 C CB  . TYR F 194 ? 0.5758 0.8159 0.9745 0.0024  -0.2778 0.0542  194 TYR F CB  
16468 C CG  . TYR F 194 ? 0.6289 0.8860 1.0899 0.0039  -0.2670 0.0517  194 TYR F CG  
16469 C CD1 . TYR F 194 ? 0.6635 0.9431 1.1667 0.0116  -0.2750 0.0637  194 TYR F CD1 
16470 C CD2 . TYR F 194 ? 0.6436 0.8948 1.1219 -0.0022 -0.2476 0.0381  194 TYR F CD2 
16471 C CE1 . TYR F 194 ? 0.6982 0.9944 1.2586 0.0130  -0.2631 0.0610  194 TYR F CE1 
16472 C CE2 . TYR F 194 ? 0.6677 0.9353 1.2010 -0.0015 -0.2348 0.0363  194 TYR F CE2 
16473 C CZ  . TYR F 194 ? 0.7093 0.9997 1.2834 0.0061  -0.2422 0.0472  194 TYR F CZ  
16474 O OH  . TYR F 194 ? 0.7398 1.0479 1.3691 0.0070  -0.2281 0.0450  194 TYR F OH  
16475 N N   . SER F 195 ? 0.5018 0.7056 0.7936 0.0156  -0.2875 0.0786  195 SER F N   
16476 C CA  . SER F 195 ? 0.5356 0.7238 0.7647 0.0108  -0.2910 0.0775  195 SER F CA  
16477 C C   . SER F 195 ? 0.5378 0.7317 0.7358 -0.0059 -0.3014 0.0590  195 SER F C   
16478 O O   . SER F 195 ? 0.5598 0.7382 0.7075 -0.0116 -0.2985 0.0510  195 SER F O   
16479 C CB  . SER F 195 ? 0.5982 0.7895 0.8063 0.0175  -0.3039 0.0979  195 SER F CB  
16480 O OG  . SER F 195 ? 0.6466 0.8648 0.8707 0.0149  -0.3258 0.1039  195 SER F OG  
16481 N N   . THR F 196 ? 0.5038 0.7194 0.7339 -0.0141 -0.3117 0.0510  196 THR F N   
16482 C CA  . THR F 196 ? 0.5006 0.7240 0.7077 -0.0313 -0.3233 0.0322  196 THR F CA  
16483 C C   . THR F 196 ? 0.5076 0.7167 0.7212 -0.0415 -0.3094 0.0108  196 THR F C   
16484 O O   . THR F 196 ? 0.5127 0.7236 0.7086 -0.0567 -0.3165 -0.0071 196 THR F O   
16485 C CB  . THR F 196 ? 0.5062 0.7619 0.7460 -0.0368 -0.3431 0.0340  196 THR F CB  
16486 O OG1 . THR F 196 ? 0.4895 0.7545 0.7927 -0.0336 -0.3338 0.0346  196 THR F OG1 
16487 C CG2 . THR F 196 ? 0.5294 0.8002 0.7625 -0.0271 -0.3599 0.0554  196 THR F CG2 
16488 N N   . SER F 197 ? 0.4949 0.6900 0.7356 -0.0336 -0.2894 0.0121  197 SER F N   
16489 C CA  . SER F 197 ? 0.5109 0.6897 0.7567 -0.0415 -0.2747 -0.0057 197 SER F CA  
16490 C C   . SER F 197 ? 0.5441 0.7012 0.7877 -0.0300 -0.2539 -0.0021 197 SER F C   
16491 O O   . SER F 197 ? 0.5773 0.7360 0.8359 -0.0161 -0.2478 0.0133  197 SER F O   
16492 C CB  . SER F 197 ? 0.5066 0.7023 0.8080 -0.0486 -0.2723 -0.0115 197 SER F CB  
16493 O OG  . SER F 197 ? 0.5075 0.7171 0.8582 -0.0363 -0.2641 0.0026  197 SER F OG  
16494 N N   . ASN F 198 ? 0.5029 0.6389 0.7261 -0.0358 -0.2434 -0.0171 198 ASN F N   
16495 C CA  . ASN F 198 ? 0.4402 0.5548 0.6505 -0.0254 -0.2205 -0.0148 198 ASN F CA  
16496 C C   . ASN F 198 ? 0.3628 0.4782 0.6163 -0.0204 -0.1974 -0.0137 198 ASN F C   
16497 O O   . ASN F 198 ? 0.3601 0.4877 0.6524 -0.0284 -0.1968 -0.0193 198 ASN F O   
16498 C CB  . ASN F 198 ? 0.4888 0.5766 0.6487 -0.0309 -0.2090 -0.0297 198 ASN F CB  
16499 C CG  . ASN F 198 ? 0.5351 0.6182 0.6420 -0.0324 -0.2231 -0.0296 198 ASN F CG  
16500 O OD1 . ASN F 198 ? 0.5628 0.6591 0.6650 -0.0274 -0.2389 -0.0143 198 ASN F OD1 
16501 N ND2 . ASN F 198 ? 0.5529 0.6169 0.6204 -0.0388 -0.2160 -0.0457 198 ASN F ND2 
16502 N N   . GLY F 199 ? 0.3388 0.4418 0.5841 -0.0080 -0.1782 -0.0066 199 GLY F N   
16503 C CA  . GLY F 199 ? 0.2916 0.3894 0.5592 -0.0038 -0.1520 -0.0079 199 GLY F CA  
16504 C C   . GLY F 199 ? 0.2805 0.3515 0.5031 -0.0043 -0.1357 -0.0149 199 GLY F C   
16505 O O   . GLY F 199 ? 0.3113 0.3712 0.4968 -0.0090 -0.1443 -0.0208 199 GLY F O   
16506 N N   . ALA F 200 ? 0.2620 0.3241 0.4874 0.0005  -0.1123 -0.0145 200 ALA F N   
16507 C CA  . ALA F 200 ? 0.3080 0.3476 0.4952 0.0004  -0.0987 -0.0193 200 ALA F CA  
16508 C C   . ALA F 200 ? 0.2887 0.3216 0.4704 0.0088  -0.0783 -0.0151 200 ALA F C   
16509 O O   . ALA F 200 ? 0.3048 0.3487 0.5151 0.0128  -0.0692 -0.0117 200 ALA F O   
16510 C CB  . ALA F 200 ? 0.3485 0.3806 0.5407 -0.0100 -0.0936 -0.0277 200 ALA F CB  
16511 N N   . ILE F 201 ? 0.2917 0.3077 0.4372 0.0111  -0.0708 -0.0167 201 ILE F N   
16512 C CA  . ILE F 201 ? 0.3016 0.3114 0.4392 0.0158  -0.0520 -0.0146 201 ILE F CA  
16513 C C   . ILE F 201 ? 0.3334 0.3310 0.4587 0.0113  -0.0424 -0.0172 201 ILE F C   
16514 O O   . ILE F 201 ? 0.3486 0.3348 0.4546 0.0087  -0.0481 -0.0217 201 ILE F O   
16515 C CB  . ILE F 201 ? 0.3203 0.3228 0.4308 0.0226  -0.0509 -0.0120 201 ILE F CB  
16516 C CG1 . ILE F 201 ? 0.3338 0.3432 0.4518 0.0263  -0.0646 -0.0073 201 ILE F CG1 
16517 C CG2 . ILE F 201 ? 0.2963 0.2966 0.4026 0.0265  -0.0335 -0.0110 201 ILE F CG2 
16518 C CD1 . ILE F 201 ? 0.3368 0.3574 0.4888 0.0309  -0.0611 -0.0042 201 ILE F CD1 
16519 N N   . LEU F 202 ? 0.3201 0.3199 0.4568 0.0106  -0.0269 -0.0139 202 LEU F N   
16520 C CA  . LEU F 202 ? 0.3337 0.3220 0.4620 0.0071  -0.0170 -0.0119 202 LEU F CA  
16521 C C   . LEU F 202 ? 0.3393 0.3237 0.4452 0.0125  -0.0047 -0.0066 202 LEU F C   
16522 O O   . LEU F 202 ? 0.3668 0.3609 0.4756 0.0152  0.0037  -0.0050 202 LEU F O   
16523 C CB  . LEU F 202 ? 0.3268 0.3215 0.4853 -0.0007 -0.0093 -0.0093 202 LEU F CB  
16524 C CG  . LEU F 202 ? 0.3779 0.3685 0.5546 -0.0101 -0.0194 -0.0146 202 LEU F CG  
16525 C CD1 . LEU F 202 ? 0.4069 0.4090 0.5952 -0.0113 -0.0373 -0.0209 202 LEU F CD1 
16526 C CD2 . LEU F 202 ? 0.4219 0.4194 0.6295 -0.0183 -0.0079 -0.0096 202 LEU F CD2 
16527 N N   . PHE F 203 ? 0.3231 0.2941 0.4087 0.0139  -0.0037 -0.0048 203 PHE F N   
16528 C CA  . PHE F 203 ? 0.3106 0.2801 0.3749 0.0188  0.0043  0.0011  203 PHE F CA  
16529 C C   . PHE F 203 ? 0.2992 0.2614 0.3639 0.0164  0.0132  0.0103  203 PHE F C   
16530 O O   . PHE F 203 ? 0.3063 0.2550 0.3744 0.0152  0.0105  0.0104  203 PHE F O   
16531 C CB  . PHE F 203 ? 0.3080 0.2712 0.3504 0.0244  -0.0025 -0.0018 203 PHE F CB  
16532 C CG  . PHE F 203 ? 0.3554 0.3241 0.3947 0.0263  -0.0111 -0.0075 203 PHE F CG  
16533 C CD1 . PHE F 203 ? 0.3400 0.3060 0.3824 0.0241  -0.0221 -0.0132 203 PHE F CD1 
16534 C CD2 . PHE F 203 ? 0.3469 0.3226 0.3795 0.0295  -0.0085 -0.0067 203 PHE F CD2 
16535 C CE1 . PHE F 203 ? 0.3167 0.2876 0.3546 0.0258  -0.0307 -0.0146 203 PHE F CE1 
16536 C CE2 . PHE F 203 ? 0.3364 0.3144 0.3685 0.0312  -0.0160 -0.0092 203 PHE F CE2 
16537 C CZ  . PHE F 203 ? 0.3410 0.3170 0.3755 0.0297  -0.0273 -0.0114 203 PHE F CZ  
16538 N N   . GLY F 204 ? 0.2996 0.2701 0.3599 0.0157  0.0242  0.0181  204 GLY F N   
16539 C CA  . GLY F 204 ? 0.2908 0.2559 0.3508 0.0127  0.0329  0.0308  204 GLY F CA  
16540 C C   . GLY F 204 ? 0.3153 0.2897 0.3925 0.0052  0.0447  0.0353  204 GLY F C   
16541 O O   . GLY F 204 ? 0.3505 0.3370 0.4426 0.0034  0.0464  0.0273  204 GLY F O   
16542 N N   . ASP F 205 ? 0.3710 0.3399 0.4485 0.0010  0.0535  0.0496  205 ASP F N   
16543 C CA  . ASP F 205 ? 0.4442 0.4226 0.5351 -0.0072 0.0682  0.0573  205 ASP F CA  
16544 C C   . ASP F 205 ? 0.4626 0.4392 0.5904 -0.0149 0.0670  0.0519  205 ASP F C   
16545 O O   . ASP F 205 ? 0.4800 0.4397 0.6205 -0.0178 0.0602  0.0526  205 ASP F O   
16546 C CB  . ASP F 205 ? 0.5580 0.5287 0.6357 -0.0097 0.0765  0.0780  205 ASP F CB  
16547 C CG  . ASP F 205 ? 0.6479 0.6306 0.7314 -0.0187 0.0946  0.0887  205 ASP F CG  
16548 O OD1 . ASP F 205 ? 0.6743 0.6744 0.7701 -0.0219 0.1029  0.0786  205 ASP F OD1 
16549 O OD2 . ASP F 205 ? 0.7123 0.6873 0.7886 -0.0223 0.1012  0.1086  205 ASP F OD2 
16550 N N   . ILE F 206 ? 0.4618 0.4567 0.6096 -0.0183 0.0732  0.0451  206 ILE F N   
16551 C CA  . ILE F 206 ? 0.4590 0.4574 0.6462 -0.0267 0.0713  0.0410  206 ILE F CA  
16552 C C   . ILE F 206 ? 0.4734 0.4775 0.6779 -0.0371 0.0896  0.0541  206 ILE F C   
16553 O O   . ILE F 206 ? 0.5011 0.5108 0.7427 -0.0463 0.0909  0.0526  206 ILE F O   
16554 C CB  . ILE F 206 ? 0.4398 0.4577 0.6492 -0.0245 0.0670  0.0280  206 ILE F CB  
16555 C CG1 . ILE F 206 ? 0.4402 0.4761 0.6430 -0.0212 0.0841  0.0283  206 ILE F CG1 
16556 C CG2 . ILE F 206 ? 0.4147 0.4269 0.6123 -0.0166 0.0478  0.0170  206 ILE F CG2 
16557 C CD1 . ILE F 206 ? 0.4538 0.5080 0.6847 -0.0176 0.0825  0.0169  206 ILE F CD1 
16558 N N   . ASN F 207 ? 0.5081 0.5130 0.6867 -0.0367 0.1037  0.0677  207 ASN F N   
16559 C CA  . ASN F 207 ? 0.6164 0.6298 0.8111 -0.0475 0.1231  0.0809  207 ASN F CA  
16560 C C   . ASN F 207 ? 0.6220 0.6159 0.8078 -0.0533 0.1282  0.1024  207 ASN F C   
16561 O O   . ASN F 207 ? 0.6168 0.6180 0.7927 -0.0592 0.1461  0.1188  207 ASN F O   
16562 C CB  . ASN F 207 ? 0.7374 0.7741 0.9170 -0.0464 0.1416  0.0803  207 ASN F CB  
16563 C CG  . ASN F 207 ? 0.8384 0.8966 1.0581 -0.0556 0.1588  0.0787  207 ASN F CG  
16564 O OD1 . ASN F 207 ? 0.8753 0.9311 1.1335 -0.0648 0.1572  0.0819  207 ASN F OD1 
16565 N ND2 . ASN F 207 ? 0.8748 0.9546 1.0882 -0.0535 0.1758  0.0724  207 ASN F ND2 
16566 N N   . ASP F 208 ? 0.6280 0.5968 0.8144 -0.0508 0.1135  0.1033  208 ASP F N   
16567 C CA  . ASP F 208 ? 0.6742 0.6218 0.8610 -0.0560 0.1190  0.1249  208 ASP F CA  
16568 C C   . ASP F 208 ? 0.6517 0.5823 0.8810 -0.0666 0.1148  0.1212  208 ASP F C   
16569 O O   . ASP F 208 ? 0.6268 0.5309 0.8581 -0.0638 0.1039  0.1199  208 ASP F O   
16570 C CB  . ASP F 208 ? 0.7022 0.6323 0.8574 -0.0443 0.1086  0.1321  208 ASP F CB  
16571 C CG  . ASP F 208 ? 0.7630 0.6718 0.9183 -0.0472 0.1144  0.1582  208 ASP F CG  
16572 O OD1 . ASP F 208 ? 0.7350 0.6445 0.9078 -0.0594 0.1290  0.1732  208 ASP F OD1 
16573 O OD2 . ASP F 208 ? 0.8187 0.7111 0.9583 -0.0371 0.1050  0.1651  208 ASP F OD2 
16574 N N   . PRO F 209 ? 0.6449 0.5912 0.9102 -0.0793 0.1239  0.1182  209 PRO F N   
16575 C CA  . PRO F 209 ? 0.6831 0.6179 0.9928 -0.0920 0.1184  0.1112  209 PRO F CA  
16576 C C   . PRO F 209 ? 0.7862 0.6861 1.1022 -0.0970 0.1190  0.1254  209 PRO F C   
16577 O O   . PRO F 209 ? 0.8273 0.7072 1.1675 -0.1027 0.1076  0.1133  209 PRO F O   
16578 C CB  . PRO F 209 ? 0.6287 0.5895 0.9719 -0.1054 0.1360  0.1168  209 PRO F CB  
16579 C CG  . PRO F 209 ? 0.6077 0.5843 0.9191 -0.1009 0.1548  0.1325  209 PRO F CG  
16580 C CD  . PRO F 209 ? 0.5894 0.5651 0.8566 -0.0840 0.1436  0.1243  209 PRO F CD  
16581 N N   . ASN F 210 ? 0.8162 0.7087 1.1107 -0.0953 0.1322  0.1514  210 ASN F N   
16582 C CA  . ASN F 210 ? 0.8267 0.6877 1.1230 -0.0961 0.1302  0.1647  210 ASN F CA  
16583 C C   . ASN F 210 ? 0.7927 0.6252 1.0791 -0.0841 0.1143  0.1555  210 ASN F C   
16584 O O   . ASN F 210 ? 0.7598 0.5664 1.0606 -0.0859 0.1087  0.1527  210 ASN F O   
16585 C CB  . ASN F 210 ? 0.8238 0.6879 1.0927 -0.0949 0.1436  0.1939  210 ASN F CB  
16586 C CG  . ASN F 210 ? 0.8002 0.6828 1.0842 -0.1094 0.1600  0.2029  210 ASN F CG  
16587 O OD1 . ASN F 210 ? 0.7906 0.6815 1.1113 -0.1202 0.1605  0.1885  210 ASN F OD1 
16588 N ND2 . ASN F 210 ? 0.8087 0.6993 1.0637 -0.1099 0.1725  0.2264  210 ASN F ND2 
16589 N N   . ASN F 211 ? 0.7644 0.6048 1.0217 -0.0701 0.1056  0.1465  211 ASN F N   
16590 C CA  . ASN F 211 ? 0.7671 0.5821 1.0194 -0.0595 0.0915  0.1345  211 ASN F CA  
16591 C C   . ASN F 211 ? 0.6685 0.4990 0.9132 -0.0550 0.0779  0.1051  211 ASN F C   
16592 O O   . ASN F 211 ? 0.6203 0.4514 0.8394 -0.0415 0.0689  0.0969  211 ASN F O   
16593 C CB  . ASN F 211 ? 0.8095 0.6158 1.0314 -0.0435 0.0896  0.1508  211 ASN F CB  
16594 C CG  . ASN F 211 ? 0.8626 0.6717 1.0715 -0.0446 0.1021  0.1852  211 ASN F CG  
16595 O OD1 . ASN F 211 ? 0.8885 0.7145 1.0643 -0.0353 0.1014  0.1953  211 ASN F OD1 
16596 N ND2 . ASN F 211 ? 0.8693 0.6747 1.0952 -0.0567 0.1110  0.1965  211 ASN F ND2 
16597 N N   . ASN F 212 ? 0.6434 0.4905 0.9109 -0.0663 0.0767  0.0916  212 ASN F N   
16598 C CA  . ASN F 212 ? 0.6136 0.4781 0.8754 -0.0626 0.0630  0.0673  212 ASN F CA  
16599 C C   . ASN F 212 ? 0.5911 0.4644 0.8911 -0.0778 0.0584  0.0536  212 ASN F C   
16600 O O   . ASN F 212 ? 0.5753 0.4749 0.8918 -0.0841 0.0652  0.0568  212 ASN F O   
16601 C CB  . ASN F 212 ? 0.5962 0.4901 0.8330 -0.0541 0.0663  0.0698  212 ASN F CB  
16602 C CG  . ASN F 212 ? 0.5974 0.5004 0.8176 -0.0450 0.0512  0.0499  212 ASN F CG  
16603 O OD1 . ASN F 212 ? 0.5985 0.4930 0.8284 -0.0476 0.0380  0.0328  212 ASN F OD1 
16604 N ND2 . ASN F 212 ? 0.5781 0.4995 0.7736 -0.0358 0.0532  0.0515  212 ASN F ND2 
16605 N N   . ASN F 213 ? 0.5822 0.4335 0.8983 -0.0844 0.0478  0.0384  213 ASN F N   
16606 C CA  . ASN F 213 ? 0.5140 0.3728 0.8678 -0.1009 0.0398  0.0235  213 ASN F CA  
16607 C C   . ASN F 213 ? 0.4289 0.3143 0.7784 -0.0985 0.0230  0.0044  213 ASN F C   
16608 O O   . ASN F 213 ? 0.3939 0.2974 0.7762 -0.1108 0.0160  -0.0041 213 ASN F O   
16609 C CB  . ASN F 213 ? 0.5130 0.3385 0.8838 -0.1104 0.0335  0.0111  213 ASN F CB  
16610 C CG  . ASN F 213 ? 0.5310 0.3392 0.9124 -0.1149 0.0481  0.0302  213 ASN F CG  
16611 O OD1 . ASN F 213 ? 0.5312 0.3554 0.9289 -0.1219 0.0607  0.0476  213 ASN F OD1 
16612 N ND2 . ASN F 213 ? 0.4896 0.2658 0.8630 -0.1112 0.0465  0.0259  213 ASN F ND2 
16613 N N   . TYR F 214 ? 0.3962 0.2840 0.7079 -0.0830 0.0162  -0.0009 214 TYR F N   
16614 C CA  . TYR F 214 ? 0.4184 0.3278 0.7210 -0.0791 -0.0004 -0.0162 214 TYR F CA  
16615 C C   . TYR F 214 ? 0.4170 0.3616 0.7404 -0.0801 0.0033  -0.0094 214 TYR F C   
16616 O O   . TYR F 214 ? 0.4189 0.3846 0.7579 -0.0830 -0.0111 -0.0199 214 TYR F O   
16617 C CB  . TYR F 214 ? 0.4299 0.3334 0.6884 -0.0627 -0.0047 -0.0194 214 TYR F CB  
16618 C CG  . TYR F 214 ? 0.3976 0.3177 0.6438 -0.0594 -0.0226 -0.0339 214 TYR F CG  
16619 C CD1 . TYR F 214 ? 0.4292 0.3410 0.6727 -0.0661 -0.0389 -0.0528 214 TYR F CD1 
16620 C CD2 . TYR F 214 ? 0.3841 0.3273 0.6208 -0.0504 -0.0233 -0.0285 214 TYR F CD2 
16621 C CE1 . TYR F 214 ? 0.4043 0.3324 0.6337 -0.0640 -0.0562 -0.0630 214 TYR F CE1 
16622 C CE2 . TYR F 214 ? 0.3619 0.3192 0.5891 -0.0473 -0.0403 -0.0382 214 TYR F CE2 
16623 C CZ  . TYR F 214 ? 0.3837 0.3341 0.6061 -0.0543 -0.0570 -0.0540 214 TYR F CZ  
16624 O OH  . TYR F 214 ? 0.3940 0.3589 0.6035 -0.0520 -0.0744 -0.0606 214 TYR F OH  
16625 N N   . ILE F 215 ? 0.3869 0.3384 0.7117 -0.0777 0.0228  0.0081  215 ILE F N   
16626 C CA  . ILE F 215 ? 0.3607 0.3443 0.7052 -0.0774 0.0307  0.0129  215 ILE F CA  
16627 C C   . ILE F 215 ? 0.3753 0.3728 0.7679 -0.0930 0.0413  0.0190  215 ILE F C   
16628 O O   . ILE F 215 ? 0.3668 0.3923 0.7804 -0.0927 0.0516  0.0231  215 ILE F O   
16629 C CB  . ILE F 215 ? 0.3472 0.3350 0.6616 -0.0660 0.0473  0.0257  215 ILE F CB  
16630 C CG1 . ILE F 215 ? 0.3824 0.3499 0.6851 -0.0693 0.0629  0.0428  215 ILE F CG1 
16631 C CG2 . ILE F 215 ? 0.3257 0.3075 0.5997 -0.0513 0.0369  0.0191  215 ILE F CG2 
16632 C CD1 . ILE F 215 ? 0.4229 0.4050 0.7459 -0.0780 0.0845  0.0579  215 ILE F CD1 
16633 N N   . HIS F 216 ? 0.6507 0.2547 0.7802 -0.0376 -0.0404 -0.0522 216 HIS F N   
16634 C CA  . HIS F 216 ? 0.7032 0.2921 0.8499 -0.0680 -0.0289 -0.0490 216 HIS F CA  
16635 C C   . HIS F 216 ? 0.6616 0.3112 0.8418 -0.0917 -0.0400 -0.0642 216 HIS F C   
16636 O O   . HIS F 216 ? 0.6704 0.3376 0.8761 -0.1099 -0.0301 -0.0551 216 HIS F O   
16637 C CB  . HIS F 216 ? 0.7404 0.2761 0.8736 -0.0809 -0.0180 -0.0631 216 HIS F CB  
16638 C CG  . HIS F 216 ? 0.8273 0.3398 0.9678 -0.1130 -0.0042 -0.0558 216 HIS F CG  
16639 N ND1 . HIS F 216 ? 0.8297 0.3659 1.0010 -0.1474 -0.0052 -0.0800 216 HIS F ND1 
16640 C CD2 . HIS F 216 ? 0.8532 0.3212 0.9700 -0.1180 0.0089  -0.0275 216 HIS F CD2 
16641 C CE1 . HIS F 216 ? 0.8086 0.3195 0.9808 -0.1720 0.0106  -0.0679 216 HIS F CE1 
16642 N NE2 . HIS F 216 ? 0.8578 0.3236 0.9940 -0.1561 0.0188  -0.0352 216 HIS F NE2 
16643 N N   . ASN F 217 ? 0.6073 0.2921 0.7854 -0.0920 -0.0606 -0.0869 217 ASN F N   
16644 C CA  . ASN F 217 ? 0.6217 0.3671 0.8329 -0.1113 -0.0798 -0.0986 217 ASN F CA  
16645 C C   . ASN F 217 ? 0.5614 0.3601 0.7937 -0.0974 -0.0861 -0.0775 217 ASN F C   
16646 O O   . ASN F 217 ? 0.5558 0.4032 0.8337 -0.1112 -0.0986 -0.0841 217 ASN F O   
16647 C CB  . ASN F 217 ? 0.6775 0.4418 0.8673 -0.1166 -0.1058 -0.1240 217 ASN F CB  
16648 C CG  . ASN F 217 ? 0.7350 0.5602 0.9599 -0.1357 -0.1359 -0.1340 217 ASN F CG  
16649 O OD1 . ASN F 217 ? 0.8176 0.6533 1.0846 -0.1636 -0.1370 -0.1496 217 ASN F OD1 
16650 N ND2 . ASN F 217 ? 0.6957 0.5600 0.9061 -0.1214 -0.1623 -0.1249 217 ASN F ND2 
16651 N N   . SER F 218 ? 0.5140 0.3040 0.7205 -0.0705 -0.0771 -0.0547 218 SER F N   
16652 C CA  . SER F 218 ? 0.4465 0.2813 0.6698 -0.0567 -0.0807 -0.0382 218 SER F CA  
16653 C C   . SER F 218 ? 0.4319 0.2606 0.6684 -0.0604 -0.0537 -0.0211 218 SER F C   
16654 O O   . SER F 218 ? 0.4602 0.3187 0.7063 -0.0487 -0.0507 -0.0101 218 SER F O   
16655 C CB  . SER F 218 ? 0.4435 0.2793 0.6275 -0.0285 -0.0886 -0.0270 218 SER F CB  
16656 O OG  . SER F 218 ? 0.4732 0.2726 0.6313 -0.0141 -0.0690 -0.0105 218 SER F OG  
16657 N N   . LEU F 219 ? 0.4928 0.2772 0.7236 -0.0787 -0.0327 -0.0191 219 LEU F N   
16658 C CA  . LEU F 219 ? 0.4786 0.2417 0.6979 -0.0857 -0.0052 0.0012  219 LEU F CA  
16659 C C   . LEU F 219 ? 0.4650 0.2796 0.7326 -0.1033 0.0096  -0.0046 219 LEU F C   
16660 O O   . LEU F 219 ? 0.5014 0.3135 0.7531 -0.1042 0.0308  0.0101  219 LEU F O   
16661 C CB  . LEU F 219 ? 0.5672 0.2605 0.7635 -0.1050 0.0118  0.0076  219 LEU F CB  
16662 C CG  . LEU F 219 ? 0.6361 0.2684 0.7840 -0.0802 0.0049  0.0226  219 LEU F CG  
16663 C CD1 . LEU F 219 ? 0.7274 0.2923 0.8518 -0.0965 0.0161  0.0266  219 LEU F CD1 
16664 C CD2 . LEU F 219 ? 0.6532 0.2818 0.7646 -0.0575 0.0066  0.0508  219 LEU F CD2 
16665 N N   . ASP F 220 ? 0.4802 0.3417 0.8089 -0.1191 -0.0007 -0.0283 220 ASP F N   
16666 C CA  . ASP F 220 ? 0.4799 0.3985 0.8727 -0.1327 0.0136  -0.0393 220 ASP F CA  
16667 C C   . ASP F 220 ? 0.3995 0.3583 0.8023 -0.1033 0.0016  -0.0336 220 ASP F C   
16668 O O   . ASP F 220 ? 0.3835 0.3670 0.8091 -0.1056 0.0249  -0.0341 220 ASP F O   
16669 C CB  . ASP F 220 ? 0.5425 0.5084 1.0101 -0.1529 -0.0018 -0.0670 220 ASP F CB  
16670 C CG  . ASP F 220 ? 0.7136 0.6428 1.1802 -0.1876 0.0134  -0.0773 220 ASP F CG  
16671 O OD1 . ASP F 220 ? 0.7796 0.6642 1.2136 -0.2063 0.0498  -0.0648 220 ASP F OD1 
16672 O OD2 . ASP F 220 ? 0.7739 0.7167 1.2610 -0.1959 -0.0123 -0.0962 220 ASP F OD2 
16673 N N   . VAL F 221 ? 0.3807 0.3437 0.7647 -0.0784 -0.0326 -0.0304 221 VAL F N   
16674 C CA  . VAL F 221 ? 0.3618 0.3498 0.7451 -0.0512 -0.0442 -0.0217 221 VAL F CA  
16675 C C   . VAL F 221 ? 0.3779 0.3331 0.7046 -0.0403 -0.0204 -0.0024 221 VAL F C   
16676 O O   . VAL F 221 ? 0.3909 0.3689 0.7331 -0.0343 -0.0065 -0.0012 221 VAL F O   
16677 C CB  . VAL F 221 ? 0.3455 0.3357 0.7063 -0.0325 -0.0833 -0.0197 221 VAL F CB  
16678 C CG1 . VAL F 221 ? 0.2969 0.3067 0.6573 -0.0078 -0.0935 -0.0092 221 VAL F CG1 
16679 C CG2 . VAL F 221 ? 0.3051 0.3271 0.7127 -0.0455 -0.1129 -0.0371 221 VAL F CG2 
16680 N N   . LEU F 222 ? 0.3807 0.2832 0.6466 -0.0384 -0.0167 0.0107  222 LEU F N   
16681 C CA  . LEU F 222 ? 0.3907 0.2638 0.6028 -0.0262 -0.0036 0.0308  222 LEU F CA  
16682 C C   . LEU F 222 ? 0.4425 0.3114 0.6497 -0.0458 0.0294  0.0366  222 LEU F C   
16683 O O   . LEU F 222 ? 0.4612 0.3291 0.6381 -0.0380 0.0390  0.0472  222 LEU F O   
16684 C CB  . LEU F 222 ? 0.4434 0.2615 0.6057 -0.0191 -0.0094 0.0424  222 LEU F CB  
16685 C CG  . LEU F 222 ? 0.4716 0.2913 0.6257 0.0001  -0.0347 0.0344  222 LEU F CG  
16686 C CD1 . LEU F 222 ? 0.5156 0.2830 0.6323 0.0104  -0.0353 0.0420  222 LEU F CD1 
16687 C CD2 . LEU F 222 ? 0.4156 0.2697 0.5670 0.0202  -0.0458 0.0373  222 LEU F CD2 
16688 N N   . HIS F 223 ? 0.4781 0.3430 0.7107 -0.0753 0.0484  0.0278  223 HIS F N   
16689 C CA  . HIS F 223 ? 0.5641 0.4238 0.7891 -0.1030 0.0861  0.0300  223 HIS F CA  
16690 C C   . HIS F 223 ? 0.5324 0.4477 0.7986 -0.1023 0.1031  0.0144  223 HIS F C   
16691 O O   . HIS F 223 ? 0.5877 0.4946 0.8202 -0.1167 0.1328  0.0194  223 HIS F O   
16692 C CB  . HIS F 223 ? 0.6690 0.5206 0.9264 -0.1382 0.1034  0.0179  223 HIS F CB  
16693 C CG  . HIS F 223 ? 0.8176 0.6645 1.0691 -0.1760 0.1484  0.0164  223 HIS F CG  
16694 N ND1 . HIS F 223 ? 0.8538 0.7585 1.1837 -0.1998 0.1732  -0.0131 223 HIS F ND1 
16695 C CD2 . HIS F 223 ? 0.9200 0.7116 1.0958 -0.1967 0.1736  0.0400  223 HIS F CD2 
16696 C CE1 . HIS F 223 ? 0.9258 0.8149 1.2202 -0.2312 0.2130  -0.0104 223 HIS F CE1 
16697 N NE2 . HIS F 223 ? 0.9750 0.7929 1.1721 -0.2325 0.2136  0.0236  223 HIS F NE2 
16698 N N   . ASP F 224 ? 0.4541 0.4223 0.7897 -0.0855 0.0827  -0.0044 224 ASP F N   
16699 C CA  . ASP F 224 ? 0.3729 0.3953 0.7699 -0.0823 0.0969  -0.0244 224 ASP F CA  
16700 C C   . ASP F 224 ? 0.3495 0.3796 0.7315 -0.0498 0.0777  -0.0176 224 ASP F C   
16701 O O   . ASP F 224 ? 0.3655 0.4365 0.8061 -0.0399 0.0805  -0.0344 224 ASP F O   
16702 C CB  . ASP F 224 ? 0.3248 0.4018 0.8233 -0.0850 0.0839  -0.0496 224 ASP F CB  
16703 C CG  . ASP F 224 ? 0.3996 0.4799 0.9286 -0.1220 0.1081  -0.0632 224 ASP F CG  
16704 O OD1 . ASP F 224 ? 0.4687 0.5182 0.9525 -0.1498 0.1479  -0.0576 224 ASP F OD1 
16705 O OD2 . ASP F 224 ? 0.3876 0.4972 0.9791 -0.1264 0.0858  -0.0779 224 ASP F OD2 
16706 N N   . LEU F 225 ? 0.3489 0.3398 0.6596 -0.0334 0.0585  0.0049  225 LEU F N   
16707 C CA  . LEU F 225 ? 0.3238 0.3196 0.6165 -0.0067 0.0421  0.0111  225 LEU F CA  
16708 C C   . LEU F 225 ? 0.3359 0.3434 0.6247 -0.0128 0.0723  0.0032  225 LEU F C   
16709 O O   . LEU F 225 ? 0.3876 0.3783 0.6409 -0.0365 0.1031  0.0049  225 LEU F O   
16710 C CB  . LEU F 225 ? 0.3205 0.2764 0.5412 0.0068  0.0247  0.0327  225 LEU F CB  
16711 C CG  . LEU F 225 ? 0.3473 0.2928 0.5668 0.0170  -0.0053 0.0356  225 LEU F CG  
16712 C CD1 . LEU F 225 ? 0.3742 0.2916 0.5370 0.0337  -0.0173 0.0502  225 LEU F CD1 
16713 C CD2 . LEU F 225 ? 0.3130 0.2925 0.5811 0.0276  -0.0285 0.0254  225 LEU F CD2 
16714 N N   . VAL F 226 ? 0.3217 0.3546 0.6450 0.0058  0.0642  -0.0064 226 VAL F N   
16715 C CA  . VAL F 226 ? 0.3442 0.3871 0.6643 0.0021  0.0917  -0.0188 226 VAL F CA  
16716 C C   . VAL F 226 ? 0.3519 0.3781 0.6245 0.0222  0.0728  -0.0056 226 VAL F C   
16717 O O   . VAL F 226 ? 0.3130 0.3380 0.5946 0.0427  0.0407  0.0032  226 VAL F O   
16718 C CB  . VAL F 226 ? 0.3565 0.4433 0.7728 0.0047  0.1041  -0.0476 226 VAL F CB  
16719 C CG1 . VAL F 226 ? 0.3832 0.4773 0.8026 0.0098  0.1243  -0.0631 226 VAL F CG1 
16720 C CG2 . VAL F 226 ? 0.3643 0.4716 0.8209 -0.0241 0.1372  -0.0660 226 VAL F CG2 
16721 N N   . TYR F 227 ? 0.3907 0.4045 0.6095 0.0124  0.0932  -0.0052 227 TYR F N   
16722 C CA  . TYR F 227 ? 0.3737 0.3729 0.5424 0.0260  0.0769  0.0064  227 TYR F CA  
16723 C C   . TYR F 227 ? 0.3685 0.3816 0.5493 0.0266  0.0933  -0.0131 227 TYR F C   
16724 O O   . TYR F 227 ? 0.4201 0.4472 0.6214 0.0100  0.1266  -0.0354 227 TYR F O   
16725 C CB  . TYR F 227 ? 0.4270 0.3963 0.5144 0.0152  0.0768  0.0265  227 TYR F CB  
16726 C CG  . TYR F 227 ? 0.4986 0.4451 0.5724 0.0184  0.0583  0.0459  227 TYR F CG  
16727 C CD1 . TYR F 227 ? 0.5727 0.5085 0.6525 -0.0013 0.0741  0.0467  227 TYR F CD1 
16728 C CD2 . TYR F 227 ? 0.5268 0.4622 0.5856 0.0388  0.0287  0.0594  227 TYR F CD2 
16729 C CE1 . TYR F 227 ? 0.6557 0.5656 0.7256 0.0005  0.0586  0.0613  227 TYR F CE1 
16730 C CE2 . TYR F 227 ? 0.6091 0.5219 0.6603 0.0419  0.0150  0.0713  227 TYR F CE2 
16731 C CZ  . TYR F 227 ? 0.6779 0.5755 0.7340 0.0232  0.0289  0.0727  227 TYR F CZ  
16732 O OH  . TYR F 227 ? 0.7466 0.6160 0.7962 0.0247  0.0168  0.0822  227 TYR F OH  
16733 N N   . THR F 228 ? 0.3515 0.3597 0.5191 0.0429  0.0732  -0.0074 228 THR F N   
16734 C CA  . THR F 228 ? 0.3550 0.3691 0.5277 0.0429  0.0863  -0.0256 228 THR F CA  
16735 C C   . THR F 228 ? 0.3463 0.3481 0.4629 0.0481  0.0676  -0.0123 228 THR F C   
16736 O O   . THR F 228 ? 0.3842 0.3780 0.4844 0.0592  0.0424  0.0073  228 THR F O   
16737 C CB  . THR F 228 ? 0.3795 0.4052 0.6343 0.0599  0.0809  -0.0399 228 THR F CB  
16738 O OG1 . THR F 228 ? 0.3684 0.3961 0.6381 0.0570  0.1017  -0.0639 228 THR F OG1 
16739 C CG2 . THR F 228 ? 0.3442 0.3581 0.5990 0.0785  0.0426  -0.0187 228 THR F CG2 
16740 N N   . PRO F 229 ? 0.3521 0.3550 0.4404 0.0375  0.0817  -0.0264 229 PRO F N   
16741 C CA  . PRO F 229 ? 0.3460 0.3447 0.3886 0.0403  0.0625  -0.0161 229 PRO F CA  
16742 C C   . PRO F 229 ? 0.3255 0.3223 0.3956 0.0575  0.0418  -0.0106 229 PRO F C   
16743 O O   . PRO F 229 ? 0.3293 0.3233 0.4471 0.0648  0.0448  -0.0199 229 PRO F O   
16744 C CB  . PRO F 229 ? 0.3553 0.3584 0.3711 0.0218  0.0837  -0.0387 229 PRO F CB  
16745 C CG  . PRO F 229 ? 0.3988 0.4042 0.4163 0.0038  0.1158  -0.0539 229 PRO F CG  
16746 C CD  . PRO F 229 ? 0.3741 0.3844 0.4639 0.0180  0.1175  -0.0546 229 PRO F CD  
16747 N N   . LEU F 230 ? 0.3328 0.3298 0.3727 0.0630  0.0209  0.0046  230 LEU F N   
16748 C CA  . LEU F 230 ? 0.3606 0.3558 0.4130 0.0727  0.0054  0.0096  230 LEU F CA  
16749 C C   . LEU F 230 ? 0.3529 0.3562 0.3865 0.0641  0.0068  -0.0015 230 LEU F C   
16750 O O   . LEU F 230 ? 0.3457 0.3613 0.3461 0.0576  0.0025  -0.0017 230 LEU F O   
16751 C CB  . LEU F 230 ? 0.3674 0.3624 0.4081 0.0825  -0.0135 0.0272  230 LEU F CB  
16752 C CG  . LEU F 230 ? 0.3700 0.3648 0.4136 0.0877  -0.0257 0.0315  230 LEU F CG  
16753 C CD1 . LEU F 230 ? 0.3322 0.3109 0.3981 0.0863  -0.0287 0.0313  230 LEU F CD1 
16754 C CD2 . LEU F 230 ? 0.3547 0.3525 0.3891 0.0825  -0.0351 0.0375  230 LEU F CD2 
16755 N N   . THR F 231 ? 0.3619 0.3564 0.4174 0.0628  0.0103  -0.0100 231 THR F N   
16756 C CA  . THR F 231 ? 0.3241 0.3260 0.3660 0.0516  0.0115  -0.0216 231 THR F CA  
16757 C C   . THR F 231 ? 0.3171 0.3121 0.3663 0.0541  0.0012  -0.0119 231 THR F C   
16758 O O   . THR F 231 ? 0.2976 0.2728 0.3621 0.0623  -0.0045 0.0008  231 THR F O   
16759 C CB  . THR F 231 ? 0.3203 0.3116 0.3755 0.0398  0.0312  -0.0455 231 THR F CB  
16760 O OG1 . THR F 231 ? 0.3631 0.3303 0.4610 0.0498  0.0367  -0.0450 231 THR F OG1 
16761 C CG2 . THR F 231 ? 0.3207 0.3243 0.3508 0.0272  0.0460  -0.0617 231 THR F CG2 
16762 N N   . ILE F 232 ? 0.3184 0.3314 0.3546 0.0442  -0.0012 -0.0192 232 ILE F N   
16763 C CA  . ILE F 232 ? 0.2966 0.3110 0.3340 0.0407  -0.0058 -0.0136 232 ILE F CA  
16764 C C   . ILE F 232 ? 0.3141 0.3227 0.3555 0.0216  0.0049  -0.0287 232 ILE F C   
16765 O O   . ILE F 232 ? 0.3330 0.3619 0.3709 0.0108  0.0084  -0.0466 232 ILE F O   
16766 C CB  . ILE F 232 ? 0.2772 0.3269 0.3083 0.0458  -0.0170 -0.0123 232 ILE F CB  
16767 C CG1 . ILE F 232 ? 0.2392 0.2873 0.2654 0.0632  -0.0268 0.0018  232 ILE F CG1 
16768 C CG2 . ILE F 232 ? 0.3077 0.3630 0.3433 0.0394  -0.0145 -0.0122 232 ILE F CG2 
16769 C CD1 . ILE F 232 ? 0.2426 0.2656 0.2725 0.0699  -0.0275 0.0150  232 ILE F CD1 
16770 N N   . SER F 233 ? 0.3268 0.3044 0.3711 0.0145  0.0090  -0.0210 233 SER F N   
16771 C CA  . SER F 233 ? 0.3572 0.3215 0.4042 -0.0071 0.0211  -0.0343 233 SER F CA  
16772 C C   . SER F 233 ? 0.3786 0.3798 0.4216 -0.0238 0.0241  -0.0452 233 SER F C   
16773 O O   . SER F 233 ? 0.3633 0.3975 0.4054 -0.0156 0.0166  -0.0413 233 SER F O   
16774 C CB  . SER F 233 ? 0.3588 0.2676 0.4057 -0.0109 0.0226  -0.0182 233 SER F CB  
16775 O OG  . SER F 233 ? 0.3726 0.2765 0.3978 -0.0160 0.0179  -0.0006 233 SER F OG  
16776 N N   . LYS F 234 ? 0.4160 0.4123 0.4638 -0.0478 0.0365  -0.0616 234 LYS F N   
16777 C CA  . LYS F 234 ? 0.3939 0.4323 0.4492 -0.0672 0.0417  -0.0770 234 LYS F CA  
16778 C C   . LYS F 234 ? 0.3877 0.4209 0.4332 -0.0728 0.0478  -0.0630 234 LYS F C   
16779 O O   . LYS F 234 ? 0.3623 0.4408 0.4222 -0.0829 0.0531  -0.0766 234 LYS F O   
16780 C CB  . LYS F 234 ? 0.4814 0.5116 0.5447 -0.0973 0.0565  -0.0991 234 LYS F CB  
16781 C CG  . LYS F 234 ? 0.5759 0.6125 0.6429 -0.0978 0.0540  -0.1198 234 LYS F CG  
16782 C CD  . LYS F 234 ? 0.6757 0.6987 0.7507 -0.1298 0.0699  -0.1460 234 LYS F CD  
16783 C CE  . LYS F 234 ? 0.7578 0.7683 0.8288 -0.1290 0.0724  -0.1658 234 LYS F CE  
16784 N NZ  . LYS F 234 ? 0.7726 0.8382 0.8321 -0.1233 0.0562  -0.1788 234 LYS F NZ  
16785 N N   . GLN F 235 ? 0.4069 0.3883 0.4293 -0.0668 0.0461  -0.0378 235 GLN F N   
16786 C CA  . GLN F 235 ? 0.4399 0.4111 0.4385 -0.0774 0.0526  -0.0247 235 GLN F CA  
16787 C C   . GLN F 235 ? 0.4279 0.4180 0.4221 -0.0533 0.0400  -0.0154 235 GLN F C   
16788 O O   . GLN F 235 ? 0.4740 0.4575 0.4446 -0.0615 0.0456  -0.0078 235 GLN F O   
16789 C CB  . GLN F 235 ? 0.5473 0.4450 0.5128 -0.0901 0.0535  0.0003  235 GLN F CB  
16790 C CG  . GLN F 235 ? 0.7135 0.5796 0.6765 -0.1211 0.0703  -0.0066 235 GLN F CG  
16791 C CD  . GLN F 235 ? 0.8446 0.7466 0.8059 -0.1548 0.0944  -0.0259 235 GLN F CD  
16792 O OE1 . GLN F 235 ? 0.8807 0.7999 0.8225 -0.1631 0.1025  -0.0230 235 GLN F OE1 
16793 N NE2 . GLN F 235 ? 0.9089 0.8258 0.8946 -0.1761 0.1079  -0.0500 235 GLN F NE2 
16794 N N   . GLY F 236 ? 0.3838 0.3956 0.3968 -0.0275 0.0255  -0.0177 236 GLY F N   
16795 C CA  . GLY F 236 ? 0.3611 0.3882 0.3736 -0.0058 0.0143  -0.0106 236 GLY F CA  
16796 C C   . GLY F 236 ? 0.3625 0.3483 0.3575 0.0074  0.0021  0.0122  236 GLY F C   
16797 O O   . GLY F 236 ? 0.3366 0.3268 0.3239 0.0180  -0.0046 0.0183  236 GLY F O   
16798 N N   . GLU F 237 ? 0.3430 0.2902 0.3380 0.0068  -0.0014 0.0221  237 GLU F N   
16799 C CA  . GLU F 237 ? 0.3579 0.2708 0.3501 0.0205  -0.0168 0.0420  237 GLU F CA  
16800 C C   . GLU F 237 ? 0.3468 0.2749 0.3660 0.0416  -0.0230 0.0377  237 GLU F C   
16801 O O   . GLU F 237 ? 0.3033 0.2516 0.3364 0.0421  -0.0149 0.0221  237 GLU F O   
16802 C CB  . GLU F 237 ? 0.4073 0.2698 0.3982 0.0127  -0.0197 0.0544  237 GLU F CB  
16803 C CG  . GLU F 237 ? 0.4528 0.2865 0.4089 -0.0141 -0.0118 0.0627  237 GLU F CG  
16804 C CD  . GLU F 237 ? 0.5159 0.3023 0.4811 -0.0231 -0.0091 0.0670  237 GLU F CD  
16805 O OE1 . GLU F 237 ? 0.5056 0.3064 0.4981 -0.0253 0.0044  0.0450  237 GLU F OE1 
16806 O OE2 . GLU F 237 ? 0.5588 0.2902 0.5020 -0.0287 -0.0221 0.0925  237 GLU F OE2 
16807 N N   . TYR F 238 ? 0.3513 0.2687 0.3746 0.0549  -0.0369 0.0508  238 TYR F N   
16808 C CA  . TYR F 238 ? 0.3152 0.2462 0.3633 0.0703  -0.0392 0.0468  238 TYR F CA  
16809 C C   . TYR F 238 ? 0.3108 0.2238 0.3891 0.0754  -0.0380 0.0446  238 TYR F C   
16810 O O   . TYR F 238 ? 0.3174 0.2113 0.3927 0.0737  -0.0451 0.0530  238 TYR F O   
16811 C CB  . TYR F 238 ? 0.3455 0.2870 0.3812 0.0747  -0.0448 0.0531  238 TYR F CB  
16812 C CG  . TYR F 238 ? 0.3373 0.2946 0.3575 0.0744  -0.0472 0.0522  238 TYR F CG  
16813 C CD1 . TYR F 238 ? 0.3088 0.2906 0.3348 0.0787  -0.0422 0.0424  238 TYR F CD1 
16814 C CD2 . TYR F 238 ? 0.3568 0.3030 0.3496 0.0673  -0.0526 0.0576  238 TYR F CD2 
16815 C CE1 . TYR F 238 ? 0.2630 0.2615 0.2805 0.0824  -0.0424 0.0371  238 TYR F CE1 
16816 C CE2 . TYR F 238 ? 0.3426 0.3097 0.3249 0.0659  -0.0455 0.0471  238 TYR F CE2 
16817 C CZ  . TYR F 238 ? 0.2798 0.2732 0.2809 0.0772  -0.0418 0.0368  238 TYR F CZ  
16818 O OH  . TYR F 238 ? 0.2938 0.3065 0.2970 0.0800  -0.0370 0.0253  238 TYR F OH  
16819 N N   . PHE F 239 ? 0.3239 0.2500 0.4243 0.0783  -0.0250 0.0286  239 PHE F N   
16820 C CA  . PHE F 239 ? 0.3244 0.2402 0.4592 0.0815  -0.0169 0.0177  239 PHE F CA  
16821 C C   . PHE F 239 ? 0.3262 0.2646 0.4769 0.0852  -0.0065 0.0065  239 PHE F C   
16822 O O   . PHE F 239 ? 0.2735 0.2302 0.4068 0.0831  0.0005  0.0027  239 PHE F O   
16823 C CB  . PHE F 239 ? 0.3375 0.2411 0.4814 0.0726  -0.0005 -0.0004 239 PHE F CB  
16824 C CG  . PHE F 239 ? 0.3622 0.2287 0.5030 0.0665  -0.0075 0.0098  239 PHE F CG  
16825 C CD1 . PHE F 239 ? 0.3638 0.2311 0.4654 0.0516  -0.0093 0.0173  239 PHE F CD1 
16826 C CD2 . PHE F 239 ? 0.3475 0.1852 0.5152 0.0711  -0.0106 0.0108  239 PHE F CD2 
16827 C CE1 . PHE F 239 ? 0.3502 0.1782 0.4411 0.0404  -0.0124 0.0285  239 PHE F CE1 
16828 C CE2 . PHE F 239 ? 0.3804 0.1780 0.5360 0.0637  -0.0179 0.0238  239 PHE F CE2 
16829 C CZ  . PHE F 239 ? 0.4050 0.1881 0.5255 0.0476  -0.0186 0.0350  239 PHE F CZ  
16830 N N   . ILE F 240 ? 0.3772 0.3155 0.5560 0.0870  -0.0053 0.0017  240 ILE F N   
16831 C CA  . ILE F 240 ? 0.3972 0.3534 0.6057 0.0867  0.0130  -0.0156 240 ILE F CA  
16832 C C   . ILE F 240 ? 0.3899 0.3405 0.6413 0.0855  0.0277  -0.0359 240 ILE F C   
16833 O O   . ILE F 240 ? 0.4016 0.3323 0.6630 0.0883  0.0176  -0.0312 240 ILE F O   
16834 C CB  . ILE F 240 ? 0.3395 0.3101 0.5565 0.0882  0.0040  -0.0075 240 ILE F CB  
16835 C CG1 . ILE F 240 ? 0.3646 0.3279 0.5971 0.0917  -0.0156 0.0020  240 ILE F CG1 
16836 C CG2 . ILE F 240 ? 0.3125 0.2880 0.4890 0.0875  -0.0051 0.0068  240 ILE F CG2 
16837 C CD1 . ILE F 240 ? 0.3485 0.3279 0.6050 0.0920  -0.0222 0.0029  240 ILE F CD1 
16838 N N   . GLN F 241 ? 0.3721 0.3394 0.6474 0.0799  0.0538  -0.0592 241 GLN F N   
16839 C CA  . GLN F 241 ? 0.3614 0.3282 0.6774 0.0753  0.0736  -0.0846 241 GLN F CA  
16840 C C   . GLN F 241 ? 0.3463 0.3277 0.7167 0.0794  0.0708  -0.0881 241 GLN F C   
16841 O O   . GLN F 241 ? 0.3149 0.3169 0.6960 0.0739  0.0833  -0.0953 241 GLN F O   
16842 C CB  . GLN F 241 ? 0.3754 0.3520 0.6711 0.0584  0.1106  -0.1149 241 GLN F CB  
16843 C CG  . GLN F 241 ? 0.4446 0.4249 0.7762 0.0475  0.1372  -0.1465 241 GLN F CG  
16844 C CD  . GLN F 241 ? 0.4791 0.4365 0.8372 0.0527  0.1303  -0.1509 241 GLN F CD  
16845 O OE1 . GLN F 241 ? 0.4724 0.4088 0.8042 0.0564  0.1148  -0.1374 241 GLN F OE1 
16846 N NE2 . GLN F 241 ? 0.3828 0.3432 0.7974 0.0521  0.1434  -0.1713 241 GLN F NE2 
16847 N N   . VAL F 242 ? 0.3539 0.3320 0.5729 0.0382  0.0653  0.0116  242 VAL F N   
16848 C CA  . VAL F 242 ? 0.3169 0.2785 0.5843 0.0276  0.0702  0.0100  242 VAL F CA  
16849 C C   . VAL F 242 ? 0.3318 0.3055 0.6034 0.0351  0.0743  -0.0008 242 VAL F C   
16850 O O   . VAL F 242 ? 0.3431 0.3246 0.6112 0.0281  0.0555  -0.0161 242 VAL F O   
16851 C CB  . VAL F 242 ? 0.2943 0.2479 0.5923 0.0067  0.0432  0.0026  242 VAL F CB  
16852 C CG1 . VAL F 242 ? 0.3064 0.2572 0.6559 0.0006  0.0449  -0.0028 242 VAL F CG1 
16853 C CG2 . VAL F 242 ? 0.3136 0.2573 0.6068 0.0004  0.0382  0.0089  242 VAL F CG2 
16854 N N   . ASN F 243 ? 0.3328 0.3051 0.6124 0.0495  0.1023  0.0068  243 ASN F N   
16855 C CA  . ASN F 243 ? 0.3303 0.3146 0.6113 0.0602  0.1084  -0.0041 243 ASN F CA  
16856 C C   . ASN F 243 ? 0.3297 0.3046 0.6598 0.0448  0.0964  -0.0136 243 ASN F C   
16857 O O   . ASN F 243 ? 0.3657 0.3445 0.6966 0.0473  0.0899  -0.0284 243 ASN F O   
16858 C CB  . ASN F 243 ? 0.3551 0.3420 0.6239 0.0858  0.1461  0.0111  243 ASN F CB  
16859 C CG  . ASN F 243 ? 0.4945 0.5042 0.7009 0.1146  0.1556  0.0157  243 ASN F CG  
16860 O OD1 . ASN F 243 ? 0.4648 0.4932 0.6426 0.1122  0.1325  0.0043  243 ASN F OD1 
16861 N ND2 . ASN F 243 ? 0.5495 0.5624 0.7344 0.1452  0.1912  0.0327  243 ASN F ND2 
16862 N N   . ALA F 244 ? 0.2982 0.2631 0.6693 0.0309  0.0938  -0.0075 244 ALA F N   
16863 C CA  . ALA F 244 ? 0.2919 0.2582 0.7093 0.0226  0.0810  -0.0156 244 ALA F CA  
16864 C C   . ALA F 244 ? 0.3080 0.2759 0.7625 0.0075  0.0682  -0.0154 244 ALA F C   
16865 O O   . ALA F 244 ? 0.3489 0.3117 0.8060 0.0012  0.0788  -0.0096 244 ALA F O   
16866 C CB  . ALA F 244 ? 0.3077 0.2815 0.7537 0.0337  0.1050  -0.0156 244 ALA F CB  
16867 N N   . ILE F 245 ? 0.3147 0.2909 0.7972 0.0049  0.0466  -0.0232 245 ILE F N   
16868 C CA  . ILE F 245 ? 0.3583 0.3524 0.8864 -0.0041 0.0330  -0.0299 245 ILE F CA  
16869 C C   . ILE F 245 ? 0.3739 0.3924 0.9604 -0.0006 0.0449  -0.0372 245 ILE F C   
16870 O O   . ILE F 245 ? 0.3679 0.3904 0.9585 0.0127  0.0428  -0.0379 245 ILE F O   
16871 C CB  . ILE F 245 ? 0.2956 0.2930 0.8128 -0.0014 -0.0006 -0.0321 245 ILE F CB  
16872 C CG1 . ILE F 245 ? 0.2828 0.2582 0.7455 -0.0050 -0.0095 -0.0245 245 ILE F CG1 
16873 C CG2 . ILE F 245 ? 0.2680 0.2967 0.8289 -0.0057 -0.0183 -0.0442 245 ILE F CG2 
16874 C CD1 . ILE F 245 ? 0.2907 0.2598 0.7361 0.0014  -0.0323 -0.0211 245 ILE F CD1 
16875 N N   . ARG F 246 ? 0.3761 0.4102 1.0108 -0.0130 0.0606  -0.0440 246 ARG F N   
16876 C CA  . ARG F 246 ? 0.3631 0.4276 1.0629 -0.0130 0.0760  -0.0532 246 ARG F CA  
16877 C C   . ARG F 246 ? 0.3532 0.4543 1.0881 -0.0159 0.0461  -0.0730 246 ARG F C   
16878 O O   . ARG F 246 ? 0.3173 0.4215 1.0491 -0.0270 0.0317  -0.0846 246 ARG F O   
16879 C CB  . ARG F 246 ? 0.3863 0.4374 1.1063 -0.0244 0.1166  -0.0499 246 ARG F CB  
16880 C CG  . ARG F 246 ? 0.4276 0.4968 1.1934 -0.0260 0.1347  -0.0588 246 ARG F CG  
16881 C CD  . ARG F 246 ? 0.5056 0.5554 1.2897 -0.0403 0.1673  -0.0619 246 ARG F CD  
16882 N NE  . ARG F 246 ? 0.5476 0.5584 1.3047 -0.0327 0.2124  -0.0365 246 ARG F NE  
16883 C CZ  . ARG F 246 ? 0.5839 0.5618 1.3315 -0.0374 0.2410  -0.0301 246 ARG F CZ  
16884 N NH1 . ARG F 246 ? 0.5791 0.5603 1.3443 -0.0529 0.2286  -0.0511 246 ARG F NH1 
16885 N NH2 . ARG F 246 ? 0.6257 0.5686 1.3410 -0.0227 0.2836  -0.0023 246 ARG F NH2 
16886 N N   . VAL F 247 ? 0.3395 0.4675 1.0951 -0.0010 0.0367  -0.0771 247 VAL F N   
16887 C CA  . VAL F 247 ? 0.3628 0.5363 1.1495 0.0013  0.0132  -0.0969 247 VAL F CA  
16888 C C   . VAL F 247 ? 0.3782 0.5783 1.2080 0.0024  0.0328  -0.1041 247 VAL F C   
16889 O O   . VAL F 247 ? 0.3672 0.5700 1.1945 0.0212  0.0377  -0.0939 247 VAL F O   
16890 C CB  . VAL F 247 ? 0.3552 0.5448 1.1202 0.0260  -0.0208 -0.0928 247 VAL F CB  
16891 C CG1 . VAL F 247 ? 0.3530 0.6007 1.1447 0.0342  -0.0447 -0.1131 247 VAL F CG1 
16892 C CG2 . VAL F 247 ? 0.3489 0.5104 1.0714 0.0253  -0.0375 -0.0833 247 VAL F CG2 
16893 N N   . ASN F 248 ? 0.4167 0.6337 1.2847 -0.0170 0.0456  -0.1223 248 ASN F N   
16894 C CA  . ASN F 248 ? 0.4422 0.6792 1.3552 -0.0211 0.0719  -0.1281 248 ASN F CA  
16895 C C   . ASN F 248 ? 0.4316 0.6307 1.3272 -0.0137 0.1075  -0.1029 248 ASN F C   
16896 O O   . ASN F 248 ? 0.4360 0.5911 1.3068 -0.0214 0.1321  -0.0890 248 ASN F O   
16897 C CB  . ASN F 248 ? 0.4631 0.7633 1.4066 -0.0051 0.0481  -0.1423 248 ASN F CB  
16898 C CG  . ASN F 248 ? 0.4544 0.8061 1.4265 -0.0142 0.0217  -0.1734 248 ASN F CG  
16899 O OD1 . ASN F 248 ? 0.4714 0.8096 1.4534 -0.0375 0.0292  -0.1887 248 ASN F OD1 
16900 N ND2 . ASN F 248 ? 0.4320 0.8433 1.4142 0.0079  -0.0077 -0.1828 248 ASN F ND2 
16901 N N   . LYS F 249 ? 0.4145 0.6298 1.3132 0.0059  0.1101  -0.0955 249 LYS F N   
16902 C CA  . LYS F 249 ? 0.4435 0.6250 1.3170 0.0158  0.1435  -0.0742 249 LYS F CA  
16903 C C   . LYS F 249 ? 0.4671 0.6255 1.2883 0.0375  0.1292  -0.0620 249 LYS F C   
16904 O O   . LYS F 249 ? 0.4858 0.6257 1.2794 0.0531  0.1481  -0.0508 249 LYS F O   
16905 C CB  . LYS F 249 ? 0.4265 0.6352 1.3337 0.0238  0.1636  -0.0751 249 LYS F CB  
16906 C CG  . LYS F 249 ? 0.4526 0.6900 1.4193 0.0030  0.1775  -0.0916 249 LYS F CG  
16907 C CD  . LYS F 249 ? 0.4908 0.7554 1.4896 0.0123  0.2005  -0.0894 249 LYS F CD  
16908 C CE  . LYS F 249 ? 0.5249 0.8314 1.5928 -0.0087 0.2085  -0.1123 249 LYS F CE  
16909 N NZ  . LYS F 249 ? 0.5643 0.8996 1.6667 0.0000  0.2341  -0.1088 249 LYS F NZ  
16910 N N   . HIS F 250 ? 0.3052 0.4626 1.1096 0.0388  0.0962  -0.0662 250 HIS F N   
16911 C CA  . HIS F 250 ? 0.3725 0.4998 1.1279 0.0559  0.0825  -0.0569 250 HIS F CA  
16912 C C   . HIS F 250 ? 0.3617 0.4559 1.0813 0.0462  0.0827  -0.0506 250 HIS F C   
16913 O O   . HIS F 250 ? 0.3775 0.4780 1.1084 0.0295  0.0730  -0.0549 250 HIS F O   
16914 C CB  . HIS F 250 ? 0.3993 0.5433 1.1530 0.0713  0.0483  -0.0607 250 HIS F CB  
16915 C CG  . HIS F 250 ? 0.4486 0.6187 1.2193 0.0934  0.0478  -0.0621 250 HIS F CG  
16916 N ND1 . HIS F 250 ? 0.4798 0.6199 1.2189 0.1150  0.0569  -0.0533 250 HIS F ND1 
16917 C CD2 . HIS F 250 ? 0.4692 0.6939 1.2827 0.0989  0.0393  -0.0730 250 HIS F CD2 
16918 C CE1 . HIS F 250 ? 0.5251 0.6976 1.2865 0.1351  0.0558  -0.0553 250 HIS F CE1 
16919 N NE2 . HIS F 250 ? 0.5290 0.7576 1.3368 0.1267  0.0442  -0.0669 250 HIS F NE2 
16920 N N   . LEU F 251 ? 0.3650 0.4256 1.0384 0.0571  0.0937  -0.0435 251 LEU F N   
16921 C CA  . LEU F 251 ? 0.3403 0.3687 0.9556 0.0484  0.0909  -0.0380 251 LEU F CA  
16922 C C   . LEU F 251 ? 0.3482 0.3497 0.9185 0.0538  0.0690  -0.0397 251 LEU F C   
16923 O O   . LEU F 251 ? 0.3490 0.3379 0.9101 0.0678  0.0733  -0.0437 251 LEU F O   
16924 C CB  . LEU F 251 ? 0.3656 0.3821 0.9520 0.0548  0.1225  -0.0318 251 LEU F CB  
16925 C CG  . LEU F 251 ? 0.4037 0.4332 1.0262 0.0487  0.1539  -0.0240 251 LEU F CG  
16926 C CD1 . LEU F 251 ? 0.4485 0.4640 1.0271 0.0641  0.1862  -0.0123 251 LEU F CD1 
16927 C CD2 . LEU F 251 ? 0.4197 0.4487 1.0577 0.0276  0.1452  -0.0240 251 LEU F CD2 
16928 N N   . VAL F 252 ? 0.3522 0.3431 0.8989 0.0426  0.0486  -0.0373 252 VAL F N   
16929 C CA  . VAL F 252 ? 0.3680 0.3295 0.8729 0.0432  0.0357  -0.0377 252 VAL F CA  
16930 C C   . VAL F 252 ? 0.3661 0.3171 0.8279 0.0346  0.0447  -0.0401 252 VAL F C   
16931 O O   . VAL F 252 ? 0.3899 0.3467 0.8406 0.0249  0.0420  -0.0345 252 VAL F O   
16932 C CB  . VAL F 252 ? 0.3445 0.3049 0.8473 0.0401  0.0105  -0.0318 252 VAL F CB  
16933 C CG1 . VAL F 252 ? 0.3455 0.2709 0.8104 0.0395  0.0054  -0.0300 252 VAL F CG1 
16934 C CG2 . VAL F 252 ? 0.3499 0.3347 0.8931 0.0556  -0.0004 -0.0310 252 VAL F CG2 
16935 N N   . ILE F 253 ? 0.3776 0.3175 0.8154 0.0407  0.0556  -0.0508 253 ILE F N   
16936 C CA  . ILE F 253 ? 0.3569 0.3029 0.7547 0.0393  0.0637  -0.0574 253 ILE F CA  
16937 C C   . ILE F 253 ? 0.3545 0.2887 0.7218 0.0293  0.0524  -0.0725 253 ILE F C   
16938 O O   . ILE F 253 ? 0.3853 0.3080 0.7481 0.0313  0.0570  -0.0913 253 ILE F O   
16939 C CB  . ILE F 253 ? 0.3721 0.3300 0.7642 0.0568  0.0869  -0.0643 253 ILE F CB  
16940 C CG1 . ILE F 253 ? 0.3654 0.3354 0.7959 0.0639  0.1040  -0.0492 253 ILE F CG1 
16941 C CG2 . ILE F 253 ? 0.3744 0.3500 0.7214 0.0640  0.0947  -0.0696 253 ILE F CG2 
16942 C CD1 . ILE F 253 ? 0.4030 0.3807 0.8423 0.0832  0.1272  -0.0535 253 ILE F CD1 
16943 N N   . PRO F 254 ? 0.3579 0.2965 0.7065 0.0177  0.0405  -0.0672 254 PRO F N   
16944 C CA  . PRO F 254 ? 0.3599 0.2947 0.6867 0.0042  0.0311  -0.0809 254 PRO F CA  
16945 C C   . PRO F 254 ? 0.3751 0.3350 0.6762 0.0084  0.0385  -0.1070 254 PRO F C   
16946 O O   . PRO F 254 ? 0.3921 0.3768 0.6775 0.0259  0.0493  -0.1050 254 PRO F O   
16947 C CB  . PRO F 254 ? 0.3600 0.3039 0.6744 -0.0028 0.0199  -0.0648 254 PRO F CB  
16948 C CG  . PRO F 254 ? 0.3402 0.2825 0.6784 0.0031  0.0207  -0.0453 254 PRO F CG  
16949 C CD  . PRO F 254 ? 0.3302 0.2792 0.6820 0.0163  0.0386  -0.0485 254 PRO F CD  
16950 N N   . THR F 255 ? 0.4091 0.3643 0.7086 -0.0053 0.0355  -0.1330 255 THR F N   
16951 C CA  . THR F 255 ? 0.4307 0.4243 0.7084 -0.0019 0.0379  -0.1662 255 THR F CA  
16952 C C   . THR F 255 ? 0.4436 0.4670 0.7085 -0.0177 0.0267  -0.1818 255 THR F C   
16953 O O   . THR F 255 ? 0.4399 0.4435 0.7153 -0.0356 0.0198  -0.1689 255 THR F O   
16954 C CB  . THR F 255 ? 0.4731 0.4502 0.7651 -0.0055 0.0468  -0.1995 255 THR F CB  
16955 O OG1 . THR F 255 ? 0.5319 0.4648 0.8489 -0.0295 0.0471  -0.2045 255 THR F OG1 
16956 C CG2 . THR F 255 ? 0.4219 0.3796 0.7242 0.0142  0.0590  -0.1871 255 THR F CG2 
16957 N N   . GLY F 271 ? 0.8398 1.2941 0.7108 0.2818  0.0524  -0.1073 271 GLY F N   
16958 C CA  . GLY F 271 ? 0.8879 1.3554 0.7381 0.2929  0.0454  -0.0841 271 GLY F CA  
16959 C C   . GLY F 271 ? 0.8860 1.3957 0.7673 0.2606  0.0212  -0.1204 271 GLY F C   
16960 O O   . GLY F 271 ? 0.8983 1.4805 0.7767 0.2679  -0.0031 -0.1418 271 GLY F O   
16961 N N   . GLU F 272 ? 0.8481 1.3028 0.7722 0.2189  0.0235  -0.1201 272 GLU F N   
16962 C CA  . GLU F 272 ? 0.8069 1.2723 0.7694 0.1754  -0.0002 -0.1434 272 GLU F CA  
16963 C C   . GLU F 272 ? 0.6968 1.0845 0.6730 0.1554  0.0070  -0.1021 272 GLU F C   
16964 O O   . GLU F 272 ? 0.7244 1.0643 0.6812 0.1761  0.0288  -0.0639 272 GLU F O   
16965 C CB  . GLU F 272 ? 0.8706 1.3343 0.8824 0.1333  -0.0135 -0.1890 272 GLU F CB  
16966 C CG  . GLU F 272 ? 0.9349 1.4455 0.9821 0.0978  -0.0341 -0.2313 272 GLU F CG  
16967 C CD  . GLU F 272 ? 0.9828 1.4358 1.0670 0.0553  -0.0370 -0.2142 272 GLU F CD  
16968 O OE1 . GLU F 272 ? 1.0228 1.3986 1.1094 0.0496  -0.0276 -0.1743 272 GLU F OE1 
16969 O OE2 . GLU F 272 ? 0.9859 1.4768 1.0990 0.0279  -0.0480 -0.2437 272 GLU F OE2 
16970 N N   . ILE F 273 ? 0.5979 0.9729 0.6080 0.1163  -0.0085 -0.1108 273 ILE F N   
16971 C CA  . ILE F 273 ? 0.5461 0.8559 0.5665 0.0997  -0.0051 -0.0768 273 ILE F CA  
16972 C C   . ILE F 273 ? 0.5241 0.7585 0.5733 0.0810  0.0036  -0.0621 273 ILE F C   
16973 O O   . ILE F 273 ? 0.5212 0.7470 0.5980 0.0632  0.0003  -0.0833 273 ILE F O   
16974 C CB  . ILE F 273 ? 0.5626 0.8816 0.6106 0.0650  -0.0226 -0.0903 273 ILE F CB  
16975 C CG1 . ILE F 273 ? 0.5311 0.9359 0.5627 0.0786  -0.0325 -0.1115 273 ILE F CG1 
16976 C CG2 . ILE F 273 ? 0.5574 0.8211 0.6050 0.0572  -0.0205 -0.0566 273 ILE F CG2 
16977 C CD1 . ILE F 273 ? 0.5192 0.9295 0.5788 0.0463  -0.0431 -0.1186 273 ILE F CD1 
16978 N N   . GLY F 274 ? 0.4681 0.6508 0.5144 0.0849  0.0150  -0.0293 274 GLY F N   
16979 C CA  . GLY F 274 ? 0.4120 0.5367 0.4912 0.0679  0.0212  -0.0194 274 GLY F CA  
16980 C C   . GLY F 274 ? 0.4173 0.5249 0.5345 0.0327  0.0028  -0.0351 274 GLY F C   
16981 O O   . GLY F 274 ? 0.4398 0.5698 0.5588 0.0187  -0.0106 -0.0480 274 GLY F O   
16982 N N   . GLY F 275 ? 0.3989 0.4691 0.5471 0.0209  0.0052  -0.0335 275 GLY F N   
16983 C CA  . GLY F 275 ? 0.3609 0.4105 0.5400 -0.0044 -0.0074 -0.0440 275 GLY F CA  
16984 C C   . GLY F 275 ? 0.3592 0.3760 0.5513 -0.0144 -0.0158 -0.0257 275 GLY F C   
16985 O O   . GLY F 275 ? 0.4000 0.3998 0.6090 -0.0293 -0.0249 -0.0278 275 GLY F O   
16986 N N   . ALA F 276 ? 0.3401 0.3475 0.5233 -0.0041 -0.0105 -0.0088 276 ALA F N   
16987 C CA  . ALA F 276 ? 0.3124 0.2956 0.5084 -0.0119 -0.0205 0.0020  276 ALA F CA  
16988 C C   . ALA F 276 ? 0.3195 0.3091 0.4883 -0.0086 -0.0254 0.0108  276 ALA F C   
16989 O O   . ALA F 276 ? 0.3507 0.3429 0.4986 0.0052  -0.0133 0.0188  276 ALA F O   
16990 C CB  . ALA F 276 ? 0.2665 0.2311 0.4865 -0.0086 -0.0107 0.0072  276 ALA F CB  
16991 N N   . LEU F 277 ? 0.2995 0.2876 0.4677 -0.0184 -0.0402 0.0117  277 LEU F N   
16992 C CA  . LEU F 277 ? 0.2684 0.2622 0.4123 -0.0149 -0.0459 0.0200  277 LEU F CA  
16993 C C   . LEU F 277 ? 0.3245 0.2962 0.4720 -0.0110 -0.0489 0.0261  277 LEU F C   
16994 O O   . LEU F 277 ? 0.3118 0.2694 0.4867 -0.0159 -0.0558 0.0222  277 LEU F O   
16995 C CB  . LEU F 277 ? 0.2918 0.2892 0.4360 -0.0257 -0.0563 0.0205  277 LEU F CB  
16996 C CG  . LEU F 277 ? 0.2764 0.2793 0.3965 -0.0214 -0.0626 0.0307  277 LEU F CG  
16997 C CD1 . LEU F 277 ? 0.2729 0.3104 0.3687 -0.0144 -0.0558 0.0289  277 LEU F CD1 
16998 C CD2 . LEU F 277 ? 0.2819 0.2761 0.4082 -0.0299 -0.0684 0.0363  277 LEU F CD2 
16999 N N   . ILE F 278 ? 0.3571 0.3290 0.4787 -0.0010 -0.0434 0.0325  278 ILE F N   
17000 C CA  . ILE F 278 ? 0.3248 0.2762 0.4495 0.0001  -0.0473 0.0321  278 ILE F CA  
17001 C C   . ILE F 278 ? 0.3374 0.2968 0.4366 0.0032  -0.0609 0.0367  278 ILE F C   
17002 O O   . ILE F 278 ? 0.3620 0.3385 0.4327 0.0108  -0.0562 0.0441  278 ILE F O   
17003 C CB  . ILE F 278 ? 0.2986 0.2315 0.4151 0.0102  -0.0247 0.0356  278 ILE F CB  
17004 C CG1 . ILE F 278 ? 0.2815 0.2077 0.4188 0.0111  -0.0047 0.0357  278 ILE F CG1 
17005 C CG2 . ILE F 278 ? 0.3075 0.2175 0.4384 0.0054  -0.0279 0.0260  278 ILE F CG2 
17006 C CD1 . ILE F 278 ? 0.3083 0.2122 0.4316 0.0264  0.0271  0.0462  278 ILE F CD1 
17007 N N   . THR F 279 ? 0.3256 0.2790 0.4344 0.0005  -0.0775 0.0319  279 THR F N   
17008 C CA  . THR F 279 ? 0.3364 0.2981 0.4182 0.0069  -0.0895 0.0385  279 THR F CA  
17009 C C   . THR F 279 ? 0.3588 0.3133 0.4425 0.0124  -0.1036 0.0275  279 THR F C   
17010 O O   . THR F 279 ? 0.4089 0.3582 0.5243 0.0074  -0.1076 0.0121  279 THR F O   
17011 C CB  . THR F 279 ? 0.3290 0.3003 0.4127 0.0027  -0.0960 0.0472  279 THR F CB  
17012 O OG1 . THR F 279 ? 0.3552 0.3334 0.4116 0.0111  -0.1024 0.0574  279 THR F OG1 
17013 C CG2 . THR F 279 ? 0.3562 0.3197 0.4676 0.0015  -0.1057 0.0424  279 THR F CG2 
17014 N N   . THR F 280 ? 0.3560 0.3152 0.4080 0.0232  -0.1104 0.0316  280 THR F N   
17015 C CA  . THR F 280 ? 0.3540 0.3141 0.4043 0.0312  -0.1270 0.0160  280 THR F CA  
17016 C C   . THR F 280 ? 0.3703 0.3472 0.3985 0.0449  -0.1429 0.0272  280 THR F C   
17017 O O   . THR F 280 ? 0.4283 0.4152 0.4444 0.0586  -0.1593 0.0155  280 THR F O   
17018 C CB  . THR F 280 ? 0.3529 0.3000 0.3799 0.0383  -0.1202 0.0072  280 THR F CB  
17019 O OG1 . THR F 280 ? 0.3755 0.3292 0.3615 0.0492  -0.1133 0.0272  280 THR F OG1 
17020 C CG2 . THR F 280 ? 0.3790 0.3003 0.4263 0.0293  -0.0984 -0.0015 280 THR F CG2 
17021 N N   . THR F 281 ? 0.3670 0.3471 0.3890 0.0430  -0.1358 0.0486  281 THR F N   
17022 C CA  . THR F 281 ? 0.4148 0.4030 0.4102 0.0585  -0.1410 0.0662  281 THR F CA  
17023 C C   . THR F 281 ? 0.4431 0.4310 0.4521 0.0669  -0.1481 0.0731  281 THR F C   
17024 O O   . THR F 281 ? 0.4439 0.4317 0.4307 0.0829  -0.1455 0.0938  281 THR F O   
17025 C CB  . THR F 281 ? 0.4076 0.3988 0.3871 0.0523  -0.1229 0.0861  281 THR F CB  
17026 O OG1 . THR F 281 ? 0.3897 0.3779 0.3972 0.0321  -0.1100 0.0852  281 THR F OG1 
17027 C CG2 . THR F 281 ? 0.4042 0.4033 0.3592 0.0564  -0.1189 0.0827  281 THR F CG2 
17028 N N   . HIS F 282 ? 0.4470 0.4341 0.4914 0.0597  -0.1542 0.0576  282 HIS F N   
17029 C CA  . HIS F 282 ? 0.4534 0.4498 0.5079 0.0771  -0.1672 0.0582  282 HIS F CA  
17030 C C   . HIS F 282 ? 0.4243 0.4376 0.5157 0.0722  -0.1823 0.0269  282 HIS F C   
17031 O O   . HIS F 282 ? 0.4142 0.4174 0.5315 0.0502  -0.1723 0.0138  282 HIS F O   
17032 C CB  . HIS F 282 ? 0.4694 0.4461 0.5369 0.0731  -0.1511 0.0781  282 HIS F CB  
17033 C CG  . HIS F 282 ? 0.4556 0.4197 0.5565 0.0466  -0.1379 0.0690  282 HIS F CG  
17034 N ND1 . HIS F 282 ? 0.4663 0.4375 0.6023 0.0398  -0.1442 0.0492  282 HIS F ND1 
17035 C CD2 . HIS F 282 ? 0.4345 0.3843 0.5398 0.0276  -0.1182 0.0755  282 HIS F CD2 
17036 C CE1 . HIS F 282 ? 0.4262 0.3846 0.5802 0.0209  -0.1281 0.0475  282 HIS F CE1 
17037 N NE2 . HIS F 282 ? 0.4188 0.3669 0.5543 0.0136  -0.1142 0.0609  282 HIS F NE2 
17038 N N   . PRO F 283 ? 0.4238 0.4672 0.5183 0.0948  -0.2048 0.0138  283 PRO F N   
17039 C CA  . PRO F 283 ? 0.3957 0.4651 0.5345 0.0872  -0.2195 -0.0232 283 PRO F CA  
17040 C C   . PRO F 283 ? 0.4007 0.4673 0.5864 0.0736  -0.2115 -0.0263 283 PRO F C   
17041 O O   . PRO F 283 ? 0.4142 0.4784 0.6396 0.0507  -0.2040 -0.0479 283 PRO F O   
17042 C CB  . PRO F 283 ? 0.4310 0.5437 0.5529 0.1175  -0.2416 -0.0358 283 PRO F CB  
17043 C CG  . PRO F 283 ? 0.4506 0.5533 0.5254 0.1416  -0.2306 0.0035  283 PRO F CG  
17044 C CD  . PRO F 283 ? 0.4463 0.5077 0.4998 0.1282  -0.2134 0.0287  283 PRO F CD  
17045 N N   . TYR F 284 ? 0.3980 0.4616 0.5801 0.0889  -0.2090 -0.0043 284 TYR F N   
17046 C CA  . TYR F 284 ? 0.3676 0.4349 0.5951 0.0808  -0.2041 -0.0112 284 TYR F CA  
17047 C C   . TYR F 284 ? 0.3666 0.3936 0.5990 0.0574  -0.1774 0.0038  284 TYR F C   
17048 O O   . TYR F 284 ? 0.4191 0.4197 0.6197 0.0517  -0.1641 0.0228  284 TYR F O   
17049 C CB  . TYR F 284 ? 0.3764 0.4635 0.6010 0.1140  -0.2148 0.0011  284 TYR F CB  
17050 C CG  . TYR F 284 ? 0.4106 0.5456 0.6164 0.1397  -0.2353 -0.0141 284 TYR F CG  
17051 C CD1 . TYR F 284 ? 0.4179 0.5937 0.6576 0.1283  -0.2489 -0.0551 284 TYR F CD1 
17052 C CD2 . TYR F 284 ? 0.4824 0.6192 0.6350 0.1711  -0.2329 0.0125  284 TYR F CD2 
17053 C CE1 . TYR F 284 ? 0.4689 0.6888 0.6901 0.1479  -0.2644 -0.0729 284 TYR F CE1 
17054 C CE2 . TYR F 284 ? 0.5149 0.6957 0.6471 0.1920  -0.2471 -0.0007 284 TYR F CE2 
17055 C CZ  . TYR F 284 ? 0.5312 0.7548 0.6969 0.1809  -0.2650 -0.0455 284 TYR F CZ  
17056 O OH  . TYR F 284 ? 0.6404 0.9086 0.7870 0.2023  -0.2808 -0.0647 284 TYR F OH  
17057 N N   . THR F 285 ? 0.3468 0.3756 0.6214 0.0445  -0.1696 -0.0078 285 THR F N   
17058 C CA  . THR F 285 ? 0.3513 0.3497 0.6305 0.0269  -0.1458 0.0021  285 THR F CA  
17059 C C   . THR F 285 ? 0.3866 0.3654 0.6535 0.0381  -0.1381 0.0229  285 THR F C   
17060 O O   . THR F 285 ? 0.4125 0.4028 0.6897 0.0591  -0.1465 0.0264  285 THR F O   
17061 C CB  . THR F 285 ? 0.3363 0.3430 0.6627 0.0132  -0.1367 -0.0156 285 THR F CB  
17062 O OG1 . THR F 285 ? 0.3427 0.3542 0.6801 -0.0004 -0.1343 -0.0327 285 THR F OG1 
17063 C CG2 . THR F 285 ? 0.2502 0.2313 0.5759 0.0018  -0.1133 -0.0062 285 THR F CG2 
17064 N N   . VAL F 286 ? 0.3762 0.3272 0.6221 0.0255  -0.1208 0.0351  286 VAL F N   
17065 C CA  . VAL F 286 ? 0.3651 0.2889 0.6016 0.0301  -0.1071 0.0516  286 VAL F CA  
17066 C C   . VAL F 286 ? 0.3600 0.2685 0.6173 0.0141  -0.0897 0.0432  286 VAL F C   
17067 O O   . VAL F 286 ? 0.3249 0.2374 0.5819 -0.0034 -0.0821 0.0330  286 VAL F O   
17068 C CB  . VAL F 286 ? 0.3938 0.3021 0.5970 0.0262  -0.0988 0.0668  286 VAL F CB  
17069 C CG1 . VAL F 286 ? 0.4019 0.2754 0.6050 0.0239  -0.0769 0.0798  286 VAL F CG1 
17070 C CG2 . VAL F 286 ? 0.4171 0.3398 0.5940 0.0486  -0.1147 0.0775  286 VAL F CG2 
17071 N N   . LEU F 287 ? 0.3882 0.2806 0.6597 0.0253  -0.0828 0.0480  287 LEU F N   
17072 C CA  . LEU F 287 ? 0.3599 0.2365 0.6504 0.0148  -0.0663 0.0382  287 LEU F CA  
17073 C C   . LEU F 287 ? 0.4316 0.2679 0.7136 0.0122  -0.0462 0.0470  287 LEU F C   
17074 O O   . LEU F 287 ? 0.4630 0.2776 0.7327 0.0305  -0.0421 0.0674  287 LEU F O   
17075 C CB  . LEU F 287 ? 0.3343 0.2241 0.6552 0.0297  -0.0709 0.0327  287 LEU F CB  
17076 C CG  . LEU F 287 ? 0.2974 0.2275 0.6420 0.0314  -0.0868 0.0204  287 LEU F CG  
17077 C CD1 . LEU F 287 ? 0.3389 0.2861 0.7179 0.0486  -0.0897 0.0159  287 LEU F CD1 
17078 C CD2 . LEU F 287 ? 0.2704 0.2072 0.6204 0.0101  -0.0776 0.0077  287 LEU F CD2 
17079 N N   . SER F 288 ? 0.4340 0.2605 0.7228 -0.0090 -0.0310 0.0306  288 SER F N   
17080 C CA  . SER F 288 ? 0.4852 0.2713 0.7769 -0.0173 -0.0080 0.0303  288 SER F CA  
17081 C C   . SER F 288 ? 0.5433 0.3022 0.8464 0.0044  0.0008  0.0384  288 SER F C   
17082 O O   . SER F 288 ? 0.5203 0.2981 0.8390 0.0178  -0.0101 0.0344  288 SER F O   
17083 C CB  . SER F 288 ? 0.4717 0.2655 0.7721 -0.0438 0.0032  0.0013  288 SER F CB  
17084 O OG  . SER F 288 ? 0.4478 0.2552 0.7618 -0.0405 0.0014  -0.0157 288 SER F OG  
17085 N N   . HIS F 289 ? 0.5811 0.3009 0.8720 0.0078  0.0235  0.0488  289 HIS F N   
17086 C CA  . HIS F 289 ? 0.5226 0.2151 0.8103 0.0348  0.0345  0.0630  289 HIS F CA  
17087 C C   . HIS F 289 ? 0.5549 0.2542 0.8626 0.0385  0.0349  0.0454  289 HIS F C   
17088 O O   . HIS F 289 ? 0.5231 0.2300 0.8373 0.0670  0.0274  0.0563  289 HIS F O   
17089 C CB  . HIS F 289 ? 0.5860 0.2298 0.8584 0.0303  0.0655  0.0706  289 HIS F CB  
17090 C CG  . HIS F 289 ? 0.7369 0.3482 1.0018 0.0595  0.0799  0.0853  289 HIS F CG  
17091 N ND1 . HIS F 289 ? 0.7606 0.3736 1.0067 0.1008  0.0715  0.1151  289 HIS F ND1 
17092 C CD2 . HIS F 289 ? 0.7715 0.3540 1.0445 0.0570  0.0998  0.0728  289 HIS F CD2 
17093 C CE1 . HIS F 289 ? 0.8097 0.3950 1.0514 0.1230  0.0869  0.1222  289 HIS F CE1 
17094 N NE2 . HIS F 289 ? 0.8187 0.3813 1.0774 0.0960  0.1052  0.0976  289 HIS F NE2 
17095 N N   . SER F 290 ? 0.5572 0.2594 0.8745 0.0127  0.0435  0.0172  290 SER F N   
17096 C CA  . SER F 290 ? 0.5979 0.3044 0.9316 0.0175  0.0473  0.0001  290 SER F CA  
17097 C C   . SER F 290 ? 0.5096 0.2580 0.8627 0.0294  0.0260  0.0000  290 SER F C   
17098 O O   . SER F 290 ? 0.5124 0.2659 0.8811 0.0478  0.0269  0.0003  290 SER F O   
17099 C CB  . SER F 290 ? 0.6981 0.4063 1.0357 -0.0097 0.0587  -0.0329 290 SER F CB  
17100 O OG  . SER F 290 ? 0.7020 0.4479 1.0395 -0.0269 0.0443  -0.0450 290 SER F OG  
17101 N N   . ILE F 291 ? 0.4579 0.2366 0.8120 0.0179  0.0093  -0.0018 291 ILE F N   
17102 C CA  . ILE F 291 ? 0.4293 0.2473 0.8020 0.0258  -0.0078 -0.0020 291 ILE F CA  
17103 C C   . ILE F 291 ? 0.4176 0.2505 0.7972 0.0503  -0.0234 0.0167  291 ILE F C   
17104 O O   . ILE F 291 ? 0.4155 0.2780 0.8206 0.0643  -0.0310 0.0141  291 ILE F O   
17105 C CB  . ILE F 291 ? 0.4039 0.2512 0.7636 0.0072  -0.0171 -0.0085 291 ILE F CB  
17106 C CG1 . ILE F 291 ? 0.3937 0.2432 0.7461 -0.0086 -0.0044 -0.0297 291 ILE F CG1 
17107 C CG2 . ILE F 291 ? 0.3540 0.2385 0.7307 0.0125  -0.0287 -0.0079 291 ILE F CG2 
17108 C CD1 . ILE F 291 ? 0.3562 0.2348 0.6906 -0.0193 -0.0104 -0.0332 291 ILE F CD1 
17109 N N   . PHE F 292 ? 0.4212 0.2393 0.7787 0.0569  -0.0277 0.0340  292 PHE F N   
17110 C CA  . PHE F 292 ? 0.4102 0.2486 0.7665 0.0866  -0.0440 0.0505  292 PHE F CA  
17111 C C   . PHE F 292 ? 0.4955 0.3277 0.8676 0.1178  -0.0377 0.0579  292 PHE F C   
17112 O O   . PHE F 292 ? 0.5043 0.3825 0.8982 0.1380  -0.0549 0.0550  292 PHE F O   
17113 C CB  . PHE F 292 ? 0.4385 0.2535 0.7609 0.0946  -0.0423 0.0720  292 PHE F CB  
17114 C CG  . PHE F 292 ? 0.4630 0.3004 0.7748 0.1341  -0.0580 0.0906  292 PHE F CG  
17115 C CD1 . PHE F 292 ? 0.4667 0.3587 0.7798 0.1392  -0.0868 0.0827  292 PHE F CD1 
17116 C CD2 . PHE F 292 ? 0.5363 0.3447 0.8294 0.1669  -0.0422 0.1121  292 PHE F CD2 
17117 C CE1 . PHE F 292 ? 0.4834 0.4082 0.7854 0.1789  -0.1048 0.0940  292 PHE F CE1 
17118 C CE2 . PHE F 292 ? 0.5751 0.4135 0.8476 0.2094  -0.0572 0.1277  292 PHE F CE2 
17119 C CZ  . PHE F 292 ? 0.5435 0.4450 0.8241 0.2170  -0.0907 0.1181  292 PHE F CZ  
17120 N N   . GLU F 293 ? 0.5310 0.3144 0.8855 0.1182  -0.0113 0.0627  293 GLU F N   
17121 C CA  . GLU F 293 ? 0.5525 0.3258 0.9047 0.1502  -0.0014 0.0723  293 GLU F CA  
17122 C C   . GLU F 293 ? 0.5130 0.3232 0.9036 0.1544  -0.0072 0.0551  293 GLU F C   
17123 O O   . GLU F 293 ? 0.5214 0.3604 0.9225 0.1869  -0.0149 0.0614  293 GLU F O   
17124 C CB  . GLU F 293 ? 0.6416 0.3491 0.9667 0.1446  0.0308  0.0769  293 GLU F CB  
17125 C CG  . GLU F 293 ? 0.7742 0.4559 1.0706 0.1846  0.0405  0.1035  293 GLU F CG  
17126 C CD  . GLU F 293 ? 0.9469 0.5610 1.2219 0.1750  0.0745  0.1081  293 GLU F CD  
17127 O OE1 . GLU F 293 ? 1.0017 0.5955 1.2909 0.1483  0.0898  0.0849  293 GLU F OE1 
17128 O OE2 . GLU F 293 ? 1.0314 0.6166 1.2775 0.1947  0.0867  0.1334  293 GLU F OE2 
17129 N N   . VAL F 294 ? 0.5000 0.3128 0.9088 0.1248  -0.0017 0.0335  294 VAL F N   
17130 C CA  . VAL F 294 ? 0.5101 0.3564 0.9545 0.1269  -0.0019 0.0182  294 VAL F CA  
17131 C C   . VAL F 294 ? 0.4978 0.4075 0.9797 0.1287  -0.0252 0.0125  294 VAL F C   
17132 O O   . VAL F 294 ? 0.5162 0.4666 1.0298 0.1442  -0.0295 0.0075  294 VAL F O   
17133 C CB  . VAL F 294 ? 0.4992 0.3308 0.9440 0.1000  0.0138  -0.0021 294 VAL F CB  
17134 C CG1 . VAL F 294 ? 0.4106 0.2806 0.8912 0.1033  0.0158  -0.0141 294 VAL F CG1 
17135 C CG2 . VAL F 294 ? 0.5458 0.3258 0.9646 0.0980  0.0366  -0.0061 294 VAL F CG2 
17136 N N   . PHE F 295 ? 0.4663 0.3877 0.9399 0.1083  -0.0378 0.0099  295 PHE F N   
17137 C CA  . PHE F 295 ? 0.4280 0.4052 0.9297 0.1019  -0.0564 -0.0005 295 PHE F CA  
17138 C C   . PHE F 295 ? 0.4672 0.4895 0.9861 0.1315  -0.0788 0.0025  295 PHE F C   
17139 O O   . PHE F 295 ? 0.4446 0.5222 1.0095 0.1344  -0.0883 -0.0132 295 PHE F O   
17140 C CB  . PHE F 295 ? 0.4097 0.3819 0.8875 0.0769  -0.0629 -0.0023 295 PHE F CB  
17141 C CG  . PHE F 295 ? 0.3693 0.3896 0.8721 0.0714  -0.0816 -0.0140 295 PHE F CG  
17142 C CD1 . PHE F 295 ? 0.3329 0.3796 0.8756 0.0547  -0.0736 -0.0302 295 PHE F CD1 
17143 C CD2 . PHE F 295 ? 0.3752 0.4130 0.8625 0.0834  -0.1039 -0.0102 295 PHE F CD2 
17144 C CE1 . PHE F 295 ? 0.2590 0.3453 0.8320 0.0454  -0.0865 -0.0462 295 PHE F CE1 
17145 C CE2 . PHE F 295 ? 0.3436 0.4275 0.8569 0.0768  -0.1215 -0.0285 295 PHE F CE2 
17146 C CZ  . PHE F 295 ? 0.2931 0.3997 0.8525 0.0555  -0.1123 -0.0484 295 PHE F CZ  
17147 N N   . THR F 296 ? 0.5290 0.5327 1.0129 0.1553  -0.0858 0.0215  296 THR F N   
17148 C CA  . THR F 296 ? 0.4049 0.4595 0.8877 0.1880  -0.1077 0.0241  296 THR F CA  
17149 C C   . THR F 296 ? 0.4804 0.5647 0.9852 0.2136  -0.1031 0.0215  296 THR F C   
17150 O O   . THR F 296 ? 0.5042 0.6574 1.0304 0.2305  -0.1214 0.0094  296 THR F O   
17151 C CB  . THR F 296 ? 0.4565 0.4790 0.8837 0.2146  -0.1079 0.0513  296 THR F CB  
17152 O OG1 . THR F 296 ? 0.5167 0.5192 0.9252 0.1907  -0.1131 0.0529  296 THR F OG1 
17153 C CG2 . THR F 296 ? 0.4777 0.5606 0.8941 0.2558  -0.1287 0.0545  296 THR F CG2 
17154 N N   . GLN F 297 ? 0.4942 0.5289 0.9921 0.2155  -0.0775 0.0304  297 GLN F N   
17155 C CA  . GLN F 297 ? 0.5290 0.5844 1.0438 0.2413  -0.0696 0.0297  297 GLN F CA  
17156 C C   . GLN F 297 ? 0.4304 0.5401 1.0031 0.2205  -0.0721 0.0041  297 GLN F C   
17157 O O   . GLN F 297 ? 0.4385 0.6090 1.0387 0.2405  -0.0809 -0.0040 297 GLN F O   
17158 C CB  . GLN F 297 ? 0.6125 0.5927 1.0983 0.2461  -0.0390 0.0425  297 GLN F CB  
17159 C CG  . GLN F 297 ? 0.7151 0.6586 1.1532 0.2890  -0.0304 0.0676  297 GLN F CG  
17160 C CD  . GLN F 297 ? 0.7164 0.7250 1.1623 0.3376  -0.0475 0.0704  297 GLN F CD  
17161 O OE1 . GLN F 297 ? 0.7471 0.7703 1.1628 0.3722  -0.0637 0.0823  297 GLN F OE1 
17162 N NE2 . GLN F 297 ? 0.6803 0.7315 1.1660 0.3420  -0.0458 0.0562  297 GLN F NE2 
17163 N N   . VAL F 298 ? 0.3937 0.4826 0.9828 0.1827  -0.0606 -0.0074 298 VAL F N   
17164 C CA  . VAL F 298 ? 0.3822 0.5146 1.0231 0.1614  -0.0554 -0.0282 298 VAL F CA  
17165 C C   . VAL F 298 ? 0.3466 0.5497 1.0214 0.1551  -0.0784 -0.0470 298 VAL F C   
17166 O O   . VAL F 298 ? 0.3462 0.6017 1.0636 0.1541  -0.0775 -0.0628 298 VAL F O   
17167 C CB  . VAL F 298 ? 0.3690 0.4664 1.0114 0.1275  -0.0370 -0.0331 298 VAL F CB  
17168 C CG1 . VAL F 298 ? 0.3535 0.4925 1.0453 0.1054  -0.0283 -0.0505 298 VAL F CG1 
17169 C CG2 . VAL F 298 ? 0.3744 0.4189 0.9902 0.1312  -0.0125 -0.0260 298 VAL F CG2 
17170 N N   . PHE F 299 ? 0.3393 0.5439 0.9934 0.1497  -0.0977 -0.0475 299 PHE F N   
17171 C CA  . PHE F 299 ? 0.3702 0.6382 1.0466 0.1434  -0.1200 -0.0699 299 PHE F CA  
17172 C C   . PHE F 299 ? 0.4290 0.7575 1.1091 0.1805  -0.1363 -0.0716 299 PHE F C   
17173 O O   . PHE F 299 ? 0.4663 0.8590 1.1879 0.1737  -0.1441 -0.0961 299 PHE F O   
17174 C CB  . PHE F 299 ? 0.3283 0.5822 0.9709 0.1360  -0.1368 -0.0684 299 PHE F CB  
17175 C CG  . PHE F 299 ? 0.3325 0.6428 0.9943 0.1240  -0.1560 -0.0969 299 PHE F CG  
17176 C CD1 . PHE F 299 ? 0.3592 0.7246 1.0075 0.1540  -0.1801 -0.1018 299 PHE F CD1 
17177 C CD2 . PHE F 299 ? 0.3328 0.6374 1.0216 0.0848  -0.1465 -0.1181 299 PHE F CD2 
17178 C CE1 . PHE F 299 ? 0.4031 0.8202 1.0680 0.1420  -0.1974 -0.1328 299 PHE F CE1 
17179 C CE2 . PHE F 299 ? 0.3625 0.7096 1.0675 0.0723  -0.1603 -0.1480 299 PHE F CE2 
17180 C CZ  . PHE F 299 ? 0.3867 0.7922 1.0816 0.0994  -0.1873 -0.1582 299 PHE F CZ  
17181 N N   . ALA F 300 ? 0.4654 0.7716 1.1009 0.2205  -0.1382 -0.0442 300 ALA F N   
17182 C CA  . ALA F 300 ? 0.4428 0.8037 1.0734 0.2650  -0.1496 -0.0364 300 ALA F CA  
17183 C C   . ALA F 300 ? 0.4449 0.8474 1.1240 0.2686  -0.1394 -0.0480 300 ALA F C   
17184 O O   . ALA F 300 ? 0.4646 0.9425 1.1697 0.2865  -0.1535 -0.0584 300 ALA F O   
17185 C CB  . ALA F 300 ? 0.4881 0.7965 1.0601 0.3079  -0.1400 0.0025  300 ALA F CB  
17186 N N   . ASN F 301 ? 0.4273 0.7818 1.1197 0.2495  -0.1145 -0.0468 301 ASN F N   
17187 C CA  . ASN F 301 ? 0.4279 0.8128 1.1643 0.2492  -0.0995 -0.0565 301 ASN F CA  
17188 C C   . ASN F 301 ? 0.4509 0.8965 1.2494 0.2129  -0.1025 -0.0895 301 ASN F C   
17189 O O   . ASN F 301 ? 0.4114 0.9047 1.2518 0.2170  -0.0952 -0.0997 301 ASN F O   
17190 C CB  . ASN F 301 ? 0.4219 0.7323 1.1473 0.2374  -0.0694 -0.0455 301 ASN F CB  
17191 C CG  . ASN F 301 ? 0.5362 0.7836 1.2071 0.2734  -0.0583 -0.0180 301 ASN F CG  
17192 O OD1 . ASN F 301 ? 0.5041 0.7640 1.1462 0.3150  -0.0685 -0.0021 301 ASN F OD1 
17193 N ND2 . ASN F 301 ? 0.5355 0.7117 1.1880 0.2573  -0.0341 -0.0124 301 ASN F ND2 
17194 N N   . ASN F 302 ? 0.4302 0.8699 1.2342 0.1776  -0.1099 -0.1060 302 ASN F N   
17195 C CA  . ASN F 302 ? 0.4262 0.9101 1.2854 0.1420  -0.1075 -0.1382 302 ASN F CA  
17196 C C   . ASN F 302 ? 0.4665 1.0168 1.3333 0.1470  -0.1380 -0.1612 302 ASN F C   
17197 O O   . ASN F 302 ? 0.4718 1.0420 1.3712 0.1139  -0.1388 -0.1910 302 ASN F O   
17198 C CB  . ASN F 302 ? 0.3399 0.7662 1.2029 0.0987  -0.0864 -0.1425 302 ASN F CB  
17199 C CG  . ASN F 302 ? 0.3308 0.7139 1.2042 0.0893  -0.0512 -0.1287 302 ASN F CG  
17200 O OD1 . ASN F 302 ? 0.3348 0.7350 1.2521 0.0709  -0.0299 -0.1409 302 ASN F OD1 
17201 N ND2 . ASN F 302 ? 0.3257 0.6530 1.1570 0.1035  -0.0435 -0.1039 302 ASN F ND2 
17202 N N   . MET F 303 ? 0.4463 0.7828 1.3444 0.1273  -0.2265 0.0515  303 MET F N   
17203 C CA  . MET F 303 ? 0.5980 0.9363 1.5117 0.0972  -0.2503 0.0494  303 MET F CA  
17204 C C   . MET F 303 ? 0.6256 1.0163 1.5331 0.1271  -0.2629 0.0498  303 MET F C   
17205 O O   . MET F 303 ? 0.6910 1.0814 1.5581 0.1719  -0.2543 0.0453  303 MET F O   
17206 C CB  . MET F 303 ? 0.4662 0.7052 1.3327 0.0846  -0.2564 0.0308  303 MET F CB  
17207 C CG  . MET F 303 ? 0.4633 0.6478 1.3181 0.0577  -0.2431 0.0277  303 MET F CG  
17208 S SD  . MET F 303 ? 0.6755 0.8759 1.5597 0.0047  -0.2562 0.0362  303 MET F SD  
17209 C CE  . MET F 303 ? 0.5182 0.6712 1.3657 -0.0065 -0.2859 0.0173  303 MET F CE  
17210 N N   . PRO F 304 ? 0.5903 1.0208 1.5252 0.1034  -0.2844 0.0537  304 PRO F N   
17211 C CA  . PRO F 304 ? 0.5856 1.0565 1.5040 0.1331  -0.2968 0.0511  304 PRO F CA  
17212 C C   . PRO F 304 ? 0.6125 0.9994 1.4758 0.1575  -0.3080 0.0324  304 PRO F C   
17213 O O   . PRO F 304 ? 0.6255 0.9632 1.4839 0.1360  -0.3241 0.0239  304 PRO F O   
17214 C CB  . PRO F 304 ? 0.5814 1.1041 1.5419 0.0919  -0.3191 0.0593  304 PRO F CB  
17215 C CG  . PRO F 304 ? 0.5866 1.0471 1.5568 0.0431  -0.3260 0.0555  304 PRO F CG  
17216 C CD  . PRO F 304 ? 0.5779 1.0166 1.5468 0.0475  -0.2979 0.0613  304 PRO F CD  
17217 N N   . LYS F 305 ? 0.6322 1.0042 1.4487 0.2031  -0.3017 0.0285  305 LYS F N   
17218 C CA  . LYS F 305 ? 0.5669 0.8520 1.3268 0.2207  -0.3123 0.0181  305 LYS F CA  
17219 C C   . LYS F 305 ? 0.5859 0.8740 1.3398 0.2205  -0.3358 0.0155  305 LYS F C   
17220 O O   . LYS F 305 ? 0.6040 0.8237 1.3247 0.2196  -0.3464 0.0130  305 LYS F O   
17221 C CB  . LYS F 305 ? 0.6037 0.8692 1.3096 0.2671  -0.3067 0.0157  305 LYS F CB  
17222 C CG  . LYS F 305 ? 0.6505 0.8357 1.2981 0.2836  -0.3243 0.0107  305 LYS F CG  
17223 C CD  . LYS F 305 ? 0.7004 0.8986 1.3046 0.3324  -0.3290 0.0094  305 LYS F CD  
17224 C CE  . LYS F 305 ? 0.7573 0.8571 1.2994 0.3434  -0.3479 0.0056  305 LYS F CE  
17225 N NZ  . LYS F 305 ? 0.8180 0.9172 1.3130 0.3914  -0.3545 0.0015  305 LYS F NZ  
17226 N N   . GLN F 306 ? 0.6174 0.9903 1.4050 0.2185  -0.3443 0.0195  306 GLN F N   
17227 C CA  . GLN F 306 ? 0.6470 1.0266 1.4203 0.2269  -0.3665 0.0155  306 GLN F CA  
17228 C C   . GLN F 306 ? 0.5979 0.9622 1.3948 0.1868  -0.3826 0.0108  306 GLN F C   
17229 O O   . GLN F 306 ? 0.6178 0.9922 1.4078 0.1872  -0.4036 0.0061  306 GLN F O   
17230 C CB  . GLN F 306 ? 0.6518 1.1371 1.4470 0.2457  -0.3702 0.0228  306 GLN F CB  
17231 C CG  . GLN F 306 ? 0.5899 1.1722 1.4552 0.2074  -0.3687 0.0355  306 GLN F CG  
17232 C CD  . GLN F 306 ? 0.5616 1.1630 1.4568 0.1911  -0.3454 0.0469  306 GLN F CD  
17233 O OE1 . GLN F 306 ? 0.5575 1.0987 1.4224 0.2090  -0.3292 0.0419  306 GLN F OE1 
17234 N NE2 . GLN F 306 ? 0.5488 1.2342 1.5015 0.1543  -0.3451 0.0647  306 GLN F NE2 
17235 N N   . ALA F 307 ? 0.5752 0.9056 1.3874 0.1570  -0.3725 0.0104  307 ALA F N   
17236 C CA  . ALA F 307 ? 0.5875 0.8817 1.3894 0.1201  -0.3791 0.0027  307 ALA F CA  
17237 C C   . ALA F 307 ? 0.5945 0.8037 1.3463 0.1226  -0.3696 -0.0010 307 ALA F C   
17238 O O   . ALA F 307 ? 0.6131 0.7886 1.3403 0.1061  -0.3756 -0.0090 307 ALA F O   
17239 C CB  . ALA F 307 ? 0.5769 0.8938 1.4179 0.0823  -0.3734 0.0066  307 ALA F CB  
17240 N N   . GLN F 308 ? 0.6400 0.8177 1.3750 0.1459  -0.3580 0.0063  308 GLN F N   
17241 C CA  . GLN F 308 ? 0.6385 0.7489 1.3354 0.1452  -0.3490 0.0117  308 GLN F CA  
17242 C C   . GLN F 308 ? 0.6823 0.7765 1.3432 0.1562  -0.3641 0.0167  308 GLN F C   
17243 O O   . GLN F 308 ? 0.7240 0.8453 1.3849 0.1744  -0.3815 0.0159  308 GLN F O   
17244 C CB  . GLN F 308 ? 0.6386 0.7184 1.3315 0.1636  -0.3416 0.0203  308 GLN F CB  
17245 C CG  . GLN F 308 ? 0.6307 0.7382 1.3566 0.1627  -0.3271 0.0157  308 GLN F CG  
17246 C CD  . GLN F 308 ? 0.6390 0.7037 1.3336 0.1777  -0.3148 0.0182  308 GLN F CD  
17247 O OE1 . GLN F 308 ? 0.6008 0.6112 1.2570 0.1825  -0.3215 0.0252  308 GLN F OE1 
17248 N NE2 . GLN F 308 ? 0.6265 0.7169 1.3343 0.1827  -0.2983 0.0143  308 GLN F NE2 
17249 N N   . VAL F 309 ? 0.6636 0.7220 1.2930 0.1488  -0.3566 0.0238  309 VAL F N   
17250 C CA  . VAL F 309 ? 0.7064 0.7565 1.2989 0.1618  -0.3672 0.0355  309 VAL F CA  
17251 C C   . VAL F 309 ? 0.7503 0.7639 1.3224 0.1619  -0.3568 0.0630  309 VAL F C   
17252 O O   . VAL F 309 ? 0.7766 0.7694 1.3624 0.1512  -0.3434 0.0673  309 VAL F O   
17253 C CB  . VAL F 309 ? 0.7052 0.7669 1.2744 0.1584  -0.3734 0.0211  309 VAL F CB  
17254 C CG1 . VAL F 309 ? 0.6974 0.7945 1.2930 0.1513  -0.3926 -0.0013 309 VAL F CG1 
17255 C CG2 . VAL F 309 ? 0.6908 0.7305 1.2456 0.1461  -0.3569 0.0166  309 VAL F CG2 
17256 N N   . LYS F 310 ? 0.7638 0.7732 1.3065 0.1728  -0.3650 0.0856  310 LYS F N   
17257 C CA  . LYS F 310 ? 0.7791 0.7649 1.3094 0.1657  -0.3577 0.1215  310 LYS F CA  
17258 C C   . LYS F 310 ? 0.7255 0.7160 1.2558 0.1518  -0.3336 0.1220  310 LYS F C   
17259 O O   . LYS F 310 ? 0.7099 0.7227 1.2185 0.1577  -0.3250 0.1103  310 LYS F O   
17260 C CB  . LYS F 310 ? 0.8655 0.8631 1.3638 0.1768  -0.3654 0.1520  310 LYS F CB  
17261 C CG  . LYS F 310 ? 0.9379 0.9168 1.4342 0.1628  -0.3641 0.2006  310 LYS F CG  
17262 C CD  . LYS F 310 ? 1.0391 1.0382 1.5067 0.1722  -0.3715 0.2401  310 LYS F CD  
17263 C CE  . LYS F 310 ? 1.0804 1.1362 1.5198 0.1866  -0.3503 0.2425  310 LYS F CE  
17264 N NZ  . LYS F 310 ? 1.1433 1.2323 1.5596 0.1927  -0.3496 0.2982  310 LYS F NZ  
17265 N N   . ALA F 311 ? 0.6979 0.6636 1.2468 0.1376  -0.3267 0.1349  311 ALA F N   
17266 C CA  . ALA F 311 ? 0.7031 0.6735 1.2540 0.1261  -0.3041 0.1359  311 ALA F CA  
17267 C C   . ALA F 311 ? 0.7684 0.7734 1.2885 0.1330  -0.2923 0.1607  311 ALA F C   
17268 O O   . ALA F 311 ? 0.8105 0.8304 1.3171 0.1377  -0.3005 0.1941  311 ALA F O   
17269 C CB  . ALA F 311 ? 0.6866 0.6255 1.2602 0.1113  -0.3047 0.1526  311 ALA F CB  
17270 N N   . VAL F 312 ? 0.7778 0.7979 1.2818 0.1383  -0.2743 0.1447  312 VAL F N   
17271 C CA  . VAL F 312 ? 0.8061 0.8679 1.2699 0.1587  -0.2630 0.1616  312 VAL F CA  
17272 C C   . VAL F 312 ? 0.7927 0.8728 1.2487 0.1602  -0.2400 0.1702  312 VAL F C   
17273 O O   . VAL F 312 ? 0.7676 0.8196 1.2382 0.1498  -0.2329 0.1452  312 VAL F O   
17274 C CB  . VAL F 312 ? 0.9484 1.0124 1.3743 0.1834  -0.2738 0.1241  312 VAL F CB  
17275 C CG1 . VAL F 312 ? 0.9751 1.0698 1.3466 0.2158  -0.2630 0.1234  312 VAL F CG1 
17276 C CG2 . VAL F 312 ? 0.9977 1.0673 1.4207 0.1908  -0.2942 0.1288  312 VAL F CG2 
17277 N N   . GLY F 313 ? 0.8012 0.9364 1.2346 0.1753  -0.2278 0.2096  313 GLY F N   
17278 C CA  . GLY F 313 ? 0.7854 0.9558 1.2041 0.1864  -0.2052 0.2202  313 GLY F CA  
17279 C C   . GLY F 313 ? 0.7440 0.9077 1.2113 0.1523  -0.1988 0.2463  313 GLY F C   
17280 O O   . GLY F 313 ? 0.7446 0.9027 1.2468 0.1251  -0.2112 0.2828  313 GLY F O   
17281 N N   . PRO F 314 ? 0.7125 0.8710 1.1772 0.1554  -0.1833 0.2272  314 PRO F N   
17282 C CA  . PRO F 314 ? 0.6926 0.8405 1.1990 0.1273  -0.1780 0.2426  314 PRO F CA  
17283 C C   . PRO F 314 ? 0.6031 0.6765 1.1391 0.1067  -0.1918 0.2067  314 PRO F C   
17284 O O   . PRO F 314 ? 0.5813 0.6326 1.1496 0.0863  -0.1932 0.2127  314 PRO F O   
17285 C CB  . PRO F 314 ? 0.7129 0.8884 1.1902 0.1514  -0.1551 0.2290  314 PRO F CB  
17286 C CG  . PRO F 314 ? 0.7339 0.8794 1.1593 0.1834  -0.1589 0.1784  314 PRO F CG  
17287 C CD  . PRO F 314 ? 0.7399 0.8971 1.1525 0.1913  -0.1742 0.1874  314 PRO F CD  
17288 N N   . PHE F 315 ? 0.6089 0.6511 1.1331 0.1150  -0.2032 0.1714  315 PHE F N   
17289 C CA  . PHE F 315 ? 0.5857 0.5769 1.1344 0.1033  -0.2122 0.1371  315 PHE F CA  
17290 C C   . PHE F 315 ? 0.6136 0.5812 1.1903 0.0906  -0.2336 0.1495  315 PHE F C   
17291 O O   . PHE F 315 ? 0.6401 0.6197 1.2108 0.0918  -0.2468 0.1742  315 PHE F O   
17292 C CB  . PHE F 315 ? 0.5963 0.5749 1.1235 0.1156  -0.2170 0.0976  315 PHE F CB  
17293 C CG  . PHE F 315 ? 0.6398 0.6235 1.1269 0.1336  -0.2054 0.0802  315 PHE F CG  
17294 C CD1 . PHE F 315 ? 0.5986 0.5660 1.0877 0.1306  -0.1906 0.0691  315 PHE F CD1 
17295 C CD2 . PHE F 315 ? 0.6805 0.6824 1.1202 0.1596  -0.2114 0.0747  315 PHE F CD2 
17296 C CE1 . PHE F 315 ? 0.6266 0.5904 1.0700 0.1526  -0.1836 0.0516  315 PHE F CE1 
17297 C CE2 . PHE F 315 ? 0.6893 0.6865 1.0796 0.1853  -0.2064 0.0551  315 PHE F CE2 
17298 C CZ  . PHE F 315 ? 0.6789 0.6548 1.0702 0.1817  -0.1930 0.0435  315 PHE F CZ  
17299 N N   . GLY F 316 ? 0.5658 0.4982 1.1674 0.0839  -0.2387 0.1304  316 GLY F N   
17300 C CA  . GLY F 316 ? 0.5774 0.4795 1.1960 0.0815  -0.2631 0.1380  316 GLY F CA  
17301 C C   . GLY F 316 ? 0.7954 0.6937 1.4179 0.0943  -0.2722 0.1082  316 GLY F C   
17302 O O   . GLY F 316 ? 0.8752 0.7577 1.4992 0.1024  -0.2946 0.1130  316 GLY F O   
17303 N N   . LEU F 317 ? 0.7221 0.6365 1.3449 0.0962  -0.2582 0.0804  317 LEU F N   
17304 C CA  . LEU F 317 ? 0.5510 0.4766 1.1878 0.1029  -0.2666 0.0578  317 LEU F CA  
17305 C C   . LEU F 317 ? 0.5591 0.5059 1.1828 0.0999  -0.2657 0.0424  317 LEU F C   
17306 O O   . LEU F 317 ? 0.6244 0.5671 1.2416 0.0923  -0.2542 0.0291  317 LEU F O   
17307 C CB  . LEU F 317 ? 0.5256 0.4478 1.1873 0.1036  -0.2577 0.0426  317 LEU F CB  
17308 C CG  . LEU F 317 ? 0.5173 0.4710 1.2029 0.1101  -0.2626 0.0271  317 LEU F CG  
17309 C CD1 . LEU F 317 ? 0.5378 0.4997 1.2214 0.1299  -0.2835 0.0311  317 LEU F CD1 
17310 C CD2 . LEU F 317 ? 0.4952 0.4536 1.2005 0.1129  -0.2482 0.0199  317 LEU F CD2 
17311 N N   . CYS F 318 ? 0.5806 0.5428 1.1951 0.1078  -0.2822 0.0436  318 CYS F N   
17312 C CA  . CYS F 318 ? 0.6875 0.6640 1.2854 0.1072  -0.2902 0.0267  318 CYS F CA  
17313 C C   . CYS F 318 ? 0.7169 0.7197 1.3392 0.1069  -0.3086 0.0141  318 CYS F C   
17314 O O   . CYS F 318 ? 0.7536 0.7680 1.3907 0.1181  -0.3167 0.0221  318 CYS F O   
17315 C CB  . CYS F 318 ? 0.6976 0.6790 1.2544 0.1210  -0.2936 0.0397  318 CYS F CB  
17316 S SG  . CYS F 318 ? 0.6351 0.6114 1.1631 0.1248  -0.2706 0.0563  318 CYS F SG  
17317 N N   . TYR F 319 ? 0.6978 0.7091 1.3217 0.0951  -0.3192 -0.0045 319 TYR F N   
17318 C CA  . TYR F 319 ? 0.6598 0.7085 1.3154 0.0878  -0.3384 -0.0129 319 TYR F CA  
17319 C C   . TYR F 319 ? 0.7066 0.7570 1.3373 0.0880  -0.3645 -0.0267 319 TYR F C   
17320 O O   . TYR F 319 ? 0.7230 0.7406 1.3081 0.0948  -0.3673 -0.0348 319 TYR F O   
17321 C CB  . TYR F 319 ? 0.6217 0.6850 1.3174 0.0635  -0.3341 -0.0171 319 TYR F CB  
17322 C CG  . TYR F 319 ? 0.6020 0.6750 1.3246 0.0691  -0.3117 -0.0062 319 TYR F CG  
17323 C CD1 . TYR F 319 ? 0.6027 0.6363 1.3100 0.0687  -0.2909 -0.0042 319 TYR F CD1 
17324 C CD2 . TYR F 319 ? 0.6089 0.7347 1.3692 0.0796  -0.3130 0.0011  319 TYR F CD2 
17325 C CE1 . TYR F 319 ? 0.6029 0.6410 1.3304 0.0771  -0.2744 0.0029  319 TYR F CE1 
17326 C CE2 . TYR F 319 ? 0.6156 0.7484 1.3914 0.0937  -0.2956 0.0079  319 TYR F CE2 
17327 C CZ  . TYR F 319 ? 0.6255 0.7100 1.3842 0.0914  -0.2776 0.0078  319 TYR F CZ  
17328 O OH  . TYR F 319 ? 0.6450 0.7312 1.4143 0.1087  -0.2641 0.0118  319 TYR F OH  
17329 N N   . ASP F 320 ? 0.7177 0.8102 1.3766 0.0842  -0.3854 -0.0300 320 ASP F N   
17330 C CA  . ASP F 320 ? 0.7371 0.8325 1.3800 0.0798  -0.4174 -0.0459 320 ASP F CA  
17331 C C   . ASP F 320 ? 0.7332 0.7990 1.3797 0.0495  -0.4305 -0.0592 320 ASP F C   
17332 O O   . ASP F 320 ? 0.7044 0.7909 1.3988 0.0231  -0.4246 -0.0510 320 ASP F O   
17333 C CB  . ASP F 320 ? 0.7414 0.8999 1.4247 0.0794  -0.4365 -0.0428 320 ASP F CB  
17334 C CG  . ASP F 320 ? 0.7909 0.9585 1.4739 0.0635  -0.4763 -0.0591 320 ASP F CG  
17335 O OD1 . ASP F 320 ? 0.8306 0.9447 1.4679 0.0623  -0.4935 -0.0767 320 ASP F OD1 
17336 O OD2 . ASP F 320 ? 0.7937 1.0238 1.5212 0.0545  -0.4939 -0.0544 320 ASP F OD2 
17337 N N   . SER F 321 ? 0.7865 0.8034 1.3795 0.0557  -0.4517 -0.0786 321 SER F N   
17338 C CA  . SER F 321 ? 0.8421 0.8132 1.4303 0.0285  -0.4699 -0.0918 321 SER F CA  
17339 C C   . SER F 321 ? 0.8730 0.8763 1.5150 -0.0103 -0.5059 -0.0907 321 SER F C   
17340 O O   . SER F 321 ? 0.8518 0.8853 1.5503 -0.0418 -0.4985 -0.0740 321 SER F O   
17341 C CB  . SER F 321 ? 0.9175 0.8198 1.4245 0.0524  -0.4903 -0.1168 321 SER F CB  
17342 O OG  . SER F 321 ? 0.9021 0.8019 1.3647 0.0913  -0.4580 -0.1101 321 SER F OG  
17343 N N   . ARG F 322 ? 0.9110 0.9231 1.5409 -0.0061 -0.5437 -0.1035 322 ARG F N   
17344 C CA  . ARG F 322 ? 0.9315 0.9821 1.6184 -0.0480 -0.5833 -0.0984 322 ARG F CA  
17345 C C   . ARG F 322 ? 0.8607 1.0128 1.6212 -0.0529 -0.5581 -0.0704 322 ARG F C   
17346 O O   . ARG F 322 ? 0.8555 1.0634 1.6294 -0.0363 -0.5662 -0.0684 322 ARG F O   
17347 C CB  . ARG F 322 ? 1.0085 1.0411 1.6630 -0.0424 -0.6369 -0.1215 322 ARG F CB  
17348 C CG  . ARG F 322 ? 1.0604 1.0883 1.7574 -0.0982 -0.6923 -0.1202 322 ARG F CG  
17349 C CD  . ARG F 322 ? 1.1468 1.1309 1.7939 -0.0872 -0.7515 -0.1504 322 ARG F CD  
17350 N NE  . ARG F 322 ? 1.1662 1.1046 1.7219 -0.0230 -0.7365 -0.1756 322 ARG F NE  
17351 C CZ  . ARG F 322 ? 1.2098 1.1393 1.7174 0.0095  -0.7692 -0.1983 322 ARG F CZ  
17352 N NH1 . ARG F 322 ? 1.2106 1.1128 1.6379 0.0697  -0.7499 -0.2130 322 ARG F NH1 
17353 N NH2 . ARG F 322 ? 1.2538 1.2113 1.7972 -0.0182 -0.8210 -0.2023 322 ARG F NH2 
17354 N N   . LYS F 323 ? 0.8123 0.9855 1.6154 -0.0727 -0.5297 -0.0498 323 LYS F N   
17355 C CA  . LYS F 323 ? 0.7457 1.0126 1.6142 -0.0725 -0.5018 -0.0218 323 LYS F CA  
17356 C C   . LYS F 323 ? 0.8649 1.1140 1.7461 -0.0829 -0.4678 -0.0086 323 LYS F C   
17357 O O   . LYS F 323 ? 0.8327 1.1550 1.7650 -0.0826 -0.4444 0.0153  323 LYS F O   
17358 C CB  . LYS F 323 ? 0.7056 1.0075 1.5590 -0.0233 -0.4804 -0.0222 323 LYS F CB  
17359 C CG  . LYS F 323 ? 0.6438 1.0090 1.5338 -0.0026 -0.4462 -0.0015 323 LYS F CG  
17360 C CD  . LYS F 323 ? 0.6318 1.0596 1.5282 0.0339  -0.4497 0.0018  323 LYS F CD  
17361 C CE  . LYS F 323 ? 0.6503 1.1581 1.5901 0.0117  -0.4798 0.0093  323 LYS F CE  
17362 N NZ  . LYS F 323 ? 0.6361 1.2232 1.6281 -0.0154 -0.4632 0.0371  323 LYS F NZ  
17363 N N   . ILE F 324 ? 0.8878 1.0462 1.7229 -0.0903 -0.4679 -0.0234 324 ILE F N   
17364 C CA  . ILE F 324 ? 0.8732 1.0103 1.7163 -0.0992 -0.4371 -0.0124 324 ILE F CA  
17365 C C   . ILE F 324 ? 0.8797 1.0941 1.7996 -0.1341 -0.4340 0.0202  324 ILE F C   
17366 O O   . ILE F 324 ? 0.8461 1.0656 1.7819 -0.1371 -0.4053 0.0347  324 ILE F O   
17367 C CB  . ILE F 324 ? 0.9522 0.9852 1.7422 -0.1135 -0.4523 -0.0307 324 ILE F CB  
17368 C CG1 . ILE F 324 ? 1.0108 0.9734 1.7231 -0.0861 -0.4743 -0.0622 324 ILE F CG1 
17369 C CG2 . ILE F 324 ? 0.9219 0.9254 1.6953 -0.0983 -0.4108 -0.0277 324 ILE F CG2 
17370 C CD1 . ILE F 324 ? 1.0286 0.9441 1.7220 -0.1125 -0.5351 -0.0788 324 ILE F CD1 
17371 N N   . SER F 325 ? 0.9409 1.2191 1.9080 -0.1616 -0.4665 0.0336  325 SER F N   
17372 C CA  . SER F 325 ? 0.9610 1.3193 1.9776 -0.1938 -0.4566 0.0716  325 SER F CA  
17373 C C   . SER F 325 ? 0.9778 1.2625 1.9800 -0.2339 -0.4660 0.0783  325 SER F C   
17374 O O   . SER F 325 ? 0.9643 1.2950 2.0009 -0.2583 -0.4488 0.1122  325 SER F O   
17375 C CB  . SER F 325 ? 0.9089 1.3611 1.9619 -0.1615 -0.4112 0.0940  325 SER F CB  
17376 O OG  . SER F 325 ? 0.8718 1.3627 1.9172 -0.1142 -0.4048 0.0814  325 SER F OG  
17377 N N   . GLY F 326 ? 1.0033 1.1736 1.9474 -0.2362 -0.4962 0.0458  326 GLY F N   
17378 C CA  . GLY F 326 ? 1.0529 1.1317 1.9622 -0.2656 -0.5127 0.0453  326 GLY F CA  
17379 C C   . GLY F 326 ? 0.9999 1.0962 1.9318 -0.2652 -0.4704 0.0667  326 GLY F C   
17380 O O   . GLY F 326 ? 1.0602 1.1419 1.9974 -0.2991 -0.4736 0.0910  326 GLY F O   
17381 N N   . GLY F 327 ? 0.8839 1.0123 1.8296 -0.2263 -0.4329 0.0598  327 GLY F N   
17382 C CA  . GLY F 327 ? 0.8130 0.9839 1.7915 -0.2216 -0.3918 0.0843  327 GLY F CA  
17383 C C   . GLY F 327 ? 0.7387 0.9216 1.6997 -0.1674 -0.3466 0.0721  327 GLY F C   
17384 O O   . GLY F 327 ? 0.7095 0.9574 1.6853 -0.1351 -0.3328 0.0731  327 GLY F O   
17385 N N   . ALA F 328 ? 0.7109 0.8234 1.6319 -0.1565 -0.3257 0.0611  328 ALA F N   
17386 C CA  . ALA F 328 ? 0.6508 0.7561 1.5467 -0.1111 -0.2851 0.0513  328 ALA F CA  
17387 C C   . ALA F 328 ? 0.6384 0.7677 1.5586 -0.1114 -0.2555 0.0725  328 ALA F C   
17388 O O   . ALA F 328 ? 0.6973 0.8203 1.6380 -0.1492 -0.2656 0.0915  328 ALA F O   
17389 C CB  . ALA F 328 ? 0.6744 0.6849 1.4994 -0.0921 -0.2856 0.0203  328 ALA F CB  
17390 N N   . PRO F 329 ? 0.5856 0.7361 1.5002 -0.0691 -0.2229 0.0700  329 PRO F N   
17391 C CA  . PRO F 329 ? 0.5545 0.7376 1.4924 -0.0650 -0.1966 0.0911  329 PRO F CA  
17392 C C   . PRO F 329 ? 0.5450 0.6441 1.4463 -0.0761 -0.1884 0.0824  329 PRO F C   
17393 O O   . PRO F 329 ? 0.5330 0.5498 1.3840 -0.0756 -0.1987 0.0564  329 PRO F O   
17394 C CB  . PRO F 329 ? 0.5142 0.7298 1.4450 -0.0102 -0.1732 0.0840  329 PRO F CB  
17395 C CG  . PRO F 329 ? 0.4444 0.6034 1.3334 0.0069  -0.1842 0.0564  329 PRO F CG  
17396 C CD  . PRO F 329 ? 0.5385 0.6853 1.4275 -0.0252 -0.2135 0.0521  329 PRO F CD  
17397 N N   . SER F 330 ? 0.5625 0.6896 1.4874 -0.0822 -0.1699 0.1062  330 SER F N   
17398 C CA  . SER F 330 ? 0.5963 0.6527 1.4862 -0.0828 -0.1567 0.0995  330 SER F CA  
17399 C C   . SER F 330 ? 0.5710 0.5825 1.4148 -0.0382 -0.1362 0.0700  330 SER F C   
17400 O O   . SER F 330 ? 0.5179 0.5744 1.3727 -0.0021 -0.1179 0.0709  330 SER F O   
17401 C CB  . SER F 330 ? 0.6198 0.7357 1.5497 -0.0906 -0.1370 0.1364  330 SER F CB  
17402 O OG  . SER F 330 ? 0.6103 0.7603 1.5354 -0.0406 -0.1042 0.1329  330 SER F OG  
17403 N N   . VAL F 331 ? 0.3830 0.6450 1.2195 0.0010  0.0089  -0.0358 331 VAL F N   
17404 C CA  . VAL F 331 ? 0.3971 0.6312 1.1765 0.0181  0.0149  -0.0374 331 VAL F CA  
17405 C C   . VAL F 331 ? 0.4121 0.6242 1.1458 0.0088  0.0395  -0.0290 331 VAL F C   
17406 O O   . VAL F 331 ? 0.4829 0.6581 1.1771 -0.0047 0.0244  -0.0214 331 VAL F O   
17407 C CB  . VAL F 331 ? 0.4140 0.6186 1.1726 0.0281  -0.0248 -0.0333 331 VAL F CB  
17408 C CG1 . VAL F 331 ? 0.4069 0.5822 1.1108 0.0449  -0.0182 -0.0288 331 VAL F CG1 
17409 C CG2 . VAL F 331 ? 0.4597 0.6743 1.2491 0.0347  -0.0517 -0.0375 331 VAL F CG2 
17410 N N   . ASP F 332 ? 0.3501 0.5705 1.0633 0.0176  0.0730  -0.0321 332 ASP F N   
17411 C CA  . ASP F 332 ? 0.3278 0.5189 0.9795 0.0063  0.0960  -0.0213 332 ASP F CA  
17412 C C   . ASP F 332 ? 0.3254 0.4851 0.9218 0.0274  0.1008  -0.0263 332 ASP F C   
17413 O O   . ASP F 332 ? 0.3265 0.5039 0.9438 0.0506  0.1002  -0.0412 332 ASP F O   
17414 C CB  . ASP F 332 ? 0.3721 0.6071 1.0499 -0.0076 0.1338  -0.0142 332 ASP F CB  
17415 C CG  . ASP F 332 ? 0.4086 0.6812 1.1595 -0.0290 0.1283  -0.0055 332 ASP F CG  
17416 O OD1 . ASP F 332 ? 0.4291 0.6788 1.1970 -0.0400 0.0930  -0.0041 332 ASP F OD1 
17417 O OD2 . ASP F 332 ? 0.3118 0.6304 1.0872 -0.0324 0.1547  -0.0002 332 ASP F OD2 
17418 N N   . LEU F 333 ? 0.2983 0.4090 0.8329 0.0209  0.0999  -0.0153 333 LEU F N   
17419 C CA  . LEU F 333 ? 0.3047 0.3846 0.7925 0.0371  0.1054  -0.0171 333 LEU F CA  
17420 C C   . LEU F 333 ? 0.3450 0.4311 0.8036 0.0305  0.1362  -0.0149 333 LEU F C   
17421 O O   . LEU F 333 ? 0.3723 0.4470 0.8122 0.0073  0.1460  0.0010  333 LEU F O   
17422 C CB  . LEU F 333 ? 0.2955 0.3216 0.7374 0.0359  0.0889  -0.0045 333 LEU F CB  
17423 C CG  . LEU F 333 ? 0.2879 0.3043 0.7364 0.0412  0.0621  0.0009  333 LEU F CG  
17424 C CD1 . LEU F 333 ? 0.2673 0.2386 0.6684 0.0436  0.0568  0.0139  333 LEU F CD1 
17425 C CD2 . LEU F 333 ? 0.2535 0.2912 0.7416 0.0611  0.0464  -0.0042 333 LEU F CD2 
17426 N N   . ILE F 334 ? 0.3117 0.4150 0.7652 0.0520  0.1486  -0.0309 334 ILE F N   
17427 C CA  . ILE F 334 ? 0.3478 0.4547 0.7560 0.0503  0.1766  -0.0285 334 ILE F CA  
17428 C C   . ILE F 334 ? 0.4193 0.4626 0.7674 0.0566  0.1610  -0.0242 334 ILE F C   
17429 O O   . ILE F 334 ? 0.4472 0.4667 0.7943 0.0805  0.1392  -0.0382 334 ILE F O   
17430 C CB  . ILE F 334 ? 0.3719 0.5288 0.7935 0.0758  0.1976  -0.0534 334 ILE F CB  
17431 C CG1 . ILE F 334 ? 0.4284 0.6476 0.9309 0.0758  0.2044  -0.0615 334 ILE F CG1 
17432 C CG2 . ILE F 334 ? 0.4213 0.5946 0.7898 0.0716  0.2326  -0.0459 334 ILE F CG2 
17433 C CD1 . ILE F 334 ? 0.4458 0.6968 0.9804 0.0421  0.2226  -0.0355 334 ILE F CD1 
17434 N N   . LEU F 335 ? 0.4027 0.4184 0.7098 0.0346  0.1692  -0.0030 335 LEU F N   
17435 C CA  . LEU F 335 ? 0.4138 0.3664 0.6767 0.0352  0.1508  0.0057  335 LEU F CA  
17436 C C   . LEU F 335 ? 0.5002 0.4352 0.7072 0.0464  0.1576  0.0016  335 LEU F C   
17437 O O   . LEU F 335 ? 0.5260 0.5006 0.7207 0.0575  0.1791  -0.0108 335 LEU F O   
17438 C CB  . LEU F 335 ? 0.4193 0.3446 0.6757 0.0063  0.1476  0.0289  335 LEU F CB  
17439 C CG  . LEU F 335 ? 0.4214 0.3596 0.7225 -0.0022 0.1362  0.0286  335 LEU F CG  
17440 C CD1 . LEU F 335 ? 0.4435 0.3501 0.7378 -0.0258 0.1279  0.0436  335 LEU F CD1 
17441 C CD2 . LEU F 335 ? 0.4100 0.3369 0.7239 0.0200  0.1152  0.0186  335 LEU F CD2 
17442 N N   . ASP F 336 ? 0.5742 0.4505 0.7475 0.0459  0.1379  0.0108  336 ASP F N   
17443 C CA  . ASP F 336 ? 0.6777 0.5214 0.7951 0.0588  0.1312  0.0061  336 ASP F CA  
17444 C C   . ASP F 336 ? 0.6953 0.5728 0.7661 0.0536  0.1617  0.0093  336 ASP F C   
17445 O O   . ASP F 336 ? 0.6803 0.5787 0.7514 0.0251  0.1831  0.0346  336 ASP F O   
17446 C CB  . ASP F 336 ? 0.7675 0.5472 0.8646 0.0458  0.1101  0.0269  336 ASP F CB  
17447 C CG  . ASP F 336 ? 0.8726 0.6070 0.9184 0.0612  0.0909  0.0216  336 ASP F CG  
17448 O OD1 . ASP F 336 ? 0.8800 0.5865 0.9428 0.0842  0.0625  0.0077  336 ASP F OD1 
17449 O OD2 . ASP F 336 ? 0.9479 0.6730 0.9392 0.0494  0.1003  0.0340  336 ASP F OD2 
17450 N N   . LYS F 337 ? 0.7419 0.6279 0.7772 0.0833  0.1622  -0.0168 337 LYS F N   
17451 C CA  . LYS F 337 ? 0.8704 0.7896 0.8439 0.0884  0.1915  -0.0179 337 LYS F CA  
17452 C C   . LYS F 337 ? 0.8654 0.8675 0.8736 0.0784  0.2351  -0.0120 337 LYS F C   
17453 O O   . LYS F 337 ? 0.8899 0.9331 0.8563 0.0727  0.2695  0.0022  337 LYS F O   
17454 C CB  . LYS F 337 ? 0.9818 0.8618 0.8950 0.0627  0.1905  0.0172  337 LYS F CB  
17455 C CG  . LYS F 337 ? 1.0823 0.8896 0.9390 0.0792  0.1526  0.0083  337 LYS F CG  
17456 C CD  . LYS F 337 ? 1.1706 0.9742 1.0108 0.1241  0.1338  -0.0380 337 LYS F CD  
17457 C CE  . LYS F 337 ? 1.2680 0.9931 1.0617 0.1384  0.0878  -0.0447 337 LYS F CE  
17458 N NZ  . LYS F 337 ? 1.3021 1.0075 1.1129 0.1803  0.0521  -0.0897 337 LYS F NZ  
17459 N N   . ASN F 338 ? 0.8284 0.8567 0.9153 0.0769  0.2323  -0.0204 338 ASN F N   
17460 C CA  . ASN F 338 ? 0.8116 0.9133 0.9555 0.0625  0.2652  -0.0111 338 ASN F CA  
17461 C C   . ASN F 338 ? 0.8246 0.9395 0.9690 0.0206  0.2863  0.0347  338 ASN F C   
17462 O O   . ASN F 338 ? 0.8414 1.0221 1.0303 0.0065  0.3172  0.0496  338 ASN F O   
17463 C CB  . ASN F 338 ? 0.8466 1.0173 0.9862 0.0933  0.2973  -0.0392 338 ASN F CB  
17464 C CG  . ASN F 338 ? 0.8353 0.9903 0.9827 0.1370  0.2700  -0.0880 338 ASN F CG  
17465 O OD1 . ASN F 338 ? 0.7847 0.9159 0.9887 0.1403  0.2379  -0.0975 338 ASN F OD1 
17466 N ND2 . ASN F 338 ? 0.8810 1.0515 0.9730 0.1720  0.2810  -0.1189 338 ASN F ND2 
17467 N N   . ASP F 339 ? 0.8164 0.8682 0.9256 0.0000  0.2653  0.0582  339 ASP F N   
17468 C CA  . ASP F 339 ? 0.8393 0.8931 0.9548 -0.0400 0.2756  0.1023  339 ASP F CA  
17469 C C   . ASP F 339 ? 0.7627 0.8195 0.9576 -0.0650 0.2625  0.1128  339 ASP F C   
17470 O O   . ASP F 339 ? 0.8150 0.8922 1.0419 -0.0971 0.2724  0.1465  339 ASP F O   
17471 C CB  . ASP F 339 ? 0.9236 0.9053 0.9784 -0.0511 0.2526  0.1210  339 ASP F CB  
17472 C CG  . ASP F 339 ? 1.0587 1.0399 1.0263 -0.0339 0.2654  0.1204  339 ASP F CG  
17473 O OD1 . ASP F 339 ? 1.1449 1.1928 1.0963 -0.0207 0.3020  0.1156  339 ASP F OD1 
17474 O OD2 . ASP F 339 ? 1.0828 0.9987 0.9975 -0.0311 0.2383  0.1230  339 ASP F OD2 
17475 N N   . ALA F 340 ? 0.6551 0.6925 0.8833 -0.0502 0.2377  0.0861  340 ALA F N   
17476 C CA  . ALA F 340 ? 0.5718 0.6018 0.8590 -0.0704 0.2187  0.0924  340 ALA F CA  
17477 C C   . ALA F 340 ? 0.4692 0.5271 0.8075 -0.0527 0.2098  0.0658  340 ALA F C   
17478 O O   . ALA F 340 ? 0.4540 0.5176 0.7818 -0.0234 0.2086  0.0413  340 ALA F O   
17479 C CB  . ALA F 340 ? 0.5703 0.5262 0.8334 -0.0774 0.1869  0.0963  340 ALA F CB  
17480 N N   . VAL F 341 ? 0.4247 0.4944 0.8201 -0.0702 0.1969  0.0707  341 VAL F N   
17481 C CA  . VAL F 341 ? 0.3922 0.4895 0.8383 -0.0566 0.1846  0.0497  341 VAL F CA  
17482 C C   . VAL F 341 ? 0.3821 0.4405 0.8413 -0.0659 0.1493  0.0474  341 VAL F C   
17483 O O   . VAL F 341 ? 0.3816 0.4241 0.8554 -0.0908 0.1394  0.0625  341 VAL F O   
17484 C CB  . VAL F 341 ? 0.3750 0.5454 0.8904 -0.0654 0.2062  0.0550  341 VAL F CB  
17485 C CG1 . VAL F 341 ? 0.3510 0.5384 0.9250 -0.0571 0.1821  0.0369  341 VAL F CG1 
17486 C CG2 . VAL F 341 ? 0.3914 0.6109 0.8934 -0.0457 0.2434  0.0476  341 VAL F CG2 
17487 N N   . TRP F 342 ? 0.3310 0.3743 0.7842 -0.0444 0.1287  0.0290  342 TRP F N   
17488 C CA  . TRP F 342 ? 0.3195 0.3376 0.7788 -0.0464 0.0975  0.0229  342 TRP F CA  
17489 C C   . TRP F 342 ? 0.3448 0.4022 0.8587 -0.0417 0.0837  0.0124  342 TRP F C   
17490 O O   . TRP F 342 ? 0.3382 0.4058 0.8554 -0.0206 0.0762  0.0024  342 TRP F O   
17491 C CB  . TRP F 342 ? 0.3252 0.3002 0.7347 -0.0266 0.0843  0.0176  342 TRP F CB  
17492 C CG  . TRP F 342 ? 0.3470 0.2904 0.7417 -0.0296 0.0597  0.0132  342 TRP F CG  
17493 C CD1 . TRP F 342 ? 0.4040 0.3527 0.8273 -0.0425 0.0397  0.0068  342 TRP F CD1 
17494 C CD2 . TRP F 342 ? 0.3970 0.2994 0.7462 -0.0173 0.0520  0.0123  342 TRP F CD2 
17495 N NE1 . TRP F 342 ? 0.4438 0.3554 0.8338 -0.0360 0.0184  -0.0032 342 TRP F NE1 
17496 C CE2 . TRP F 342 ? 0.4401 0.3269 0.7847 -0.0201 0.0293  0.0009  342 TRP F CE2 
17497 C CE3 . TRP F 342 ? 0.4353 0.3144 0.7523 -0.0028 0.0606  0.0195  342 TRP F CE3 
17498 C CZ2 . TRP F 342 ? 0.4660 0.3202 0.7696 -0.0059 0.0208  -0.0056 342 TRP F CZ2 
17499 C CZ3 . TRP F 342 ? 0.4550 0.3036 0.7416 0.0079  0.0527  0.0187  342 TRP F CZ3 
17500 C CH2 . TRP F 342 ? 0.4812 0.3202 0.7587 0.0075  0.0359  0.0053  342 TRP F CH2 
17501 N N   . ARG F 343 ? 0.3743 0.4511 0.9381 -0.0627 0.0754  0.0171  343 ARG F N   
17502 C CA  . ARG F 343 ? 0.4066 0.5202 1.0333 -0.0622 0.0582  0.0091  343 ARG F CA  
17503 C C   . ARG F 343 ? 0.3908 0.4720 0.9921 -0.0502 0.0189  -0.0044 343 ARG F C   
17504 O O   . ARG F 343 ? 0.4263 0.4652 0.9905 -0.0550 0.0009  -0.0072 343 ARG F O   
17505 C CB  . ARG F 343 ? 0.4837 0.6220 1.1766 -0.0913 0.0573  0.0228  343 ARG F CB  
17506 C CG  . ARG F 343 ? 0.5438 0.7268 1.2599 -0.1026 0.1023  0.0430  343 ARG F CG  
17507 C CD  . ARG F 343 ? 0.6711 0.8534 1.4125 -0.1329 0.0997  0.0686  343 ARG F CD  
17508 N NE  . ARG F 343 ? 0.7346 0.9423 1.4526 -0.1410 0.1408  0.0929  343 ARG F NE  
17509 C CZ  . ARG F 343 ? 0.7920 1.0618 1.5262 -0.1332 0.1780  0.0984  343 ARG F CZ  
17510 N NH1 . ARG F 343 ? 0.8208 1.1121 1.5224 -0.1407 0.2134  0.1211  343 ARG F NH1 
17511 N NH2 . ARG F 343 ? 0.8099 1.1204 1.5890 -0.1165 0.1780  0.0804  343 ARG F NH2 
17512 N N   . ILE F 344 ? 0.3507 0.4521 0.9700 -0.0330 0.0046  -0.0126 344 ILE F N   
17513 C CA  . ILE F 344 ? 0.3393 0.4163 0.9283 -0.0213 -0.0323 -0.0204 344 ILE F CA  
17514 C C   . ILE F 344 ? 0.4046 0.5032 1.0503 -0.0266 -0.0670 -0.0277 344 ILE F C   
17515 O O   . ILE F 344 ? 0.3192 0.4589 1.0277 -0.0240 -0.0662 -0.0276 344 ILE F O   
17516 C CB  . ILE F 344 ? 0.3174 0.3915 0.8738 0.0031  -0.0323 -0.0169 344 ILE F CB  
17517 C CG1 . ILE F 344 ? 0.3034 0.3547 0.8131 0.0100  -0.0042 -0.0094 344 ILE F CG1 
17518 C CG2 . ILE F 344 ? 0.3326 0.3853 0.8448 0.0147  -0.0650 -0.0178 344 ILE F CG2 
17519 C CD1 . ILE F 344 ? 0.3099 0.3607 0.8073 0.0319  -0.0079 -0.0017 344 ILE F CD1 
17520 N N   . SER F 345 ? 0.4916 0.5601 1.1165 -0.0320 -0.1011 -0.0370 345 SER F N   
17521 C CA  . SER F 345 ? 0.5417 0.6194 1.2144 -0.0375 -0.1447 -0.0464 345 SER F CA  
17522 C C   . SER F 345 ? 0.5352 0.6201 1.1921 -0.0176 -0.1719 -0.0483 345 SER F C   
17523 O O   . SER F 345 ? 0.5198 0.5874 1.1048 0.0012  -0.1689 -0.0440 345 SER F O   
17524 C CB  . SER F 345 ? 0.6284 0.6635 1.2743 -0.0444 -0.1806 -0.0616 345 SER F CB  
17525 O OG  . SER F 345 ? 0.7061 0.7404 1.3758 -0.0418 -0.2322 -0.0744 345 SER F OG  
17526 N N   . SER F 346 ? 0.5568 0.6691 1.2879 -0.0232 -0.2003 -0.0507 346 SER F N   
17527 C CA  . SER F 346 ? 0.5810 0.7006 1.3091 -0.0076 -0.2340 -0.0492 346 SER F CA  
17528 C C   . SER F 346 ? 0.6145 0.6944 1.2595 0.0038  -0.2776 -0.0588 346 SER F C   
17529 O O   . SER F 346 ? 0.6048 0.6859 1.2201 0.0188  -0.3039 -0.0518 346 SER F O   
17530 C CB  . SER F 346 ? 0.6234 0.7814 1.4621 -0.0176 -0.2563 -0.0506 346 SER F CB  
17531 O OG  . SER F 346 ? 0.7053 0.8463 1.5695 -0.0319 -0.2978 -0.0622 346 SER F OG  
17532 N N   . GLU F 347 ? 0.6698 0.7149 1.2739 -0.0013 -0.2859 -0.0746 347 GLU F N   
17533 C CA  . GLU F 347 ? 0.7724 0.7808 1.2859 0.0160  -0.3246 -0.0907 347 GLU F CA  
17534 C C   . GLU F 347 ? 0.7681 0.7655 1.1860 0.0359  -0.2900 -0.0809 347 GLU F C   
17535 O O   . GLU F 347 ? 0.8331 0.8157 1.1640 0.0575  -0.3074 -0.0845 347 GLU F O   
17536 C CB  . GLU F 347 ? 0.8414 0.8125 1.3512 0.0073  -0.3526 -0.1179 347 GLU F CB  
17537 C CG  . GLU F 347 ? 0.9106 0.8877 1.5287 -0.0171 -0.3885 -0.1253 347 GLU F CG  
17538 C CD  . GLU F 347 ? 1.0689 0.9975 1.6695 -0.0193 -0.4324 -0.1552 347 GLU F CD  
17539 O OE1 . GLU F 347 ? 1.1558 1.0482 1.6493 0.0056  -0.4470 -0.1777 347 GLU F OE1 
17540 O OE2 . GLU F 347 ? 1.1083 1.0367 1.8059 -0.0446 -0.4523 -0.1559 347 GLU F OE2 
17541 N N   . ASN F 348 ? 0.7116 0.7204 1.1480 0.0298  -0.2402 -0.0660 348 ASN F N   
17542 C CA  . ASN F 348 ? 0.7203 0.7211 1.0857 0.0463  -0.2062 -0.0524 348 ASN F CA  
17543 C C   . ASN F 348 ? 0.6563 0.6846 1.0286 0.0573  -0.1972 -0.0242 348 ASN F C   
17544 O O   . ASN F 348 ? 0.6962 0.7232 1.0046 0.0757  -0.1995 -0.0090 348 ASN F O   
17545 C CB  . ASN F 348 ? 0.7459 0.7359 1.1252 0.0340  -0.1654 -0.0522 348 ASN F CB  
17546 C CG  . ASN F 348 ? 0.7772 0.7545 1.0937 0.0494  -0.1329 -0.0395 348 ASN F CG  
17547 O OD1 . ASN F 348 ? 0.7844 0.7735 1.0690 0.0663  -0.1291 -0.0206 348 ASN F OD1 
17548 N ND2 . ASN F 348 ? 0.7950 0.7480 1.1006 0.0422  -0.1117 -0.0465 348 ASN F ND2 
17549 N N   . PHE F 349 ? 0.5666 0.6228 1.0207 0.0477  -0.1895 -0.0162 349 PHE F N   
17550 C CA  . PHE F 349 ? 0.5239 0.6001 0.9932 0.0592  -0.1833 0.0086  349 PHE F CA  
17551 C C   . PHE F 349 ? 0.5507 0.6444 1.0447 0.0647  -0.2258 0.0190  349 PHE F C   
17552 O O   . PHE F 349 ? 0.5127 0.6186 1.0139 0.0749  -0.2302 0.0443  349 PHE F O   
17553 C CB  . PHE F 349 ? 0.4513 0.5459 0.9884 0.0532  -0.1520 0.0085  349 PHE F CB  
17554 C CG  . PHE F 349 ? 0.4514 0.5746 1.0763 0.0406  -0.1582 -0.0064 349 PHE F CG  
17555 C CD1 . PHE F 349 ? 0.4717 0.6209 1.1594 0.0445  -0.1881 -0.0038 349 PHE F CD1 
17556 C CD2 . PHE F 349 ? 0.4547 0.5825 1.1062 0.0247  -0.1331 -0.0193 349 PHE F CD2 
17557 C CE1 . PHE F 349 ? 0.4739 0.6522 1.2457 0.0339  -0.1889 -0.0172 349 PHE F CE1 
17558 C CE2 . PHE F 349 ? 0.4446 0.6081 1.1837 0.0132  -0.1328 -0.0277 349 PHE F CE2 
17559 C CZ  . PHE F 349 ? 0.4594 0.6504 1.2623 0.0189  -0.1598 -0.0283 349 PHE F CZ  
17560 N N   . MET F 350 ? 0.4981 0.7235 0.9660 0.0775  -0.2099 0.0180  350 MET F N   
17561 C CA  . MET F 350 ? 0.5819 0.8166 1.0425 0.0892  -0.2386 0.0273  350 MET F CA  
17562 C C   . MET F 350 ? 0.6705 0.8772 1.0764 0.0831  -0.2698 0.0227  350 MET F C   
17563 O O   . MET F 350 ? 0.7088 0.9134 1.1078 0.0629  -0.2854 0.0098  350 MET F O   
17564 C CB  . MET F 350 ? 0.5925 0.8761 1.1087 0.0851  -0.2506 0.0297  350 MET F CB  
17565 C CG  . MET F 350 ? 0.5584 0.8674 1.1212 0.0982  -0.2207 0.0383  350 MET F CG  
17566 S SD  . MET F 350 ? 0.4846 0.7699 1.0207 0.1312  -0.2042 0.0524  350 MET F SD  
17567 C CE  . MET F 350 ? 0.4086 0.7046 0.9280 0.1455  -0.2434 0.0639  350 MET F CE  
17568 N N   . VAL F 351 ? 0.7060 0.8854 1.0665 0.1021  -0.2776 0.0339  351 VAL F N   
17569 C CA  . VAL F 351 ? 0.7458 0.8873 1.0375 0.1029  -0.3018 0.0332  351 VAL F CA  
17570 C C   . VAL F 351 ? 0.7766 0.9308 1.0561 0.1140  -0.3327 0.0403  351 VAL F C   
17571 O O   . VAL F 351 ? 0.7888 0.9667 1.0979 0.1307  -0.3283 0.0529  351 VAL F O   
17572 C CB  . VAL F 351 ? 0.6097 0.7041 0.8518 0.1174  -0.2820 0.0442  351 VAL F CB  
17573 C CG1 . VAL F 351 ? 0.6965 0.7439 0.8531 0.1165  -0.2902 0.0449  351 VAL F CG1 
17574 C CG2 . VAL F 351 ? 0.5231 0.6130 0.7809 0.1050  -0.2420 0.0375  351 VAL F CG2 
17575 N N   . GLN F 352 ? 0.8044 0.9423 1.0378 0.1059  -0.3638 0.0320  352 GLN F N   
17576 C CA  . GLN F 352 ? 0.8773 1.0286 1.0958 0.1163  -0.3953 0.0376  352 GLN F CA  
17577 C C   . GLN F 352 ? 0.9551 1.0553 1.0907 0.1401  -0.3968 0.0515  352 GLN F C   
17578 O O   . GLN F 352 ? 1.0749 1.1463 1.1446 0.1421  -0.4215 0.0478  352 GLN F O   
17579 C CB  . GLN F 352 ? 0.9184 1.0804 1.1333 0.0933  -0.4293 0.0195  352 GLN F CB  
17580 C CG  . GLN F 352 ? 0.9212 1.1501 1.2187 0.0836  -0.4429 0.0186  352 GLN F CG  
17581 C CD  . GLN F 352 ? 0.9859 1.2427 1.2849 0.1066  -0.4658 0.0344  352 GLN F CD  
17582 O OE1 . GLN F 352 ? 1.0322 1.2767 1.2820 0.1088  -0.5003 0.0312  352 GLN F OE1 
17583 N NE2 . GLN F 352 ? 0.9946 1.2872 1.3463 0.1255  -0.4457 0.0517  352 GLN F NE2 
17584 N N   . ALA F 353 ? 0.9028 0.9886 1.0408 0.1578  -0.3672 0.0675  353 ALA F N   
17585 C CA  . ALA F 353 ? 0.9186 0.9545 0.9883 0.1809  -0.3569 0.0856  353 ALA F CA  
17586 C C   . ALA F 353 ? 0.9507 0.9715 0.9610 0.1951  -0.3848 0.0920  353 ALA F C   
17587 O O   . ALA F 353 ? 1.0013 0.9695 0.9314 0.2035  -0.3815 0.0972  353 ALA F O   
17588 C CB  . ALA F 353 ? 0.9062 0.9468 1.0096 0.1989  -0.3305 0.1030  353 ALA F CB  
17589 N N   . GLN F 354 ? 0.9313 0.9988 0.9799 0.1990  -0.4101 0.0930  354 GLN F N   
17590 C CA  . GLN F 354 ? 0.9776 1.0352 0.9729 0.2139  -0.4387 0.0997  354 GLN F CA  
17591 C C   . GLN F 354 ? 1.0211 1.1305 1.0554 0.1986  -0.4778 0.0853  354 GLN F C   
17592 O O   . GLN F 354 ? 0.9786 1.1371 1.0914 0.1800  -0.4776 0.0754  354 GLN F O   
17593 C CB  . GLN F 354 ? 0.9682 1.0226 0.9592 0.2451  -0.4264 0.1274  354 GLN F CB  
17594 C CG  . GLN F 354 ? 1.0146 1.0021 0.9135 0.2635  -0.4143 0.1416  354 GLN F CG  
17595 C CD  . GLN F 354 ? 1.0016 0.9700 0.9016 0.2883  -0.3856 0.1692  354 GLN F CD  
17596 O OE1 . GLN F 354 ? 0.9685 0.9737 0.9304 0.2974  -0.3810 0.1795  354 GLN F OE1 
17597 N NE2 . GLN F 354 ? 1.0331 0.9405 0.8644 0.2991  -0.3629 0.1820  354 GLN F NE2 
17598 N N   . ASP F 355 ? 1.1189 1.2132 1.0945 0.2060  -0.5094 0.0843  355 ASP F N   
17599 C CA  . ASP F 355 ? 1.1447 1.2875 1.1500 0.1954  -0.5520 0.0744  355 ASP F CA  
17600 C C   . ASP F 355 ? 1.0452 1.2639 1.1417 0.2045  -0.5559 0.0894  355 ASP F C   
17601 O O   . ASP F 355 ? 1.0847 1.3199 1.1726 0.2300  -0.5689 0.1092  355 ASP F O   
17602 C CB  . ASP F 355 ? 1.2879 1.3952 1.2039 0.2109  -0.5819 0.0763  355 ASP F CB  
17603 C CG  . ASP F 355 ? 1.3647 1.3963 1.1850 0.2026  -0.5794 0.0595  355 ASP F CG  
17604 O OD1 . ASP F 355 ? 1.3294 1.3226 1.1323 0.1989  -0.5440 0.0588  355 ASP F OD1 
17605 O OD2 . ASP F 355 ? 1.4610 1.4706 1.2206 0.2016  -0.6122 0.0480  355 ASP F OD2 
17606 N N   . GLY F 356 ? 0.9377 1.1995 1.1185 0.1863  -0.5404 0.0823  356 GLY F N   
17607 C CA  . GLY F 356 ? 0.9224 1.2564 1.1916 0.1953  -0.5381 0.0957  356 GLY F CA  
17608 C C   . GLY F 356 ? 0.8914 1.2202 1.1892 0.2141  -0.4929 0.1119  356 GLY F C   
17609 O O   . GLY F 356 ? 0.9189 1.2906 1.2664 0.2355  -0.4840 0.1299  356 GLY F O   
17610 N N   . VAL F 357 ? 0.8384 1.1133 1.1028 0.2066  -0.4642 0.1047  357 VAL F N   
17611 C CA  . VAL F 357 ? 0.7700 1.0322 1.0580 0.2179  -0.4211 0.1142  357 VAL F CA  
17612 C C   . VAL F 357 ? 0.6849 0.9393 0.9980 0.1902  -0.4004 0.0947  357 VAL F C   
17613 O O   . VAL F 357 ? 0.6607 0.8767 0.9284 0.1731  -0.4048 0.0808  357 VAL F O   
17614 C CB  . VAL F 357 ? 0.8097 1.0094 1.0296 0.2399  -0.4023 0.1298  357 VAL F CB  
17615 C CG1 . VAL F 357 ? 0.7748 0.9577 1.0195 0.2472  -0.3598 0.1358  357 VAL F CG1 
17616 C CG2 . VAL F 357 ? 0.8638 1.0676 1.0583 0.2690  -0.4185 0.1528  357 VAL F CG2 
17617 N N   . SER F 358 ? 0.6364 0.9252 1.0173 0.1877  -0.3766 0.0945  358 SER F N   
17618 C CA  . SER F 358 ? 0.6016 0.8829 1.0052 0.1636  -0.3541 0.0785  358 SER F CA  
17619 C C   . SER F 358 ? 0.5881 0.8450 0.9953 0.1773  -0.3130 0.0855  358 SER F C   
17620 O O   . SER F 358 ? 0.5925 0.8722 1.0366 0.1952  -0.2964 0.0959  358 SER F O   
17621 C CB  . SER F 358 ? 0.5830 0.9201 1.0588 0.1447  -0.3589 0.0700  358 SER F CB  
17622 O OG  . SER F 358 ? 0.5570 0.8849 1.0520 0.1234  -0.3341 0.0568  358 SER F OG  
17623 N N   . CYS F 359 ? 0.5927 0.8025 0.9604 0.1692  -0.2969 0.0790  359 CYS F N   
17624 C CA  . CYS F 359 ? 0.5621 0.7391 0.9211 0.1809  -0.2626 0.0847  359 CYS F CA  
17625 C C   . CYS F 359 ? 0.4786 0.6538 0.8626 0.1649  -0.2344 0.0719  359 CYS F C   
17626 O O   . CYS F 359 ? 0.4057 0.5860 0.7938 0.1430  -0.2376 0.0586  359 CYS F O   
17627 C CB  . CYS F 359 ? 0.5964 0.7168 0.8882 0.1882  -0.2622 0.0920  359 CYS F CB  
17628 S SG  . CYS F 359 ? 0.8476 0.9512 1.0963 0.2171  -0.2793 0.1141  359 CYS F SG  
17629 N N   . LEU F 360 ? 0.4735 0.6374 0.8686 0.1781  -0.2063 0.0763  360 LEU F N   
17630 C CA  . LEU F 360 ? 0.4444 0.5979 0.8502 0.1676  -0.1777 0.0654  360 LEU F CA  
17631 C C   . LEU F 360 ? 0.4709 0.5811 0.8333 0.1582  -0.1739 0.0616  360 LEU F C   
17632 O O   . LEU F 360 ? 0.5247 0.5970 0.8544 0.1695  -0.1710 0.0710  360 LEU F O   
17633 C CB  . LEU F 360 ? 0.4391 0.5844 0.8571 0.1868  -0.1520 0.0701  360 LEU F CB  
17634 C CG  . LEU F 360 ? 0.3931 0.5235 0.8123 0.1783  -0.1235 0.0580  360 LEU F CG  
17635 C CD1 . LEU F 360 ? 0.3299 0.4985 0.7839 0.1623  -0.1189 0.0492  360 LEU F CD1 
17636 C CD2 . LEU F 360 ? 0.3810 0.4918 0.7981 0.1998  -0.1014 0.0614  360 LEU F CD2 
17637 N N   . GLY F 361 ? 0.4711 0.5865 0.8342 0.1383  -0.1729 0.0497  361 GLY F N   
17638 C CA  . GLY F 361 ? 0.4684 0.5507 0.7928 0.1298  -0.1727 0.0482  361 GLY F CA  
17639 C C   . GLY F 361 ? 0.4338 0.4900 0.7449 0.1252  -0.1432 0.0443  361 GLY F C   
17640 O O   . GLY F 361 ? 0.4293 0.4806 0.7237 0.1091  -0.1299 0.0362  361 GLY F O   
17641 N N   . PHE F 362 ? 0.4490 0.4873 0.7666 0.1399  -0.1338 0.0499  362 PHE F N   
17642 C CA  . PHE F 362 ? 0.4315 0.4388 0.7313 0.1339  -0.1120 0.0451  362 PHE F CA  
17643 C C   . PHE F 362 ? 0.5201 0.4850 0.7908 0.1418  -0.1122 0.0580  362 PHE F C   
17644 O O   . PHE F 362 ? 0.5662 0.5246 0.8434 0.1619  -0.1206 0.0688  362 PHE F O   
17645 C CB  . PHE F 362 ? 0.3840 0.3984 0.7122 0.1419  -0.0955 0.0358  362 PHE F CB  
17646 C CG  . PHE F 362 ? 0.3463 0.3975 0.6966 0.1329  -0.0874 0.0252  362 PHE F CG  
17647 C CD1 . PHE F 362 ? 0.3382 0.4262 0.7147 0.1332  -0.0958 0.0274  362 PHE F CD1 
17648 C CD2 . PHE F 362 ? 0.3419 0.3893 0.6868 0.1239  -0.0710 0.0139  362 PHE F CD2 
17649 C CE1 . PHE F 362 ? 0.2619 0.3772 0.6596 0.1234  -0.0855 0.0195  362 PHE F CE1 
17650 C CE2 . PHE F 362 ? 0.3063 0.3816 0.6656 0.1170  -0.0597 0.0066  362 PHE F CE2 
17651 C CZ  . PHE F 362 ? 0.2872 0.3939 0.6735 0.1162  -0.0658 0.0099  362 PHE F CZ  
17652 N N   . VAL F 363 ? 0.5411 0.4777 0.7841 0.1267  -0.1011 0.0583  363 VAL F N   
17653 C CA  . VAL F 363 ? 0.5488 0.4430 0.7654 0.1298  -0.0984 0.0728  363 VAL F CA  
17654 C C   . VAL F 363 ? 0.5077 0.3689 0.7247 0.1213  -0.0833 0.0660  363 VAL F C   
17655 O O   . VAL F 363 ? 0.4642 0.3361 0.6899 0.1081  -0.0762 0.0509  363 VAL F O   
17656 C CB  . VAL F 363 ? 0.5539 0.4410 0.7384 0.1187  -0.0987 0.0840  363 VAL F CB  
17657 C CG1 . VAL F 363 ? 0.6443 0.4867 0.8041 0.1235  -0.0920 0.1030  363 VAL F CG1 
17658 C CG2 . VAL F 363 ? 0.5350 0.4462 0.7094 0.1270  -0.1171 0.0868  363 VAL F CG2 
17659 N N   . ASP F 364 ? 0.5394 0.3574 0.7441 0.1297  -0.0796 0.0766  364 ASP F N   
17660 C CA  . ASP F 364 ? 0.5650 0.3414 0.7663 0.1206  -0.0685 0.0690  364 ASP F CA  
17661 C C   . ASP F 364 ? 0.5819 0.3478 0.7755 0.0927  -0.0625 0.0717  364 ASP F C   
17662 O O   . ASP F 364 ? 0.6248 0.3770 0.8054 0.0895  -0.0594 0.0908  364 ASP F O   
17663 C CB  . ASP F 364 ? 0.6467 0.3754 0.8366 0.1403  -0.0650 0.0812  364 ASP F CB  
17664 C CG  . ASP F 364 ? 0.7105 0.3888 0.8940 0.1350  -0.0548 0.0689  364 ASP F CG  
17665 O OD1 . ASP F 364 ? 0.7172 0.3949 0.9025 0.1113  -0.0533 0.0524  364 ASP F OD1 
17666 O OD2 . ASP F 364 ? 0.7698 0.4069 0.9436 0.1561  -0.0492 0.0755  364 ASP F OD2 
17667 N N   . GLY F 365 ? 0.5201 0.2938 0.7224 0.0740  -0.0602 0.0546  365 GLY F N   
17668 C CA  . GLY F 365 ? 0.5248 0.2970 0.7297 0.0473  -0.0561 0.0592  365 GLY F CA  
17669 C C   . GLY F 365 ? 0.5706 0.2915 0.7746 0.0325  -0.0520 0.0623  365 GLY F C   
17670 O O   . GLY F 365 ? 0.6118 0.3334 0.8274 0.0081  -0.0488 0.0689  365 GLY F O   
17671 N N   . GLY F 366 ? 0.5898 0.2651 0.7825 0.0471  -0.0509 0.0591  366 GLY F N   
17672 C CA  . GLY F 366 ? 0.6704 0.2861 0.8588 0.0324  -0.0464 0.0598  366 GLY F CA  
17673 C C   . GLY F 366 ? 0.7242 0.3250 0.9129 0.0146  -0.0540 0.0322  366 GLY F C   
17674 O O   . GLY F 366 ? 0.6857 0.3213 0.8748 0.0193  -0.0601 0.0148  366 GLY F O   
17675 N N   . VAL F 367 ? 0.8408 0.3876 1.0273 -0.0066 -0.0542 0.0280  367 VAL F N   
17676 C CA  . VAL F 367 ? 0.9125 0.4312 1.0879 -0.0209 -0.0654 -0.0015 367 VAL F CA  
17677 C C   . VAL F 367 ? 0.9257 0.4813 1.1253 -0.0560 -0.0788 -0.0098 367 VAL F C   
17678 O O   . VAL F 367 ? 0.9610 0.5085 1.1487 -0.0658 -0.0929 -0.0358 367 VAL F O   
17679 C CB  . VAL F 367 ? 0.8975 0.3270 1.0514 -0.0262 -0.0620 -0.0076 367 VAL F CB  
17680 C CG1 . VAL F 367 ? 0.9170 0.3135 1.0431 0.0141  -0.0480 -0.0013 367 VAL F CG1 
17681 C CG2 . VAL F 367 ? 0.9238 0.3348 1.0960 -0.0534 -0.0547 0.0133  367 VAL F CG2 
17682 N N   . HIS F 368 ? 0.9006 0.4965 1.1318 -0.0722 -0.0741 0.0134  368 HIS F N   
17683 C CA  . HIS F 368 ? 0.8579 0.5006 1.1197 -0.1017 -0.0852 0.0107  368 HIS F CA  
17684 C C   . HIS F 368 ? 0.7756 0.4904 1.0487 -0.0896 -0.0789 0.0239  368 HIS F C   
17685 O O   . HIS F 368 ? 0.7658 0.5198 1.0688 -0.1056 -0.0742 0.0426  368 HIS F O   
17686 C CB  . HIS F 368 ? 0.8831 0.5070 1.1789 -0.1358 -0.0832 0.0271  368 HIS F CB  
17687 C CG  . HIS F 368 ? 0.9659 0.5136 1.2466 -0.1510 -0.0898 0.0111  368 HIS F CG  
17688 N ND1 . HIS F 368 ? 1.0215 0.5142 1.2827 -0.1421 -0.0713 0.0251  368 HIS F ND1 
17689 C CD2 . HIS F 368 ? 1.0048 0.5274 1.2679 -0.1683 -0.1087 -0.0195 368 HIS F CD2 
17690 C CE1 . HIS F 368 ? 1.0916 0.5264 1.3274 -0.1557 -0.0766 0.0045  368 HIS F CE1 
17691 N NE2 . HIS F 368 ? 1.0864 0.5375 1.3217 -0.1719 -0.0997 -0.0235 368 HIS F NE2 
17692 N N   . ALA F 369 ? 0.7244 0.4527 0.9736 -0.0599 -0.0764 0.0154  369 ALA F N   
17693 C CA  . ALA F 369 ? 0.6409 0.4284 0.8940 -0.0475 -0.0713 0.0227  369 ALA F CA  
17694 C C   . ALA F 369 ? 0.6462 0.4739 0.9122 -0.0629 -0.0811 0.0104  369 ALA F C   
17695 O O   . ALA F 369 ? 0.6750 0.4841 0.9337 -0.0724 -0.0952 -0.0119 369 ALA F O   
17696 C CB  . ALA F 369 ? 0.5782 0.3690 0.8101 -0.0164 -0.0684 0.0146  369 ALA F CB  
17697 N N   . ARG F 370 ? 0.6045 0.4840 0.8837 -0.0624 -0.0736 0.0248  370 ARG F N   
17698 C CA  . ARG F 370 ? 0.5958 0.5213 0.8907 -0.0741 -0.0800 0.0202  370 ARG F CA  
17699 C C   . ARG F 370 ? 0.5346 0.4660 0.8056 -0.0597 -0.0883 -0.0060 370 ARG F C   
17700 O O   . ARG F 370 ? 0.5409 0.4810 0.8127 -0.0705 -0.1030 -0.0212 370 ARG F O   
17701 C CB  . ARG F 370 ? 0.6177 0.5894 0.9230 -0.0684 -0.0641 0.0437  370 ARG F CB  
17702 C CG  . ARG F 370 ? 0.6402 0.6623 0.9532 -0.0686 -0.0660 0.0398  370 ARG F CG  
17703 C CD  . ARG F 370 ? 0.7253 0.7633 1.0711 -0.0952 -0.0813 0.0390  370 ARG F CD  
17704 N NE  . ARG F 370 ? 0.7521 0.8384 1.1043 -0.0939 -0.0882 0.0335  370 ARG F NE  
17705 C CZ  . ARG F 370 ? 0.7977 0.8803 1.1305 -0.0909 -0.1061 0.0075  370 ARG F CZ  
17706 N NH1 . ARG F 370 ? 0.8636 0.8946 1.1689 -0.0883 -0.1166 -0.0156 370 ARG F NH1 
17707 N NH2 . ARG F 370 ? 0.7739 0.9014 1.1100 -0.0868 -0.1117 0.0058  370 ARG F NH2 
17708 N N   . ALA F 371 ? 0.4662 0.3921 0.7163 -0.0346 -0.0790 -0.0104 371 ALA F N   
17709 C CA  . ALA F 371 ? 0.4320 0.3598 0.6605 -0.0172 -0.0801 -0.0312 371 ALA F CA  
17710 C C   . ALA F 371 ? 0.4545 0.3472 0.6667 0.0046  -0.0742 -0.0382 371 ALA F C   
17711 O O   . ALA F 371 ? 0.4638 0.3412 0.6817 0.0089  -0.0698 -0.0249 371 ALA F O   
17712 C CB  . ALA F 371 ? 0.3739 0.3504 0.6042 -0.0071 -0.0695 -0.0255 371 ALA F CB  
17713 N N   . GLY F 372 ? 0.4467 0.3277 0.6382 0.0212  -0.0729 -0.0567 372 GLY F N   
17714 C CA  . GLY F 372 ? 0.4719 0.3258 0.6539 0.0450  -0.0641 -0.0605 372 GLY F CA  
17715 C C   . GLY F 372 ? 0.4026 0.2893 0.6039 0.0591  -0.0531 -0.0460 372 GLY F C   
17716 O O   . GLY F 372 ? 0.4181 0.2906 0.6261 0.0714  -0.0507 -0.0385 372 GLY F O   
17717 N N   . ILE F 373 ? 0.3872 0.3169 0.5966 0.0572  -0.0477 -0.0423 373 ILE F N   
17718 C CA  . ILE F 373 ? 0.3349 0.2958 0.5605 0.0648  -0.0402 -0.0311 373 ILE F CA  
17719 C C   . ILE F 373 ? 0.3196 0.3076 0.5480 0.0493  -0.0403 -0.0192 373 ILE F C   
17720 O O   . ILE F 373 ? 0.3163 0.3196 0.5395 0.0413  -0.0388 -0.0222 373 ILE F O   
17721 C CB  . ILE F 373 ? 0.3033 0.2831 0.5324 0.0819  -0.0271 -0.0392 373 ILE F CB  
17722 C CG1 . ILE F 373 ? 0.3545 0.3058 0.5780 0.1016  -0.0218 -0.0489 373 ILE F CG1 
17723 C CG2 . ILE F 373 ? 0.2816 0.2911 0.5318 0.0848  -0.0224 -0.0294 373 ILE F CG2 
17724 C CD1 . ILE F 373 ? 0.3492 0.3149 0.5742 0.1202  -0.0039 -0.0553 373 ILE F CD1 
17725 N N   . ALA F 374 ? 0.3227 0.3147 0.5556 0.0474  -0.0418 -0.0049 374 ALA F N   
17726 C CA  . ALA F 374 ? 0.2794 0.2920 0.5078 0.0381  -0.0372 0.0071  374 ALA F CA  
17727 C C   . ALA F 374 ? 0.3043 0.3299 0.5311 0.0460  -0.0346 0.0107  374 ALA F C   
17728 O O   . ALA F 374 ? 0.3467 0.3612 0.5709 0.0498  -0.0426 0.0182  374 ALA F O   
17729 C CB  . ALA F 374 ? 0.2832 0.2803 0.5090 0.0264  -0.0404 0.0229  374 ALA F CB  
17730 N N   . LEU F 375 ? 0.2746 0.3214 0.5012 0.0483  -0.0246 0.0051  375 LEU F N   
17731 C CA  . LEU F 375 ? 0.2458 0.3018 0.4725 0.0517  -0.0231 0.0056  375 LEU F CA  
17732 C C   . LEU F 375 ? 0.2710 0.3222 0.4734 0.0458  -0.0214 0.0177  375 LEU F C   
17733 O O   . LEU F 375 ? 0.3154 0.3732 0.5061 0.0421  -0.0096 0.0232  375 LEU F O   
17734 C CB  . LEU F 375 ? 0.2260 0.2995 0.4602 0.0559  -0.0088 -0.0037 375 LEU F CB  
17735 C CG  . LEU F 375 ? 0.2260 0.3009 0.4755 0.0660  -0.0042 -0.0144 375 LEU F CG  
17736 C CD1 . LEU F 375 ? 0.2246 0.3135 0.4733 0.0720  0.0147  -0.0197 375 LEU F CD1 
17737 C CD2 . LEU F 375 ? 0.2157 0.2882 0.4898 0.0745  -0.0119 -0.0161 375 LEU F CD2 
17738 N N   . GLY F 376 ? 0.2621 0.3016 0.4540 0.0473  -0.0329 0.0225  376 GLY F N   
17739 C CA  . GLY F 376 ? 0.2739 0.2985 0.4314 0.0456  -0.0305 0.0351  376 GLY F CA  
17740 C C   . GLY F 376 ? 0.3089 0.3302 0.4458 0.0453  -0.0300 0.0301  376 GLY F C   
17741 O O   . GLY F 376 ? 0.3031 0.3386 0.4575 0.0433  -0.0258 0.0185  376 GLY F O   
17742 N N   . ALA F 377 ? 0.3454 0.3430 0.4415 0.0475  -0.0326 0.0392  377 ALA F N   
17743 C CA  . ALA F 377 ? 0.3601 0.3430 0.4242 0.0461  -0.0321 0.0332  377 ALA F CA  
17744 C C   . ALA F 377 ? 0.3820 0.3721 0.4670 0.0412  -0.0542 0.0176  377 ALA F C   
17745 O O   . ALA F 377 ? 0.4287 0.4173 0.5118 0.0343  -0.0512 0.0070  377 ALA F O   
17746 C CB  . ALA F 377 ? 0.4087 0.3568 0.4155 0.0531  -0.0316 0.0460  377 ALA F CB  
17747 N N   . HIS F 378 ? 0.3996 0.3971 0.5062 0.0447  -0.0762 0.0178  378 HIS F N   
17748 C CA  . HIS F 378 ? 0.3754 0.3879 0.5106 0.0405  -0.0994 0.0063  378 HIS F CA  
17749 C C   . HIS F 378 ? 0.3403 0.3829 0.5283 0.0348  -0.0867 -0.0035 378 HIS F C   
17750 O O   . HIS F 378 ? 0.3617 0.4163 0.5738 0.0259  -0.0950 -0.0133 378 HIS F O   
17751 C CB  A HIS F 378 ? 0.3694 0.3876 0.5196 0.0500  -0.1241 0.0122  378 HIS F CB  
17752 C CB  B HIS F 378 ? 0.3686 0.3869 0.5193 0.0504  -0.1229 0.0127  378 HIS F CB  
17753 C CG  A HIS F 378 ? 0.4167 0.4075 0.5162 0.0552  -0.1468 0.0170  378 HIS F CG  
17754 C CG  B HIS F 378 ? 0.3758 0.4061 0.5418 0.0482  -0.1548 0.0057  378 HIS F CG  
17755 N ND1 A HIS F 378 ? 0.4543 0.4525 0.5631 0.0634  -0.1775 0.0193  378 HIS F ND1 
17756 N ND1 B HIS F 378 ? 0.4388 0.4440 0.5555 0.0478  -0.1777 0.0045  378 HIS F ND1 
17757 C CD2 A HIS F 378 ? 0.4402 0.3939 0.4740 0.0564  -0.1427 0.0209  378 HIS F CD2 
17758 C CD2 B HIS F 378 ? 0.3547 0.4214 0.5815 0.0471  -0.1687 0.0005  378 HIS F CD2 
17759 C CE1 A HIS F 378 ? 0.5027 0.4682 0.5501 0.0690  -0.1936 0.0231  378 HIS F CE1 
17760 C CE1 B HIS F 378 ? 0.4504 0.4786 0.5991 0.0437  -0.2089 -0.0029 378 HIS F CE1 
17761 N NE2 A HIS F 378 ? 0.4835 0.4190 0.4825 0.0653  -0.1715 0.0240  378 HIS F NE2 
17762 N NE2 B HIS F 378 ? 0.3937 0.4628 0.6144 0.0431  -0.2028 -0.0039 378 HIS F NE2 
17763 N N   . HIS F 379 ? 0.3025 0.3558 0.5084 0.0399  -0.0673 -0.0005 379 HIS F N   
17764 C CA  . HIS F 379 ? 0.2619 0.3375 0.5062 0.0393  -0.0505 -0.0080 379 HIS F CA  
17765 C C   . HIS F 379 ? 0.3098 0.3796 0.5386 0.0316  -0.0321 -0.0130 379 HIS F C   
17766 O O   . HIS F 379 ? 0.3317 0.4149 0.5913 0.0270  -0.0247 -0.0200 379 HIS F O   
17767 C CB  . HIS F 379 ? 0.2714 0.3510 0.5224 0.0476  -0.0360 -0.0052 379 HIS F CB  
17768 C CG  . HIS F 379 ? 0.2457 0.3421 0.5242 0.0519  -0.0168 -0.0120 379 HIS F CG  
17769 N ND1 . HIS F 379 ? 0.2271 0.3390 0.5461 0.0601  -0.0171 -0.0151 379 HIS F ND1 
17770 C CD2 . HIS F 379 ? 0.2412 0.3396 0.5093 0.0525  0.0056  -0.0143 379 HIS F CD2 
17771 C CE1 . HIS F 379 ? 0.1799 0.2999 0.5095 0.0658  0.0055  -0.0192 379 HIS F CE1 
17772 N NE2 . HIS F 379 ? 0.2240 0.3360 0.5222 0.0612  0.0184  -0.0191 379 HIS F NE2 
17773 N N   . LEU F 380 ? 0.3225 0.3709 0.5045 0.0316  -0.0217 -0.0070 380 LEU F N   
17774 C CA  . LEU F 380 ? 0.3121 0.3492 0.4708 0.0288  0.0006  -0.0087 380 LEU F CA  
17775 C C   . LEU F 380 ? 0.3314 0.3468 0.4721 0.0180  -0.0079 -0.0171 380 LEU F C   
17776 O O   . LEU F 380 ? 0.3941 0.4002 0.5291 0.0138  0.0104  -0.0217 380 LEU F O   
17777 C CB  . LEU F 380 ? 0.2909 0.3147 0.4082 0.0354  0.0159  0.0036  380 LEU F CB  
17778 C CG  . LEU F 380 ? 0.2855 0.3303 0.4201 0.0420  0.0233  0.0110  380 LEU F CG  
17779 C CD1 . LEU F 380 ? 0.2480 0.2848 0.3515 0.0460  0.0340  0.0265  380 LEU F CD1 
17780 C CD2 . LEU F 380 ? 0.2654 0.3294 0.4215 0.0463  0.0410  0.0055  380 LEU F CD2 
17781 N N   . GLU F 381 ? 0.3552 0.3582 0.4819 0.0141  -0.0361 -0.0190 381 GLU F N   
17782 C CA  . GLU F 381 ? 0.4272 0.4029 0.5268 0.0025  -0.0509 -0.0292 381 GLU F CA  
17783 C C   . GLU F 381 ? 0.4071 0.3985 0.5556 -0.0129 -0.0530 -0.0420 381 GLU F C   
17784 O O   . GLU F 381 ? 0.3486 0.3786 0.5610 -0.0135 -0.0577 -0.0423 381 GLU F O   
17785 C CB  . GLU F 381 ? 0.4623 0.4269 0.5404 0.0038  -0.0861 -0.0289 381 GLU F CB  
17786 C CG  . GLU F 381 ? 0.5018 0.4350 0.5163 0.0173  -0.0793 -0.0159 381 GLU F CG  
17787 C CD  . GLU F 381 ? 0.5222 0.4485 0.5193 0.0249  -0.1092 -0.0104 381 GLU F CD  
17788 O OE1 . GLU F 381 ? 0.4947 0.4434 0.5296 0.0203  -0.1388 -0.0172 381 GLU F OE1 
17789 O OE2 . GLU F 381 ? 0.5596 0.4589 0.5060 0.0375  -0.1010 0.0032  381 GLU F OE2 
17790 N N   . GLU F 382 ? 0.4303 0.3881 0.5473 -0.0240 -0.0453 -0.0507 382 GLU F N   
17791 C CA  . GLU F 382 ? 0.4355 0.3977 0.5935 -0.0427 -0.0437 -0.0625 382 GLU F CA  
17792 C C   . GLU F 382 ? 0.3860 0.3801 0.5969 -0.0370 -0.0106 -0.0566 382 GLU F C   
17793 O O   . GLU F 382 ? 0.3576 0.3719 0.6264 -0.0492 -0.0082 -0.0614 382 GLU F O   
17794 C CB  . GLU F 382 ? 0.4197 0.4034 0.6222 -0.0587 -0.0855 -0.0718 382 GLU F CB  
17795 C CG  . GLU F 382 ? 0.4713 0.4183 0.6145 -0.0648 -0.1222 -0.0803 382 GLU F CG  
17796 C CD  . GLU F 382 ? 0.5351 0.4199 0.6087 -0.0744 -0.1125 -0.0912 382 GLU F CD  
17797 O OE1 . GLU F 382 ? 0.5444 0.4211 0.6411 -0.0897 -0.0940 -0.0987 382 GLU F OE1 
17798 O OE2 . GLU F 382 ? 0.5985 0.4380 0.5914 -0.0653 -0.1211 -0.0913 382 GLU F OE2 
17799 N N   . ASN F 383 ? 0.3689 0.3665 0.5584 -0.0179 0.0148  -0.0455 383 ASN F N   
17800 C CA  . ASN F 383 ? 0.3280 0.3429 0.5422 -0.0079 0.0491  -0.0400 383 ASN F CA  
17801 C C   . ASN F 383 ? 0.3569 0.3433 0.5146 0.0028  0.0782  -0.0334 383 ASN F C   
17802 O O   . ASN F 383 ? 0.4121 0.3810 0.5219 0.0095  0.0741  -0.0277 383 ASN F O   
17803 C CB  . ASN F 383 ? 0.2925 0.3429 0.5372 0.0073  0.0490  -0.0331 383 ASN F CB  
17804 C CG  . ASN F 383 ? 0.3238 0.4049 0.6293 0.0028  0.0289  -0.0361 383 ASN F CG  
17805 O OD1 . ASN F 383 ? 0.3271 0.4247 0.6816 -0.0025 0.0393  -0.0380 383 ASN F OD1 
17806 N ND2 . ASN F 383 ? 0.3502 0.4403 0.6558 0.0072  0.0031  -0.0337 383 ASN F ND2 
17807 N N   . LEU F 384 ? 0.3255 0.3020 0.5639 0.0503  -0.0687 0.0333  384 LEU F N   
17808 C CA  . LEU F 384 ? 0.3477 0.3089 0.5501 0.0399  -0.0499 0.0402  384 LEU F CA  
17809 C C   . LEU F 384 ? 0.3715 0.3294 0.5686 0.0448  -0.0350 0.0399  384 LEU F C   
17810 O O   . LEU F 384 ? 0.3544 0.3336 0.5771 0.0455  -0.0216 0.0307  384 LEU F O   
17811 C CB  . LEU F 384 ? 0.3614 0.3307 0.5681 0.0273  -0.0375 0.0374  384 LEU F CB  
17812 C CG  . LEU F 384 ? 0.3794 0.3274 0.5546 0.0248  -0.0263 0.0422  384 LEU F CG  
17813 C CD1 . LEU F 384 ? 0.3839 0.3200 0.5338 0.0273  -0.0344 0.0406  384 LEU F CD1 
17814 C CD2 . LEU F 384 ? 0.3800 0.3180 0.5525 0.0116  -0.0195 0.0432  384 LEU F CD2 
17815 N N   . VAL F 385 ? 0.3959 0.3331 0.5579 0.0432  -0.0356 0.0470  385 VAL F N   
17816 C CA  . VAL F 385 ? 0.3690 0.3011 0.5216 0.0451  -0.0245 0.0463  385 VAL F CA  
17817 C C   . VAL F 385 ? 0.3513 0.2867 0.4793 0.0380  -0.0120 0.0492  385 VAL F C   
17818 O O   . VAL F 385 ? 0.3566 0.2917 0.4639 0.0327  -0.0161 0.0498  385 VAL F O   
17819 C CB  . VAL F 385 ? 0.3490 0.2514 0.4811 0.0464  -0.0407 0.0505  385 VAL F CB  
17820 C CG1 . VAL F 385 ? 0.3187 0.2136 0.4417 0.0466  -0.0289 0.0464  385 VAL F CG1 
17821 C CG2 . VAL F 385 ? 0.3513 0.2437 0.5102 0.0609  -0.0648 0.0468  385 VAL F CG2 
17822 N N   . VAL F 386 ? 0.3554 0.2986 0.4870 0.0373  0.0017  0.0480  386 VAL F N   
17823 C CA  . VAL F 386 ? 0.3475 0.2914 0.4601 0.0359  0.0054  0.0507  386 VAL F CA  
17824 C C   . VAL F 386 ? 0.3206 0.2695 0.4160 0.0332  0.0112  0.0499  386 VAL F C   
17825 O O   . VAL F 386 ? 0.3210 0.2695 0.4163 0.0296  0.0200  0.0485  386 VAL F O   
17826 C CB  . VAL F 386 ? 0.3157 0.2531 0.4282 0.0308  0.0092  0.0552  386 VAL F CB  
17827 C CG1 . VAL F 386 ? 0.3449 0.2719 0.4364 0.0353  0.0020  0.0593  386 VAL F CG1 
17828 C CG2 . VAL F 386 ? 0.3083 0.2392 0.4337 0.0274  0.0035  0.0550  386 VAL F CG2 
17829 N N   . PHE F 387 ? 0.3226 0.2830 0.4051 0.0324  0.0076  0.0462  387 PHE F N   
17830 C CA  . PHE F 387 ? 0.3318 0.3047 0.3989 0.0258  0.0125  0.0435  387 PHE F CA  
17831 C C   . PHE F 387 ? 0.3299 0.3167 0.3971 0.0340  0.0082  0.0420  387 PHE F C   
17832 O O   . PHE F 387 ? 0.3177 0.3272 0.3922 0.0428  0.0003  0.0315  387 PHE F O   
17833 C CB  . PHE F 387 ? 0.3323 0.3186 0.3834 0.0122  0.0116  0.0371  387 PHE F CB  
17834 C CG  . PHE F 387 ? 0.3420 0.2969 0.3784 0.0013  0.0071  0.0439  387 PHE F CG  
17835 C CD1 . PHE F 387 ? 0.3191 0.2590 0.3614 0.0049  -0.0026 0.0480  387 PHE F CD1 
17836 C CD2 . PHE F 387 ? 0.4081 0.3414 0.4219 -0.0120 0.0076  0.0460  387 PHE F CD2 
17837 C CE1 . PHE F 387 ? 0.3679 0.2715 0.3956 -0.0011 -0.0161 0.0558  387 PHE F CE1 
17838 C CE2 . PHE F 387 ? 0.4425 0.3304 0.4390 -0.0180 -0.0058 0.0531  387 PHE F CE2 
17839 C CZ  . PHE F 387 ? 0.4366 0.3091 0.4405 -0.0110 -0.0200 0.0590  387 PHE F CZ  
17840 N N   . ASP F 388 ? 0.3528 0.3272 0.4115 0.0309  0.0115  0.0499  388 ASP F N   
17841 C CA  . ASP F 388 ? 0.3650 0.3380 0.4121 0.0356  0.0004  0.0549  388 ASP F CA  
17842 C C   . ASP F 388 ? 0.3477 0.3463 0.3836 0.0296  0.0012  0.0494  388 ASP F C   
17843 O O   . ASP F 388 ? 0.3822 0.3762 0.4000 0.0154  0.0105  0.0528  388 ASP F O   
17844 C CB  . ASP F 388 ? 0.4212 0.3667 0.4515 0.0238  0.0040  0.0679  388 ASP F CB  
17845 C CG  . ASP F 388 ? 0.5142 0.4386 0.5184 0.0247  -0.0161 0.0800  388 ASP F CG  
17846 O OD1 . ASP F 388 ? 0.5810 0.5180 0.5886 0.0412  -0.0349 0.0754  388 ASP F OD1 
17847 O OD2 . ASP F 388 ? 0.5341 0.4303 0.5123 0.0063  -0.0150 0.0933  388 ASP F OD2 
17848 N N   . LEU F 389 ? 0.2835 0.3163 0.3323 0.0384  -0.0077 0.0362  389 LEU F N   
17849 C CA  . LEU F 389 ? 0.2966 0.3651 0.3391 0.0282  -0.0063 0.0270  389 LEU F CA  
17850 C C   . LEU F 389 ? 0.3805 0.4471 0.4110 0.0347  -0.0238 0.0343  389 LEU F C   
17851 O O   . LEU F 389 ? 0.3973 0.4794 0.4109 0.0204  -0.0218 0.0334  389 LEU F O   
17852 C CB  . LEU F 389 ? 0.2691 0.3903 0.3345 0.0319  -0.0086 0.0045  389 LEU F CB  
17853 C CG  . LEU F 389 ? 0.2674 0.3740 0.3320 0.0229  0.0036  0.0041  389 LEU F CG  
17854 C CD1 . LEU F 389 ? 0.2427 0.4001 0.3282 0.0262  0.0026  -0.0204 389 LEU F CD1 
17855 C CD2 . LEU F 389 ? 0.2926 0.3809 0.3286 -0.0066 0.0179  0.0108  389 LEU F CD2 
17856 N N   . GLU F 390 ? 0.4276 0.4653 0.4590 0.0533  -0.0441 0.0436  390 GLU F N   
17857 C CA  . GLU F 390 ? 0.4852 0.5075 0.4962 0.0598  -0.0711 0.0548  390 GLU F CA  
17858 C C   . GLU F 390 ? 0.4689 0.4625 0.4350 0.0303  -0.0588 0.0733  390 GLU F C   
17859 O O   . GLU F 390 ? 0.4760 0.4705 0.4149 0.0227  -0.0740 0.0805  390 GLU F O   
17860 C CB  . GLU F 390 ? 0.5969 0.5755 0.6098 0.0838  -0.1005 0.0625  390 GLU F CB  
17861 C CG  . GLU F 390 ? 0.7536 0.6910 0.7307 0.0876  -0.1366 0.0819  390 GLU F CG  
17862 C CD  . GLU F 390 ? 0.8546 0.7208 0.8148 0.0990  -0.1631 0.0969  390 GLU F CD  
17863 O OE1 . GLU F 390 ? 0.9179 0.7243 0.8226 0.0707  -0.1669 0.1254  390 GLU F OE1 
17864 O OE2 . GLU F 390 ? 0.8440 0.7158 0.8436 0.1317  -0.1778 0.0771  390 GLU F OE2 
17865 N N   . ARG F 391 ? 0.4407 0.4149 0.4005 0.0131  -0.0319 0.0773  391 ARG F N   
17866 C CA  . ARG F 391 ? 0.4838 0.4448 0.4080 -0.0159 -0.0148 0.0844  391 ARG F CA  
17867 C C   . ARG F 391 ? 0.4298 0.4131 0.3657 -0.0270 0.0142  0.0670  391 ARG F C   
17868 O O   . ARG F 391 ? 0.4663 0.4466 0.3832 -0.0476 0.0331  0.0624  391 ARG F O   
17869 C CB  . ARG F 391 ? 0.5465 0.4721 0.4535 -0.0303 -0.0088 0.0972  391 ARG F CB  
17870 C CG  . ARG F 391 ? 0.6736 0.5542 0.5519 -0.0263 -0.0427 0.1187  391 ARG F CG  
17871 C CD  . ARG F 391 ? 0.8005 0.6449 0.6444 -0.0581 -0.0333 0.1331  391 ARG F CD  
17872 N NE  . ARG F 391 ? 0.8926 0.7577 0.7082 -0.0957 -0.0033 0.1278  391 ARG F NE  
17873 C CZ  . ARG F 391 ? 0.9721 0.8232 0.7485 -0.1368 0.0111  0.1351  391 ARG F CZ  
17874 N NH1 . ARG F 391 ? 0.9967 0.8023 0.7503 -0.1490 -0.0045 0.1537  391 ARG F NH1 
17875 N NH2 . ARG F 391 ? 1.0137 0.8983 0.7715 -0.1695 0.0421  0.1204  391 ARG F NH2 
17876 N N   . SER F 392 ? 0.3642 0.3667 0.3280 -0.0152 0.0160  0.0554  392 SER F N   
17877 C CA  . SER F 392 ? 0.3430 0.3479 0.3107 -0.0253 0.0347  0.0419  392 SER F CA  
17878 C C   . SER F 392 ? 0.3739 0.3579 0.3509 -0.0270 0.0515  0.0370  392 SER F C   
17879 O O   . SER F 392 ? 0.3975 0.3777 0.3652 -0.0383 0.0661  0.0245  392 SER F O   
17880 C CB  . SER F 392 ? 0.3632 0.3796 0.3047 -0.0441 0.0392  0.0344  392 SER F CB  
17881 O OG  . SER F 392 ? 0.3587 0.3682 0.3002 -0.0532 0.0491  0.0218  392 SER F OG  
17882 N N   . ARG F 393 ? 0.3671 0.3429 0.3668 -0.0146 0.0487  0.0419  393 ARG F N   
17883 C CA  . ARG F 393 ? 0.3619 0.3311 0.3819 -0.0133 0.0615  0.0331  393 ARG F CA  
17884 C C   . ARG F 393 ? 0.3772 0.3389 0.4247 0.0020  0.0527  0.0356  393 ARG F C   
17885 O O   . ARG F 393 ? 0.3722 0.3341 0.4194 0.0086  0.0402  0.0446  393 ARG F O   
17886 C CB  . ARG F 393 ? 0.3257 0.3006 0.3351 -0.0282 0.0710  0.0361  393 ARG F CB  
17887 C CG  . ARG F 393 ? 0.3671 0.3281 0.3680 -0.0274 0.0557  0.0557  393 ARG F CG  
17888 C CD  . ARG F 393 ? 0.4151 0.3698 0.3846 -0.0549 0.0623  0.0638  393 ARG F CD  
17889 N NE  . ARG F 393 ? 0.4630 0.3881 0.4222 -0.0545 0.0436  0.0825  393 ARG F NE  
17890 C CZ  . ARG F 393 ? 0.4836 0.3915 0.4148 -0.0831 0.0461  0.0928  393 ARG F CZ  
17891 N NH1 . ARG F 393 ? 0.5172 0.4472 0.4291 -0.1175 0.0707  0.0839  393 ARG F NH1 
17892 N NH2 . ARG F 393 ? 0.4918 0.3598 0.4111 -0.0808 0.0244  0.1095  393 ARG F NH2 
17893 N N   . VAL F 394 ? 0.3596 0.3184 0.4330 0.0087  0.0575  0.0235  394 VAL F N   
17894 C CA  . VAL F 394 ? 0.3791 0.3322 0.4777 0.0212  0.0464  0.0259  394 VAL F CA  
17895 C C   . VAL F 394 ? 0.3235 0.2974 0.4521 0.0205  0.0546  0.0179  394 VAL F C   
17896 O O   . VAL F 394 ? 0.3475 0.3424 0.4923 0.0164  0.0696  -0.0010 394 VAL F O   
17897 C CB  . VAL F 394 ? 0.4009 0.3297 0.5057 0.0313  0.0341  0.0195  394 VAL F CB  
17898 C CG1 . VAL F 394 ? 0.4302 0.3528 0.5552 0.0419  0.0180  0.0243  394 VAL F CG1 
17899 C CG2 . VAL F 394 ? 0.4042 0.3150 0.4729 0.0205  0.0276  0.0280  394 VAL F CG2 
17900 N N   . GLY F 395 ? 0.3043 0.2775 0.4403 0.0213  0.0462  0.0280  395 GLY F N   
17901 C CA  . GLY F 395 ? 0.2609 0.2561 0.4238 0.0146  0.0524  0.0206  395 GLY F CA  
17902 C C   . GLY F 395 ? 0.2709 0.2681 0.4661 0.0298  0.0364  0.0167  395 GLY F C   
17903 O O   . GLY F 395 ? 0.3181 0.2915 0.5003 0.0388  0.0198  0.0274  395 GLY F O   
17904 N N   . PHE F 396 ? 0.2526 0.2844 0.4894 0.0299  0.0408  -0.0012 396 PHE F N   
17905 C CA  . PHE F 396 ? 0.2447 0.2822 0.5147 0.0450  0.0202  -0.0056 396 PHE F CA  
17906 C C   . PHE F 396 ? 0.2738 0.3603 0.5824 0.0316  0.0297  -0.0215 396 PHE F C   
17907 O O   . PHE F 396 ? 0.3136 0.4334 0.6267 0.0111  0.0543  -0.0346 396 PHE F O   
17908 C CB  . PHE F 396 ? 0.2424 0.2700 0.5357 0.0719  0.0022  -0.0186 396 PHE F CB  
17909 C CG  . PHE F 396 ? 0.2936 0.3533 0.6203 0.0796  0.0178  -0.0491 396 PHE F CG  
17910 C CD1 . PHE F 396 ? 0.3171 0.4361 0.7077 0.0882  0.0214  -0.0819 396 PHE F CD1 
17911 C CD2 . PHE F 396 ? 0.3057 0.3452 0.6031 0.0766  0.0303  -0.0506 396 PHE F CD2 
17912 C CE1 . PHE F 396 ? 0.2937 0.4511 0.7148 0.0941  0.0386  -0.1178 396 PHE F CE1 
17913 C CE2 . PHE F 396 ? 0.2795 0.3502 0.6057 0.0822  0.0466  -0.0840 396 PHE F CE2 
17914 C CZ  . PHE F 396 ? 0.2819 0.4139 0.6734 0.0923  0.0522  -0.1202 396 PHE F CZ  
17915 N N   . ASN F 397 ? 0.2738 0.3682 0.6057 0.0370  0.0111  -0.0213 397 ASN F N   
17916 C CA  . ASN F 397 ? 0.2751 0.4248 0.6473 0.0198  0.0196  -0.0394 397 ASN F CA  
17917 C C   . ASN F 397 ? 0.2479 0.4635 0.6848 0.0328  0.0275  -0.0779 397 ASN F C   
17918 O O   . ASN F 397 ? 0.2351 0.4470 0.7039 0.0688  0.0050  -0.0903 397 ASN F O   
17919 C CB  . ASN F 397 ? 0.2891 0.4345 0.6718 0.0225  -0.0054 -0.0323 397 ASN F CB  
17920 C CG  . ASN F 397 ? 0.3207 0.4373 0.7075 0.0547  -0.0392 -0.0264 397 ASN F CG  
17921 O OD1 . ASN F 397 ? 0.3608 0.4244 0.7007 0.0603  -0.0465 -0.0062 397 ASN F OD1 
17922 N ND2 . ASN F 397 ? 0.3144 0.4664 0.7548 0.0731  -0.0621 -0.0447 397 ASN F ND2 
17923 N N   . SER F 398 ? 0.3051 0.5797 0.7590 0.0017  0.0581  -0.0992 398 SER F N   
17924 C CA  . SER F 398 ? 0.3283 0.6734 0.8353 0.0108  0.0706  -0.1431 398 SER F CA  
17925 C C   . SER F 398 ? 0.3053 0.6990 0.8575 0.0199  0.0534  -0.1647 398 SER F C   
17926 O O   . SER F 398 ? 0.3290 0.7627 0.9153 0.0378  0.0516  -0.1987 398 SER F O   
17927 C CB  . SER F 398 ? 0.3746 0.7548 0.8533 -0.0341 0.1115  -0.1549 398 SER F CB  
17928 O OG  . SER F 398 ? 0.4102 0.8020 0.8626 -0.0835 0.1252  -0.1415 398 SER F OG  
17929 N N   . ASN F 399 ? 0.2789 0.6690 0.8332 0.0070  0.0397  -0.1473 399 ASN F N   
17930 C CA  . ASN F 399 ? 0.2952 0.7208 0.8889 0.0199  0.0153  -0.1615 399 ASN F CA  
17931 C C   . ASN F 399 ? 0.2729 0.6395 0.8525 0.0410  -0.0229 -0.1319 399 ASN F C   
17932 O O   . ASN F 399 ? 0.2900 0.6012 0.8340 0.0357  -0.0235 -0.1032 399 ASN F O   
17933 C CB  . ASN F 399 ? 0.3143 0.7999 0.9166 -0.0271 0.0362  -0.1725 399 ASN F CB  
17934 C CG  . ASN F 399 ? 0.3552 0.8983 0.9590 -0.0553 0.0730  -0.2021 399 ASN F CG  
17935 O OD1 . ASN F 399 ? 0.4034 0.9987 1.0512 -0.0342 0.0720  -0.2396 399 ASN F OD1 
17936 N ND2 . ASN F 399 ? 0.3721 0.9005 0.9219 -0.1059 0.1027  -0.1861 399 ASN F ND2 
17937 N N   . SER F 400 ? 0.3014 0.6774 0.9049 0.0637  -0.0558 -0.1388 400 SER F N   
17938 C CA  . SER F 400 ? 0.3232 0.6403 0.8993 0.0777  -0.0938 -0.1105 400 SER F CA  
17939 C C   . SER F 400 ? 0.3175 0.6285 0.8777 0.0438  -0.0906 -0.0912 400 SER F C   
17940 O O   . SER F 400 ? 0.3433 0.7022 0.9205 0.0083  -0.0678 -0.1029 400 SER F O   
17941 C CB  . SER F 400 ? 0.3857 0.7159 0.9878 0.1043  -0.1307 -0.1227 400 SER F CB  
17942 O OG  . SER F 400 ? 0.4115 0.8135 1.0548 0.0858  -0.1278 -0.1412 400 SER F OG  
17943 N N   . LEU F 401 ? 0.3034 0.5485 0.8207 0.0491  -0.1129 -0.0618 401 LEU F N   
17944 C CA  . LEU F 401 ? 0.3212 0.5360 0.7904 0.0180  -0.1084 -0.0436 401 LEU F CA  
17945 C C   . LEU F 401 ? 0.3514 0.6184 0.8608 0.0047  -0.1263 -0.0588 401 LEU F C   
17946 O O   . LEU F 401 ? 0.3810 0.6541 0.8754 -0.0313 -0.1116 -0.0592 401 LEU F O   
17947 C CB  . LEU F 401 ? 0.3358 0.4759 0.7400 0.0262  -0.1259 -0.0162 401 LEU F CB  
17948 C CG  . LEU F 401 ? 0.3215 0.4155 0.6830 0.0324  -0.1062 -0.0024 401 LEU F CG  
17949 C CD1 . LEU F 401 ? 0.3346 0.3728 0.6328 0.0284  -0.1158 0.0177  401 LEU F CD1 
17950 C CD2 . LEU F 401 ? 0.2882 0.3883 0.6418 0.0120  -0.0700 -0.0049 401 LEU F CD2 
17951 N N   . LYS F 402 ? 0.3731 0.6646 0.9157 0.0332  -0.1578 -0.0697 402 LYS F N   
17952 C CA  . LYS F 402 ? 0.3814 0.7181 0.9486 0.0241  -0.1765 -0.0821 402 LYS F CA  
17953 C C   . LYS F 402 ? 0.3461 0.7646 0.9585 -0.0041 -0.1445 -0.1100 402 LYS F C   
17954 O O   . LYS F 402 ? 0.3541 0.8039 0.9723 -0.0359 -0.1448 -0.1154 402 LYS F O   
17955 C CB  . LYS F 402 ? 0.4237 0.7541 1.0001 0.0629  -0.2139 -0.0852 402 LYS F CB  
17956 C CG  . LYS F 402 ? 0.4479 0.8360 1.0630 0.0634  -0.2363 -0.1021 402 LYS F CG  
17957 C CD  . LYS F 402 ? 0.7351 1.1007 1.3582 0.1067  -0.2757 -0.1044 402 LYS F CD  
17958 C CE  . LYS F 402 ? 0.7817 1.1724 1.4207 0.1112  -0.3161 -0.1071 402 LYS F CE  
17959 N NZ  . LYS F 402 ? 0.8271 1.1346 1.4005 0.1177  -0.3593 -0.0752 402 LYS F NZ  
17960 N N   . SER F 403 ? 0.3069 0.7542 0.9393 -0.0003 -0.1143 -0.1264 403 SER F N   
17961 C CA  . SER F 403 ? 0.2735 0.7943 0.9334 -0.0352 -0.0801 -0.1512 403 SER F CA  
17962 C C   . SER F 403 ? 0.2705 0.7700 0.8893 -0.0914 -0.0537 -0.1369 403 SER F C   
17963 O O   . SER F 403 ? 0.3106 0.8524 0.9298 -0.1333 -0.0295 -0.1489 403 SER F O   
17964 C CB  . SER F 403 ? 0.2755 0.8252 0.9541 -0.0221 -0.0536 -0.1729 403 SER F CB  
17965 O OG  . SER F 403 ? 0.2571 0.7705 0.8940 -0.0470 -0.0229 -0.1580 403 SER F OG  
17966 N N   . TYR F 404 ? 0.3355 0.7583 0.9125 -0.0936 -0.0592 -0.1106 404 TYR F N   
17967 C CA  . TYR F 404 ? 0.3267 0.6947 0.8416 -0.1411 -0.0416 -0.0919 404 TYR F CA  
17968 C C   . TYR F 404 ? 0.3690 0.7078 0.8634 -0.1504 -0.0678 -0.0834 404 TYR F C   
17969 O O   . TYR F 404 ? 0.4226 0.7031 0.8602 -0.1848 -0.0610 -0.0698 404 TYR F O   
17970 C CB  . TYR F 404 ? 0.3047 0.5814 0.7500 -0.1309 -0.0306 -0.0628 404 TYR F CB  
17971 C CG  . TYR F 404 ? 0.2686 0.5650 0.7201 -0.1286 -0.0036 -0.0689 404 TYR F CG  
17972 C CD1 . TYR F 404 ? 0.3051 0.6120 0.7323 -0.1777 0.0270  -0.0714 404 TYR F CD1 
17973 C CD2 . TYR F 404 ? 0.2386 0.5331 0.7079 -0.0833 -0.0099 -0.0701 404 TYR F CD2 
17974 C CE1 . TYR F 404 ? 0.3255 0.6515 0.7502 -0.1811 0.0526  -0.0778 404 TYR F CE1 
17975 C CE2 . TYR F 404 ? 0.2332 0.5441 0.7045 -0.0832 0.0155  -0.0783 404 TYR F CE2 
17976 C CZ  . TYR F 404 ? 0.3076 0.6383 0.7575 -0.1319 0.0476  -0.0831 404 TYR F CZ  
17977 O OH  . TYR F 404 ? 0.3126 0.6621 0.7567 -0.1384 0.0739  -0.0925 404 TYR F OH  
17978 N N   . GLY F 405 ? 0.3384 0.7120 0.8756 -0.1194 -0.1016 -0.0922 405 GLY F N   
17979 C CA  . GLY F 405 ? 0.3612 0.7074 0.8736 -0.1265 -0.1298 -0.0843 405 GLY F CA  
17980 C C   . GLY F 405 ? 0.3915 0.6423 0.8313 -0.1085 -0.1384 -0.0568 405 GLY F C   
17981 O O   . GLY F 405 ? 0.4072 0.6174 0.8043 -0.1240 -0.1494 -0.0505 405 GLY F O   
17982 N N   . LYS F 406 ? 0.3782 0.5990 0.8047 -0.0787 -0.1315 -0.0448 406 LYS F N   
17983 C CA  . LYS F 406 ? 0.4019 0.5464 0.7634 -0.0668 -0.1334 -0.0240 406 LYS F CA  
17984 C C   . LYS F 406 ? 0.4249 0.5579 0.7822 -0.0342 -0.1605 -0.0141 406 LYS F C   
17985 O O   . LYS F 406 ? 0.4051 0.5765 0.8116 -0.0111 -0.1783 -0.0216 406 LYS F O   
17986 C CB  . LYS F 406 ? 0.4046 0.5098 0.7360 -0.0678 -0.1025 -0.0149 406 LYS F CB  
17987 C CG  . LYS F 406 ? 0.4447 0.5421 0.7651 -0.1037 -0.0796 -0.0184 406 LYS F CG  
17988 C CD  . LYS F 406 ? 0.5101 0.5525 0.7844 -0.1246 -0.0857 -0.0162 406 LYS F CD  
17989 C CE  . LYS F 406 ? 0.5664 0.5939 0.8261 -0.1677 -0.0714 -0.0183 406 LYS F CE  
17990 N NZ  . LYS F 406 ? 0.5742 0.5973 0.8265 -0.1747 -0.0490 -0.0098 406 LYS F NZ  
17991 N N   . THR F 407 ? 0.4416 0.5203 0.7380 -0.0348 -0.1649 0.0000  407 THR F N   
17992 C CA  . THR F 407 ? 0.4475 0.4967 0.7141 -0.0162 -0.1845 0.0149  407 THR F CA  
17993 C C   . THR F 407 ? 0.4261 0.4333 0.6424 -0.0183 -0.1594 0.0226  407 THR F C   
17994 O O   . THR F 407 ? 0.4366 0.4334 0.6423 -0.0286 -0.1349 0.0159  407 THR F O   
17995 C CB  . THR F 407 ? 0.4922 0.5298 0.7266 -0.0252 -0.2220 0.0219  407 THR F CB  
17996 O OG1 . THR F 407 ? 0.5061 0.5196 0.6870 -0.0500 -0.2097 0.0192  407 THR F OG1 
17997 C CG2 . THR F 407 ? 0.5089 0.5946 0.7950 -0.0250 -0.2501 0.0109  407 THR F CG2 
17998 N N   . CYS F 408 ? 0.3970 0.3783 0.5820 -0.0093 -0.1686 0.0355  408 CYS F N   
17999 C CA  . CYS F 408 ? 0.3782 0.3342 0.5202 -0.0137 -0.1460 0.0384  408 CYS F CA  
18000 C C   . CYS F 408 ? 0.4258 0.3742 0.5249 -0.0347 -0.1424 0.0293  408 CYS F C   
18001 O O   . CYS F 408 ? 0.4305 0.3729 0.5063 -0.0371 -0.1213 0.0208  408 CYS F O   
18002 C CB  . CYS F 408 ? 0.3938 0.3255 0.5084 -0.0077 -0.1565 0.0532  408 CYS F CB  
18003 S SG  . CYS F 408 ? 0.4224 0.3580 0.5746 0.0159  -0.1376 0.0531  408 CYS F SG  
18004 N N   . SER F 409 ? 0.4557 0.4098 0.5464 -0.0490 -0.1644 0.0272  409 SER F N   
18005 C CA  . SER F 409 ? 0.4910 0.4423 0.5420 -0.0714 -0.1603 0.0120  409 SER F CA  
18006 C C   . SER F 409 ? 0.4628 0.4152 0.5359 -0.0723 -0.1430 -0.0088 409 SER F C   
18007 O O   . SER F 409 ? 0.4804 0.4248 0.5277 -0.0807 -0.1311 -0.0297 409 SER F O   
18008 C CB  . SER F 409 ? 0.5515 0.5035 0.5747 -0.0909 -0.1943 0.0191  409 SER F CB  
18009 O OG  . SER F 409 ? 0.6123 0.5439 0.5992 -0.0941 -0.2158 0.0412  409 SER F OG  
18010 N N   . ASN F 410 ? 0.4303 0.3917 0.5481 -0.0671 -0.1435 -0.0064 410 ASN F N   
18011 C CA  . ASN F 410 ? 0.4439 0.3911 0.5690 -0.0767 -0.1322 -0.0216 410 ASN F CA  
18012 C C   . ASN F 410 ? 0.4297 0.3626 0.5762 -0.0674 -0.1135 -0.0171 410 ASN F C   
18013 O O   . ASN F 410 ? 0.4804 0.3907 0.6273 -0.0805 -0.1090 -0.0239 410 ASN F O   
18014 C CB  . ASN F 410 ? 0.4823 0.4490 0.6242 -0.0981 -0.1498 -0.0272 410 ASN F CB  
18015 C CG  . ASN F 410 ? 0.4925 0.5020 0.6871 -0.0948 -0.1590 -0.0182 410 ASN F CG  
18016 O OD1 . ASN F 410 ? 0.4818 0.5001 0.7038 -0.0833 -0.1438 -0.0126 410 ASN F OD1 
18017 N ND2 . ASN F 410 ? 0.5044 0.5473 0.7164 -0.1059 -0.1847 -0.0217 410 ASN F ND2 
18018 N N   . LEU F 411 ? 0.3843 0.3246 0.5412 -0.0497 -0.1048 -0.0046 411 LEU F N   
18019 C CA  . LEU F 411 ? 0.3677 0.2921 0.5331 -0.0445 -0.0879 0.0005  411 LEU F CA  
18020 C C   . LEU F 411 ? 0.4133 0.2924 0.5495 -0.0390 -0.0829 -0.0096 411 LEU F C   
18021 O O   . LEU F 411 ? 0.4470 0.2904 0.5766 -0.0447 -0.0800 -0.0077 411 LEU F O   
18022 C CB  . LEU F 411 ? 0.3583 0.2980 0.5345 -0.0266 -0.0802 0.0121  411 LEU F CB  
18023 C CG  . LEU F 411 ? 0.3776 0.3095 0.5615 -0.0263 -0.0636 0.0187  411 LEU F CG  
18024 C CD1 . LEU F 411 ? 0.3776 0.3318 0.5875 -0.0491 -0.0586 0.0168  411 LEU F CD1 
18025 C CD2 . LEU F 411 ? 0.3569 0.3035 0.5477 -0.0092 -0.0572 0.0260  411 LEU F CD2 
18026 N N   . PHE F 412 ? 0.3946 0.2755 0.5116 -0.0290 -0.0843 -0.0224 412 PHE F N   
18027 C CA  . PHE F 412 ? 0.4014 0.2534 0.5021 -0.0169 -0.0826 -0.0437 412 PHE F CA  
18028 C C   . PHE F 412 ? 0.4310 0.2904 0.5145 -0.0271 -0.0880 -0.0687 412 PHE F C   
18029 O O   . PHE F 412 ? 0.4467 0.3358 0.5219 -0.0431 -0.0930 -0.0639 412 PHE F O   
18030 C CB  . PHE F 412 ? 0.4093 0.2749 0.5097 0.0049  -0.0730 -0.0461 412 PHE F CB  
18031 C CG  . PHE F 412 ? 0.4247 0.2862 0.5366 0.0117  -0.0674 -0.0223 412 PHE F CG  
18032 C CD1 . PHE F 412 ? 0.4728 0.2921 0.5822 0.0170  -0.0710 -0.0162 412 PHE F CD1 
18033 C CD2 . PHE F 412 ? 0.4382 0.3308 0.5565 0.0103  -0.0612 -0.0066 412 PHE F CD2 
18034 C CE1 . PHE F 412 ? 0.4700 0.2879 0.5820 0.0168  -0.0646 0.0043  412 PHE F CE1 
18035 C CE2 . PHE F 412 ? 0.4250 0.3166 0.5533 0.0152  -0.0540 0.0097  412 PHE F CE2 
18036 C CZ  . PHE F 412 ? 0.4350 0.2941 0.5596 0.0165  -0.0537 0.0147  412 PHE F CZ  
18037 N N   . ASP F 413 ? 0.4935 0.3213 0.5692 -0.0177 -0.0906 -0.0966 413 ASP F N   
18038 C CA  . ASP F 413 ? 0.5450 0.3806 0.6035 -0.0274 -0.0928 -0.1296 413 ASP F CA  
18039 C C   . ASP F 413 ? 0.5625 0.4484 0.6115 -0.0226 -0.0797 -0.1503 413 ASP F C   
18040 O O   . ASP F 413 ? 0.5397 0.4322 0.6016 0.0029  -0.0725 -0.1719 413 ASP F O   
18041 C CB  . ASP F 413 ? 0.5665 0.3461 0.6230 -0.0146 -0.1019 -0.1592 413 ASP F CB  
18042 C CG  . ASP F 413 ? 0.6207 0.4020 0.6586 -0.0317 -0.1052 -0.1933 413 ASP F CG  
18043 O OD1 . ASP F 413 ? 0.6171 0.4521 0.6404 -0.0470 -0.0964 -0.2056 413 ASP F OD1 
18044 O OD2 . ASP F 413 ? 0.6988 0.4218 0.7296 -0.0345 -0.1181 -0.2077 413 ASP F OD2 
18045 N N   . LEU F 414 ? 0.5529 0.4747 0.5767 -0.0500 -0.0792 -0.1450 414 LEU F N   
18046 C CA  . LEU F 414 ? 0.5367 0.5069 0.5373 -0.0603 -0.0654 -0.1605 414 LEU F CA  
18047 C C   . LEU F 414 ? 0.5941 0.5906 0.5624 -0.0846 -0.0600 -0.2000 414 LEU F C   
18048 O O   . LEU F 414 ? 0.6279 0.6672 0.5610 -0.1107 -0.0495 -0.2085 414 LEU F O   
18049 C CB  . LEU F 414 ? 0.5187 0.5008 0.4993 -0.0789 -0.0716 -0.1198 414 LEU F CB  
18050 C CG  . LEU F 414 ? 0.4762 0.4419 0.4867 -0.0575 -0.0733 -0.0864 414 LEU F CG  
18051 C CD1 . LEU F 414 ? 0.4763 0.4453 0.4656 -0.0733 -0.0851 -0.0528 414 LEU F CD1 
18052 C CD2 . LEU F 414 ? 0.4587 0.4369 0.4869 -0.0344 -0.0565 -0.1014 414 LEU F CD2 
18053 N N   . ASN F 415 ? 0.6338 0.6025 0.6081 -0.0809 -0.0669 -0.2253 415 ASN F N   
18054 C CA  . ASN F 415 ? 0.7174 0.7077 0.6632 -0.1025 -0.0611 -0.2708 415 ASN F CA  
18055 C C   . ASN F 415 ? 0.7668 0.7918 0.7312 -0.0798 -0.0411 -0.3309 415 ASN F C   
18056 O O   . ASN F 415 ? 0.7586 0.7601 0.7654 -0.0375 -0.0434 -0.3427 415 ASN F O   
18057 C CB  . ASN F 415 ? 0.7785 0.7197 0.7250 -0.1074 -0.0783 -0.2759 415 ASN F CB  
18058 C CG  . ASN F 415 ? 0.7916 0.7163 0.7325 -0.1284 -0.0986 -0.2246 415 ASN F CG  
18059 O OD1 . ASN F 415 ? 0.8303 0.7836 0.7429 -0.1540 -0.1058 -0.2003 415 ASN F OD1 
18060 N ND2 . ASN F 415 ? 0.7482 0.6267 0.7156 -0.1187 -0.1103 -0.2093 415 ASN F ND2 
18061 N N   . ASN F 416 ? 0.8473 0.9323 0.7794 -0.1093 -0.0231 -0.3706 416 ASN F N   
18062 C CA  . ASN F 416 ? 0.9160 1.0542 0.8775 -0.0862 0.0003  -0.4187 416 ASN F CA  
18063 C C   . ASN F 416 ? 0.9602 1.0597 0.9733 -0.0341 -0.0091 -0.4515 416 ASN F C   
18064 O O   . ASN F 416 ? 0.9347 1.0639 0.9957 0.0033  -0.0034 -0.4742 416 ASN F O   
18065 C CB  . ASN F 416 ? 0.9861 1.1813 0.9083 -0.1274 0.0200  -0.4386 416 ASN F CB  
18066 C CG  . ASN F 416 ? 0.9639 1.1944 0.8318 -0.1777 0.0283  -0.4023 416 ASN F CG  
18067 O OD1 . ASN F 416 ? 0.9284 1.1578 0.7973 -0.1764 0.0257  -0.3731 416 ASN F OD1 
18068 N ND2 . ASN F 416 ? 0.9961 1.2512 0.8127 -0.2236 0.0362  -0.4010 416 ASN F ND2 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   LEU 1   1   ?   ?   ?   A . n 
A 1 2   TYR 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   GLN 6   6   ?   ?   ?   A . n 
A 1 7   PRO 7   7   ?   ?   ?   A . n 
A 1 8   THR 8   8   ?   ?   ?   A . n 
A 1 9   SER 9   9   ?   ?   ?   A . n 
A 1 10  SER 10  10  ?   ?   ?   A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  GLN 20  20  20  GLN GLN A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  HIS 28  28  28  HIS HIS A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  MET 39  39  39  MET MET A . n 
A 1 40  GLN 40  40  40  GLN GLN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  TRP 53  53  53  TRP TRP A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  CYS 56  56  56  CYS CYS A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  HIS 59  59  59  HIS HIS A . n 
A 1 60  TYR 60  60  60  TYR TYR A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  TYR 65  65  65  TYR TYR A . n 
A 1 66  GLN 66  66  66  GLN GLN A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  PHE 69  69  69  PHE PHE A . n 
A 1 70  CYS 70  70  70  CYS CYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  CYS 75  75  75  CYS CYS A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  ARG 77  77  77  ARG ARG A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  HIS 81  81  81  HIS HIS A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  CYS 83  83  83  CYS CYS A . n 
A 1 84  PHE 84  84  84  PHE PHE A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  CYS 86  86  86  CYS CYS A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  CYS 96  96  96  CYS CYS A . n 
A 1 97  HIS 97  97  97  HIS HIS A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 THR 110 110 110 THR THR A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 HIS 126 126 126 HIS HIS A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 HIS 129 129 129 HIS HIS A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 GLN 141 141 141 GLN GLN A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 GLN 168 168 168 GLN GLN A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 GLN 174 174 174 GLN GLN A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 GLN 186 186 186 GLN GLN A . n 
A 1 187 PHE 187 187 187 PHE PHE A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 CYS 190 190 190 CYS CYS A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 ASN 198 198 198 ASN ASN A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 HIS 216 216 216 HIS HIS A . n 
A 1 217 ASN 217 217 217 ASN ASN A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 PRO 229 229 229 PRO PRO A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 LYS 234 234 234 LYS LYS A . n 
A 1 235 GLN 235 235 235 GLN GLN A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 PHE 239 239 239 PHE PHE A . n 
A 1 240 ILE 240 240 240 ILE ILE A . n 
A 1 241 GLN 241 241 241 GLN GLN A . n 
A 1 242 VAL 242 242 242 VAL VAL A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 ARG 246 246 246 ARG ARG A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 LYS 249 249 249 LYS LYS A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 ILE 253 253 253 ILE ILE A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 LYS 256 256 ?   ?   ?   A . n 
A 1 257 ASN 257 257 ?   ?   ?   A . n 
A 1 258 PRO 258 258 ?   ?   ?   A . n 
A 1 259 PHE 259 259 ?   ?   ?   A . n 
A 1 260 ILE 260 260 ?   ?   ?   A . n 
A 1 261 SER 261 261 ?   ?   ?   A . n 
A 1 262 PRO 262 262 ?   ?   ?   A . n 
A 1 263 SER 263 263 ?   ?   ?   A . n 
A 1 264 SER 264 264 ?   ?   ?   A . n 
A 1 265 THR 265 265 ?   ?   ?   A . n 
A 1 266 SER 266 266 ?   ?   ?   A . n 
A 1 267 TYR 267 267 ?   ?   ?   A . n 
A 1 268 HIS 268 268 ?   ?   ?   A . n 
A 1 269 GLY 269 269 ?   ?   ?   A . n 
A 1 270 SER 270 270 ?   ?   ?   A . n 
A 1 271 GLY 271 271 ?   ?   ?   A . n 
A 1 272 GLU 272 272 272 GLU GLU A . n 
A 1 273 ILE 273 273 273 ILE ILE A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 ILE 278 278 278 ILE ILE A . n 
A 1 279 THR 279 279 279 THR THR A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 THR 281 281 281 THR THR A . n 
A 1 282 HIS 282 282 282 HIS HIS A . n 
A 1 283 PRO 283 283 283 PRO PRO A . n 
A 1 284 TYR 284 284 284 TYR TYR A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 HIS 289 289 289 HIS HIS A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 PHE 292 292 292 PHE PHE A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 VAL 294 294 294 VAL VAL A . n 
A 1 295 PHE 295 295 295 PHE PHE A . n 
A 1 296 THR 296 296 296 THR THR A . n 
A 1 297 GLN 297 297 297 GLN GLN A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 PHE 299 299 299 PHE PHE A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 ASN 302 302 302 ASN ASN A . n 
A 1 303 MET 303 303 303 MET MET A . n 
A 1 304 PRO 304 304 304 PRO PRO A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 GLN 306 306 306 GLN GLN A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 GLN 308 308 308 GLN GLN A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 ALA 311 311 311 ALA ALA A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 PRO 314 314 314 PRO PRO A . n 
A 1 315 PHE 315 315 315 PHE PHE A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 CYS 318 318 318 CYS CYS A . n 
A 1 319 TYR 319 319 319 TYR TYR A . n 
A 1 320 ASP 320 320 320 ASP ASP A . n 
A 1 321 SER 321 321 321 SER SER A . n 
A 1 322 ARG 322 322 322 ARG ARG A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 ILE 324 324 324 ILE ILE A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 ASP 332 332 332 ASP ASP A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 ILE 334 334 334 ILE ILE A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 LYS 337 337 337 LYS LYS A . n 
A 1 338 ASN 338 338 338 ASN ASN A . n 
A 1 339 ASP 339 339 339 ASP ASP A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 TRP 342 342 342 TRP TRP A . n 
A 1 343 ARG 343 343 343 ARG ARG A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 GLU 347 347 347 GLU GLU A . n 
A 1 348 ASN 348 348 348 ASN ASN A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 MET 350 350 350 MET MET A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 GLN 352 352 352 GLN GLN A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 GLN 354 354 354 GLN GLN A . n 
A 1 355 ASP 355 355 355 ASP ASP A . n 
A 1 356 GLY 356 356 356 GLY GLY A . n 
A 1 357 VAL 357 357 357 VAL VAL A . n 
A 1 358 SER 358 358 358 SER SER A . n 
A 1 359 CYS 359 359 359 CYS CYS A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 GLY 361 361 361 GLY GLY A . n 
A 1 362 PHE 362 362 362 PHE PHE A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 ASP 364 364 364 ASP ASP A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 HIS 368 368 368 HIS HIS A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 ARG 370 370 370 ARG ARG A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 GLY 376 376 376 GLY GLY A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 HIS 378 378 378 HIS HIS A . n 
A 1 379 HIS 379 379 379 HIS HIS A . n 
A 1 380 LEU 380 380 380 LEU LEU A . n 
A 1 381 GLU 381 381 381 GLU GLU A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 ASN 383 383 383 ASN ASN A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 VAL 386 386 386 VAL VAL A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 ASP 388 388 388 ASP ASP A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 ARG 393 393 393 ARG ARG A . n 
A 1 394 VAL 394 394 394 VAL VAL A . n 
A 1 395 GLY 395 395 395 GLY GLY A . n 
A 1 396 PHE 396 396 396 PHE PHE A . n 
A 1 397 ASN 397 397 397 ASN ASN A . n 
A 1 398 SER 398 398 398 SER SER A . n 
A 1 399 ASN 399 399 399 ASN ASN A . n 
A 1 400 SER 400 400 400 SER SER A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 LYS 402 402 402 LYS LYS A . n 
A 1 403 SER 403 403 403 SER SER A . n 
A 1 404 TYR 404 404 404 TYR TYR A . n 
A 1 405 GLY 405 405 405 GLY GLY A . n 
A 1 406 LYS 406 406 406 LYS LYS A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 CYS 408 408 408 CYS CYS A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 ASP 413 413 413 ASP ASP A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ASN 415 415 415 ASN ASN A . n 
A 1 416 ASN 416 416 416 ASN ASN A . n 
A 1 417 PRO 417 417 ?   ?   ?   A . n 
B 1 1   LEU 1   1   ?   ?   ?   B . n 
B 1 2   TYR 2   2   ?   ?   ?   B . n 
B 1 3   HIS 3   3   ?   ?   ?   B . n 
B 1 4   ASN 4   4   ?   ?   ?   B . n 
B 1 5   SER 5   5   ?   ?   ?   B . n 
B 1 6   GLN 6   6   ?   ?   ?   B . n 
B 1 7   PRO 7   7   ?   ?   ?   B . n 
B 1 8   THR 8   8   ?   ?   ?   B . n 
B 1 9   SER 9   9   ?   ?   ?   B . n 
B 1 10  SER 10  10  ?   ?   ?   B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  PRO 18  18  18  PRO PRO B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  GLN 20  20  20  GLN GLN B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  SER 24  24  24  SER SER B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  HIS 28  28  28  HIS HIS B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  ALA 30  30  30  ALA ALA B . n 
B 1 31  ASN 31  31  31  ASN ASN B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  ARG 35  35  35  ARG ARG B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  PRO 37  37  37  PRO PRO B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  MET 39  39  39  MET MET B . n 
B 1 40  GLN 40  40  40  GLN GLN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  ASP 46  46  46  ASP ASP B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  ASN 48  48  48  ASN ASN B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  HIS 51  51  51  HIS HIS B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  TRP 53  53  53  TRP TRP B . n 
B 1 54  VAL 54  54  54  VAL VAL B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  CYS 56  56  56  CYS CYS B . n 
B 1 57  SER 57  57  57  SER SER B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  HIS 59  59  59  HIS HIS B . n 
B 1 60  TYR 60  60  60  TYR TYR B . n 
B 1 61  SER 61  61  61  SER SER B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  SER 63  63  63  SER SER B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  TYR 65  65  65  TYR TYR B . n 
B 1 66  GLN 66  66  66  GLN GLN B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  PRO 68  68  68  PRO PRO B . n 
B 1 69  PHE 69  69  69  PHE PHE B . n 
B 1 70  CYS 70  70  70  CYS CYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  THR 73  73  73  THR THR B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  CYS 75  75  75  CYS CYS B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  ARG 77  77  77  ARG ARG B . n 
B 1 78  ALA 78  78  78  ALA ALA B . n 
B 1 79  ASN 79  79  79  ASN ASN B . n 
B 1 80  THR 80  80  80  THR THR B . n 
B 1 81  HIS 81  81  81  HIS HIS B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  CYS 83  83  83  CYS CYS B . n 
B 1 84  PHE 84  84  84  PHE PHE B . n 
B 1 85  THR 85  85  85  THR THR B . n 
B 1 86  CYS 86  86  86  CYS CYS B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  ASP 88  88  88  ASP ASP B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  THR 92  92  92  THR THR B . n 
B 1 93  ARG 93  93  93  ARG ARG B . n 
B 1 94  PRO 94  94  94  PRO PRO B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  CYS 96  96  96  CYS CYS B . n 
B 1 97  HIS 97  97  97  HIS HIS B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 THR 100 100 100 THR THR B . n 
B 1 101 CYS 101 101 101 CYS CYS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 ASN 107 107 107 ASN ASN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 THR 110 110 110 THR THR B . n 
B 1 111 GLN 111 111 111 GLN GLN B . n 
B 1 112 GLU 112 112 112 GLU GLU B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 GLY 116 116 116 GLY GLY B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 GLN 120 120 120 GLN GLN B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 HIS 126 126 126 HIS HIS B . n 
B 1 127 SER 127 127 127 SER SER B . n 
B 1 128 THR 128 128 128 THR THR B . n 
B 1 129 HIS 129 129 129 HIS HIS B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 SER 131 131 131 SER SER B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 GLY 134 134 134 GLY GLY B . n 
B 1 135 PRO 135 135 135 PRO PRO B . n 
B 1 136 MET 136 136 136 MET MET B . n 
B 1 137 VAL 137 137 137 VAL VAL B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 VAL 139 139 139 VAL VAL B . n 
B 1 140 PRO 140 140 140 PRO PRO B . n 
B 1 141 GLN 141 141 141 GLN GLN B . n 
B 1 142 PHE 142 142 142 PHE PHE B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 SER 145 145 145 SER SER B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 PRO 148 148 148 PRO PRO B . n 
B 1 149 SER 149 149 149 SER SER B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
B 1 154 LYS 154 154 154 LYS LYS B . n 
B 1 155 GLY 155 155 155 GLY GLY B . n 
B 1 156 LEU 156 156 156 LEU LEU B . n 
B 1 157 PRO 157 157 157 PRO PRO B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 VAL 160 160 160 VAL VAL B . n 
B 1 161 GLN 161 161 161 GLN GLN B . n 
B 1 162 GLY 162 162 162 GLY GLY B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 GLN 168 168 168 GLN GLN B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 ILE 171 171 171 ILE ILE B . n 
B 1 172 SER 172 172 172 SER SER B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 GLN 174 174 174 GLN GLN B . n 
B 1 175 ASN 175 175 175 ASN ASN B . n 
B 1 176 GLN 176 176 176 GLN GLN B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 SER 179 179 179 SER SER B . n 
B 1 180 HIS 180 180 180 HIS HIS B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 LYS 184 184 184 LYS LYS B . n 
B 1 185 ARG 185 185 185 ARG ARG B . n 
B 1 186 GLN 186 186 186 GLN GLN B . n 
B 1 187 PHE 187 187 187 PHE PHE B . n 
B 1 188 SER 188 188 188 SER SER B . n 
B 1 189 VAL 189 189 189 VAL VAL B . n 
B 1 190 CYS 190 190 190 CYS CYS B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 SER 192 192 192 SER SER B . n 
B 1 193 ARG 193 193 193 ARG ARG B . n 
B 1 194 TYR 194 194 194 TYR TYR B . n 
B 1 195 SER 195 195 195 SER SER B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 ASN 198 198 198 ASN ASN B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 ALA 200 200 200 ALA ALA B . n 
B 1 201 ILE 201 201 201 ILE ILE B . n 
B 1 202 LEU 202 202 202 LEU LEU B . n 
B 1 203 PHE 203 203 203 PHE PHE B . n 
B 1 204 GLY 204 204 204 GLY GLY B . n 
B 1 205 ASP 205 205 205 ASP ASP B . n 
B 1 206 ILE 206 206 206 ILE ILE B . n 
B 1 207 ASN 207 207 207 ASN ASN B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 ASN 210 210 210 ASN ASN B . n 
B 1 211 ASN 211 211 211 ASN ASN B . n 
B 1 212 ASN 212 212 212 ASN ASN B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 TYR 214 214 214 TYR TYR B . n 
B 1 215 ILE 215 215 215 ILE ILE B . n 
B 1 216 HIS 216 216 216 HIS HIS B . n 
B 1 217 ASN 217 217 217 ASN ASN B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 LEU 219 219 219 LEU LEU B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 VAL 221 221 221 VAL VAL B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 HIS 223 223 223 HIS HIS B . n 
B 1 224 ASP 224 224 224 ASP ASP B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 TYR 227 227 227 TYR TYR B . n 
B 1 228 THR 228 228 228 THR THR B . n 
B 1 229 PRO 229 229 229 PRO PRO B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 ILE 232 232 232 ILE ILE B . n 
B 1 233 SER 233 233 233 SER SER B . n 
B 1 234 LYS 234 234 234 LYS LYS B . n 
B 1 235 GLN 235 235 235 GLN GLN B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 GLU 237 237 237 GLU GLU B . n 
B 1 238 TYR 238 238 238 TYR TYR B . n 
B 1 239 PHE 239 239 239 PHE PHE B . n 
B 1 240 ILE 240 240 240 ILE ILE B . n 
B 1 241 GLN 241 241 241 GLN GLN B . n 
B 1 242 VAL 242 242 242 VAL VAL B . n 
B 1 243 ASN 243 243 243 ASN ASN B . n 
B 1 244 ALA 244 244 244 ALA ALA B . n 
B 1 245 ILE 245 245 245 ILE ILE B . n 
B 1 246 ARG 246 246 246 ARG ARG B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASN 248 248 248 ASN ASN B . n 
B 1 249 LYS 249 249 249 LYS LYS B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 VAL 252 252 252 VAL VAL B . n 
B 1 253 ILE 253 253 253 ILE ILE B . n 
B 1 254 PRO 254 254 254 PRO PRO B . n 
B 1 255 THR 255 255 255 THR THR B . n 
B 1 256 LYS 256 256 ?   ?   ?   B . n 
B 1 257 ASN 257 257 ?   ?   ?   B . n 
B 1 258 PRO 258 258 ?   ?   ?   B . n 
B 1 259 PHE 259 259 ?   ?   ?   B . n 
B 1 260 ILE 260 260 ?   ?   ?   B . n 
B 1 261 SER 261 261 ?   ?   ?   B . n 
B 1 262 PRO 262 262 ?   ?   ?   B . n 
B 1 263 SER 263 263 ?   ?   ?   B . n 
B 1 264 SER 264 264 ?   ?   ?   B . n 
B 1 265 THR 265 265 ?   ?   ?   B . n 
B 1 266 SER 266 266 ?   ?   ?   B . n 
B 1 267 TYR 267 267 ?   ?   ?   B . n 
B 1 268 HIS 268 268 ?   ?   ?   B . n 
B 1 269 GLY 269 269 ?   ?   ?   B . n 
B 1 270 SER 270 270 ?   ?   ?   B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 GLU 272 272 272 GLU GLU B . n 
B 1 273 ILE 273 273 273 ILE ILE B . n 
B 1 274 GLY 274 274 274 GLY GLY B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 ILE 278 278 278 ILE ILE B . n 
B 1 279 THR 279 279 279 THR THR B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 THR 281 281 281 THR THR B . n 
B 1 282 HIS 282 282 282 HIS HIS B . n 
B 1 283 PRO 283 283 283 PRO PRO B . n 
B 1 284 TYR 284 284 284 TYR TYR B . n 
B 1 285 THR 285 285 285 THR THR B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 SER 288 288 288 SER SER B . n 
B 1 289 HIS 289 289 289 HIS HIS B . n 
B 1 290 SER 290 290 290 SER SER B . n 
B 1 291 ILE 291 291 291 ILE ILE B . n 
B 1 292 PHE 292 292 292 PHE PHE B . n 
B 1 293 GLU 293 293 293 GLU GLU B . n 
B 1 294 VAL 294 294 294 VAL VAL B . n 
B 1 295 PHE 295 295 295 PHE PHE B . n 
B 1 296 THR 296 296 296 THR THR B . n 
B 1 297 GLN 297 297 297 GLN GLN B . n 
B 1 298 VAL 298 298 298 VAL VAL B . n 
B 1 299 PHE 299 299 299 PHE PHE B . n 
B 1 300 ALA 300 300 300 ALA ALA B . n 
B 1 301 ASN 301 301 301 ASN ASN B . n 
B 1 302 ASN 302 302 302 ASN ASN B . n 
B 1 303 MET 303 303 303 MET MET B . n 
B 1 304 PRO 304 304 304 PRO PRO B . n 
B 1 305 LYS 305 305 305 LYS LYS B . n 
B 1 306 GLN 306 306 306 GLN GLN B . n 
B 1 307 ALA 307 307 307 ALA ALA B . n 
B 1 308 GLN 308 308 308 GLN GLN B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 LYS 310 310 310 LYS LYS B . n 
B 1 311 ALA 311 311 311 ALA ALA B . n 
B 1 312 VAL 312 312 312 VAL VAL B . n 
B 1 313 GLY 313 313 313 GLY GLY B . n 
B 1 314 PRO 314 314 314 PRO PRO B . n 
B 1 315 PHE 315 315 315 PHE PHE B . n 
B 1 316 GLY 316 316 316 GLY GLY B . n 
B 1 317 LEU 317 317 317 LEU LEU B . n 
B 1 318 CYS 318 318 318 CYS CYS B . n 
B 1 319 TYR 319 319 319 TYR TYR B . n 
B 1 320 ASP 320 320 320 ASP ASP B . n 
B 1 321 SER 321 321 321 SER SER B . n 
B 1 322 ARG 322 322 322 ARG ARG B . n 
B 1 323 LYS 323 323 323 LYS LYS B . n 
B 1 324 ILE 324 324 324 ILE ILE B . n 
B 1 325 SER 325 325 325 SER SER B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 GLY 327 327 327 GLY GLY B . n 
B 1 328 ALA 328 328 328 ALA ALA B . n 
B 1 329 PRO 329 329 329 PRO PRO B . n 
B 1 330 SER 330 330 330 SER SER B . n 
B 1 331 VAL 331 331 331 VAL VAL B . n 
B 1 332 ASP 332 332 332 ASP ASP B . n 
B 1 333 LEU 333 333 333 LEU LEU B . n 
B 1 334 ILE 334 334 334 ILE ILE B . n 
B 1 335 LEU 335 335 335 LEU LEU B . n 
B 1 336 ASP 336 336 336 ASP ASP B . n 
B 1 337 LYS 337 337 337 LYS LYS B . n 
B 1 338 ASN 338 338 338 ASN ASN B . n 
B 1 339 ASP 339 339 339 ASP ASP B . n 
B 1 340 ALA 340 340 340 ALA ALA B . n 
B 1 341 VAL 341 341 341 VAL VAL B . n 
B 1 342 TRP 342 342 342 TRP TRP B . n 
B 1 343 ARG 343 343 343 ARG ARG B . n 
B 1 344 ILE 344 344 344 ILE ILE B . n 
B 1 345 SER 345 345 345 SER SER B . n 
B 1 346 SER 346 346 346 SER SER B . n 
B 1 347 GLU 347 347 347 GLU GLU B . n 
B 1 348 ASN 348 348 348 ASN ASN B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 MET 350 350 350 MET MET B . n 
B 1 351 VAL 351 351 351 VAL VAL B . n 
B 1 352 GLN 352 352 352 GLN GLN B . n 
B 1 353 ALA 353 353 353 ALA ALA B . n 
B 1 354 GLN 354 354 354 GLN GLN B . n 
B 1 355 ASP 355 355 355 ASP ASP B . n 
B 1 356 GLY 356 356 356 GLY GLY B . n 
B 1 357 VAL 357 357 357 VAL VAL B . n 
B 1 358 SER 358 358 358 SER SER B . n 
B 1 359 CYS 359 359 359 CYS CYS B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 GLY 361 361 361 GLY GLY B . n 
B 1 362 PHE 362 362 362 PHE PHE B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 ASP 364 364 364 ASP ASP B . n 
B 1 365 GLY 365 365 365 GLY GLY B . n 
B 1 366 GLY 366 366 366 GLY GLY B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 HIS 368 368 368 HIS HIS B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 ARG 370 370 370 ARG ARG B . n 
B 1 371 ALA 371 371 371 ALA ALA B . n 
B 1 372 GLY 372 372 372 GLY GLY B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 ALA 374 374 374 ALA ALA B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 GLY 376 376 376 GLY GLY B . n 
B 1 377 ALA 377 377 377 ALA ALA B . n 
B 1 378 HIS 378 378 378 HIS HIS B . n 
B 1 379 HIS 379 379 379 HIS HIS B . n 
B 1 380 LEU 380 380 380 LEU LEU B . n 
B 1 381 GLU 381 381 381 GLU GLU B . n 
B 1 382 GLU 382 382 382 GLU GLU B . n 
B 1 383 ASN 383 383 383 ASN ASN B . n 
B 1 384 LEU 384 384 384 LEU LEU B . n 
B 1 385 VAL 385 385 385 VAL VAL B . n 
B 1 386 VAL 386 386 386 VAL VAL B . n 
B 1 387 PHE 387 387 387 PHE PHE B . n 
B 1 388 ASP 388 388 388 ASP ASP B . n 
B 1 389 LEU 389 389 389 LEU LEU B . n 
B 1 390 GLU 390 390 390 GLU GLU B . n 
B 1 391 ARG 391 391 391 ARG ARG B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 ARG 393 393 393 ARG ARG B . n 
B 1 394 VAL 394 394 394 VAL VAL B . n 
B 1 395 GLY 395 395 395 GLY GLY B . n 
B 1 396 PHE 396 396 396 PHE PHE B . n 
B 1 397 ASN 397 397 397 ASN ASN B . n 
B 1 398 SER 398 398 398 SER SER B . n 
B 1 399 ASN 399 399 399 ASN ASN B . n 
B 1 400 SER 400 400 400 SER SER B . n 
B 1 401 LEU 401 401 401 LEU LEU B . n 
B 1 402 LYS 402 402 402 LYS LYS B . n 
B 1 403 SER 403 403 403 SER SER B . n 
B 1 404 TYR 404 404 404 TYR TYR B . n 
B 1 405 GLY 405 405 405 GLY GLY B . n 
B 1 406 LYS 406 406 406 LYS LYS B . n 
B 1 407 THR 407 407 407 THR THR B . n 
B 1 408 CYS 408 408 408 CYS CYS B . n 
B 1 409 SER 409 409 409 SER SER B . n 
B 1 410 ASN 410 410 410 ASN ASN B . n 
B 1 411 LEU 411 411 411 LEU LEU B . n 
B 1 412 PHE 412 412 412 PHE PHE B . n 
B 1 413 ASP 413 413 413 ASP ASP B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 ASN 415 415 415 ASN ASN B . n 
B 1 416 ASN 416 416 416 ASN ASN B . n 
B 1 417 PRO 417 417 ?   ?   ?   B . n 
C 1 1   LEU 1   1   ?   ?   ?   C . n 
C 1 2   TYR 2   2   ?   ?   ?   C . n 
C 1 3   HIS 3   3   ?   ?   ?   C . n 
C 1 4   ASN 4   4   ?   ?   ?   C . n 
C 1 5   SER 5   5   ?   ?   ?   C . n 
C 1 6   GLN 6   6   ?   ?   ?   C . n 
C 1 7   PRO 7   7   ?   ?   ?   C . n 
C 1 8   THR 8   8   ?   ?   ?   C . n 
C 1 9   SER 9   9   ?   ?   ?   C . n 
C 1 10  SER 10  10  ?   ?   ?   C . n 
C 1 11  LYS 11  11  11  LYS LYS C . n 
C 1 12  PRO 12  12  12  PRO PRO C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  LEU 14  14  14  LEU LEU C . n 
C 1 15  LEU 15  15  15  LEU LEU C . n 
C 1 16  VAL 16  16  16  VAL VAL C . n 
C 1 17  LEU 17  17  17  LEU LEU C . n 
C 1 18  PRO 18  18  18  PRO PRO C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  GLN 20  20  20  GLN GLN C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  ASP 22  22  22  ASP ASP C . n 
C 1 23  ALA 23  23  23  ALA ALA C . n 
C 1 24  SER 24  24  24  SER SER C . n 
C 1 25  THR 25  25  25  THR THR C . n 
C 1 26  GLY 26  26  26  GLY GLY C . n 
C 1 27  LEU 27  27  27  LEU LEU C . n 
C 1 28  HIS 28  28  28  HIS HIS C . n 
C 1 29  TRP 29  29  29  TRP TRP C . n 
C 1 30  ALA 30  30  30  ALA ALA C . n 
C 1 31  ASN 31  31  31  ASN ASN C . n 
C 1 32  ILE 32  32  32  ILE ILE C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  LYS 34  34  34  LYS LYS C . n 
C 1 35  ARG 35  35  35  ARG ARG C . n 
C 1 36  THR 36  36  36  THR THR C . n 
C 1 37  PRO 37  37  37  PRO PRO C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  MET 39  39  39  MET MET C . n 
C 1 40  GLN 40  40  40  GLN GLN C . n 
C 1 41  VAL 41  41  41  VAL VAL C . n 
C 1 42  PRO 42  42  42  PRO PRO C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  LEU 44  44  44  LEU LEU C . n 
C 1 45  LEU 45  45  45  LEU LEU C . n 
C 1 46  ASP 46  46  46  ASP ASP C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  ASN 48  48  48  ASN ASN C . n 
C 1 49  GLY 49  49  49  GLY GLY C . n 
C 1 50  LYS 50  50  50  LYS LYS C . n 
C 1 51  HIS 51  51  51  HIS HIS C . n 
C 1 52  LEU 52  52  52  LEU LEU C . n 
C 1 53  TRP 53  53  53  TRP TRP C . n 
C 1 54  VAL 54  54  54  VAL VAL C . n 
C 1 55  THR 55  55  55  THR THR C . n 
C 1 56  CYS 56  56  56  CYS CYS C . n 
C 1 57  SER 57  57  57  SER SER C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  HIS 59  59  59  HIS HIS C . n 
C 1 60  TYR 60  60  60  TYR TYR C . n 
C 1 61  SER 61  61  61  SER SER C . n 
C 1 62  SER 62  62  62  SER SER C . n 
C 1 63  SER 63  63  63  SER SER C . n 
C 1 64  THR 64  64  64  THR THR C . n 
C 1 65  TYR 65  65  65  TYR TYR C . n 
C 1 66  GLN 66  66  66  GLN GLN C . n 
C 1 67  ALA 67  67  67  ALA ALA C . n 
C 1 68  PRO 68  68  68  PRO PRO C . n 
C 1 69  PHE 69  69  69  PHE PHE C . n 
C 1 70  CYS 70  70  70  CYS CYS C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  SER 72  72  72  SER SER C . n 
C 1 73  THR 73  73  73  THR THR C . n 
C 1 74  GLN 74  74  74  GLN GLN C . n 
C 1 75  CYS 75  75  75  CYS CYS C . n 
C 1 76  SER 76  76  76  SER SER C . n 
C 1 77  ARG 77  77  77  ARG ARG C . n 
C 1 78  ALA 78  78  78  ALA ALA C . n 
C 1 79  ASN 79  79  79  ASN ASN C . n 
C 1 80  THR 80  80  80  THR THR C . n 
C 1 81  HIS 81  81  81  HIS HIS C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  CYS 83  83  83  CYS CYS C . n 
C 1 84  PHE 84  84  84  PHE PHE C . n 
C 1 85  THR 85  85  85  THR THR C . n 
C 1 86  CYS 86  86  86  CYS CYS C . n 
C 1 87  THR 87  87  87  THR THR C . n 
C 1 88  ASP 88  88  88  ASP ASP C . n 
C 1 89  SER 89  89  89  SER SER C . n 
C 1 90  THR 90  90  90  THR THR C . n 
C 1 91  THR 91  91  91  THR THR C . n 
C 1 92  THR 92  92  92  THR THR C . n 
C 1 93  ARG 93  93  93  ARG ARG C . n 
C 1 94  PRO 94  94  94  PRO PRO C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  CYS 96  96  96  CYS CYS C . n 
C 1 97  HIS 97  97  97  HIS HIS C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASN 99  99  99  ASN ASN C . n 
C 1 100 THR 100 100 100 THR THR C . n 
C 1 101 CYS 101 101 101 CYS CYS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 LEU 103 103 103 LEU LEU C . n 
C 1 104 LEU 104 104 104 LEU LEU C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 SER 106 106 106 SER SER C . n 
C 1 107 ASN 107 107 107 ASN ASN C . n 
C 1 108 PRO 108 108 108 PRO PRO C . n 
C 1 109 VAL 109 109 109 VAL VAL C . n 
C 1 110 THR 110 110 110 THR THR C . n 
C 1 111 GLN 111 111 111 GLN GLN C . n 
C 1 112 GLU 112 112 112 GLU GLU C . n 
C 1 113 SER 113 113 113 SER SER C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 LEU 115 115 115 LEU LEU C . n 
C 1 116 GLY 116 116 116 GLY GLY C . n 
C 1 117 GLU 117 117 117 GLU GLU C . n 
C 1 118 LEU 118 118 118 LEU LEU C . n 
C 1 119 ALA 119 119 119 ALA ALA C . n 
C 1 120 GLN 120 120 120 GLN GLN C . n 
C 1 121 ASP 121 121 121 ASP ASP C . n 
C 1 122 VAL 122 122 122 VAL VAL C . n 
C 1 123 LEU 123 123 123 LEU LEU C . n 
C 1 124 ALA 124 124 124 ALA ALA C . n 
C 1 125 ILE 125 125 125 ILE ILE C . n 
C 1 126 HIS 126 126 126 HIS HIS C . n 
C 1 127 SER 127 127 127 SER SER C . n 
C 1 128 THR 128 128 128 THR THR C . n 
C 1 129 HIS 129 129 129 HIS HIS C . n 
C 1 130 GLY 130 130 130 GLY GLY C . n 
C 1 131 SER 131 131 131 SER SER C . n 
C 1 132 LYS 132 132 132 LYS LYS C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 GLY 134 134 134 GLY GLY C . n 
C 1 135 PRO 135 135 135 PRO PRO C . n 
C 1 136 MET 136 136 136 MET MET C . n 
C 1 137 VAL 137 137 137 VAL VAL C . n 
C 1 138 LYS 138 138 138 LYS LYS C . n 
C 1 139 VAL 139 139 139 VAL VAL C . n 
C 1 140 PRO 140 140 140 PRO PRO C . n 
C 1 141 GLN 141 141 141 GLN GLN C . n 
C 1 142 PHE 142 142 142 PHE PHE C . n 
C 1 143 LEU 143 143 143 LEU LEU C . n 
C 1 144 PHE 144 144 144 PHE PHE C . n 
C 1 145 SER 145 145 145 SER SER C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 ALA 147 147 147 ALA ALA C . n 
C 1 148 PRO 148 148 148 PRO PRO C . n 
C 1 149 SER 149 149 149 SER SER C . n 
C 1 150 PHE 150 150 150 PHE PHE C . n 
C 1 151 LEU 151 151 151 LEU LEU C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . n 
C 1 154 LYS 154 154 154 LYS LYS C . n 
C 1 155 GLY 155 155 155 GLY GLY C . n 
C 1 156 LEU 156 156 156 LEU LEU C . n 
C 1 157 PRO 157 157 157 PRO PRO C . n 
C 1 158 ASN 158 158 158 ASN ASN C . n 
C 1 159 ASN 159 159 159 ASN ASN C . n 
C 1 160 VAL 160 160 160 VAL VAL C . n 
C 1 161 GLN 161 161 161 GLN GLN C . n 
C 1 162 GLY 162 162 162 GLY GLY C . n 
C 1 163 ALA 163 163 163 ALA ALA C . n 
C 1 164 LEU 164 164 164 LEU LEU C . n 
C 1 165 GLY 165 165 165 GLY GLY C . n 
C 1 166 LEU 166 166 166 LEU LEU C . n 
C 1 167 GLY 167 167 167 GLY GLY C . n 
C 1 168 GLN 168 168 168 GLN GLN C . n 
C 1 169 ALA 169 169 169 ALA ALA C . n 
C 1 170 PRO 170 170 170 PRO PRO C . n 
C 1 171 ILE 171 171 171 ILE ILE C . n 
C 1 172 SER 172 172 172 SER SER C . n 
C 1 173 LEU 173 173 173 LEU LEU C . n 
C 1 174 GLN 174 174 174 GLN GLN C . n 
C 1 175 ASN 175 175 175 ASN ASN C . n 
C 1 176 GLN 176 176 176 GLN GLN C . n 
C 1 177 LEU 177 177 177 LEU LEU C . n 
C 1 178 PHE 178 178 178 PHE PHE C . n 
C 1 179 SER 179 179 179 SER SER C . n 
C 1 180 HIS 180 180 180 HIS HIS C . n 
C 1 181 PHE 181 181 181 PHE PHE C . n 
C 1 182 GLY 182 182 182 GLY GLY C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 LYS 184 184 184 LYS LYS C . n 
C 1 185 ARG 185 185 185 ARG ARG C . n 
C 1 186 GLN 186 186 186 GLN GLN C . n 
C 1 187 PHE 187 187 187 PHE PHE C . n 
C 1 188 SER 188 188 188 SER SER C . n 
C 1 189 VAL 189 189 189 VAL VAL C . n 
C 1 190 CYS 190 190 190 CYS CYS C . n 
C 1 191 LEU 191 191 191 LEU LEU C . n 
C 1 192 SER 192 192 192 SER SER C . n 
C 1 193 ARG 193 193 193 ARG ARG C . n 
C 1 194 TYR 194 194 194 TYR TYR C . n 
C 1 195 SER 195 195 195 SER SER C . n 
C 1 196 THR 196 196 196 THR THR C . n 
C 1 197 SER 197 197 197 SER SER C . n 
C 1 198 ASN 198 198 198 ASN ASN C . n 
C 1 199 GLY 199 199 199 GLY GLY C . n 
C 1 200 ALA 200 200 200 ALA ALA C . n 
C 1 201 ILE 201 201 201 ILE ILE C . n 
C 1 202 LEU 202 202 202 LEU LEU C . n 
C 1 203 PHE 203 203 203 PHE PHE C . n 
C 1 204 GLY 204 204 204 GLY GLY C . n 
C 1 205 ASP 205 205 205 ASP ASP C . n 
C 1 206 ILE 206 206 206 ILE ILE C . n 
C 1 207 ASN 207 207 207 ASN ASN C . n 
C 1 208 ASP 208 208 208 ASP ASP C . n 
C 1 209 PRO 209 209 209 PRO PRO C . n 
C 1 210 ASN 210 210 210 ASN ASN C . n 
C 1 211 ASN 211 211 211 ASN ASN C . n 
C 1 212 ASN 212 212 212 ASN ASN C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 TYR 214 214 214 TYR TYR C . n 
C 1 215 ILE 215 215 215 ILE ILE C . n 
C 1 216 HIS 216 216 216 HIS HIS C . n 
C 1 217 ASN 217 217 217 ASN ASN C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 LEU 219 219 219 LEU LEU C . n 
C 1 220 ASP 220 220 220 ASP ASP C . n 
C 1 221 VAL 221 221 221 VAL VAL C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 HIS 223 223 223 HIS HIS C . n 
C 1 224 ASP 224 224 224 ASP ASP C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 VAL 226 226 226 VAL VAL C . n 
C 1 227 TYR 227 227 227 TYR TYR C . n 
C 1 228 THR 228 228 228 THR THR C . n 
C 1 229 PRO 229 229 229 PRO PRO C . n 
C 1 230 LEU 230 230 230 LEU LEU C . n 
C 1 231 THR 231 231 231 THR THR C . n 
C 1 232 ILE 232 232 232 ILE ILE C . n 
C 1 233 SER 233 233 233 SER SER C . n 
C 1 234 LYS 234 234 234 LYS LYS C . n 
C 1 235 GLN 235 235 235 GLN GLN C . n 
C 1 236 GLY 236 236 236 GLY GLY C . n 
C 1 237 GLU 237 237 237 GLU GLU C . n 
C 1 238 TYR 238 238 238 TYR TYR C . n 
C 1 239 PHE 239 239 239 PHE PHE C . n 
C 1 240 ILE 240 240 240 ILE ILE C . n 
C 1 241 GLN 241 241 241 GLN GLN C . n 
C 1 242 VAL 242 242 242 VAL VAL C . n 
C 1 243 ASN 243 243 243 ASN ASN C . n 
C 1 244 ALA 244 244 244 ALA ALA C . n 
C 1 245 ILE 245 245 245 ILE ILE C . n 
C 1 246 ARG 246 246 246 ARG ARG C . n 
C 1 247 VAL 247 247 247 VAL VAL C . n 
C 1 248 ASN 248 248 248 ASN ASN C . n 
C 1 249 LYS 249 249 249 LYS LYS C . n 
C 1 250 HIS 250 250 250 HIS HIS C . n 
C 1 251 LEU 251 251 251 LEU LEU C . n 
C 1 252 VAL 252 252 252 VAL VAL C . n 
C 1 253 ILE 253 253 253 ILE ILE C . n 
C 1 254 PRO 254 254 254 PRO PRO C . n 
C 1 255 THR 255 255 255 THR THR C . n 
C 1 256 LYS 256 256 ?   ?   ?   C . n 
C 1 257 ASN 257 257 ?   ?   ?   C . n 
C 1 258 PRO 258 258 ?   ?   ?   C . n 
C 1 259 PHE 259 259 ?   ?   ?   C . n 
C 1 260 ILE 260 260 ?   ?   ?   C . n 
C 1 261 SER 261 261 ?   ?   ?   C . n 
C 1 262 PRO 262 262 ?   ?   ?   C . n 
C 1 263 SER 263 263 ?   ?   ?   C . n 
C 1 264 SER 264 264 ?   ?   ?   C . n 
C 1 265 THR 265 265 ?   ?   ?   C . n 
C 1 266 SER 266 266 ?   ?   ?   C . n 
C 1 267 TYR 267 267 ?   ?   ?   C . n 
C 1 268 HIS 268 268 ?   ?   ?   C . n 
C 1 269 GLY 269 269 ?   ?   ?   C . n 
C 1 270 SER 270 270 ?   ?   ?   C . n 
C 1 271 GLY 271 271 271 GLY GLY C . n 
C 1 272 GLU 272 272 272 GLU GLU C . n 
C 1 273 ILE 273 273 273 ILE ILE C . n 
C 1 274 GLY 274 274 274 GLY GLY C . n 
C 1 275 GLY 275 275 275 GLY GLY C . n 
C 1 276 ALA 276 276 276 ALA ALA C . n 
C 1 277 LEU 277 277 277 LEU LEU C . n 
C 1 278 ILE 278 278 278 ILE ILE C . n 
C 1 279 THR 279 279 279 THR THR C . n 
C 1 280 THR 280 280 280 THR THR C . n 
C 1 281 THR 281 281 281 THR THR C . n 
C 1 282 HIS 282 282 282 HIS HIS C . n 
C 1 283 PRO 283 283 283 PRO PRO C . n 
C 1 284 TYR 284 284 284 TYR TYR C . n 
C 1 285 THR 285 285 285 THR THR C . n 
C 1 286 VAL 286 286 286 VAL VAL C . n 
C 1 287 LEU 287 287 287 LEU LEU C . n 
C 1 288 SER 288 288 288 SER SER C . n 
C 1 289 HIS 289 289 289 HIS HIS C . n 
C 1 290 SER 290 290 290 SER SER C . n 
C 1 291 ILE 291 291 291 ILE ILE C . n 
C 1 292 PHE 292 292 292 PHE PHE C . n 
C 1 293 GLU 293 293 293 GLU GLU C . n 
C 1 294 VAL 294 294 294 VAL VAL C . n 
C 1 295 PHE 295 295 295 PHE PHE C . n 
C 1 296 THR 296 296 296 THR THR C . n 
C 1 297 GLN 297 297 297 GLN GLN C . n 
C 1 298 VAL 298 298 298 VAL VAL C . n 
C 1 299 PHE 299 299 299 PHE PHE C . n 
C 1 300 ALA 300 300 300 ALA ALA C . n 
C 1 301 ASN 301 301 301 ASN ASN C . n 
C 1 302 ASN 302 302 302 ASN ASN C . n 
C 1 303 MET 303 303 303 MET MET C . n 
C 1 304 PRO 304 304 304 PRO PRO C . n 
C 1 305 LYS 305 305 305 LYS LYS C . n 
C 1 306 GLN 306 306 306 GLN GLN C . n 
C 1 307 ALA 307 307 307 ALA ALA C . n 
C 1 308 GLN 308 308 308 GLN GLN C . n 
C 1 309 VAL 309 309 309 VAL VAL C . n 
C 1 310 LYS 310 310 310 LYS LYS C . n 
C 1 311 ALA 311 311 311 ALA ALA C . n 
C 1 312 VAL 312 312 312 VAL VAL C . n 
C 1 313 GLY 313 313 313 GLY GLY C . n 
C 1 314 PRO 314 314 314 PRO PRO C . n 
C 1 315 PHE 315 315 315 PHE PHE C . n 
C 1 316 GLY 316 316 316 GLY GLY C . n 
C 1 317 LEU 317 317 317 LEU LEU C . n 
C 1 318 CYS 318 318 318 CYS CYS C . n 
C 1 319 TYR 319 319 319 TYR TYR C . n 
C 1 320 ASP 320 320 320 ASP ASP C . n 
C 1 321 SER 321 321 321 SER SER C . n 
C 1 322 ARG 322 322 322 ARG ARG C . n 
C 1 323 LYS 323 323 323 LYS LYS C . n 
C 1 324 ILE 324 324 324 ILE ILE C . n 
C 1 325 SER 325 325 325 SER SER C . n 
C 1 326 GLY 326 326 326 GLY GLY C . n 
C 1 327 GLY 327 327 327 GLY GLY C . n 
C 1 328 ALA 328 328 328 ALA ALA C . n 
C 1 329 PRO 329 329 329 PRO PRO C . n 
C 1 330 SER 330 330 330 SER SER C . n 
C 1 331 VAL 331 331 331 VAL VAL C . n 
C 1 332 ASP 332 332 332 ASP ASP C . n 
C 1 333 LEU 333 333 333 LEU LEU C . n 
C 1 334 ILE 334 334 334 ILE ILE C . n 
C 1 335 LEU 335 335 335 LEU LEU C . n 
C 1 336 ASP 336 336 336 ASP ASP C . n 
C 1 337 LYS 337 337 337 LYS LYS C . n 
C 1 338 ASN 338 338 338 ASN ASN C . n 
C 1 339 ASP 339 339 339 ASP ASP C . n 
C 1 340 ALA 340 340 340 ALA ALA C . n 
C 1 341 VAL 341 341 341 VAL VAL C . n 
C 1 342 TRP 342 342 342 TRP TRP C . n 
C 1 343 ARG 343 343 343 ARG ARG C . n 
C 1 344 ILE 344 344 344 ILE ILE C . n 
C 1 345 SER 345 345 345 SER SER C . n 
C 1 346 SER 346 346 346 SER SER C . n 
C 1 347 GLU 347 347 347 GLU GLU C . n 
C 1 348 ASN 348 348 348 ASN ASN C . n 
C 1 349 PHE 349 349 349 PHE PHE C . n 
C 1 350 MET 350 350 350 MET MET C . n 
C 1 351 VAL 351 351 351 VAL VAL C . n 
C 1 352 GLN 352 352 352 GLN GLN C . n 
C 1 353 ALA 353 353 353 ALA ALA C . n 
C 1 354 GLN 354 354 354 GLN GLN C . n 
C 1 355 ASP 355 355 355 ASP ASP C . n 
C 1 356 GLY 356 356 356 GLY GLY C . n 
C 1 357 VAL 357 357 357 VAL VAL C . n 
C 1 358 SER 358 358 358 SER SER C . n 
C 1 359 CYS 359 359 359 CYS CYS C . n 
C 1 360 LEU 360 360 360 LEU LEU C . n 
C 1 361 GLY 361 361 361 GLY GLY C . n 
C 1 362 PHE 362 362 362 PHE PHE C . n 
C 1 363 VAL 363 363 363 VAL VAL C . n 
C 1 364 ASP 364 364 364 ASP ASP C . n 
C 1 365 GLY 365 365 365 GLY GLY C . n 
C 1 366 GLY 366 366 366 GLY GLY C . n 
C 1 367 VAL 367 367 367 VAL VAL C . n 
C 1 368 HIS 368 368 368 HIS HIS C . n 
C 1 369 ALA 369 369 369 ALA ALA C . n 
C 1 370 ARG 370 370 370 ARG ARG C . n 
C 1 371 ALA 371 371 371 ALA ALA C . n 
C 1 372 GLY 372 372 372 GLY GLY C . n 
C 1 373 ILE 373 373 373 ILE ILE C . n 
C 1 374 ALA 374 374 374 ALA ALA C . n 
C 1 375 LEU 375 375 375 LEU LEU C . n 
C 1 376 GLY 376 376 376 GLY GLY C . n 
C 1 377 ALA 377 377 377 ALA ALA C . n 
C 1 378 HIS 378 378 378 HIS HIS C . n 
C 1 379 HIS 379 379 379 HIS HIS C . n 
C 1 380 LEU 380 380 380 LEU LEU C . n 
C 1 381 GLU 381 381 381 GLU GLU C . n 
C 1 382 GLU 382 382 382 GLU GLU C . n 
C 1 383 ASN 383 383 383 ASN ASN C . n 
C 1 384 LEU 384 384 384 LEU LEU C . n 
C 1 385 VAL 385 385 385 VAL VAL C . n 
C 1 386 VAL 386 386 386 VAL VAL C . n 
C 1 387 PHE 387 387 387 PHE PHE C . n 
C 1 388 ASP 388 388 388 ASP ASP C . n 
C 1 389 LEU 389 389 389 LEU LEU C . n 
C 1 390 GLU 390 390 390 GLU GLU C . n 
C 1 391 ARG 391 391 391 ARG ARG C . n 
C 1 392 SER 392 392 392 SER SER C . n 
C 1 393 ARG 393 393 393 ARG ARG C . n 
C 1 394 VAL 394 394 394 VAL VAL C . n 
C 1 395 GLY 395 395 395 GLY GLY C . n 
C 1 396 PHE 396 396 396 PHE PHE C . n 
C 1 397 ASN 397 397 397 ASN ASN C . n 
C 1 398 SER 398 398 398 SER SER C . n 
C 1 399 ASN 399 399 399 ASN ASN C . n 
C 1 400 SER 400 400 400 SER SER C . n 
C 1 401 LEU 401 401 401 LEU LEU C . n 
C 1 402 LYS 402 402 402 LYS LYS C . n 
C 1 403 SER 403 403 403 SER SER C . n 
C 1 404 TYR 404 404 404 TYR TYR C . n 
C 1 405 GLY 405 405 405 GLY GLY C . n 
C 1 406 LYS 406 406 406 LYS LYS C . n 
C 1 407 THR 407 407 407 THR THR C . n 
C 1 408 CYS 408 408 408 CYS CYS C . n 
C 1 409 SER 409 409 409 SER SER C . n 
C 1 410 ASN 410 410 410 ASN ASN C . n 
C 1 411 LEU 411 411 411 LEU LEU C . n 
C 1 412 PHE 412 412 412 PHE PHE C . n 
C 1 413 ASP 413 413 413 ASP ASP C . n 
C 1 414 LEU 414 414 414 LEU LEU C . n 
C 1 415 ASN 415 415 415 ASN ASN C . n 
C 1 416 ASN 416 416 416 ASN ASN C . n 
C 1 417 PRO 417 417 417 PRO PRO C . n 
D 1 1   LEU 1   1   ?   ?   ?   D . n 
D 1 2   TYR 2   2   ?   ?   ?   D . n 
D 1 3   HIS 3   3   ?   ?   ?   D . n 
D 1 4   ASN 4   4   ?   ?   ?   D . n 
D 1 5   SER 5   5   ?   ?   ?   D . n 
D 1 6   GLN 6   6   ?   ?   ?   D . n 
D 1 7   PRO 7   7   ?   ?   ?   D . n 
D 1 8   THR 8   8   ?   ?   ?   D . n 
D 1 9   SER 9   9   ?   ?   ?   D . n 
D 1 10  SER 10  10  10  SER SER D . n 
D 1 11  LYS 11  11  11  LYS LYS D . n 
D 1 12  PRO 12  12  12  PRO PRO D . n 
D 1 13  ASN 13  13  13  ASN ASN D . n 
D 1 14  LEU 14  14  14  LEU LEU D . n 
D 1 15  LEU 15  15  15  LEU LEU D . n 
D 1 16  VAL 16  16  16  VAL VAL D . n 
D 1 17  LEU 17  17  17  LEU LEU D . n 
D 1 18  PRO 18  18  18  PRO PRO D . n 
D 1 19  VAL 19  19  19  VAL VAL D . n 
D 1 20  GLN 20  20  20  GLN GLN D . n 
D 1 21  GLU 21  21  21  GLU GLU D . n 
D 1 22  ASP 22  22  22  ASP ASP D . n 
D 1 23  ALA 23  23  23  ALA ALA D . n 
D 1 24  SER 24  24  24  SER SER D . n 
D 1 25  THR 25  25  25  THR THR D . n 
D 1 26  GLY 26  26  26  GLY GLY D . n 
D 1 27  LEU 27  27  27  LEU LEU D . n 
D 1 28  HIS 28  28  28  HIS HIS D . n 
D 1 29  TRP 29  29  29  TRP TRP D . n 
D 1 30  ALA 30  30  30  ALA ALA D . n 
D 1 31  ASN 31  31  31  ASN ASN D . n 
D 1 32  ILE 32  32  32  ILE ILE D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  LYS 34  34  34  LYS LYS D . n 
D 1 35  ARG 35  35  35  ARG ARG D . n 
D 1 36  THR 36  36  36  THR THR D . n 
D 1 37  PRO 37  37  37  PRO PRO D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  MET 39  39  39  MET MET D . n 
D 1 40  GLN 40  40  40  GLN GLN D . n 
D 1 41  VAL 41  41  41  VAL VAL D . n 
D 1 42  PRO 42  42  42  PRO PRO D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  LEU 44  44  44  LEU LEU D . n 
D 1 45  LEU 45  45  45  LEU LEU D . n 
D 1 46  ASP 46  46  46  ASP ASP D . n 
D 1 47  LEU 47  47  47  LEU LEU D . n 
D 1 48  ASN 48  48  48  ASN ASN D . n 
D 1 49  GLY 49  49  49  GLY GLY D . n 
D 1 50  LYS 50  50  50  LYS LYS D . n 
D 1 51  HIS 51  51  51  HIS HIS D . n 
D 1 52  LEU 52  52  52  LEU LEU D . n 
D 1 53  TRP 53  53  53  TRP TRP D . n 
D 1 54  VAL 54  54  54  VAL VAL D . n 
D 1 55  THR 55  55  55  THR THR D . n 
D 1 56  CYS 56  56  56  CYS CYS D . n 
D 1 57  SER 57  57  57  SER SER D . n 
D 1 58  GLN 58  58  58  GLN GLN D . n 
D 1 59  HIS 59  59  59  HIS HIS D . n 
D 1 60  TYR 60  60  60  TYR TYR D . n 
D 1 61  SER 61  61  61  SER SER D . n 
D 1 62  SER 62  62  62  SER SER D . n 
D 1 63  SER 63  63  63  SER SER D . n 
D 1 64  THR 64  64  64  THR THR D . n 
D 1 65  TYR 65  65  65  TYR TYR D . n 
D 1 66  GLN 66  66  66  GLN GLN D . n 
D 1 67  ALA 67  67  67  ALA ALA D . n 
D 1 68  PRO 68  68  68  PRO PRO D . n 
D 1 69  PHE 69  69  69  PHE PHE D . n 
D 1 70  CYS 70  70  70  CYS CYS D . n 
D 1 71  HIS 71  71  71  HIS HIS D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  THR 73  73  73  THR THR D . n 
D 1 74  GLN 74  74  74  GLN GLN D . n 
D 1 75  CYS 75  75  75  CYS CYS D . n 
D 1 76  SER 76  76  76  SER SER D . n 
D 1 77  ARG 77  77  77  ARG ARG D . n 
D 1 78  ALA 78  78  78  ALA ALA D . n 
D 1 79  ASN 79  79  79  ASN ASN D . n 
D 1 80  THR 80  80  80  THR THR D . n 
D 1 81  HIS 81  81  81  HIS HIS D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  CYS 83  83  83  CYS CYS D . n 
D 1 84  PHE 84  84  84  PHE PHE D . n 
D 1 85  THR 85  85  85  THR THR D . n 
D 1 86  CYS 86  86  86  CYS CYS D . n 
D 1 87  THR 87  87  87  THR THR D . n 
D 1 88  ASP 88  88  88  ASP ASP D . n 
D 1 89  SER 89  89  89  SER SER D . n 
D 1 90  THR 90  90  90  THR THR D . n 
D 1 91  THR 91  91  91  THR THR D . n 
D 1 92  THR 92  92  92  THR THR D . n 
D 1 93  ARG 93  93  93  ARG ARG D . n 
D 1 94  PRO 94  94  94  PRO PRO D . n 
D 1 95  GLY 95  95  95  GLY GLY D . n 
D 1 96  CYS 96  96  96  CYS CYS D . n 
D 1 97  HIS 97  97  97  HIS HIS D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  ASN 99  99  99  ASN ASN D . n 
D 1 100 THR 100 100 100 THR THR D . n 
D 1 101 CYS 101 101 101 CYS CYS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 LEU 103 103 103 LEU LEU D . n 
D 1 104 LEU 104 104 104 LEU LEU D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 SER 106 106 106 SER SER D . n 
D 1 107 ASN 107 107 107 ASN ASN D . n 
D 1 108 PRO 108 108 108 PRO PRO D . n 
D 1 109 VAL 109 109 109 VAL VAL D . n 
D 1 110 THR 110 110 110 THR THR D . n 
D 1 111 GLN 111 111 111 GLN GLN D . n 
D 1 112 GLU 112 112 112 GLU GLU D . n 
D 1 113 SER 113 113 113 SER SER D . n 
D 1 114 GLY 114 114 114 GLY GLY D . n 
D 1 115 LEU 115 115 115 LEU LEU D . n 
D 1 116 GLY 116 116 116 GLY GLY D . n 
D 1 117 GLU 117 117 117 GLU GLU D . n 
D 1 118 LEU 118 118 118 LEU LEU D . n 
D 1 119 ALA 119 119 119 ALA ALA D . n 
D 1 120 GLN 120 120 120 GLN GLN D . n 
D 1 121 ASP 121 121 121 ASP ASP D . n 
D 1 122 VAL 122 122 122 VAL VAL D . n 
D 1 123 LEU 123 123 123 LEU LEU D . n 
D 1 124 ALA 124 124 124 ALA ALA D . n 
D 1 125 ILE 125 125 125 ILE ILE D . n 
D 1 126 HIS 126 126 126 HIS HIS D . n 
D 1 127 SER 127 127 127 SER SER D . n 
D 1 128 THR 128 128 128 THR THR D . n 
D 1 129 HIS 129 129 129 HIS HIS D . n 
D 1 130 GLY 130 130 130 GLY GLY D . n 
D 1 131 SER 131 131 131 SER SER D . n 
D 1 132 LYS 132 132 132 LYS LYS D . n 
D 1 133 LEU 133 133 133 LEU LEU D . n 
D 1 134 GLY 134 134 134 GLY GLY D . n 
D 1 135 PRO 135 135 135 PRO PRO D . n 
D 1 136 MET 136 136 136 MET MET D . n 
D 1 137 VAL 137 137 137 VAL VAL D . n 
D 1 138 LYS 138 138 138 LYS LYS D . n 
D 1 139 VAL 139 139 139 VAL VAL D . n 
D 1 140 PRO 140 140 140 PRO PRO D . n 
D 1 141 GLN 141 141 141 GLN GLN D . n 
D 1 142 PHE 142 142 142 PHE PHE D . n 
D 1 143 LEU 143 143 143 LEU LEU D . n 
D 1 144 PHE 144 144 144 PHE PHE D . n 
D 1 145 SER 145 145 145 SER SER D . n 
D 1 146 CYS 146 146 146 CYS CYS D . n 
D 1 147 ALA 147 147 147 ALA ALA D . n 
D 1 148 PRO 148 148 148 PRO PRO D . n 
D 1 149 SER 149 149 149 SER SER D . n 
D 1 150 PHE 150 150 150 PHE PHE D . n 
D 1 151 LEU 151 151 151 LEU LEU D . n 
D 1 152 ALA 152 152 152 ALA ALA D . n 
D 1 153 GLN 153 153 153 GLN GLN D . n 
D 1 154 LYS 154 154 154 LYS LYS D . n 
D 1 155 GLY 155 155 155 GLY GLY D . n 
D 1 156 LEU 156 156 156 LEU LEU D . n 
D 1 157 PRO 157 157 157 PRO PRO D . n 
D 1 158 ASN 158 158 158 ASN ASN D . n 
D 1 159 ASN 159 159 159 ASN ASN D . n 
D 1 160 VAL 160 160 160 VAL VAL D . n 
D 1 161 GLN 161 161 161 GLN GLN D . n 
D 1 162 GLY 162 162 162 GLY GLY D . n 
D 1 163 ALA 163 163 163 ALA ALA D . n 
D 1 164 LEU 164 164 164 LEU LEU D . n 
D 1 165 GLY 165 165 165 GLY GLY D . n 
D 1 166 LEU 166 166 166 LEU LEU D . n 
D 1 167 GLY 167 167 167 GLY GLY D . n 
D 1 168 GLN 168 168 168 GLN GLN D . n 
D 1 169 ALA 169 169 169 ALA ALA D . n 
D 1 170 PRO 170 170 170 PRO PRO D . n 
D 1 171 ILE 171 171 171 ILE ILE D . n 
D 1 172 SER 172 172 172 SER SER D . n 
D 1 173 LEU 173 173 173 LEU LEU D . n 
D 1 174 GLN 174 174 174 GLN GLN D . n 
D 1 175 ASN 175 175 175 ASN ASN D . n 
D 1 176 GLN 176 176 176 GLN GLN D . n 
D 1 177 LEU 177 177 177 LEU LEU D . n 
D 1 178 PHE 178 178 178 PHE PHE D . n 
D 1 179 SER 179 179 179 SER SER D . n 
D 1 180 HIS 180 180 180 HIS HIS D . n 
D 1 181 PHE 181 181 181 PHE PHE D . n 
D 1 182 GLY 182 182 182 GLY GLY D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 LYS 184 184 184 LYS LYS D . n 
D 1 185 ARG 185 185 185 ARG ARG D . n 
D 1 186 GLN 186 186 186 GLN GLN D . n 
D 1 187 PHE 187 187 187 PHE PHE D . n 
D 1 188 SER 188 188 188 SER SER D . n 
D 1 189 VAL 189 189 189 VAL VAL D . n 
D 1 190 CYS 190 190 190 CYS CYS D . n 
D 1 191 LEU 191 191 191 LEU LEU D . n 
D 1 192 SER 192 192 192 SER SER D . n 
D 1 193 ARG 193 193 193 ARG ARG D . n 
D 1 194 TYR 194 194 194 TYR TYR D . n 
D 1 195 SER 195 195 195 SER SER D . n 
D 1 196 THR 196 196 196 THR THR D . n 
D 1 197 SER 197 197 197 SER SER D . n 
D 1 198 ASN 198 198 198 ASN ASN D . n 
D 1 199 GLY 199 199 199 GLY GLY D . n 
D 1 200 ALA 200 200 200 ALA ALA D . n 
D 1 201 ILE 201 201 201 ILE ILE D . n 
D 1 202 LEU 202 202 202 LEU LEU D . n 
D 1 203 PHE 203 203 203 PHE PHE D . n 
D 1 204 GLY 204 204 204 GLY GLY D . n 
D 1 205 ASP 205 205 205 ASP ASP D . n 
D 1 206 ILE 206 206 206 ILE ILE D . n 
D 1 207 ASN 207 207 207 ASN ASN D . n 
D 1 208 ASP 208 208 208 ASP ASP D . n 
D 1 209 PRO 209 209 209 PRO PRO D . n 
D 1 210 ASN 210 210 210 ASN ASN D . n 
D 1 211 ASN 211 211 211 ASN ASN D . n 
D 1 212 ASN 212 212 212 ASN ASN D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 TYR 214 214 214 TYR TYR D . n 
D 1 215 ILE 215 215 215 ILE ILE D . n 
D 1 216 HIS 216 216 216 HIS HIS D . n 
D 1 217 ASN 217 217 217 ASN ASN D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 LEU 219 219 219 LEU LEU D . n 
D 1 220 ASP 220 220 220 ASP ASP D . n 
D 1 221 VAL 221 221 221 VAL VAL D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 HIS 223 223 223 HIS HIS D . n 
D 1 224 ASP 224 224 224 ASP ASP D . n 
D 1 225 LEU 225 225 225 LEU LEU D . n 
D 1 226 VAL 226 226 226 VAL VAL D . n 
D 1 227 TYR 227 227 227 TYR TYR D . n 
D 1 228 THR 228 228 228 THR THR D . n 
D 1 229 PRO 229 229 229 PRO PRO D . n 
D 1 230 LEU 230 230 230 LEU LEU D . n 
D 1 231 THR 231 231 231 THR THR D . n 
D 1 232 ILE 232 232 232 ILE ILE D . n 
D 1 233 SER 233 233 233 SER SER D . n 
D 1 234 LYS 234 234 234 LYS LYS D . n 
D 1 235 GLN 235 235 235 GLN GLN D . n 
D 1 236 GLY 236 236 236 GLY GLY D . n 
D 1 237 GLU 237 237 237 GLU GLU D . n 
D 1 238 TYR 238 238 238 TYR TYR D . n 
D 1 239 PHE 239 239 239 PHE PHE D . n 
D 1 240 ILE 240 240 240 ILE ILE D . n 
D 1 241 GLN 241 241 241 GLN GLN D . n 
D 1 242 VAL 242 242 242 VAL VAL D . n 
D 1 243 ASN 243 243 243 ASN ASN D . n 
D 1 244 ALA 244 244 244 ALA ALA D . n 
D 1 245 ILE 245 245 245 ILE ILE D . n 
D 1 246 ARG 246 246 246 ARG ARG D . n 
D 1 247 VAL 247 247 247 VAL VAL D . n 
D 1 248 ASN 248 248 248 ASN ASN D . n 
D 1 249 LYS 249 249 249 LYS LYS D . n 
D 1 250 HIS 250 250 250 HIS HIS D . n 
D 1 251 LEU 251 251 251 LEU LEU D . n 
D 1 252 VAL 252 252 252 VAL VAL D . n 
D 1 253 ILE 253 253 253 ILE ILE D . n 
D 1 254 PRO 254 254 254 PRO PRO D . n 
D 1 255 THR 255 255 255 THR THR D . n 
D 1 256 LYS 256 256 ?   ?   ?   D . n 
D 1 257 ASN 257 257 ?   ?   ?   D . n 
D 1 258 PRO 258 258 ?   ?   ?   D . n 
D 1 259 PHE 259 259 ?   ?   ?   D . n 
D 1 260 ILE 260 260 ?   ?   ?   D . n 
D 1 261 SER 261 261 ?   ?   ?   D . n 
D 1 262 PRO 262 262 ?   ?   ?   D . n 
D 1 263 SER 263 263 ?   ?   ?   D . n 
D 1 264 SER 264 264 ?   ?   ?   D . n 
D 1 265 THR 265 265 ?   ?   ?   D . n 
D 1 266 SER 266 266 ?   ?   ?   D . n 
D 1 267 TYR 267 267 ?   ?   ?   D . n 
D 1 268 HIS 268 268 ?   ?   ?   D . n 
D 1 269 GLY 269 269 ?   ?   ?   D . n 
D 1 270 SER 270 270 ?   ?   ?   D . n 
D 1 271 GLY 271 271 ?   ?   ?   D . n 
D 1 272 GLU 272 272 272 GLU GLU D . n 
D 1 273 ILE 273 273 273 ILE ILE D . n 
D 1 274 GLY 274 274 274 GLY GLY D . n 
D 1 275 GLY 275 275 275 GLY GLY D . n 
D 1 276 ALA 276 276 276 ALA ALA D . n 
D 1 277 LEU 277 277 277 LEU LEU D . n 
D 1 278 ILE 278 278 278 ILE ILE D . n 
D 1 279 THR 279 279 279 THR THR D . n 
D 1 280 THR 280 280 280 THR THR D . n 
D 1 281 THR 281 281 281 THR THR D . n 
D 1 282 HIS 282 282 282 HIS HIS D . n 
D 1 283 PRO 283 283 283 PRO PRO D . n 
D 1 284 TYR 284 284 284 TYR TYR D . n 
D 1 285 THR 285 285 285 THR THR D . n 
D 1 286 VAL 286 286 286 VAL VAL D . n 
D 1 287 LEU 287 287 287 LEU LEU D . n 
D 1 288 SER 288 288 288 SER SER D . n 
D 1 289 HIS 289 289 289 HIS HIS D . n 
D 1 290 SER 290 290 290 SER SER D . n 
D 1 291 ILE 291 291 291 ILE ILE D . n 
D 1 292 PHE 292 292 292 PHE PHE D . n 
D 1 293 GLU 293 293 293 GLU GLU D . n 
D 1 294 VAL 294 294 294 VAL VAL D . n 
D 1 295 PHE 295 295 295 PHE PHE D . n 
D 1 296 THR 296 296 296 THR THR D . n 
D 1 297 GLN 297 297 297 GLN GLN D . n 
D 1 298 VAL 298 298 298 VAL VAL D . n 
D 1 299 PHE 299 299 299 PHE PHE D . n 
D 1 300 ALA 300 300 300 ALA ALA D . n 
D 1 301 ASN 301 301 301 ASN ASN D . n 
D 1 302 ASN 302 302 302 ASN ASN D . n 
D 1 303 MET 303 303 303 MET MET D . n 
D 1 304 PRO 304 304 304 PRO PRO D . n 
D 1 305 LYS 305 305 305 LYS LYS D . n 
D 1 306 GLN 306 306 306 GLN GLN D . n 
D 1 307 ALA 307 307 307 ALA ALA D . n 
D 1 308 GLN 308 308 308 GLN GLN D . n 
D 1 309 VAL 309 309 309 VAL VAL D . n 
D 1 310 LYS 310 310 310 LYS LYS D . n 
D 1 311 ALA 311 311 311 ALA ALA D . n 
D 1 312 VAL 312 312 312 VAL VAL D . n 
D 1 313 GLY 313 313 313 GLY GLY D . n 
D 1 314 PRO 314 314 314 PRO PRO D . n 
D 1 315 PHE 315 315 315 PHE PHE D . n 
D 1 316 GLY 316 316 316 GLY GLY D . n 
D 1 317 LEU 317 317 317 LEU LEU D . n 
D 1 318 CYS 318 318 318 CYS CYS D . n 
D 1 319 TYR 319 319 319 TYR TYR D . n 
D 1 320 ASP 320 320 320 ASP ASP D . n 
D 1 321 SER 321 321 321 SER SER D . n 
D 1 322 ARG 322 322 322 ARG ARG D . n 
D 1 323 LYS 323 323 323 LYS LYS D . n 
D 1 324 ILE 324 324 324 ILE ILE D . n 
D 1 325 SER 325 325 325 SER SER D . n 
D 1 326 GLY 326 326 326 GLY GLY D . n 
D 1 327 GLY 327 327 327 GLY GLY D . n 
D 1 328 ALA 328 328 328 ALA ALA D . n 
D 1 329 PRO 329 329 329 PRO PRO D . n 
D 1 330 SER 330 330 330 SER SER D . n 
D 1 331 VAL 331 331 331 VAL VAL D . n 
D 1 332 ASP 332 332 332 ASP ASP D . n 
D 1 333 LEU 333 333 333 LEU LEU D . n 
D 1 334 ILE 334 334 334 ILE ILE D . n 
D 1 335 LEU 335 335 335 LEU LEU D . n 
D 1 336 ASP 336 336 336 ASP ASP D . n 
D 1 337 LYS 337 337 337 LYS LYS D . n 
D 1 338 ASN 338 338 338 ASN ASN D . n 
D 1 339 ASP 339 339 339 ASP ASP D . n 
D 1 340 ALA 340 340 340 ALA ALA D . n 
D 1 341 VAL 341 341 341 VAL VAL D . n 
D 1 342 TRP 342 342 342 TRP TRP D . n 
D 1 343 ARG 343 343 343 ARG ARG D . n 
D 1 344 ILE 344 344 344 ILE ILE D . n 
D 1 345 SER 345 345 345 SER SER D . n 
D 1 346 SER 346 346 346 SER SER D . n 
D 1 347 GLU 347 347 347 GLU GLU D . n 
D 1 348 ASN 348 348 348 ASN ASN D . n 
D 1 349 PHE 349 349 349 PHE PHE D . n 
D 1 350 MET 350 350 350 MET MET D . n 
D 1 351 VAL 351 351 351 VAL VAL D . n 
D 1 352 GLN 352 352 352 GLN GLN D . n 
D 1 353 ALA 353 353 353 ALA ALA D . n 
D 1 354 GLN 354 354 354 GLN GLN D . n 
D 1 355 ASP 355 355 355 ASP ASP D . n 
D 1 356 GLY 356 356 356 GLY GLY D . n 
D 1 357 VAL 357 357 357 VAL VAL D . n 
D 1 358 SER 358 358 358 SER SER D . n 
D 1 359 CYS 359 359 359 CYS CYS D . n 
D 1 360 LEU 360 360 360 LEU LEU D . n 
D 1 361 GLY 361 361 361 GLY GLY D . n 
D 1 362 PHE 362 362 362 PHE PHE D . n 
D 1 363 VAL 363 363 363 VAL VAL D . n 
D 1 364 ASP 364 364 364 ASP ASP D . n 
D 1 365 GLY 365 365 365 GLY GLY D . n 
D 1 366 GLY 366 366 366 GLY GLY D . n 
D 1 367 VAL 367 367 367 VAL VAL D . n 
D 1 368 HIS 368 368 368 HIS HIS D . n 
D 1 369 ALA 369 369 369 ALA ALA D . n 
D 1 370 ARG 370 370 370 ARG ARG D . n 
D 1 371 ALA 371 371 371 ALA ALA D . n 
D 1 372 GLY 372 372 372 GLY GLY D . n 
D 1 373 ILE 373 373 373 ILE ILE D . n 
D 1 374 ALA 374 374 374 ALA ALA D . n 
D 1 375 LEU 375 375 375 LEU LEU D . n 
D 1 376 GLY 376 376 376 GLY GLY D . n 
D 1 377 ALA 377 377 377 ALA ALA D . n 
D 1 378 HIS 378 378 378 HIS HIS D . n 
D 1 379 HIS 379 379 379 HIS HIS D . n 
D 1 380 LEU 380 380 380 LEU LEU D . n 
D 1 381 GLU 381 381 381 GLU GLU D . n 
D 1 382 GLU 382 382 382 GLU GLU D . n 
D 1 383 ASN 383 383 383 ASN ASN D . n 
D 1 384 LEU 384 384 384 LEU LEU D . n 
D 1 385 VAL 385 385 385 VAL VAL D . n 
D 1 386 VAL 386 386 386 VAL VAL D . n 
D 1 387 PHE 387 387 387 PHE PHE D . n 
D 1 388 ASP 388 388 388 ASP ASP D . n 
D 1 389 LEU 389 389 389 LEU LEU D . n 
D 1 390 GLU 390 390 390 GLU GLU D . n 
D 1 391 ARG 391 391 391 ARG ARG D . n 
D 1 392 SER 392 392 392 SER SER D . n 
D 1 393 ARG 393 393 393 ARG ARG D . n 
D 1 394 VAL 394 394 394 VAL VAL D . n 
D 1 395 GLY 395 395 395 GLY GLY D . n 
D 1 396 PHE 396 396 396 PHE PHE D . n 
D 1 397 ASN 397 397 397 ASN ASN D . n 
D 1 398 SER 398 398 398 SER SER D . n 
D 1 399 ASN 399 399 399 ASN ASN D . n 
D 1 400 SER 400 400 400 SER SER D . n 
D 1 401 LEU 401 401 401 LEU LEU D . n 
D 1 402 LYS 402 402 402 LYS LYS D . n 
D 1 403 SER 403 403 403 SER SER D . n 
D 1 404 TYR 404 404 404 TYR TYR D . n 
D 1 405 GLY 405 405 405 GLY GLY D . n 
D 1 406 LYS 406 406 406 LYS LYS D . n 
D 1 407 THR 407 407 407 THR THR D . n 
D 1 408 CYS 408 408 408 CYS CYS D . n 
D 1 409 SER 409 409 409 SER SER D . n 
D 1 410 ASN 410 410 410 ASN ASN D . n 
D 1 411 LEU 411 411 411 LEU LEU D . n 
D 1 412 PHE 412 412 412 PHE PHE D . n 
D 1 413 ASP 413 413 413 ASP ASP D . n 
D 1 414 LEU 414 414 414 LEU LEU D . n 
D 1 415 ASN 415 415 415 ASN ASN D . n 
D 1 416 ASN 416 416 416 ASN ASN D . n 
D 1 417 PRO 417 417 417 PRO PRO D . n 
E 1 1   LEU 1   1   ?   ?   ?   E . n 
E 1 2   TYR 2   2   ?   ?   ?   E . n 
E 1 3   HIS 3   3   ?   ?   ?   E . n 
E 1 4   ASN 4   4   ?   ?   ?   E . n 
E 1 5   SER 5   5   ?   ?   ?   E . n 
E 1 6   GLN 6   6   ?   ?   ?   E . n 
E 1 7   PRO 7   7   ?   ?   ?   E . n 
E 1 8   THR 8   8   ?   ?   ?   E . n 
E 1 9   SER 9   9   ?   ?   ?   E . n 
E 1 10  SER 10  10  ?   ?   ?   E . n 
E 1 11  LYS 11  11  11  LYS LYS E . n 
E 1 12  PRO 12  12  12  PRO PRO E . n 
E 1 13  ASN 13  13  13  ASN ASN E . n 
E 1 14  LEU 14  14  14  LEU LEU E . n 
E 1 15  LEU 15  15  15  LEU LEU E . n 
E 1 16  VAL 16  16  16  VAL VAL E . n 
E 1 17  LEU 17  17  17  LEU LEU E . n 
E 1 18  PRO 18  18  18  PRO PRO E . n 
E 1 19  VAL 19  19  19  VAL VAL E . n 
E 1 20  GLN 20  20  20  GLN GLN E . n 
E 1 21  GLU 21  21  21  GLU GLU E . n 
E 1 22  ASP 22  22  22  ASP ASP E . n 
E 1 23  ALA 23  23  23  ALA ALA E . n 
E 1 24  SER 24  24  24  SER SER E . n 
E 1 25  THR 25  25  25  THR THR E . n 
E 1 26  GLY 26  26  26  GLY GLY E . n 
E 1 27  LEU 27  27  27  LEU LEU E . n 
E 1 28  HIS 28  28  28  HIS HIS E . n 
E 1 29  TRP 29  29  29  TRP TRP E . n 
E 1 30  ALA 30  30  30  ALA ALA E . n 
E 1 31  ASN 31  31  31  ASN ASN E . n 
E 1 32  ILE 32  32  32  ILE ILE E . n 
E 1 33  HIS 33  33  33  HIS HIS E . n 
E 1 34  LYS 34  34  34  LYS LYS E . n 
E 1 35  ARG 35  35  35  ARG ARG E . n 
E 1 36  THR 36  36  36  THR THR E . n 
E 1 37  PRO 37  37  37  PRO PRO E . n 
E 1 38  LEU 38  38  38  LEU LEU E . n 
E 1 39  MET 39  39  39  MET MET E . n 
E 1 40  GLN 40  40  40  GLN GLN E . n 
E 1 41  VAL 41  41  41  VAL VAL E . n 
E 1 42  PRO 42  42  42  PRO PRO E . n 
E 1 43  LEU 43  43  43  LEU LEU E . n 
E 1 44  LEU 44  44  44  LEU LEU E . n 
E 1 45  LEU 45  45  45  LEU LEU E . n 
E 1 46  ASP 46  46  46  ASP ASP E . n 
E 1 47  LEU 47  47  47  LEU LEU E . n 
E 1 48  ASN 48  48  48  ASN ASN E . n 
E 1 49  GLY 49  49  49  GLY GLY E . n 
E 1 50  LYS 50  50  50  LYS LYS E . n 
E 1 51  HIS 51  51  51  HIS HIS E . n 
E 1 52  LEU 52  52  52  LEU LEU E . n 
E 1 53  TRP 53  53  53  TRP TRP E . n 
E 1 54  VAL 54  54  54  VAL VAL E . n 
E 1 55  THR 55  55  55  THR THR E . n 
E 1 56  CYS 56  56  56  CYS CYS E . n 
E 1 57  SER 57  57  57  SER SER E . n 
E 1 58  GLN 58  58  58  GLN GLN E . n 
E 1 59  HIS 59  59  59  HIS HIS E . n 
E 1 60  TYR 60  60  60  TYR TYR E . n 
E 1 61  SER 61  61  61  SER SER E . n 
E 1 62  SER 62  62  62  SER SER E . n 
E 1 63  SER 63  63  63  SER SER E . n 
E 1 64  THR 64  64  64  THR THR E . n 
E 1 65  TYR 65  65  65  TYR TYR E . n 
E 1 66  GLN 66  66  66  GLN GLN E . n 
E 1 67  ALA 67  67  67  ALA ALA E . n 
E 1 68  PRO 68  68  68  PRO PRO E . n 
E 1 69  PHE 69  69  69  PHE PHE E . n 
E 1 70  CYS 70  70  70  CYS CYS E . n 
E 1 71  HIS 71  71  71  HIS HIS E . n 
E 1 72  SER 72  72  72  SER SER E . n 
E 1 73  THR 73  73  73  THR THR E . n 
E 1 74  GLN 74  74  74  GLN GLN E . n 
E 1 75  CYS 75  75  75  CYS CYS E . n 
E 1 76  SER 76  76  76  SER SER E . n 
E 1 77  ARG 77  77  77  ARG ARG E . n 
E 1 78  ALA 78  78  78  ALA ALA E . n 
E 1 79  ASN 79  79  79  ASN ASN E . n 
E 1 80  THR 80  80  80  THR THR E . n 
E 1 81  HIS 81  81  81  HIS HIS E . n 
E 1 82  GLN 82  82  82  GLN GLN E . n 
E 1 83  CYS 83  83  83  CYS CYS E . n 
E 1 84  PHE 84  84  84  PHE PHE E . n 
E 1 85  THR 85  85  85  THR THR E . n 
E 1 86  CYS 86  86  86  CYS CYS E . n 
E 1 87  THR 87  87  87  THR THR E . n 
E 1 88  ASP 88  88  88  ASP ASP E . n 
E 1 89  SER 89  89  89  SER SER E . n 
E 1 90  THR 90  90  90  THR THR E . n 
E 1 91  THR 91  91  91  THR THR E . n 
E 1 92  THR 92  92  92  THR THR E . n 
E 1 93  ARG 93  93  93  ARG ARG E . n 
E 1 94  PRO 94  94  94  PRO PRO E . n 
E 1 95  GLY 95  95  95  GLY GLY E . n 
E 1 96  CYS 96  96  96  CYS CYS E . n 
E 1 97  HIS 97  97  97  HIS HIS E . n 
E 1 98  ASN 98  98  98  ASN ASN E . n 
E 1 99  ASN 99  99  99  ASN ASN E . n 
E 1 100 THR 100 100 100 THR THR E . n 
E 1 101 CYS 101 101 101 CYS CYS E . n 
E 1 102 GLY 102 102 102 GLY GLY E . n 
E 1 103 LEU 103 103 103 LEU LEU E . n 
E 1 104 LEU 104 104 104 LEU LEU E . n 
E 1 105 SER 105 105 105 SER SER E . n 
E 1 106 SER 106 106 106 SER SER E . n 
E 1 107 ASN 107 107 107 ASN ASN E . n 
E 1 108 PRO 108 108 108 PRO PRO E . n 
E 1 109 VAL 109 109 109 VAL VAL E . n 
E 1 110 THR 110 110 110 THR THR E . n 
E 1 111 GLN 111 111 111 GLN GLN E . n 
E 1 112 GLU 112 112 112 GLU GLU E . n 
E 1 113 SER 113 113 113 SER SER E . n 
E 1 114 GLY 114 114 114 GLY GLY E . n 
E 1 115 LEU 115 115 115 LEU LEU E . n 
E 1 116 GLY 116 116 116 GLY GLY E . n 
E 1 117 GLU 117 117 117 GLU GLU E . n 
E 1 118 LEU 118 118 118 LEU LEU E . n 
E 1 119 ALA 119 119 119 ALA ALA E . n 
E 1 120 GLN 120 120 120 GLN GLN E . n 
E 1 121 ASP 121 121 121 ASP ASP E . n 
E 1 122 VAL 122 122 122 VAL VAL E . n 
E 1 123 LEU 123 123 123 LEU LEU E . n 
E 1 124 ALA 124 124 124 ALA ALA E . n 
E 1 125 ILE 125 125 125 ILE ILE E . n 
E 1 126 HIS 126 126 126 HIS HIS E . n 
E 1 127 SER 127 127 127 SER SER E . n 
E 1 128 THR 128 128 128 THR THR E . n 
E 1 129 HIS 129 129 129 HIS HIS E . n 
E 1 130 GLY 130 130 130 GLY GLY E . n 
E 1 131 SER 131 131 131 SER SER E . n 
E 1 132 LYS 132 132 132 LYS LYS E . n 
E 1 133 LEU 133 133 133 LEU LEU E . n 
E 1 134 GLY 134 134 134 GLY GLY E . n 
E 1 135 PRO 135 135 135 PRO PRO E . n 
E 1 136 MET 136 136 136 MET MET E . n 
E 1 137 VAL 137 137 137 VAL VAL E . n 
E 1 138 LYS 138 138 138 LYS LYS E . n 
E 1 139 VAL 139 139 139 VAL VAL E . n 
E 1 140 PRO 140 140 140 PRO PRO E . n 
E 1 141 GLN 141 141 141 GLN GLN E . n 
E 1 142 PHE 142 142 142 PHE PHE E . n 
E 1 143 LEU 143 143 143 LEU LEU E . n 
E 1 144 PHE 144 144 144 PHE PHE E . n 
E 1 145 SER 145 145 145 SER SER E . n 
E 1 146 CYS 146 146 146 CYS CYS E . n 
E 1 147 ALA 147 147 147 ALA ALA E . n 
E 1 148 PRO 148 148 148 PRO PRO E . n 
E 1 149 SER 149 149 149 SER SER E . n 
E 1 150 PHE 150 150 150 PHE PHE E . n 
E 1 151 LEU 151 151 151 LEU LEU E . n 
E 1 152 ALA 152 152 152 ALA ALA E . n 
E 1 153 GLN 153 153 153 GLN GLN E . n 
E 1 154 LYS 154 154 154 LYS LYS E . n 
E 1 155 GLY 155 155 155 GLY GLY E . n 
E 1 156 LEU 156 156 156 LEU LEU E . n 
E 1 157 PRO 157 157 157 PRO PRO E . n 
E 1 158 ASN 158 158 158 ASN ASN E . n 
E 1 159 ASN 159 159 159 ASN ASN E . n 
E 1 160 VAL 160 160 160 VAL VAL E . n 
E 1 161 GLN 161 161 161 GLN GLN E . n 
E 1 162 GLY 162 162 162 GLY GLY E . n 
E 1 163 ALA 163 163 163 ALA ALA E . n 
E 1 164 LEU 164 164 164 LEU LEU E . n 
E 1 165 GLY 165 165 165 GLY GLY E . n 
E 1 166 LEU 166 166 166 LEU LEU E . n 
E 1 167 GLY 167 167 167 GLY GLY E . n 
E 1 168 GLN 168 168 168 GLN GLN E . n 
E 1 169 ALA 169 169 169 ALA ALA E . n 
E 1 170 PRO 170 170 170 PRO PRO E . n 
E 1 171 ILE 171 171 171 ILE ILE E . n 
E 1 172 SER 172 172 172 SER SER E . n 
E 1 173 LEU 173 173 173 LEU LEU E . n 
E 1 174 GLN 174 174 174 GLN GLN E . n 
E 1 175 ASN 175 175 175 ASN ASN E . n 
E 1 176 GLN 176 176 176 GLN GLN E . n 
E 1 177 LEU 177 177 177 LEU LEU E . n 
E 1 178 PHE 178 178 178 PHE PHE E . n 
E 1 179 SER 179 179 179 SER SER E . n 
E 1 180 HIS 180 180 180 HIS HIS E . n 
E 1 181 PHE 181 181 181 PHE PHE E . n 
E 1 182 GLY 182 182 182 GLY GLY E . n 
E 1 183 LEU 183 183 183 LEU LEU E . n 
E 1 184 LYS 184 184 184 LYS LYS E . n 
E 1 185 ARG 185 185 185 ARG ARG E . n 
E 1 186 GLN 186 186 186 GLN GLN E . n 
E 1 187 PHE 187 187 187 PHE PHE E . n 
E 1 188 SER 188 188 188 SER SER E . n 
E 1 189 VAL 189 189 189 VAL VAL E . n 
E 1 190 CYS 190 190 190 CYS CYS E . n 
E 1 191 LEU 191 191 191 LEU LEU E . n 
E 1 192 SER 192 192 192 SER SER E . n 
E 1 193 ARG 193 193 193 ARG ARG E . n 
E 1 194 TYR 194 194 194 TYR TYR E . n 
E 1 195 SER 195 195 195 SER SER E . n 
E 1 196 THR 196 196 196 THR THR E . n 
E 1 197 SER 197 197 197 SER SER E . n 
E 1 198 ASN 198 198 198 ASN ASN E . n 
E 1 199 GLY 199 199 199 GLY GLY E . n 
E 1 200 ALA 200 200 200 ALA ALA E . n 
E 1 201 ILE 201 201 201 ILE ILE E . n 
E 1 202 LEU 202 202 202 LEU LEU E . n 
E 1 203 PHE 203 203 203 PHE PHE E . n 
E 1 204 GLY 204 204 204 GLY GLY E . n 
E 1 205 ASP 205 205 205 ASP ASP E . n 
E 1 206 ILE 206 206 206 ILE ILE E . n 
E 1 207 ASN 207 207 207 ASN ASN E . n 
E 1 208 ASP 208 208 208 ASP ASP E . n 
E 1 209 PRO 209 209 209 PRO PRO E . n 
E 1 210 ASN 210 210 210 ASN ASN E . n 
E 1 211 ASN 211 211 211 ASN ASN E . n 
E 1 212 ASN 212 212 212 ASN ASN E . n 
E 1 213 ASN 213 213 213 ASN ASN E . n 
E 1 214 TYR 214 214 214 TYR TYR E . n 
E 1 215 ILE 215 215 215 ILE ILE E . n 
E 1 216 HIS 216 216 216 HIS HIS E . n 
E 1 217 ASN 217 217 217 ASN ASN E . n 
E 1 218 SER 218 218 218 SER SER E . n 
E 1 219 LEU 219 219 219 LEU LEU E . n 
E 1 220 ASP 220 220 220 ASP ASP E . n 
E 1 221 VAL 221 221 221 VAL VAL E . n 
E 1 222 LEU 222 222 222 LEU LEU E . n 
E 1 223 HIS 223 223 223 HIS HIS E . n 
E 1 224 ASP 224 224 224 ASP ASP E . n 
E 1 225 LEU 225 225 225 LEU LEU E . n 
E 1 226 VAL 226 226 226 VAL VAL E . n 
E 1 227 TYR 227 227 227 TYR TYR E . n 
E 1 228 THR 228 228 228 THR THR E . n 
E 1 229 PRO 229 229 229 PRO PRO E . n 
E 1 230 LEU 230 230 230 LEU LEU E . n 
E 1 231 THR 231 231 231 THR THR E . n 
E 1 232 ILE 232 232 232 ILE ILE E . n 
E 1 233 SER 233 233 233 SER SER E . n 
E 1 234 LYS 234 234 234 LYS LYS E . n 
E 1 235 GLN 235 235 235 GLN GLN E . n 
E 1 236 GLY 236 236 236 GLY GLY E . n 
E 1 237 GLU 237 237 237 GLU GLU E . n 
E 1 238 TYR 238 238 238 TYR TYR E . n 
E 1 239 PHE 239 239 239 PHE PHE E . n 
E 1 240 ILE 240 240 240 ILE ILE E . n 
E 1 241 GLN 241 241 241 GLN GLN E . n 
E 1 242 VAL 242 242 242 VAL VAL E . n 
E 1 243 ASN 243 243 243 ASN ASN E . n 
E 1 244 ALA 244 244 244 ALA ALA E . n 
E 1 245 ILE 245 245 245 ILE ILE E . n 
E 1 246 ARG 246 246 246 ARG ARG E . n 
E 1 247 VAL 247 247 247 VAL VAL E . n 
E 1 248 ASN 248 248 248 ASN ASN E . n 
E 1 249 LYS 249 249 249 LYS LYS E . n 
E 1 250 HIS 250 250 250 HIS HIS E . n 
E 1 251 LEU 251 251 251 LEU LEU E . n 
E 1 252 VAL 252 252 252 VAL VAL E . n 
E 1 253 ILE 253 253 253 ILE ILE E . n 
E 1 254 PRO 254 254 254 PRO PRO E . n 
E 1 255 THR 255 255 255 THR THR E . n 
E 1 256 LYS 256 256 ?   ?   ?   E . n 
E 1 257 ASN 257 257 ?   ?   ?   E . n 
E 1 258 PRO 258 258 ?   ?   ?   E . n 
E 1 259 PHE 259 259 ?   ?   ?   E . n 
E 1 260 ILE 260 260 ?   ?   ?   E . n 
E 1 261 SER 261 261 ?   ?   ?   E . n 
E 1 262 PRO 262 262 ?   ?   ?   E . n 
E 1 263 SER 263 263 ?   ?   ?   E . n 
E 1 264 SER 264 264 ?   ?   ?   E . n 
E 1 265 THR 265 265 ?   ?   ?   E . n 
E 1 266 SER 266 266 ?   ?   ?   E . n 
E 1 267 TYR 267 267 ?   ?   ?   E . n 
E 1 268 HIS 268 268 ?   ?   ?   E . n 
E 1 269 GLY 269 269 ?   ?   ?   E . n 
E 1 270 SER 270 270 ?   ?   ?   E . n 
E 1 271 GLY 271 271 271 GLY GLY E . n 
E 1 272 GLU 272 272 272 GLU GLU E . n 
E 1 273 ILE 273 273 273 ILE ILE E . n 
E 1 274 GLY 274 274 274 GLY GLY E . n 
E 1 275 GLY 275 275 275 GLY GLY E . n 
E 1 276 ALA 276 276 276 ALA ALA E . n 
E 1 277 LEU 277 277 277 LEU LEU E . n 
E 1 278 ILE 278 278 278 ILE ILE E . n 
E 1 279 THR 279 279 279 THR THR E . n 
E 1 280 THR 280 280 280 THR THR E . n 
E 1 281 THR 281 281 281 THR THR E . n 
E 1 282 HIS 282 282 282 HIS HIS E . n 
E 1 283 PRO 283 283 283 PRO PRO E . n 
E 1 284 TYR 284 284 284 TYR TYR E . n 
E 1 285 THR 285 285 285 THR THR E . n 
E 1 286 VAL 286 286 286 VAL VAL E . n 
E 1 287 LEU 287 287 287 LEU LEU E . n 
E 1 288 SER 288 288 288 SER SER E . n 
E 1 289 HIS 289 289 289 HIS HIS E . n 
E 1 290 SER 290 290 290 SER SER E . n 
E 1 291 ILE 291 291 291 ILE ILE E . n 
E 1 292 PHE 292 292 292 PHE PHE E . n 
E 1 293 GLU 293 293 293 GLU GLU E . n 
E 1 294 VAL 294 294 294 VAL VAL E . n 
E 1 295 PHE 295 295 295 PHE PHE E . n 
E 1 296 THR 296 296 296 THR THR E . n 
E 1 297 GLN 297 297 297 GLN GLN E . n 
E 1 298 VAL 298 298 298 VAL VAL E . n 
E 1 299 PHE 299 299 299 PHE PHE E . n 
E 1 300 ALA 300 300 300 ALA ALA E . n 
E 1 301 ASN 301 301 301 ASN ASN E . n 
E 1 302 ASN 302 302 302 ASN ASN E . n 
E 1 303 MET 303 303 303 MET MET E . n 
E 1 304 PRO 304 304 304 PRO PRO E . n 
E 1 305 LYS 305 305 305 LYS LYS E . n 
E 1 306 GLN 306 306 306 GLN GLN E . n 
E 1 307 ALA 307 307 307 ALA ALA E . n 
E 1 308 GLN 308 308 308 GLN GLN E . n 
E 1 309 VAL 309 309 309 VAL VAL E . n 
E 1 310 LYS 310 310 310 LYS LYS E . n 
E 1 311 ALA 311 311 311 ALA ALA E . n 
E 1 312 VAL 312 312 312 VAL VAL E . n 
E 1 313 GLY 313 313 313 GLY GLY E . n 
E 1 314 PRO 314 314 314 PRO PRO E . n 
E 1 315 PHE 315 315 315 PHE PHE E . n 
E 1 316 GLY 316 316 316 GLY GLY E . n 
E 1 317 LEU 317 317 317 LEU LEU E . n 
E 1 318 CYS 318 318 318 CYS CYS E . n 
E 1 319 TYR 319 319 319 TYR TYR E . n 
E 1 320 ASP 320 320 320 ASP ASP E . n 
E 1 321 SER 321 321 321 SER SER E . n 
E 1 322 ARG 322 322 322 ARG ARG E . n 
E 1 323 LYS 323 323 323 LYS LYS E . n 
E 1 324 ILE 324 324 324 ILE ILE E . n 
E 1 325 SER 325 325 325 SER SER E . n 
E 1 326 GLY 326 326 326 GLY GLY E . n 
E 1 327 GLY 327 327 327 GLY GLY E . n 
E 1 328 ALA 328 328 328 ALA ALA E . n 
E 1 329 PRO 329 329 329 PRO PRO E . n 
E 1 330 SER 330 330 330 SER SER E . n 
E 1 331 VAL 331 331 331 VAL VAL E . n 
E 1 332 ASP 332 332 332 ASP ASP E . n 
E 1 333 LEU 333 333 333 LEU LEU E . n 
E 1 334 ILE 334 334 334 ILE ILE E . n 
E 1 335 LEU 335 335 335 LEU LEU E . n 
E 1 336 ASP 336 336 336 ASP ASP E . n 
E 1 337 LYS 337 337 337 LYS LYS E . n 
E 1 338 ASN 338 338 338 ASN ASN E . n 
E 1 339 ASP 339 339 339 ASP ASP E . n 
E 1 340 ALA 340 340 340 ALA ALA E . n 
E 1 341 VAL 341 341 341 VAL VAL E . n 
E 1 342 TRP 342 342 342 TRP TRP E . n 
E 1 343 ARG 343 343 343 ARG ARG E . n 
E 1 344 ILE 344 344 344 ILE ILE E . n 
E 1 345 SER 345 345 345 SER SER E . n 
E 1 346 SER 346 346 346 SER SER E . n 
E 1 347 GLU 347 347 347 GLU GLU E . n 
E 1 348 ASN 348 348 348 ASN ASN E . n 
E 1 349 PHE 349 349 349 PHE PHE E . n 
E 1 350 MET 350 350 350 MET MET E . n 
E 1 351 VAL 351 351 351 VAL VAL E . n 
E 1 352 GLN 352 352 352 GLN GLN E . n 
E 1 353 ALA 353 353 353 ALA ALA E . n 
E 1 354 GLN 354 354 354 GLN GLN E . n 
E 1 355 ASP 355 355 355 ASP ASP E . n 
E 1 356 GLY 356 356 356 GLY GLY E . n 
E 1 357 VAL 357 357 357 VAL VAL E . n 
E 1 358 SER 358 358 358 SER SER E . n 
E 1 359 CYS 359 359 359 CYS CYS E . n 
E 1 360 LEU 360 360 360 LEU LEU E . n 
E 1 361 GLY 361 361 361 GLY GLY E . n 
E 1 362 PHE 362 362 362 PHE PHE E . n 
E 1 363 VAL 363 363 363 VAL VAL E . n 
E 1 364 ASP 364 364 364 ASP ASP E . n 
E 1 365 GLY 365 365 365 GLY GLY E . n 
E 1 366 GLY 366 366 366 GLY GLY E . n 
E 1 367 VAL 367 367 367 VAL VAL E . n 
E 1 368 HIS 368 368 368 HIS HIS E . n 
E 1 369 ALA 369 369 369 ALA ALA E . n 
E 1 370 ARG 370 370 370 ARG ARG E . n 
E 1 371 ALA 371 371 371 ALA ALA E . n 
E 1 372 GLY 372 372 372 GLY GLY E . n 
E 1 373 ILE 373 373 373 ILE ILE E . n 
E 1 374 ALA 374 374 374 ALA ALA E . n 
E 1 375 LEU 375 375 375 LEU LEU E . n 
E 1 376 GLY 376 376 376 GLY GLY E . n 
E 1 377 ALA 377 377 377 ALA ALA E . n 
E 1 378 HIS 378 378 378 HIS HIS E . n 
E 1 379 HIS 379 379 379 HIS HIS E . n 
E 1 380 LEU 380 380 380 LEU LEU E . n 
E 1 381 GLU 381 381 381 GLU GLU E . n 
E 1 382 GLU 382 382 382 GLU GLU E . n 
E 1 383 ASN 383 383 383 ASN ASN E . n 
E 1 384 LEU 384 384 384 LEU LEU E . n 
E 1 385 VAL 385 385 385 VAL VAL E . n 
E 1 386 VAL 386 386 386 VAL VAL E . n 
E 1 387 PHE 387 387 387 PHE PHE E . n 
E 1 388 ASP 388 388 388 ASP ASP E . n 
E 1 389 LEU 389 389 389 LEU LEU E . n 
E 1 390 GLU 390 390 390 GLU GLU E . n 
E 1 391 ARG 391 391 391 ARG ARG E . n 
E 1 392 SER 392 392 392 SER SER E . n 
E 1 393 ARG 393 393 393 ARG ARG E . n 
E 1 394 VAL 394 394 394 VAL VAL E . n 
E 1 395 GLY 395 395 395 GLY GLY E . n 
E 1 396 PHE 396 396 396 PHE PHE E . n 
E 1 397 ASN 397 397 397 ASN ASN E . n 
E 1 398 SER 398 398 398 SER SER E . n 
E 1 399 ASN 399 399 399 ASN ASN E . n 
E 1 400 SER 400 400 400 SER SER E . n 
E 1 401 LEU 401 401 401 LEU LEU E . n 
E 1 402 LYS 402 402 402 LYS LYS E . n 
E 1 403 SER 403 403 403 SER SER E . n 
E 1 404 TYR 404 404 404 TYR TYR E . n 
E 1 405 GLY 405 405 405 GLY GLY E . n 
E 1 406 LYS 406 406 406 LYS LYS E . n 
E 1 407 THR 407 407 407 THR THR E . n 
E 1 408 CYS 408 408 408 CYS CYS E . n 
E 1 409 SER 409 409 409 SER SER E . n 
E 1 410 ASN 410 410 410 ASN ASN E . n 
E 1 411 LEU 411 411 411 LEU LEU E . n 
E 1 412 PHE 412 412 412 PHE PHE E . n 
E 1 413 ASP 413 413 413 ASP ASP E . n 
E 1 414 LEU 414 414 414 LEU LEU E . n 
E 1 415 ASN 415 415 415 ASN ASN E . n 
E 1 416 ASN 416 416 416 ASN ASN E . n 
E 1 417 PRO 417 417 ?   ?   ?   E . n 
F 1 1   LEU 1   1   ?   ?   ?   F . n 
F 1 2   TYR 2   2   ?   ?   ?   F . n 
F 1 3   HIS 3   3   ?   ?   ?   F . n 
F 1 4   ASN 4   4   ?   ?   ?   F . n 
F 1 5   SER 5   5   ?   ?   ?   F . n 
F 1 6   GLN 6   6   ?   ?   ?   F . n 
F 1 7   PRO 7   7   ?   ?   ?   F . n 
F 1 8   THR 8   8   ?   ?   ?   F . n 
F 1 9   SER 9   9   ?   ?   ?   F . n 
F 1 10  SER 10  10  10  SER SER F . n 
F 1 11  LYS 11  11  11  LYS LYS F . n 
F 1 12  PRO 12  12  12  PRO PRO F . n 
F 1 13  ASN 13  13  13  ASN ASN F . n 
F 1 14  LEU 14  14  14  LEU LEU F . n 
F 1 15  LEU 15  15  15  LEU LEU F . n 
F 1 16  VAL 16  16  16  VAL VAL F . n 
F 1 17  LEU 17  17  17  LEU LEU F . n 
F 1 18  PRO 18  18  18  PRO PRO F . n 
F 1 19  VAL 19  19  19  VAL VAL F . n 
F 1 20  GLN 20  20  20  GLN GLN F . n 
F 1 21  GLU 21  21  21  GLU GLU F . n 
F 1 22  ASP 22  22  22  ASP ASP F . n 
F 1 23  ALA 23  23  23  ALA ALA F . n 
F 1 24  SER 24  24  24  SER SER F . n 
F 1 25  THR 25  25  25  THR THR F . n 
F 1 26  GLY 26  26  26  GLY GLY F . n 
F 1 27  LEU 27  27  27  LEU LEU F . n 
F 1 28  HIS 28  28  28  HIS HIS F . n 
F 1 29  TRP 29  29  29  TRP TRP F . n 
F 1 30  ALA 30  30  30  ALA ALA F . n 
F 1 31  ASN 31  31  31  ASN ASN F . n 
F 1 32  ILE 32  32  32  ILE ILE F . n 
F 1 33  HIS 33  33  33  HIS HIS F . n 
F 1 34  LYS 34  34  34  LYS LYS F . n 
F 1 35  ARG 35  35  35  ARG ARG F . n 
F 1 36  THR 36  36  36  THR THR F . n 
F 1 37  PRO 37  37  37  PRO PRO F . n 
F 1 38  LEU 38  38  38  LEU LEU F . n 
F 1 39  MET 39  39  39  MET MET F . n 
F 1 40  GLN 40  40  40  GLN GLN F . n 
F 1 41  VAL 41  41  41  VAL VAL F . n 
F 1 42  PRO 42  42  42  PRO PRO F . n 
F 1 43  LEU 43  43  43  LEU LEU F . n 
F 1 44  LEU 44  44  44  LEU LEU F . n 
F 1 45  LEU 45  45  45  LEU LEU F . n 
F 1 46  ASP 46  46  46  ASP ASP F . n 
F 1 47  LEU 47  47  47  LEU LEU F . n 
F 1 48  ASN 48  48  48  ASN ASN F . n 
F 1 49  GLY 49  49  49  GLY GLY F . n 
F 1 50  LYS 50  50  50  LYS LYS F . n 
F 1 51  HIS 51  51  51  HIS HIS F . n 
F 1 52  LEU 52  52  52  LEU LEU F . n 
F 1 53  TRP 53  53  53  TRP TRP F . n 
F 1 54  VAL 54  54  54  VAL VAL F . n 
F 1 55  THR 55  55  55  THR THR F . n 
F 1 56  CYS 56  56  56  CYS CYS F . n 
F 1 57  SER 57  57  57  SER SER F . n 
F 1 58  GLN 58  58  58  GLN GLN F . n 
F 1 59  HIS 59  59  59  HIS HIS F . n 
F 1 60  TYR 60  60  60  TYR TYR F . n 
F 1 61  SER 61  61  61  SER SER F . n 
F 1 62  SER 62  62  62  SER SER F . n 
F 1 63  SER 63  63  63  SER SER F . n 
F 1 64  THR 64  64  64  THR THR F . n 
F 1 65  TYR 65  65  65  TYR TYR F . n 
F 1 66  GLN 66  66  66  GLN GLN F . n 
F 1 67  ALA 67  67  67  ALA ALA F . n 
F 1 68  PRO 68  68  68  PRO PRO F . n 
F 1 69  PHE 69  69  69  PHE PHE F . n 
F 1 70  CYS 70  70  70  CYS CYS F . n 
F 1 71  HIS 71  71  71  HIS HIS F . n 
F 1 72  SER 72  72  72  SER SER F . n 
F 1 73  THR 73  73  73  THR THR F . n 
F 1 74  GLN 74  74  74  GLN GLN F . n 
F 1 75  CYS 75  75  75  CYS CYS F . n 
F 1 76  SER 76  76  76  SER SER F . n 
F 1 77  ARG 77  77  77  ARG ARG F . n 
F 1 78  ALA 78  78  78  ALA ALA F . n 
F 1 79  ASN 79  79  79  ASN ASN F . n 
F 1 80  THR 80  80  80  THR THR F . n 
F 1 81  HIS 81  81  81  HIS HIS F . n 
F 1 82  GLN 82  82  82  GLN GLN F . n 
F 1 83  CYS 83  83  83  CYS CYS F . n 
F 1 84  PHE 84  84  84  PHE PHE F . n 
F 1 85  THR 85  85  85  THR THR F . n 
F 1 86  CYS 86  86  86  CYS CYS F . n 
F 1 87  THR 87  87  87  THR THR F . n 
F 1 88  ASP 88  88  88  ASP ASP F . n 
F 1 89  SER 89  89  89  SER SER F . n 
F 1 90  THR 90  90  90  THR THR F . n 
F 1 91  THR 91  91  91  THR THR F . n 
F 1 92  THR 92  92  92  THR THR F . n 
F 1 93  ARG 93  93  93  ARG ARG F . n 
F 1 94  PRO 94  94  94  PRO PRO F . n 
F 1 95  GLY 95  95  95  GLY GLY F . n 
F 1 96  CYS 96  96  96  CYS CYS F . n 
F 1 97  HIS 97  97  97  HIS HIS F . n 
F 1 98  ASN 98  98  98  ASN ASN F . n 
F 1 99  ASN 99  99  99  ASN ASN F . n 
F 1 100 THR 100 100 100 THR THR F . n 
F 1 101 CYS 101 101 101 CYS CYS F . n 
F 1 102 GLY 102 102 102 GLY GLY F . n 
F 1 103 LEU 103 103 103 LEU LEU F . n 
F 1 104 LEU 104 104 104 LEU LEU F . n 
F 1 105 SER 105 105 105 SER SER F . n 
F 1 106 SER 106 106 106 SER SER F . n 
F 1 107 ASN 107 107 107 ASN ASN F . n 
F 1 108 PRO 108 108 108 PRO PRO F . n 
F 1 109 VAL 109 109 109 VAL VAL F . n 
F 1 110 THR 110 110 110 THR THR F . n 
F 1 111 GLN 111 111 111 GLN GLN F . n 
F 1 112 GLU 112 112 112 GLU GLU F . n 
F 1 113 SER 113 113 113 SER SER F . n 
F 1 114 GLY 114 114 114 GLY GLY F . n 
F 1 115 LEU 115 115 115 LEU LEU F . n 
F 1 116 GLY 116 116 116 GLY GLY F . n 
F 1 117 GLU 117 117 117 GLU GLU F . n 
F 1 118 LEU 118 118 118 LEU LEU F . n 
F 1 119 ALA 119 119 119 ALA ALA F . n 
F 1 120 GLN 120 120 120 GLN GLN F . n 
F 1 121 ASP 121 121 121 ASP ASP F . n 
F 1 122 VAL 122 122 122 VAL VAL F . n 
F 1 123 LEU 123 123 123 LEU LEU F . n 
F 1 124 ALA 124 124 124 ALA ALA F . n 
F 1 125 ILE 125 125 125 ILE ILE F . n 
F 1 126 HIS 126 126 126 HIS HIS F . n 
F 1 127 SER 127 127 127 SER SER F . n 
F 1 128 THR 128 128 128 THR THR F . n 
F 1 129 HIS 129 129 129 HIS HIS F . n 
F 1 130 GLY 130 130 130 GLY GLY F . n 
F 1 131 SER 131 131 131 SER SER F . n 
F 1 132 LYS 132 132 132 LYS LYS F . n 
F 1 133 LEU 133 133 133 LEU LEU F . n 
F 1 134 GLY 134 134 134 GLY GLY F . n 
F 1 135 PRO 135 135 135 PRO PRO F . n 
F 1 136 MET 136 136 136 MET MET F . n 
F 1 137 VAL 137 137 137 VAL VAL F . n 
F 1 138 LYS 138 138 138 LYS LYS F . n 
F 1 139 VAL 139 139 139 VAL VAL F . n 
F 1 140 PRO 140 140 140 PRO PRO F . n 
F 1 141 GLN 141 141 141 GLN GLN F . n 
F 1 142 PHE 142 142 142 PHE PHE F . n 
F 1 143 LEU 143 143 143 LEU LEU F . n 
F 1 144 PHE 144 144 144 PHE PHE F . n 
F 1 145 SER 145 145 145 SER SER F . n 
F 1 146 CYS 146 146 146 CYS CYS F . n 
F 1 147 ALA 147 147 147 ALA ALA F . n 
F 1 148 PRO 148 148 148 PRO PRO F . n 
F 1 149 SER 149 149 149 SER SER F . n 
F 1 150 PHE 150 150 150 PHE PHE F . n 
F 1 151 LEU 151 151 151 LEU LEU F . n 
F 1 152 ALA 152 152 152 ALA ALA F . n 
F 1 153 GLN 153 153 153 GLN GLN F . n 
F 1 154 LYS 154 154 154 LYS LYS F . n 
F 1 155 GLY 155 155 155 GLY GLY F . n 
F 1 156 LEU 156 156 156 LEU LEU F . n 
F 1 157 PRO 157 157 157 PRO PRO F . n 
F 1 158 ASN 158 158 158 ASN ASN F . n 
F 1 159 ASN 159 159 159 ASN ASN F . n 
F 1 160 VAL 160 160 160 VAL VAL F . n 
F 1 161 GLN 161 161 161 GLN GLN F . n 
F 1 162 GLY 162 162 162 GLY GLY F . n 
F 1 163 ALA 163 163 163 ALA ALA F . n 
F 1 164 LEU 164 164 164 LEU LEU F . n 
F 1 165 GLY 165 165 165 GLY GLY F . n 
F 1 166 LEU 166 166 166 LEU LEU F . n 
F 1 167 GLY 167 167 167 GLY GLY F . n 
F 1 168 GLN 168 168 168 GLN GLN F . n 
F 1 169 ALA 169 169 169 ALA ALA F . n 
F 1 170 PRO 170 170 170 PRO PRO F . n 
F 1 171 ILE 171 171 171 ILE ILE F . n 
F 1 172 SER 172 172 172 SER SER F . n 
F 1 173 LEU 173 173 173 LEU LEU F . n 
F 1 174 GLN 174 174 174 GLN GLN F . n 
F 1 175 ASN 175 175 175 ASN ASN F . n 
F 1 176 GLN 176 176 176 GLN GLN F . n 
F 1 177 LEU 177 177 177 LEU LEU F . n 
F 1 178 PHE 178 178 178 PHE PHE F . n 
F 1 179 SER 179 179 179 SER SER F . n 
F 1 180 HIS 180 180 180 HIS HIS F . n 
F 1 181 PHE 181 181 181 PHE PHE F . n 
F 1 182 GLY 182 182 182 GLY GLY F . n 
F 1 183 LEU 183 183 183 LEU LEU F . n 
F 1 184 LYS 184 184 184 LYS LYS F . n 
F 1 185 ARG 185 185 185 ARG ARG F . n 
F 1 186 GLN 186 186 186 GLN GLN F . n 
F 1 187 PHE 187 187 187 PHE PHE F . n 
F 1 188 SER 188 188 188 SER SER F . n 
F 1 189 VAL 189 189 189 VAL VAL F . n 
F 1 190 CYS 190 190 190 CYS CYS F . n 
F 1 191 LEU 191 191 191 LEU LEU F . n 
F 1 192 SER 192 192 192 SER SER F . n 
F 1 193 ARG 193 193 193 ARG ARG F . n 
F 1 194 TYR 194 194 194 TYR TYR F . n 
F 1 195 SER 195 195 195 SER SER F . n 
F 1 196 THR 196 196 196 THR THR F . n 
F 1 197 SER 197 197 197 SER SER F . n 
F 1 198 ASN 198 198 198 ASN ASN F . n 
F 1 199 GLY 199 199 199 GLY GLY F . n 
F 1 200 ALA 200 200 200 ALA ALA F . n 
F 1 201 ILE 201 201 201 ILE ILE F . n 
F 1 202 LEU 202 202 202 LEU LEU F . n 
F 1 203 PHE 203 203 203 PHE PHE F . n 
F 1 204 GLY 204 204 204 GLY GLY F . n 
F 1 205 ASP 205 205 205 ASP ASP F . n 
F 1 206 ILE 206 206 206 ILE ILE F . n 
F 1 207 ASN 207 207 207 ASN ASN F . n 
F 1 208 ASP 208 208 208 ASP ASP F . n 
F 1 209 PRO 209 209 209 PRO PRO F . n 
F 1 210 ASN 210 210 210 ASN ASN F . n 
F 1 211 ASN 211 211 211 ASN ASN F . n 
F 1 212 ASN 212 212 212 ASN ASN F . n 
F 1 213 ASN 213 213 213 ASN ASN F . n 
F 1 214 TYR 214 214 214 TYR TYR F . n 
F 1 215 ILE 215 215 215 ILE ILE F . n 
F 1 216 HIS 216 216 216 HIS HIS F . n 
F 1 217 ASN 217 217 217 ASN ASN F . n 
F 1 218 SER 218 218 218 SER SER F . n 
F 1 219 LEU 219 219 219 LEU LEU F . n 
F 1 220 ASP 220 220 220 ASP ASP F . n 
F 1 221 VAL 221 221 221 VAL VAL F . n 
F 1 222 LEU 222 222 222 LEU LEU F . n 
F 1 223 HIS 223 223 223 HIS HIS F . n 
F 1 224 ASP 224 224 224 ASP ASP F . n 
F 1 225 LEU 225 225 225 LEU LEU F . n 
F 1 226 VAL 226 226 226 VAL VAL F . n 
F 1 227 TYR 227 227 227 TYR TYR F . n 
F 1 228 THR 228 228 228 THR THR F . n 
F 1 229 PRO 229 229 229 PRO PRO F . n 
F 1 230 LEU 230 230 230 LEU LEU F . n 
F 1 231 THR 231 231 231 THR THR F . n 
F 1 232 ILE 232 232 232 ILE ILE F . n 
F 1 233 SER 233 233 233 SER SER F . n 
F 1 234 LYS 234 234 234 LYS LYS F . n 
F 1 235 GLN 235 235 235 GLN GLN F . n 
F 1 236 GLY 236 236 236 GLY GLY F . n 
F 1 237 GLU 237 237 237 GLU GLU F . n 
F 1 238 TYR 238 238 238 TYR TYR F . n 
F 1 239 PHE 239 239 239 PHE PHE F . n 
F 1 240 ILE 240 240 240 ILE ILE F . n 
F 1 241 GLN 241 241 241 GLN GLN F . n 
F 1 242 VAL 242 242 242 VAL VAL F . n 
F 1 243 ASN 243 243 243 ASN ASN F . n 
F 1 244 ALA 244 244 244 ALA ALA F . n 
F 1 245 ILE 245 245 245 ILE ILE F . n 
F 1 246 ARG 246 246 246 ARG ARG F . n 
F 1 247 VAL 247 247 247 VAL VAL F . n 
F 1 248 ASN 248 248 248 ASN ASN F . n 
F 1 249 LYS 249 249 249 LYS LYS F . n 
F 1 250 HIS 250 250 250 HIS HIS F . n 
F 1 251 LEU 251 251 251 LEU LEU F . n 
F 1 252 VAL 252 252 252 VAL VAL F . n 
F 1 253 ILE 253 253 253 ILE ILE F . n 
F 1 254 PRO 254 254 254 PRO PRO F . n 
F 1 255 THR 255 255 255 THR THR F . n 
F 1 256 LYS 256 256 ?   ?   ?   F . n 
F 1 257 ASN 257 257 ?   ?   ?   F . n 
F 1 258 PRO 258 258 ?   ?   ?   F . n 
F 1 259 PHE 259 259 ?   ?   ?   F . n 
F 1 260 ILE 260 260 ?   ?   ?   F . n 
F 1 261 SER 261 261 ?   ?   ?   F . n 
F 1 262 PRO 262 262 ?   ?   ?   F . n 
F 1 263 SER 263 263 ?   ?   ?   F . n 
F 1 264 SER 264 264 ?   ?   ?   F . n 
F 1 265 THR 265 265 ?   ?   ?   F . n 
F 1 266 SER 266 266 ?   ?   ?   F . n 
F 1 267 TYR 267 267 ?   ?   ?   F . n 
F 1 268 HIS 268 268 ?   ?   ?   F . n 
F 1 269 GLY 269 269 ?   ?   ?   F . n 
F 1 270 SER 270 270 ?   ?   ?   F . n 
F 1 271 GLY 271 271 271 GLY GLY F . n 
F 1 272 GLU 272 272 272 GLU GLU F . n 
F 1 273 ILE 273 273 273 ILE ILE F . n 
F 1 274 GLY 274 274 274 GLY GLY F . n 
F 1 275 GLY 275 275 275 GLY GLY F . n 
F 1 276 ALA 276 276 276 ALA ALA F . n 
F 1 277 LEU 277 277 277 LEU LEU F . n 
F 1 278 ILE 278 278 278 ILE ILE F . n 
F 1 279 THR 279 279 279 THR THR F . n 
F 1 280 THR 280 280 280 THR THR F . n 
F 1 281 THR 281 281 281 THR THR F . n 
F 1 282 HIS 282 282 282 HIS HIS F . n 
F 1 283 PRO 283 283 283 PRO PRO F . n 
F 1 284 TYR 284 284 284 TYR TYR F . n 
F 1 285 THR 285 285 285 THR THR F . n 
F 1 286 VAL 286 286 286 VAL VAL F . n 
F 1 287 LEU 287 287 287 LEU LEU F . n 
F 1 288 SER 288 288 288 SER SER F . n 
F 1 289 HIS 289 289 289 HIS HIS F . n 
F 1 290 SER 290 290 290 SER SER F . n 
F 1 291 ILE 291 291 291 ILE ILE F . n 
F 1 292 PHE 292 292 292 PHE PHE F . n 
F 1 293 GLU 293 293 293 GLU GLU F . n 
F 1 294 VAL 294 294 294 VAL VAL F . n 
F 1 295 PHE 295 295 295 PHE PHE F . n 
F 1 296 THR 296 296 296 THR THR F . n 
F 1 297 GLN 297 297 297 GLN GLN F . n 
F 1 298 VAL 298 298 298 VAL VAL F . n 
F 1 299 PHE 299 299 299 PHE PHE F . n 
F 1 300 ALA 300 300 300 ALA ALA F . n 
F 1 301 ASN 301 301 301 ASN ASN F . n 
F 1 302 ASN 302 302 302 ASN ASN F . n 
F 1 303 MET 303 303 303 MET MET F . n 
F 1 304 PRO 304 304 304 PRO PRO F . n 
F 1 305 LYS 305 305 305 LYS LYS F . n 
F 1 306 GLN 306 306 306 GLN GLN F . n 
F 1 307 ALA 307 307 307 ALA ALA F . n 
F 1 308 GLN 308 308 308 GLN GLN F . n 
F 1 309 VAL 309 309 309 VAL VAL F . n 
F 1 310 LYS 310 310 310 LYS LYS F . n 
F 1 311 ALA 311 311 311 ALA ALA F . n 
F 1 312 VAL 312 312 312 VAL VAL F . n 
F 1 313 GLY 313 313 313 GLY GLY F . n 
F 1 314 PRO 314 314 314 PRO PRO F . n 
F 1 315 PHE 315 315 315 PHE PHE F . n 
F 1 316 GLY 316 316 316 GLY GLY F . n 
F 1 317 LEU 317 317 317 LEU LEU F . n 
F 1 318 CYS 318 318 318 CYS CYS F . n 
F 1 319 TYR 319 319 319 TYR TYR F . n 
F 1 320 ASP 320 320 320 ASP ASP F . n 
F 1 321 SER 321 321 321 SER SER F . n 
F 1 322 ARG 322 322 322 ARG ARG F . n 
F 1 323 LYS 323 323 323 LYS LYS F . n 
F 1 324 ILE 324 324 324 ILE ILE F . n 
F 1 325 SER 325 325 325 SER SER F . n 
F 1 326 GLY 326 326 326 GLY GLY F . n 
F 1 327 GLY 327 327 327 GLY GLY F . n 
F 1 328 ALA 328 328 328 ALA ALA F . n 
F 1 329 PRO 329 329 329 PRO PRO F . n 
F 1 330 SER 330 330 330 SER SER F . n 
F 1 331 VAL 331 331 331 VAL VAL F . n 
F 1 332 ASP 332 332 332 ASP ASP F . n 
F 1 333 LEU 333 333 333 LEU LEU F . n 
F 1 334 ILE 334 334 334 ILE ILE F . n 
F 1 335 LEU 335 335 335 LEU LEU F . n 
F 1 336 ASP 336 336 336 ASP ASP F . n 
F 1 337 LYS 337 337 337 LYS LYS F . n 
F 1 338 ASN 338 338 338 ASN ASN F . n 
F 1 339 ASP 339 339 339 ASP ASP F . n 
F 1 340 ALA 340 340 340 ALA ALA F . n 
F 1 341 VAL 341 341 341 VAL VAL F . n 
F 1 342 TRP 342 342 342 TRP TRP F . n 
F 1 343 ARG 343 343 343 ARG ARG F . n 
F 1 344 ILE 344 344 344 ILE ILE F . n 
F 1 345 SER 345 345 345 SER SER F . n 
F 1 346 SER 346 346 346 SER SER F . n 
F 1 347 GLU 347 347 347 GLU GLU F . n 
F 1 348 ASN 348 348 348 ASN ASN F . n 
F 1 349 PHE 349 349 349 PHE PHE F . n 
F 1 350 MET 350 350 350 MET MET F . n 
F 1 351 VAL 351 351 351 VAL VAL F . n 
F 1 352 GLN 352 352 352 GLN GLN F . n 
F 1 353 ALA 353 353 353 ALA ALA F . n 
F 1 354 GLN 354 354 354 GLN GLN F . n 
F 1 355 ASP 355 355 355 ASP ASP F . n 
F 1 356 GLY 356 356 356 GLY GLY F . n 
F 1 357 VAL 357 357 357 VAL VAL F . n 
F 1 358 SER 358 358 358 SER SER F . n 
F 1 359 CYS 359 359 359 CYS CYS F . n 
F 1 360 LEU 360 360 360 LEU LEU F . n 
F 1 361 GLY 361 361 361 GLY GLY F . n 
F 1 362 PHE 362 362 362 PHE PHE F . n 
F 1 363 VAL 363 363 363 VAL VAL F . n 
F 1 364 ASP 364 364 364 ASP ASP F . n 
F 1 365 GLY 365 365 365 GLY GLY F . n 
F 1 366 GLY 366 366 366 GLY GLY F . n 
F 1 367 VAL 367 367 367 VAL VAL F . n 
F 1 368 HIS 368 368 368 HIS HIS F . n 
F 1 369 ALA 369 369 369 ALA ALA F . n 
F 1 370 ARG 370 370 370 ARG ARG F . n 
F 1 371 ALA 371 371 371 ALA ALA F . n 
F 1 372 GLY 372 372 372 GLY GLY F . n 
F 1 373 ILE 373 373 373 ILE ILE F . n 
F 1 374 ALA 374 374 374 ALA ALA F . n 
F 1 375 LEU 375 375 375 LEU LEU F . n 
F 1 376 GLY 376 376 376 GLY GLY F . n 
F 1 377 ALA 377 377 377 ALA ALA F . n 
F 1 378 HIS 378 378 378 HIS HIS F . n 
F 1 379 HIS 379 379 379 HIS HIS F . n 
F 1 380 LEU 380 380 380 LEU LEU F . n 
F 1 381 GLU 381 381 381 GLU GLU F . n 
F 1 382 GLU 382 382 382 GLU GLU F . n 
F 1 383 ASN 383 383 383 ASN ASN F . n 
F 1 384 LEU 384 384 384 LEU LEU F . n 
F 1 385 VAL 385 385 385 VAL VAL F . n 
F 1 386 VAL 386 386 386 VAL VAL F . n 
F 1 387 PHE 387 387 387 PHE PHE F . n 
F 1 388 ASP 388 388 388 ASP ASP F . n 
F 1 389 LEU 389 389 389 LEU LEU F . n 
F 1 390 GLU 390 390 390 GLU GLU F . n 
F 1 391 ARG 391 391 391 ARG ARG F . n 
F 1 392 SER 392 392 392 SER SER F . n 
F 1 393 ARG 393 393 393 ARG ARG F . n 
F 1 394 VAL 394 394 394 VAL VAL F . n 
F 1 395 GLY 395 395 395 GLY GLY F . n 
F 1 396 PHE 396 396 396 PHE PHE F . n 
F 1 397 ASN 397 397 397 ASN ASN F . n 
F 1 398 SER 398 398 398 SER SER F . n 
F 1 399 ASN 399 399 399 ASN ASN F . n 
F 1 400 SER 400 400 400 SER SER F . n 
F 1 401 LEU 401 401 401 LEU LEU F . n 
F 1 402 LYS 402 402 402 LYS LYS F . n 
F 1 403 SER 403 403 403 SER SER F . n 
F 1 404 TYR 404 404 404 TYR TYR F . n 
F 1 405 GLY 405 405 405 GLY GLY F . n 
F 1 406 LYS 406 406 406 LYS LYS F . n 
F 1 407 THR 407 407 407 THR THR F . n 
F 1 408 CYS 408 408 408 CYS CYS F . n 
F 1 409 SER 409 409 409 SER SER F . n 
F 1 410 ASN 410 410 410 ASN ASN F . n 
F 1 411 LEU 411 411 411 LEU LEU F . n 
F 1 412 PHE 412 412 412 PHE PHE F . n 
F 1 413 ASP 413 413 413 ASP ASP F . n 
F 1 414 LEU 414 414 414 LEU LEU F . n 
F 1 415 ASN 415 415 415 ASN ASN F . n 
F 1 416 ASN 416 416 416 ASN ASN F . n 
F 1 417 PRO 417 417 ?   ?   ?   F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G  2 NAG 1   501 501 NAG NAG A . 
H  2 NAG 2   502 502 NAG NAG A . 
I  3 FUC 3   503 503 FUC FUC A . 
J  4 EDO 1   504 504 EDO EDO A . 
K  4 EDO 1   505 505 EDO EDO A . 
L  4 EDO 1   506 506 EDO EDO A . 
M  4 EDO 1   507 507 EDO EDO A . 
N  4 EDO 1   508 508 EDO EDO A . 
O  4 EDO 1   509 509 EDO EDO A . 
P  2 NAG 1   501 501 NAG NAG B . 
Q  4 EDO 1   502 502 EDO EDO B . 
R  4 EDO 1   503 503 EDO EDO B . 
S  4 EDO 1   504 504 EDO EDO B . 
T  4 EDO 1   505 505 EDO EDO B . 
U  4 EDO 1   506 506 EDO EDO B . 
V  2 NAG 1   501 501 NAG NAG C . 
W  4 EDO 1   502 502 EDO EDO C . 
X  4 EDO 1   503 503 EDO EDO C . 
Y  4 EDO 1   504 504 EDO EDO C . 
Z  4 EDO 1   505 505 EDO EDO C . 
AA 4 EDO 1   506 506 EDO EDO C . 
BA 2 NAG 1   501 501 NAG NAG D . 
CA 4 EDO 1   502 502 EDO EDO D . 
DA 4 EDO 1   503 503 EDO EDO D . 
EA 4 EDO 1   504 504 EDO EDO D . 
FA 4 EDO 1   505 505 EDO EDO D . 
GA 4 EDO 1   506 506 EDO EDO D . 
HA 4 EDO 1   507 507 EDO EDO D . 
IA 4 EDO 1   508 508 EDO EDO D . 
JA 4 EDO 1   509 509 EDO EDO D . 
KA 4 EDO 1   510 510 EDO EDO D . 
LA 4 EDO 1   501 501 EDO EDO E . 
MA 2 NAG 1   501 501 NAG NAG F . 
NA 2 NAG 2   502 502 NAG NAG F . 
OA 4 EDO 1   503 503 EDO EDO F . 
PA 4 EDO 1   504 504 EDO EDO F . 
QA 4 EDO 1   505 505 EDO EDO F . 
RA 4 EDO 1   506 506 EDO EDO F . 
SA 4 EDO 1   507 507 EDO EDO F . 
TA 4 EDO 1   508 508 EDO EDO F . 
UA 5 HOH 1   601 601 HOH HOH A . 
UA 5 HOH 2   602 602 HOH HOH A . 
UA 5 HOH 3   603 603 HOH HOH A . 
UA 5 HOH 4   604 604 HOH HOH A . 
UA 5 HOH 5   605 605 HOH HOH A . 
UA 5 HOH 6   606 606 HOH HOH A . 
UA 5 HOH 7   607 607 HOH HOH A . 
UA 5 HOH 8   608 608 HOH HOH A . 
UA 5 HOH 9   609 609 HOH HOH A . 
UA 5 HOH 10  610 610 HOH HOH A . 
UA 5 HOH 11  611 611 HOH HOH A . 
UA 5 HOH 12  612 612 HOH HOH A . 
UA 5 HOH 13  613 613 HOH HOH A . 
UA 5 HOH 14  614 614 HOH HOH A . 
UA 5 HOH 15  615 615 HOH HOH A . 
UA 5 HOH 16  616 616 HOH HOH A . 
UA 5 HOH 17  617 617 HOH HOH A . 
UA 5 HOH 18  618 618 HOH HOH A . 
UA 5 HOH 19  619 619 HOH HOH A . 
UA 5 HOH 20  620 620 HOH HOH A . 
UA 5 HOH 21  621 621 HOH HOH A . 
UA 5 HOH 22  622 622 HOH HOH A . 
UA 5 HOH 23  623 623 HOH HOH A . 
UA 5 HOH 24  624 624 HOH HOH A . 
UA 5 HOH 25  625 625 HOH HOH A . 
UA 5 HOH 26  626 626 HOH HOH A . 
UA 5 HOH 27  627 627 HOH HOH A . 
UA 5 HOH 28  628 628 HOH HOH A . 
UA 5 HOH 29  629 629 HOH HOH A . 
UA 5 HOH 30  630 630 HOH HOH A . 
UA 5 HOH 31  631 632 HOH HOH A . 
UA 5 HOH 32  632 633 HOH HOH A . 
UA 5 HOH 33  633 634 HOH HOH A . 
UA 5 HOH 34  634 635 HOH HOH A . 
UA 5 HOH 35  635 636 HOH HOH A . 
UA 5 HOH 36  636 637 HOH HOH A . 
UA 5 HOH 37  637 638 HOH HOH A . 
UA 5 HOH 38  638 639 HOH HOH A . 
UA 5 HOH 39  639 640 HOH HOH A . 
UA 5 HOH 40  640 641 HOH HOH A . 
UA 5 HOH 41  641 642 HOH HOH A . 
UA 5 HOH 42  642 643 HOH HOH A . 
UA 5 HOH 43  643 644 HOH HOH A . 
UA 5 HOH 44  644 645 HOH HOH A . 
UA 5 HOH 45  645 646 HOH HOH A . 
UA 5 HOH 46  646 647 HOH HOH A . 
UA 5 HOH 47  647 648 HOH HOH A . 
UA 5 HOH 48  648 649 HOH HOH A . 
UA 5 HOH 49  649 650 HOH HOH A . 
UA 5 HOH 50  650 651 HOH HOH A . 
UA 5 HOH 51  651 652 HOH HOH A . 
UA 5 HOH 52  652 653 HOH HOH A . 
UA 5 HOH 53  653 654 HOH HOH A . 
UA 5 HOH 54  654 655 HOH HOH A . 
UA 5 HOH 55  655 656 HOH HOH A . 
UA 5 HOH 56  656 657 HOH HOH A . 
UA 5 HOH 57  657 658 HOH HOH A . 
UA 5 HOH 58  658 659 HOH HOH A . 
UA 5 HOH 59  659 660 HOH HOH A . 
UA 5 HOH 60  660 661 HOH HOH A . 
UA 5 HOH 61  661 662 HOH HOH A . 
UA 5 HOH 62  662 663 HOH HOH A . 
UA 5 HOH 63  663 664 HOH HOH A . 
UA 5 HOH 64  664 665 HOH HOH A . 
UA 5 HOH 65  665 666 HOH HOH A . 
UA 5 HOH 66  666 667 HOH HOH A . 
UA 5 HOH 67  667 668 HOH HOH A . 
UA 5 HOH 68  668 670 HOH HOH A . 
UA 5 HOH 69  669 671 HOH HOH A . 
UA 5 HOH 70  670 672 HOH HOH A . 
UA 5 HOH 71  671 673 HOH HOH A . 
UA 5 HOH 72  672 674 HOH HOH A . 
UA 5 HOH 73  673 675 HOH HOH A . 
UA 5 HOH 74  674 676 HOH HOH A . 
UA 5 HOH 75  675 677 HOH HOH A . 
UA 5 HOH 76  676 678 HOH HOH A . 
UA 5 HOH 77  677 679 HOH HOH A . 
UA 5 HOH 78  678 680 HOH HOH A . 
UA 5 HOH 79  679 681 HOH HOH A . 
UA 5 HOH 80  680 682 HOH HOH A . 
UA 5 HOH 81  681 683 HOH HOH A . 
UA 5 HOH 82  682 684 HOH HOH A . 
UA 5 HOH 83  683 685 HOH HOH A . 
UA 5 HOH 84  684 686 HOH HOH A . 
UA 5 HOH 85  685 687 HOH HOH A . 
UA 5 HOH 86  686 688 HOH HOH A . 
UA 5 HOH 87  687 689 HOH HOH A . 
UA 5 HOH 88  688 690 HOH HOH A . 
UA 5 HOH 89  689 691 HOH HOH A . 
UA 5 HOH 90  690 692 HOH HOH A . 
UA 5 HOH 91  691 693 HOH HOH A . 
UA 5 HOH 92  692 694 HOH HOH A . 
UA 5 HOH 93  693 695 HOH HOH A . 
UA 5 HOH 94  694 696 HOH HOH A . 
UA 5 HOH 95  695 697 HOH HOH A . 
UA 5 HOH 96  696 698 HOH HOH A . 
UA 5 HOH 97  697 699 HOH HOH A . 
UA 5 HOH 98  698 700 HOH HOH A . 
UA 5 HOH 99  699 701 HOH HOH A . 
UA 5 HOH 100 700 702 HOH HOH A . 
UA 5 HOH 101 701 703 HOH HOH A . 
UA 5 HOH 102 702 704 HOH HOH A . 
UA 5 HOH 103 703 705 HOH HOH A . 
UA 5 HOH 104 704 706 HOH HOH A . 
UA 5 HOH 105 705 707 HOH HOH A . 
UA 5 HOH 106 706 708 HOH HOH A . 
UA 5 HOH 107 707 709 HOH HOH A . 
UA 5 HOH 108 708 710 HOH HOH A . 
UA 5 HOH 109 709 711 HOH HOH A . 
UA 5 HOH 110 710 712 HOH HOH A . 
UA 5 HOH 111 711 713 HOH HOH A . 
UA 5 HOH 112 712 714 HOH HOH A . 
UA 5 HOH 113 713 715 HOH HOH A . 
UA 5 HOH 114 714 716 HOH HOH A . 
UA 5 HOH 115 715 717 HOH HOH A . 
UA 5 HOH 116 716 718 HOH HOH A . 
UA 5 HOH 117 717 719 HOH HOH A . 
UA 5 HOH 118 718 720 HOH HOH A . 
UA 5 HOH 119 719 721 HOH HOH A . 
UA 5 HOH 120 720 722 HOH HOH A . 
UA 5 HOH 121 721 723 HOH HOH A . 
UA 5 HOH 122 722 724 HOH HOH A . 
UA 5 HOH 123 723 725 HOH HOH A . 
UA 5 HOH 124 724 726 HOH HOH A . 
UA 5 HOH 125 725 727 HOH HOH A . 
UA 5 HOH 126 726 728 HOH HOH A . 
UA 5 HOH 127 727 729 HOH HOH A . 
UA 5 HOH 128 728 730 HOH HOH A . 
UA 5 HOH 129 729 731 HOH HOH A . 
UA 5 HOH 130 730 732 HOH HOH A . 
UA 5 HOH 131 731 733 HOH HOH A . 
UA 5 HOH 132 732 734 HOH HOH A . 
UA 5 HOH 133 733 735 HOH HOH A . 
UA 5 HOH 134 734 736 HOH HOH A . 
UA 5 HOH 135 735 737 HOH HOH A . 
UA 5 HOH 136 736 738 HOH HOH A . 
UA 5 HOH 137 737 739 HOH HOH A . 
UA 5 HOH 138 738 740 HOH HOH A . 
UA 5 HOH 139 739 741 HOH HOH A . 
UA 5 HOH 140 740 742 HOH HOH A . 
UA 5 HOH 141 741 743 HOH HOH A . 
UA 5 HOH 142 742 744 HOH HOH A . 
UA 5 HOH 143 743 745 HOH HOH A . 
VA 5 HOH 1   601 601 HOH HOH B . 
VA 5 HOH 2   602 602 HOH HOH B . 
VA 5 HOH 3   603 603 HOH HOH B . 
VA 5 HOH 4   604 604 HOH HOH B . 
VA 5 HOH 5   605 605 HOH HOH B . 
VA 5 HOH 6   606 606 HOH HOH B . 
VA 5 HOH 7   607 607 HOH HOH B . 
VA 5 HOH 8   608 608 HOH HOH B . 
VA 5 HOH 9   609 609 HOH HOH B . 
VA 5 HOH 10  610 610 HOH HOH B . 
VA 5 HOH 11  611 611 HOH HOH B . 
VA 5 HOH 12  612 612 HOH HOH B . 
VA 5 HOH 13  613 613 HOH HOH B . 
VA 5 HOH 14  614 614 HOH HOH B . 
VA 5 HOH 15  615 615 HOH HOH B . 
VA 5 HOH 16  616 616 HOH HOH B . 
VA 5 HOH 17  617 617 HOH HOH B . 
VA 5 HOH 18  618 618 HOH HOH B . 
VA 5 HOH 19  619 619 HOH HOH B . 
VA 5 HOH 20  620 620 HOH HOH B . 
VA 5 HOH 21  621 621 HOH HOH B . 
VA 5 HOH 22  622 622 HOH HOH B . 
VA 5 HOH 23  623 623 HOH HOH B . 
VA 5 HOH 24  624 624 HOH HOH B . 
VA 5 HOH 25  625 625 HOH HOH B . 
VA 5 HOH 26  626 626 HOH HOH B . 
VA 5 HOH 27  627 627 HOH HOH B . 
VA 5 HOH 28  628 628 HOH HOH B . 
VA 5 HOH 29  629 629 HOH HOH B . 
VA 5 HOH 30  630 630 HOH HOH B . 
VA 5 HOH 31  631 631 HOH HOH B . 
VA 5 HOH 32  632 632 HOH HOH B . 
VA 5 HOH 33  633 633 HOH HOH B . 
VA 5 HOH 34  634 634 HOH HOH B . 
VA 5 HOH 35  635 635 HOH HOH B . 
VA 5 HOH 36  636 636 HOH HOH B . 
VA 5 HOH 37  637 637 HOH HOH B . 
VA 5 HOH 38  638 638 HOH HOH B . 
VA 5 HOH 39  639 639 HOH HOH B . 
VA 5 HOH 40  640 640 HOH HOH B . 
VA 5 HOH 41  641 641 HOH HOH B . 
VA 5 HOH 42  642 642 HOH HOH B . 
VA 5 HOH 43  643 643 HOH HOH B . 
VA 5 HOH 44  644 644 HOH HOH B . 
VA 5 HOH 45  645 645 HOH HOH B . 
VA 5 HOH 46  646 646 HOH HOH B . 
VA 5 HOH 47  647 647 HOH HOH B . 
VA 5 HOH 48  648 648 HOH HOH B . 
VA 5 HOH 49  649 649 HOH HOH B . 
VA 5 HOH 50  650 650 HOH HOH B . 
VA 5 HOH 51  651 651 HOH HOH B . 
VA 5 HOH 52  652 652 HOH HOH B . 
VA 5 HOH 53  653 653 HOH HOH B . 
VA 5 HOH 54  654 654 HOH HOH B . 
VA 5 HOH 55  655 655 HOH HOH B . 
VA 5 HOH 56  656 656 HOH HOH B . 
VA 5 HOH 57  657 657 HOH HOH B . 
VA 5 HOH 58  658 658 HOH HOH B . 
VA 5 HOH 59  659 659 HOH HOH B . 
VA 5 HOH 60  660 660 HOH HOH B . 
VA 5 HOH 61  661 661 HOH HOH B . 
VA 5 HOH 62  662 662 HOH HOH B . 
VA 5 HOH 63  663 663 HOH HOH B . 
VA 5 HOH 64  664 664 HOH HOH B . 
VA 5 HOH 65  665 665 HOH HOH B . 
VA 5 HOH 66  666 666 HOH HOH B . 
VA 5 HOH 67  667 667 HOH HOH B . 
VA 5 HOH 68  668 668 HOH HOH B . 
VA 5 HOH 69  669 669 HOH HOH B . 
VA 5 HOH 70  670 670 HOH HOH B . 
VA 5 HOH 71  671 672 HOH HOH B . 
VA 5 HOH 72  672 673 HOH HOH B . 
VA 5 HOH 73  673 674 HOH HOH B . 
VA 5 HOH 74  674 675 HOH HOH B . 
VA 5 HOH 75  675 676 HOH HOH B . 
VA 5 HOH 76  676 677 HOH HOH B . 
VA 5 HOH 77  677 678 HOH HOH B . 
VA 5 HOH 78  678 679 HOH HOH B . 
VA 5 HOH 79  679 680 HOH HOH B . 
VA 5 HOH 80  680 681 HOH HOH B . 
VA 5 HOH 81  681 682 HOH HOH B . 
VA 5 HOH 82  682 683 HOH HOH B . 
VA 5 HOH 83  683 684 HOH HOH B . 
VA 5 HOH 84  684 685 HOH HOH B . 
VA 5 HOH 85  685 686 HOH HOH B . 
VA 5 HOH 86  686 687 HOH HOH B . 
VA 5 HOH 87  687 688 HOH HOH B . 
VA 5 HOH 88  688 689 HOH HOH B . 
VA 5 HOH 89  689 690 HOH HOH B . 
VA 5 HOH 90  690 691 HOH HOH B . 
VA 5 HOH 91  691 692 HOH HOH B . 
VA 5 HOH 92  692 693 HOH HOH B . 
VA 5 HOH 93  693 694 HOH HOH B . 
VA 5 HOH 94  694 695 HOH HOH B . 
VA 5 HOH 95  695 696 HOH HOH B . 
VA 5 HOH 96  696 697 HOH HOH B . 
VA 5 HOH 97  697 698 HOH HOH B . 
VA 5 HOH 98  698 699 HOH HOH B . 
VA 5 HOH 99  699 700 HOH HOH B . 
VA 5 HOH 100 700 701 HOH HOH B . 
VA 5 HOH 101 701 702 HOH HOH B . 
VA 5 HOH 102 702 703 HOH HOH B . 
VA 5 HOH 103 703 704 HOH HOH B . 
VA 5 HOH 104 704 705 HOH HOH B . 
VA 5 HOH 105 705 706 HOH HOH B . 
VA 5 HOH 106 706 707 HOH HOH B . 
VA 5 HOH 107 707 708 HOH HOH B . 
VA 5 HOH 108 708 709 HOH HOH B . 
VA 5 HOH 109 709 710 HOH HOH B . 
VA 5 HOH 110 710 711 HOH HOH B . 
VA 5 HOH 111 711 712 HOH HOH B . 
VA 5 HOH 112 712 713 HOH HOH B . 
VA 5 HOH 113 713 714 HOH HOH B . 
VA 5 HOH 114 714 715 HOH HOH B . 
VA 5 HOH 115 715 716 HOH HOH B . 
VA 5 HOH 116 716 717 HOH HOH B . 
VA 5 HOH 117 717 718 HOH HOH B . 
VA 5 HOH 118 718 719 HOH HOH B . 
VA 5 HOH 119 719 720 HOH HOH B . 
VA 5 HOH 120 720 721 HOH HOH B . 
VA 5 HOH 121 721 722 HOH HOH B . 
VA 5 HOH 122 722 723 HOH HOH B . 
VA 5 HOH 123 723 724 HOH HOH B . 
VA 5 HOH 124 724 725 HOH HOH B . 
VA 5 HOH 125 725 726 HOH HOH B . 
VA 5 HOH 126 726 727 HOH HOH B . 
VA 5 HOH 127 727 728 HOH HOH B . 
VA 5 HOH 128 728 729 HOH HOH B . 
VA 5 HOH 129 729 730 HOH HOH B . 
VA 5 HOH 130 730 731 HOH HOH B . 
VA 5 HOH 131 731 732 HOH HOH B . 
VA 5 HOH 132 732 733 HOH HOH B . 
VA 5 HOH 133 733 734 HOH HOH B . 
VA 5 HOH 134 734 735 HOH HOH B . 
VA 5 HOH 135 735 736 HOH HOH B . 
VA 5 HOH 136 736 737 HOH HOH B . 
VA 5 HOH 137 737 738 HOH HOH B . 
VA 5 HOH 138 738 739 HOH HOH B . 
VA 5 HOH 139 739 740 HOH HOH B . 
VA 5 HOH 140 740 741 HOH HOH B . 
VA 5 HOH 141 741 742 HOH HOH B . 
VA 5 HOH 142 742 743 HOH HOH B . 
VA 5 HOH 143 743 744 HOH HOH B . 
VA 5 HOH 144 744 745 HOH HOH B . 
VA 5 HOH 145 745 746 HOH HOH B . 
VA 5 HOH 146 746 711 HOH HOH B . 
WA 5 HOH 1   601 671 HOH HOH C . 
WA 5 HOH 2   602 601 HOH HOH C . 
WA 5 HOH 3   603 602 HOH HOH C . 
WA 5 HOH 4   604 603 HOH HOH C . 
WA 5 HOH 5   605 604 HOH HOH C . 
WA 5 HOH 6   606 605 HOH HOH C . 
WA 5 HOH 7   607 606 HOH HOH C . 
WA 5 HOH 8   608 607 HOH HOH C . 
WA 5 HOH 9   609 608 HOH HOH C . 
WA 5 HOH 10  610 609 HOH HOH C . 
WA 5 HOH 11  611 610 HOH HOH C . 
WA 5 HOH 12  612 611 HOH HOH C . 
WA 5 HOH 13  613 612 HOH HOH C . 
WA 5 HOH 14  614 613 HOH HOH C . 
WA 5 HOH 15  615 614 HOH HOH C . 
WA 5 HOH 16  616 615 HOH HOH C . 
WA 5 HOH 17  617 616 HOH HOH C . 
WA 5 HOH 18  618 617 HOH HOH C . 
WA 5 HOH 19  619 618 HOH HOH C . 
WA 5 HOH 20  620 619 HOH HOH C . 
WA 5 HOH 21  621 620 HOH HOH C . 
WA 5 HOH 22  622 621 HOH HOH C . 
WA 5 HOH 23  623 622 HOH HOH C . 
WA 5 HOH 24  624 623 HOH HOH C . 
WA 5 HOH 25  625 624 HOH HOH C . 
WA 5 HOH 26  626 625 HOH HOH C . 
WA 5 HOH 27  627 626 HOH HOH C . 
WA 5 HOH 28  628 627 HOH HOH C . 
WA 5 HOH 29  629 628 HOH HOH C . 
WA 5 HOH 30  630 629 HOH HOH C . 
WA 5 HOH 31  631 630 HOH HOH C . 
WA 5 HOH 32  632 631 HOH HOH C . 
WA 5 HOH 33  633 632 HOH HOH C . 
WA 5 HOH 34  634 633 HOH HOH C . 
WA 5 HOH 35  635 634 HOH HOH C . 
WA 5 HOH 36  636 635 HOH HOH C . 
WA 5 HOH 37  637 636 HOH HOH C . 
WA 5 HOH 38  638 637 HOH HOH C . 
WA 5 HOH 39  639 638 HOH HOH C . 
WA 5 HOH 40  640 639 HOH HOH C . 
WA 5 HOH 41  641 640 HOH HOH C . 
WA 5 HOH 42  642 641 HOH HOH C . 
WA 5 HOH 43  643 642 HOH HOH C . 
WA 5 HOH 44  644 643 HOH HOH C . 
WA 5 HOH 45  645 644 HOH HOH C . 
WA 5 HOH 46  646 645 HOH HOH C . 
WA 5 HOH 47  647 646 HOH HOH C . 
WA 5 HOH 48  648 647 HOH HOH C . 
WA 5 HOH 49  649 648 HOH HOH C . 
WA 5 HOH 50  650 649 HOH HOH C . 
WA 5 HOH 51  651 650 HOH HOH C . 
WA 5 HOH 52  652 651 HOH HOH C . 
WA 5 HOH 53  653 652 HOH HOH C . 
WA 5 HOH 54  654 653 HOH HOH C . 
WA 5 HOH 55  655 654 HOH HOH C . 
WA 5 HOH 56  656 655 HOH HOH C . 
WA 5 HOH 57  657 656 HOH HOH C . 
WA 5 HOH 58  658 657 HOH HOH C . 
WA 5 HOH 59  659 658 HOH HOH C . 
WA 5 HOH 60  660 659 HOH HOH C . 
WA 5 HOH 61  661 660 HOH HOH C . 
WA 5 HOH 62  662 661 HOH HOH C . 
WA 5 HOH 63  663 662 HOH HOH C . 
WA 5 HOH 64  664 663 HOH HOH C . 
WA 5 HOH 65  665 664 HOH HOH C . 
WA 5 HOH 66  666 665 HOH HOH C . 
WA 5 HOH 67  667 666 HOH HOH C . 
WA 5 HOH 68  668 667 HOH HOH C . 
WA 5 HOH 69  669 668 HOH HOH C . 
WA 5 HOH 70  670 669 HOH HOH C . 
WA 5 HOH 71  671 670 HOH HOH C . 
WA 5 HOH 72  672 671 HOH HOH C . 
WA 5 HOH 73  673 672 HOH HOH C . 
WA 5 HOH 74  674 673 HOH HOH C . 
WA 5 HOH 75  675 674 HOH HOH C . 
WA 5 HOH 76  676 675 HOH HOH C . 
WA 5 HOH 77  677 676 HOH HOH C . 
WA 5 HOH 78  678 677 HOH HOH C . 
WA 5 HOH 79  679 678 HOH HOH C . 
WA 5 HOH 80  680 679 HOH HOH C . 
WA 5 HOH 81  681 680 HOH HOH C . 
WA 5 HOH 82  682 681 HOH HOH C . 
WA 5 HOH 83  683 682 HOH HOH C . 
WA 5 HOH 84  684 683 HOH HOH C . 
WA 5 HOH 85  685 684 HOH HOH C . 
WA 5 HOH 86  686 685 HOH HOH C . 
WA 5 HOH 87  687 686 HOH HOH C . 
WA 5 HOH 88  688 687 HOH HOH C . 
WA 5 HOH 89  689 688 HOH HOH C . 
WA 5 HOH 90  690 689 HOH HOH C . 
WA 5 HOH 91  691 690 HOH HOH C . 
WA 5 HOH 92  692 691 HOH HOH C . 
WA 5 HOH 93  693 692 HOH HOH C . 
WA 5 HOH 94  694 693 HOH HOH C . 
WA 5 HOH 95  695 694 HOH HOH C . 
WA 5 HOH 96  696 695 HOH HOH C . 
WA 5 HOH 97  697 696 HOH HOH C . 
WA 5 HOH 98  698 697 HOH HOH C . 
WA 5 HOH 99  699 698 HOH HOH C . 
WA 5 HOH 100 700 699 HOH HOH C . 
WA 5 HOH 101 701 700 HOH HOH C . 
WA 5 HOH 102 702 701 HOH HOH C . 
WA 5 HOH 103 703 702 HOH HOH C . 
WA 5 HOH 104 704 703 HOH HOH C . 
WA 5 HOH 105 705 704 HOH HOH C . 
WA 5 HOH 106 706 705 HOH HOH C . 
WA 5 HOH 107 707 706 HOH HOH C . 
WA 5 HOH 108 708 707 HOH HOH C . 
WA 5 HOH 109 709 708 HOH HOH C . 
WA 5 HOH 110 710 709 HOH HOH C . 
WA 5 HOH 111 711 710 HOH HOH C . 
WA 5 HOH 112 712 712 HOH HOH C . 
WA 5 HOH 113 713 713 HOH HOH C . 
WA 5 HOH 114 714 714 HOH HOH C . 
WA 5 HOH 115 715 715 HOH HOH C . 
WA 5 HOH 116 716 716 HOH HOH C . 
WA 5 HOH 117 717 717 HOH HOH C . 
WA 5 HOH 118 718 718 HOH HOH C . 
WA 5 HOH 119 719 719 HOH HOH C . 
WA 5 HOH 120 720 720 HOH HOH C . 
WA 5 HOH 121 721 721 HOH HOH C . 
WA 5 HOH 122 722 722 HOH HOH C . 
WA 5 HOH 123 723 723 HOH HOH C . 
WA 5 HOH 124 724 724 HOH HOH C . 
WA 5 HOH 125 725 725 HOH HOH C . 
WA 5 HOH 126 726 726 HOH HOH C . 
WA 5 HOH 127 727 727 HOH HOH C . 
WA 5 HOH 128 728 728 HOH HOH C . 
XA 5 HOH 1   601 601 HOH HOH D . 
XA 5 HOH 2   602 602 HOH HOH D . 
XA 5 HOH 3   603 603 HOH HOH D . 
XA 5 HOH 4   604 604 HOH HOH D . 
XA 5 HOH 5   605 605 HOH HOH D . 
XA 5 HOH 6   606 606 HOH HOH D . 
XA 5 HOH 7   607 607 HOH HOH D . 
XA 5 HOH 8   608 608 HOH HOH D . 
XA 5 HOH 9   609 609 HOH HOH D . 
XA 5 HOH 10  610 610 HOH HOH D . 
XA 5 HOH 11  611 611 HOH HOH D . 
XA 5 HOH 12  612 612 HOH HOH D . 
XA 5 HOH 13  613 613 HOH HOH D . 
XA 5 HOH 14  614 614 HOH HOH D . 
XA 5 HOH 15  615 615 HOH HOH D . 
XA 5 HOH 16  616 616 HOH HOH D . 
XA 5 HOH 17  617 617 HOH HOH D . 
XA 5 HOH 18  618 618 HOH HOH D . 
XA 5 HOH 19  619 619 HOH HOH D . 
XA 5 HOH 20  620 620 HOH HOH D . 
XA 5 HOH 21  621 621 HOH HOH D . 
XA 5 HOH 22  622 622 HOH HOH D . 
XA 5 HOH 23  623 623 HOH HOH D . 
XA 5 HOH 24  624 624 HOH HOH D . 
XA 5 HOH 25  625 625 HOH HOH D . 
XA 5 HOH 26  626 626 HOH HOH D . 
XA 5 HOH 27  627 627 HOH HOH D . 
XA 5 HOH 28  628 628 HOH HOH D . 
XA 5 HOH 29  629 629 HOH HOH D . 
XA 5 HOH 30  630 630 HOH HOH D . 
XA 5 HOH 31  631 631 HOH HOH D . 
XA 5 HOH 32  632 632 HOH HOH D . 
XA 5 HOH 33  633 633 HOH HOH D . 
XA 5 HOH 34  634 634 HOH HOH D . 
XA 5 HOH 35  635 635 HOH HOH D . 
XA 5 HOH 36  636 636 HOH HOH D . 
XA 5 HOH 37  637 637 HOH HOH D . 
XA 5 HOH 38  638 638 HOH HOH D . 
XA 5 HOH 39  639 639 HOH HOH D . 
XA 5 HOH 40  640 640 HOH HOH D . 
XA 5 HOH 41  641 641 HOH HOH D . 
XA 5 HOH 42  642 642 HOH HOH D . 
XA 5 HOH 43  643 643 HOH HOH D . 
XA 5 HOH 44  644 644 HOH HOH D . 
XA 5 HOH 45  645 645 HOH HOH D . 
XA 5 HOH 46  646 646 HOH HOH D . 
XA 5 HOH 47  647 647 HOH HOH D . 
XA 5 HOH 48  648 648 HOH HOH D . 
XA 5 HOH 49  649 649 HOH HOH D . 
XA 5 HOH 50  650 650 HOH HOH D . 
XA 5 HOH 51  651 651 HOH HOH D . 
XA 5 HOH 52  652 652 HOH HOH D . 
XA 5 HOH 53  653 653 HOH HOH D . 
XA 5 HOH 54  654 654 HOH HOH D . 
XA 5 HOH 55  655 655 HOH HOH D . 
XA 5 HOH 56  656 656 HOH HOH D . 
XA 5 HOH 57  657 657 HOH HOH D . 
XA 5 HOH 58  658 658 HOH HOH D . 
XA 5 HOH 59  659 659 HOH HOH D . 
XA 5 HOH 60  660 660 HOH HOH D . 
XA 5 HOH 61  661 661 HOH HOH D . 
XA 5 HOH 62  662 662 HOH HOH D . 
XA 5 HOH 63  663 663 HOH HOH D . 
XA 5 HOH 64  664 664 HOH HOH D . 
XA 5 HOH 65  665 665 HOH HOH D . 
XA 5 HOH 66  666 666 HOH HOH D . 
XA 5 HOH 67  667 667 HOH HOH D . 
XA 5 HOH 68  668 668 HOH HOH D . 
XA 5 HOH 69  669 669 HOH HOH D . 
XA 5 HOH 70  670 670 HOH HOH D . 
XA 5 HOH 71  671 671 HOH HOH D . 
XA 5 HOH 72  672 672 HOH HOH D . 
XA 5 HOH 73  673 673 HOH HOH D . 
XA 5 HOH 74  674 674 HOH HOH D . 
XA 5 HOH 75  675 676 HOH HOH D . 
XA 5 HOH 76  676 677 HOH HOH D . 
XA 5 HOH 77  677 678 HOH HOH D . 
XA 5 HOH 78  678 679 HOH HOH D . 
XA 5 HOH 79  679 680 HOH HOH D . 
XA 5 HOH 80  680 681 HOH HOH D . 
XA 5 HOH 81  681 682 HOH HOH D . 
XA 5 HOH 82  682 683 HOH HOH D . 
XA 5 HOH 83  683 684 HOH HOH D . 
XA 5 HOH 84  684 685 HOH HOH D . 
XA 5 HOH 85  685 686 HOH HOH D . 
XA 5 HOH 86  686 687 HOH HOH D . 
XA 5 HOH 87  687 688 HOH HOH D . 
XA 5 HOH 88  688 689 HOH HOH D . 
XA 5 HOH 89  689 690 HOH HOH D . 
XA 5 HOH 90  690 691 HOH HOH D . 
XA 5 HOH 91  691 692 HOH HOH D . 
XA 5 HOH 92  692 693 HOH HOH D . 
XA 5 HOH 93  693 694 HOH HOH D . 
XA 5 HOH 94  694 695 HOH HOH D . 
XA 5 HOH 95  695 696 HOH HOH D . 
XA 5 HOH 96  696 697 HOH HOH D . 
XA 5 HOH 97  697 698 HOH HOH D . 
XA 5 HOH 98  698 699 HOH HOH D . 
XA 5 HOH 99  699 700 HOH HOH D . 
XA 5 HOH 100 700 701 HOH HOH D . 
XA 5 HOH 101 701 702 HOH HOH D . 
XA 5 HOH 102 702 703 HOH HOH D . 
XA 5 HOH 103 703 704 HOH HOH D . 
XA 5 HOH 104 704 705 HOH HOH D . 
XA 5 HOH 105 705 706 HOH HOH D . 
XA 5 HOH 106 706 707 HOH HOH D . 
XA 5 HOH 107 707 708 HOH HOH D . 
XA 5 HOH 108 708 709 HOH HOH D . 
XA 5 HOH 109 709 710 HOH HOH D . 
XA 5 HOH 110 710 711 HOH HOH D . 
XA 5 HOH 111 711 712 HOH HOH D . 
XA 5 HOH 112 712 714 HOH HOH D . 
XA 5 HOH 113 713 715 HOH HOH D . 
XA 5 HOH 114 714 716 HOH HOH D . 
XA 5 HOH 115 715 717 HOH HOH D . 
XA 5 HOH 116 716 718 HOH HOH D . 
XA 5 HOH 117 717 719 HOH HOH D . 
XA 5 HOH 118 718 720 HOH HOH D . 
XA 5 HOH 119 719 721 HOH HOH D . 
XA 5 HOH 120 720 722 HOH HOH D . 
XA 5 HOH 121 721 723 HOH HOH D . 
XA 5 HOH 122 722 724 HOH HOH D . 
XA 5 HOH 123 723 725 HOH HOH D . 
XA 5 HOH 124 724 683 HOH HOH D . 
YA 5 HOH 1   601 675 HOH HOH E . 
YA 5 HOH 2   602 601 HOH HOH E . 
YA 5 HOH 3   603 602 HOH HOH E . 
YA 5 HOH 4   604 603 HOH HOH E . 
YA 5 HOH 5   605 604 HOH HOH E . 
YA 5 HOH 6   606 605 HOH HOH E . 
YA 5 HOH 7   607 606 HOH HOH E . 
YA 5 HOH 8   608 607 HOH HOH E . 
YA 5 HOH 9   609 608 HOH HOH E . 
YA 5 HOH 10  610 609 HOH HOH E . 
YA 5 HOH 11  611 610 HOH HOH E . 
YA 5 HOH 12  612 611 HOH HOH E . 
YA 5 HOH 13  613 612 HOH HOH E . 
YA 5 HOH 14  614 613 HOH HOH E . 
YA 5 HOH 15  615 614 HOH HOH E . 
YA 5 HOH 16  616 615 HOH HOH E . 
YA 5 HOH 17  617 616 HOH HOH E . 
YA 5 HOH 18  618 617 HOH HOH E . 
YA 5 HOH 19  619 618 HOH HOH E . 
YA 5 HOH 20  620 619 HOH HOH E . 
YA 5 HOH 21  621 620 HOH HOH E . 
YA 5 HOH 22  622 621 HOH HOH E . 
YA 5 HOH 23  623 622 HOH HOH E . 
YA 5 HOH 24  624 623 HOH HOH E . 
YA 5 HOH 25  625 624 HOH HOH E . 
YA 5 HOH 26  626 625 HOH HOH E . 
YA 5 HOH 27  627 626 HOH HOH E . 
YA 5 HOH 28  628 627 HOH HOH E . 
YA 5 HOH 29  629 628 HOH HOH E . 
YA 5 HOH 30  630 629 HOH HOH E . 
YA 5 HOH 31  631 630 HOH HOH E . 
YA 5 HOH 32  632 631 HOH HOH E . 
YA 5 HOH 33  633 632 HOH HOH E . 
YA 5 HOH 34  634 633 HOH HOH E . 
YA 5 HOH 35  635 634 HOH HOH E . 
YA 5 HOH 36  636 635 HOH HOH E . 
YA 5 HOH 37  637 636 HOH HOH E . 
YA 5 HOH 38  638 637 HOH HOH E . 
YA 5 HOH 39  639 638 HOH HOH E . 
YA 5 HOH 40  640 639 HOH HOH E . 
YA 5 HOH 41  641 640 HOH HOH E . 
YA 5 HOH 42  642 641 HOH HOH E . 
YA 5 HOH 43  643 642 HOH HOH E . 
YA 5 HOH 44  644 643 HOH HOH E . 
YA 5 HOH 45  645 644 HOH HOH E . 
YA 5 HOH 46  646 645 HOH HOH E . 
YA 5 HOH 47  647 646 HOH HOH E . 
YA 5 HOH 48  648 647 HOH HOH E . 
YA 5 HOH 49  649 648 HOH HOH E . 
YA 5 HOH 50  650 649 HOH HOH E . 
YA 5 HOH 51  651 650 HOH HOH E . 
YA 5 HOH 52  652 651 HOH HOH E . 
YA 5 HOH 53  653 652 HOH HOH E . 
YA 5 HOH 54  654 653 HOH HOH E . 
YA 5 HOH 55  655 654 HOH HOH E . 
YA 5 HOH 56  656 655 HOH HOH E . 
YA 5 HOH 57  657 656 HOH HOH E . 
YA 5 HOH 58  658 657 HOH HOH E . 
YA 5 HOH 59  659 658 HOH HOH E . 
YA 5 HOH 60  660 659 HOH HOH E . 
YA 5 HOH 61  661 660 HOH HOH E . 
YA 5 HOH 62  662 661 HOH HOH E . 
YA 5 HOH 63  663 662 HOH HOH E . 
YA 5 HOH 64  664 663 HOH HOH E . 
YA 5 HOH 65  665 664 HOH HOH E . 
YA 5 HOH 66  666 665 HOH HOH E . 
YA 5 HOH 67  667 666 HOH HOH E . 
YA 5 HOH 68  668 667 HOH HOH E . 
YA 5 HOH 69  669 668 HOH HOH E . 
YA 5 HOH 70  670 670 HOH HOH E . 
YA 5 HOH 71  671 671 HOH HOH E . 
YA 5 HOH 72  672 672 HOH HOH E . 
YA 5 HOH 73  673 673 HOH HOH E . 
YA 5 HOH 74  674 674 HOH HOH E . 
YA 5 HOH 75  675 675 HOH HOH E . 
YA 5 HOH 76  676 676 HOH HOH E . 
YA 5 HOH 77  677 677 HOH HOH E . 
YA 5 HOH 78  678 678 HOH HOH E . 
YA 5 HOH 79  679 679 HOH HOH E . 
YA 5 HOH 80  680 680 HOH HOH E . 
YA 5 HOH 81  681 681 HOH HOH E . 
YA 5 HOH 82  682 682 HOH HOH E . 
YA 5 HOH 83  683 684 HOH HOH E . 
YA 5 HOH 84  684 685 HOH HOH E . 
YA 5 HOH 85  685 686 HOH HOH E . 
YA 5 HOH 86  686 687 HOH HOH E . 
YA 5 HOH 87  687 688 HOH HOH E . 
YA 5 HOH 88  688 689 HOH HOH E . 
YA 5 HOH 89  689 690 HOH HOH E . 
YA 5 HOH 90  690 691 HOH HOH E . 
YA 5 HOH 91  691 692 HOH HOH E . 
YA 5 HOH 92  692 693 HOH HOH E . 
YA 5 HOH 93  693 694 HOH HOH E . 
YA 5 HOH 94  694 695 HOH HOH E . 
YA 5 HOH 95  695 696 HOH HOH E . 
YA 5 HOH 96  696 697 HOH HOH E . 
YA 5 HOH 97  697 698 HOH HOH E . 
YA 5 HOH 98  698 699 HOH HOH E . 
YA 5 HOH 99  699 700 HOH HOH E . 
YA 5 HOH 100 700 701 HOH HOH E . 
YA 5 HOH 101 701 702 HOH HOH E . 
YA 5 HOH 102 702 703 HOH HOH E . 
ZA 5 HOH 1   601 631 HOH HOH F . 
ZA 5 HOH 2   602 669 HOH HOH F . 
ZA 5 HOH 3   603 601 HOH HOH F . 
ZA 5 HOH 4   604 602 HOH HOH F . 
ZA 5 HOH 5   605 603 HOH HOH F . 
ZA 5 HOH 6   606 604 HOH HOH F . 
ZA 5 HOH 7   607 605 HOH HOH F . 
ZA 5 HOH 8   608 606 HOH HOH F . 
ZA 5 HOH 9   609 607 HOH HOH F . 
ZA 5 HOH 10  610 608 HOH HOH F . 
ZA 5 HOH 11  611 609 HOH HOH F . 
ZA 5 HOH 12  612 610 HOH HOH F . 
ZA 5 HOH 13  613 611 HOH HOH F . 
ZA 5 HOH 14  614 612 HOH HOH F . 
ZA 5 HOH 15  615 613 HOH HOH F . 
ZA 5 HOH 16  616 614 HOH HOH F . 
ZA 5 HOH 17  617 615 HOH HOH F . 
ZA 5 HOH 18  618 616 HOH HOH F . 
ZA 5 HOH 19  619 617 HOH HOH F . 
ZA 5 HOH 20  620 618 HOH HOH F . 
ZA 5 HOH 21  621 619 HOH HOH F . 
ZA 5 HOH 22  622 620 HOH HOH F . 
ZA 5 HOH 23  623 621 HOH HOH F . 
ZA 5 HOH 24  624 622 HOH HOH F . 
ZA 5 HOH 25  625 623 HOH HOH F . 
ZA 5 HOH 26  626 624 HOH HOH F . 
ZA 5 HOH 27  627 625 HOH HOH F . 
ZA 5 HOH 28  628 626 HOH HOH F . 
ZA 5 HOH 29  629 627 HOH HOH F . 
ZA 5 HOH 30  630 628 HOH HOH F . 
ZA 5 HOH 31  631 629 HOH HOH F . 
ZA 5 HOH 32  632 630 HOH HOH F . 
ZA 5 HOH 33  633 631 HOH HOH F . 
ZA 5 HOH 34  634 632 HOH HOH F . 
ZA 5 HOH 35  635 633 HOH HOH F . 
ZA 5 HOH 36  636 634 HOH HOH F . 
ZA 5 HOH 37  637 635 HOH HOH F . 
ZA 5 HOH 38  638 636 HOH HOH F . 
ZA 5 HOH 39  639 637 HOH HOH F . 
ZA 5 HOH 40  640 638 HOH HOH F . 
ZA 5 HOH 41  641 639 HOH HOH F . 
ZA 5 HOH 42  642 640 HOH HOH F . 
ZA 5 HOH 43  643 641 HOH HOH F . 
ZA 5 HOH 44  644 642 HOH HOH F . 
ZA 5 HOH 45  645 643 HOH HOH F . 
ZA 5 HOH 46  646 644 HOH HOH F . 
ZA 5 HOH 47  647 645 HOH HOH F . 
ZA 5 HOH 48  648 646 HOH HOH F . 
ZA 5 HOH 49  649 647 HOH HOH F . 
ZA 5 HOH 50  650 648 HOH HOH F . 
ZA 5 HOH 51  651 649 HOH HOH F . 
ZA 5 HOH 52  652 650 HOH HOH F . 
ZA 5 HOH 53  653 651 HOH HOH F . 
ZA 5 HOH 54  654 652 HOH HOH F . 
ZA 5 HOH 55  655 653 HOH HOH F . 
ZA 5 HOH 56  656 654 HOH HOH F . 
ZA 5 HOH 57  657 655 HOH HOH F . 
ZA 5 HOH 58  658 656 HOH HOH F . 
ZA 5 HOH 59  659 657 HOH HOH F . 
ZA 5 HOH 60  660 658 HOH HOH F . 
ZA 5 HOH 61  661 659 HOH HOH F . 
ZA 5 HOH 62  662 660 HOH HOH F . 
ZA 5 HOH 63  663 661 HOH HOH F . 
ZA 5 HOH 64  664 662 HOH HOH F . 
ZA 5 HOH 65  665 663 HOH HOH F . 
ZA 5 HOH 66  666 664 HOH HOH F . 
ZA 5 HOH 67  667 665 HOH HOH F . 
ZA 5 HOH 68  668 666 HOH HOH F . 
ZA 5 HOH 69  669 667 HOH HOH F . 
ZA 5 HOH 70  670 668 HOH HOH F . 
ZA 5 HOH 71  671 669 HOH HOH F . 
ZA 5 HOH 72  672 670 HOH HOH F . 
ZA 5 HOH 73  673 671 HOH HOH F . 
ZA 5 HOH 74  674 672 HOH HOH F . 
ZA 5 HOH 75  675 673 HOH HOH F . 
ZA 5 HOH 76  676 674 HOH HOH F . 
ZA 5 HOH 77  677 675 HOH HOH F . 
ZA 5 HOH 78  678 676 HOH HOH F . 
ZA 5 HOH 79  679 677 HOH HOH F . 
ZA 5 HOH 80  680 678 HOH HOH F . 
ZA 5 HOH 81  681 679 HOH HOH F . 
ZA 5 HOH 82  682 680 HOH HOH F . 
ZA 5 HOH 83  683 681 HOH HOH F . 
ZA 5 HOH 84  684 682 HOH HOH F . 
ZA 5 HOH 85  685 683 HOH HOH F . 
ZA 5 HOH 86  686 684 HOH HOH F . 
ZA 5 HOH 87  687 685 HOH HOH F . 
ZA 5 HOH 88  688 686 HOH HOH F . 
ZA 5 HOH 89  689 687 HOH HOH F . 
ZA 5 HOH 90  690 688 HOH HOH F . 
ZA 5 HOH 91  691 689 HOH HOH F . 
ZA 5 HOH 92  692 690 HOH HOH F . 
ZA 5 HOH 93  693 691 HOH HOH F . 
ZA 5 HOH 94  694 692 HOH HOH F . 
ZA 5 HOH 95  695 693 HOH HOH F . 
ZA 5 HOH 96  696 694 HOH HOH F . 
ZA 5 HOH 97  697 695 HOH HOH F . 
ZA 5 HOH 98  698 696 HOH HOH F . 
ZA 5 HOH 99  699 697 HOH HOH F . 
ZA 5 HOH 100 700 698 HOH HOH F . 
ZA 5 HOH 101 701 699 HOH HOH F . 
ZA 5 HOH 102 702 700 HOH HOH F . 
ZA 5 HOH 103 703 701 HOH HOH F . 
ZA 5 HOH 104 704 702 HOH HOH F . 
ZA 5 HOH 105 705 703 HOH HOH F . 
ZA 5 HOH 106 706 704 HOH HOH F . 
ZA 5 HOH 107 707 705 HOH HOH F . 
ZA 5 HOH 108 708 706 HOH HOH F . 
ZA 5 HOH 109 709 707 HOH HOH F . 
ZA 5 HOH 110 710 708 HOH HOH F . 
ZA 5 HOH 111 711 709 HOH HOH F . 
ZA 5 HOH 112 712 710 HOH HOH F . 
ZA 5 HOH 113 713 711 HOH HOH F . 
ZA 5 HOH 114 714 712 HOH HOH F . 
ZA 5 HOH 115 715 713 HOH HOH F . 
ZA 5 HOH 116 716 714 HOH HOH F . 
ZA 5 HOH 117 717 715 HOH HOH F . 
ZA 5 HOH 118 718 716 HOH HOH F . 
ZA 5 HOH 119 719 717 HOH HOH F . 
ZA 5 HOH 120 720 718 HOH HOH F . 
ZA 5 HOH 121 721 719 HOH HOH F . 
ZA 5 HOH 122 722 720 HOH HOH F . 
ZA 5 HOH 123 723 721 HOH HOH F . 
ZA 5 HOH 124 724 722 HOH HOH F . 
ZA 5 HOH 125 725 723 HOH HOH F . 
ZA 5 HOH 126 726 724 HOH HOH F . 
ZA 5 HOH 127 727 725 HOH HOH F . 
ZA 5 HOH 128 728 726 HOH HOH F . 
ZA 5 HOH 129 729 727 HOH HOH F . 
ZA 5 HOH 130 730 728 HOH HOH F . 
ZA 5 HOH 131 731 729 HOH HOH F . 
ZA 5 HOH 132 732 730 HOH HOH F . 
ZA 5 HOH 133 733 731 HOH HOH F . 
ZA 5 HOH 134 734 732 HOH HOH F . 
ZA 5 HOH 135 735 733 HOH HOH F . 
ZA 5 HOH 136 736 734 HOH HOH F . 
ZA 5 HOH 137 737 735 HOH HOH F . 
ZA 5 HOH 138 738 736 HOH HOH F . 
ZA 5 HOH 139 739 737 HOH HOH F . 
ZA 5 HOH 140 740 738 HOH HOH F . 
ZA 5 HOH 141 741 739 HOH HOH F . 
ZA 5 HOH 142 742 740 HOH HOH F . 
ZA 5 HOH 143 743 741 HOH HOH F . 
ZA 5 HOH 144 744 742 HOH HOH F . 
ZA 5 HOH 145 745 743 HOH HOH F . 
ZA 5 HOH 146 746 744 HOH HOH F . 
ZA 5 HOH 147 747 746 HOH HOH F . 
ZA 5 HOH 148 748 747 HOH HOH F . 
ZA 5 HOH 149 749 749 HOH HOH F . 
ZA 5 HOH 150 750 750 HOH HOH F . 
ZA 5 HOH 151 751 751 HOH HOH F . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 C ASN 98 C ASN 98 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 98 A ASN 98 ? ASN 'GLYCOSYLATION SITE' 
3 F ASN 98 F ASN 98 ? ASN 'GLYCOSYLATION SITE' 
4 B ASN 98 B ASN 98 ? ASN 'GLYCOSYLATION SITE' 
5 D ASN 98 D ASN 98 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      
A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-02-11 
2 'Structure model' 1 1 2015-02-25 
3 'Structure model' 1 2 2017-11-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' Advisory                 
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' citation                        
2 3 'Structure model' pdbx_unobs_or_zero_occ_atoms    
3 3 'Structure model' pdbx_unobs_or_zero_occ_residues 
4 3 'Structure model' software                        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_citation.journal_abbrev' 
2 3 'Structure model' '_software.name'           
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined 115.9456 75.0278  -14.3344 0.3090 0.4270 0.2044 0.0507  0.0095  0.0457  3.9139 1.6025 1.1490 
-0.9379 -0.4579 -0.1608 0.2287  0.9438  0.1828  -0.4379 -0.1732 -0.0545 0.0291  -0.0722 -0.0465 
'X-RAY DIFFRACTION' 2  ? refined 110.1069 80.5227  -9.9170  0.2460 0.3487 0.2178 0.0442  0.0137  0.1015  3.2912 2.1906 1.4886 
-0.6176 -0.1977 0.1983  0.0924  0.7012  0.2818  -0.3112 -0.0351 0.1414  -0.0925 -0.1554 -0.0514 
'X-RAY DIFFRACTION' 3  ? refined 96.1259  82.1801  4.9256   0.2482 0.2549 0.1937 0.0535  -0.0059 -0.0043 6.7922 2.1641 1.1499 
-0.5108 -1.5336 -0.3160 0.0609  -0.2697 0.6051  0.2461  0.0610  0.1176  -0.1497 0.0700  -0.1140 
'X-RAY DIFFRACTION' 4  ? refined 77.4627  74.1370  -7.9420  0.2795 0.5635 0.4799 0.0395  -0.0681 -0.0085 7.3472 1.8667 1.7190 
-0.1339 0.1297  -0.0730 -0.0269 1.2692  0.2376  -0.3136 -0.0274 0.7430  -0.0754 -0.5161 0.0408  
'X-RAY DIFFRACTION' 5  ? refined 90.0422  82.2625  -1.8552  0.1970 0.3004 0.2898 0.0707  0.0240  0.0530  5.1212 3.4031 1.6213 
1.3232  -0.0288 0.3884  0.0345  0.4957  0.4868  -0.1620 -0.0082 0.3907  -0.1058 -0.2572 -0.0145 
'X-RAY DIFFRACTION' 6  ? refined 72.3894  37.2586  31.3354  0.2138 0.3027 0.2047 0.0205  0.0052  0.0157  1.8301 5.4543 2.4266 
-1.9697 -1.1686 -0.6445 -0.1330 -0.2434 -0.2272 0.5109  0.1832  0.1981  0.0683  -0.0495 -0.0309 
'X-RAY DIFFRACTION' 7  ? refined 82.8771  27.7288  27.0430  0.1991 0.2933 0.2470 0.0141  -0.0675 0.0296  1.3617 6.9625 1.8521 
-1.6454 -1.0453 -0.3704 -0.0481 -0.3931 -0.2263 0.5916  0.1489  0.0799  0.1287  0.2766  -0.0544 
'X-RAY DIFFRACTION' 8  ? refined 90.0469  24.3552  20.6982  0.2305 0.3533 0.3491 0.0595  -0.0497 -0.0385 2.2954 6.5507 2.5676 
-0.6771 -1.7505 0.8517  -0.1420 -0.4447 0.1910  0.4364  0.2283  -0.7461 0.1988  0.6865  -0.0662 
'X-RAY DIFFRACTION' 9  ? refined 74.3569  35.5336  25.6714  0.2252 0.2472 0.1881 0.0174  -0.0174 0.0253  2.6082 3.1143 1.7615 
-0.5525 -0.3556 0.3402  -0.0035 -0.2228 -0.0116 0.2096  0.0986  0.0307  -0.0001 0.0676  -0.0937 
'X-RAY DIFFRACTION' 10 ? refined 62.7635  46.8811  16.6023  0.1819 0.2369 0.3696 0.0140  -0.0335 0.0002  2.1496 2.8140 2.9051 
-0.3230 -0.9255 -0.9956 0.0231  0.1400  0.1136  -0.0699 0.1412  0.7205  -0.0952 -0.4939 -0.1500 
'X-RAY DIFFRACTION' 11 ? refined 77.5618  63.5295  15.6797  0.1919 0.2075 0.3370 -0.0226 0.0751  -0.0058 2.8693 6.7903 4.0727 
0.0842  0.4387  -0.6985 0.1482  0.0766  0.6021  0.0694  0.0120  -0.0697 -0.5522 0.2336  -0.1442 
'X-RAY DIFFRACTION' 12 ? refined 75.2580  73.6749  29.9195  0.5933 0.4860 0.6737 -0.0448 0.1328  -0.1874 0.0191 7.0389 4.8370 
0.3600  0.1390  1.6720  -0.0003 -0.6995 0.7115  0.8825  -0.0935 0.1876  -0.8728 -0.3523 0.0126  
'X-RAY DIFFRACTION' 13 ? refined 66.2641  61.3420  15.3646  0.2925 0.2526 0.5337 0.0085  0.0654  0.0531  4.9044 9.6878 2.0211 
0.4060  0.9058  4.1131  0.1577  -0.1859 0.2928  -0.2442 -0.2894 0.8696  -0.5419 -0.6897 0.1063  
'X-RAY DIFFRACTION' 14 ? refined 68.1245  53.7836  23.3341  0.1979 0.1901 0.2573 0.0563  0.0063  0.0217  3.3100 4.6047 2.8568 
1.0309  -0.5604 0.3466  0.0485  -0.3068 0.2699  0.2393  -0.0379 0.4458  -0.2805 -0.0926 -0.0193 
'X-RAY DIFFRACTION' 15 ? refined 65.7144  20.4191  -6.1758  0.4497 0.2749 0.3563 -0.0236 -0.2111 -0.0228 5.7064 3.5268 0.6272 
-1.2307 -0.8673 0.2454  0.0238  0.5504  0.0853  -0.8549 -0.2069 0.7299  -0.0401 -0.2406 0.1540  
'X-RAY DIFFRACTION' 16 ? refined 71.2092  39.7027  -5.4687  0.5200 0.3025 0.2668 0.0045  -0.0884 0.0403  6.3194 2.4984 3.4346 
-0.4991 0.3950  0.5118  0.1549  0.9084  0.2449  -0.8898 -0.0836 0.3411  -0.4375 0.0761  -0.0521 
'X-RAY DIFFRACTION' 17 ? refined 67.8428  21.1363  -1.9221  0.3213 0.2332 0.3135 -0.0031 -0.1558 -0.0162 1.6923 3.1104 2.0865 
-0.0148 -0.2873 -0.1243 0.0045  0.3054  -0.1895 -0.5797 0.0425  0.4877  0.1062  -0.1290 -0.0506 
'X-RAY DIFFRACTION' 18 ? refined 73.7120  7.8230   9.5988   0.2767 0.1554 0.2146 0.0060  -0.0343 -0.0089 6.3470 4.1234 1.5850 
-1.4071 -0.0279 -0.2541 -0.1024 -0.3004 -0.5360 0.2083  0.0715  0.4246  0.0899  -0.1011 0.0268  
'X-RAY DIFFRACTION' 19 ? refined 91.2326  2.5545   -3.1595  0.2703 0.1875 0.3422 -0.0189 0.0377  -0.0150 7.2408 9.2237 2.6958 
-6.5561 0.2007  -1.9070 0.1611  0.2247  -0.2255 -0.5344 -0.2348 -0.3806 0.1428  0.2802  0.0566  
'X-RAY DIFFRACTION' 20 ? refined 86.9071  -10.1757 -14.3421 0.6921 0.4294 0.6275 0.0309  0.0336  -0.1367 3.6122 7.8492 8.4421 
-2.7017 -0.2574 2.4126  0.3288  0.7038  -0.8272 -1.1858 -0.3902 0.4393  1.2652  -0.4483 0.0381  
'X-RAY DIFFRACTION' 21 ? refined 83.9643  -2.1603  5.0355   0.3166 0.2889 0.4526 0.0558  -0.0160 0.0070  5.6186 5.5874 9.2455 
2.8162  2.5185  2.4928  0.1741  -0.1009 -0.8118 0.2544  0.0504  -0.0742 0.2391  -0.1470 -0.3694 
'X-RAY DIFFRACTION' 22 ? refined 75.8440  3.5381   -0.8034  0.3013 0.1766 0.3415 0.0240  -0.0887 -0.0264 3.3018 3.1868 2.7175 
-1.3263 -1.3641 0.3684  0.0688  0.3492  -0.4323 -0.3864 -0.1324 0.3894  0.1764  -0.2027 0.0432  
'X-RAY DIFFRACTION' 23 ? refined 135.0264 16.2836  17.2816  0.4260 0.4125 0.2356 0.0365  0.1035  -0.0521 2.8974 4.6917 1.7316 
1.6590  -0.1241 -1.4399 0.2709  -0.5764 0.2485  0.9444  -0.1351 0.1853  -0.4355 0.0409  -0.0971 
'X-RAY DIFFRACTION' 24 ? refined 122.8233 1.2242   11.7919  0.2855 0.3046 0.3445 0.0627  0.1092  0.0780  3.0528 1.1164 0.8682 
1.0093  0.3484  -0.1255 0.0628  -0.4841 -0.2461 0.1903  -0.0294 0.2207  -0.0271 -0.1155 -0.0206 
'X-RAY DIFFRACTION' 25 ? refined 115.8097 -7.9139  13.1728  0.2790 0.3459 0.4522 0.0505  0.1081  0.1109  4.7203 1.5836 2.1226 
-0.1773 -0.6278 0.0486  -0.1167 -0.5792 -0.5574 0.2506  0.1599  0.3426  0.1347  -0.3138 -0.0354 
'X-RAY DIFFRACTION' 26 ? refined 138.8010 13.2351  -18.9831 0.3816 0.3648 0.2179 -0.0552 0.0437  -0.0205 4.8692 4.3163 1.6037 
2.6562  -1.5738 -0.3434 -0.4327 0.7135  -0.2040 -0.8249 0.4361  -0.1499 0.2615  -0.1230 -0.0214 
'X-RAY DIFFRACTION' 27 ? refined 121.1034 12.1166  -14.1130 0.3425 0.5328 0.4185 -0.0649 -0.0572 0.1049  5.7643 7.0159 0.6682 
2.7939  -1.4085 -1.2842 -0.5121 0.7534  0.1787  -0.8688 0.6383  0.8620  0.0860  -0.6850 -0.0432 
'X-RAY DIFFRACTION' 28 ? refined 137.4013 14.4159  -18.1345 0.3444 0.3316 0.1929 -0.0920 0.0584  -0.0313 4.4555 2.8382 1.4571 
1.0256  -0.4326 -0.0182 -0.3119 0.5189  0.0743  -0.5934 0.3051  -0.0588 0.1157  -0.0811 -0.0092 
'X-RAY DIFFRACTION' 29 ? refined 149.6257 19.8879  -6.5326  0.2112 0.2537 0.2285 0.0058  0.0497  -0.0062 2.0207 4.2563 1.3207 
1.7140  -0.1111 -0.0001 -0.0246 -0.0402 -0.1151 0.0381  -0.0205 -0.3985 0.0335  0.1943  0.0593  
'X-RAY DIFFRACTION' 30 ? refined 148.2209 46.3069  -12.5314 0.4570 0.2680 0.5585 -0.0040 0.0981  0.0572  4.6107 6.3525 2.1799 
1.3712  1.6491  0.9769  -0.3232 0.2536  1.0693  -1.0283 0.2705  -0.1031 -0.6076 0.0649  0.0261  
'X-RAY DIFFRACTION' 31 ? refined 152.4386 42.8935  -16.4313 0.5247 0.3743 0.7024 -0.0708 0.1713  -0.0095 5.6264 6.5833 7.9185 
1.3461  0.4285  -1.6880 -0.3780 0.9874  0.3875  -1.0840 0.2010  -0.8591 0.0027  0.9800  0.1379  
'X-RAY DIFFRACTION' 32 ? refined 155.6467 25.5170  -9.9901  0.2314 0.2358 0.2935 -0.0382 0.0618  -0.0059 5.5221 6.6027 2.8274 
-1.4779 -0.9183 0.5271  -0.0500 0.0552  -0.0500 -0.1514 0.0911  -0.6285 0.0767  0.2834  0.0068  
'X-RAY DIFFRACTION' 33 ? refined 130.2407 76.6442  20.7730  0.3360 0.2514 0.2587 -0.0156 -0.0934 -0.0096 5.9449 1.0654 2.6930 
0.3864  -1.9569 1.3113  0.0286  -0.6724 0.0192  0.3582  0.0918  -0.2085 -0.1053 0.1917  -0.1174 
'X-RAY DIFFRACTION' 34 ? refined 111.7435 67.7486  19.5230  0.3636 0.3328 0.2305 -0.0247 0.0157  0.1144  3.8951 2.0919 1.3872 
-0.5300 0.9453  1.1813  0.0713  -0.6780 -0.3717 0.5779  0.0025  0.1190  0.3437  -0.3552 -0.0447 
'X-RAY DIFFRACTION' 35 ? refined 128.1497 76.2185  14.9921  0.2105 0.1818 0.2021 0.0319  -0.0460 -0.0093 3.7248 2.9211 1.9097 
0.5835  -0.3314 -0.1833 0.0517  -0.2555 0.0079  0.2745  -0.0263 -0.4119 -0.0725 0.0813  -0.0106 
'X-RAY DIFFRACTION' 36 ? refined 138.7936 73.1649  1.3326   0.1679 0.1402 0.2968 0.0924  -0.0368 0.0507  5.4866 6.9015 4.3385 
2.7114  -0.0773 2.0264  -0.1000 0.2245  -0.1837 -0.1659 0.1747  -0.8562 -0.1815 0.1606  -0.0849 
'X-RAY DIFFRACTION' 37 ? refined 147.3299 56.0201  4.1087   0.2583 0.2123 0.6739 0.0084  -0.0509 -0.0121 5.9485 3.2477 5.2054 
-3.2208 -3.2560 1.4372  -0.1013 -0.2192 -0.2042 0.0637  0.1686  -0.8452 0.3739  0.4234  -0.0840 
'X-RAY DIFFRACTION' 38 ? refined 159.9681 54.9611  16.6848  0.5781 0.6375 1.2808 0.0674  -0.3198 -0.0111 4.6121 2.6536 8.1984 
-3.4318 4.2479  -2.4692 -0.1325 -0.4383 0.2716  0.6724  0.0865  -0.7326 -0.2582 1.0167  0.0830  
'X-RAY DIFFRACTION' 39 ? refined 149.8245 66.0189  1.5864   0.2893 0.3685 0.8002 -0.0142 0.0969  0.0027  7.6604 6.6130 2.0268 
-1.4536 3.6872  -1.1448 -0.0127 0.4756  0.1670  -0.1651 0.0685  -1.2768 -0.3440 1.0186  0.0205  
'X-RAY DIFFRACTION' 40 ? refined 146.2387 59.4138  13.7874  0.3103 0.3339 0.5491 0.0938  -0.1221 0.0385  2.4388 5.3317 4.1736 
-1.8799 -1.1918 -1.5736 -0.0459 -0.3838 -0.3949 0.6654  0.0842  -0.7093 0.3739  0.5081  -0.0551 
'X-RAY DIFFRACTION' 41 ? refined 142.8916 79.0371  7.5733   0.2154 0.1727 0.4073 0.0188  -0.0304 0.0389  5.2724 5.1267 8.5190 
3.5144  2.9330  3.5370  -0.0037 -0.0056 0.0529  0.0912  0.1138  -0.6666 -0.2631 0.4832  -0.0793 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 11 through 106 )
;
'X-RAY DIFFRACTION' 2  2  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 107 through 198 )
;
'X-RAY DIFFRACTION' 3  3  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 199 through 275 )
;
'X-RAY DIFFRACTION' 4  4  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 276 through 330 )
;
'X-RAY DIFFRACTION' 5  5  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 331 through 416 )
;
'X-RAY DIFFRACTION' 6  6  ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 11 through 46 )
;
'X-RAY DIFFRACTION' 7  7  ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 47 through 70 )
;
'X-RAY DIFFRACTION' 8  8  ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 71 through 106 )
;
'X-RAY DIFFRACTION' 9  9  ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 107 through 198 )
;
'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 199 through 247 )
;
'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 248 through 302 )
;
'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 303 through 330 )
;
'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 331 through 349 )
;
'X-RAY DIFFRACTION' 14 14 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 350 through 416 )
;
'X-RAY DIFFRACTION' 15 15 ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 11 through 60 )
;
'X-RAY DIFFRACTION' 16 16 ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 61 through 106 )
;
'X-RAY DIFFRACTION' 17 17 ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 107 through 198 )
;
'X-RAY DIFFRACTION' 18 18 ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 199 through 247 )
;
'X-RAY DIFFRACTION' 19 19 ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 248 through 302 )
;
'X-RAY DIFFRACTION' 20 20 ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 303 through 330 )
;
'X-RAY DIFFRACTION' 21 21 ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 331 through 349 )
;
'X-RAY DIFFRACTION' 22 22 ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 350 through 417 )
;
'X-RAY DIFFRACTION' 23 23 ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 10 through 106 )
;
'X-RAY DIFFRACTION' 24 24 ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 107 through 317 )
;
'X-RAY DIFFRACTION' 25 25 ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 318 through 417 )
;
'X-RAY DIFFRACTION' 26 26 ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 11 through 70 )
;
'X-RAY DIFFRACTION' 27 27 ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 71 through 106 )
;
'X-RAY DIFFRACTION' 28 28 ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 107 through 162 )
;
'X-RAY DIFFRACTION' 29 29 ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 163 through 241 )
;
'X-RAY DIFFRACTION' 30 30 ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 242 through 312 )
;
'X-RAY DIFFRACTION' 31 31 ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 313 through 372 )
;
'X-RAY DIFFRACTION' 32 32 ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 373 through 416 )
;
'X-RAY DIFFRACTION' 33 33 ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 10 through 46 )
;
'X-RAY DIFFRACTION' 34 34 ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 47 through 106 )
;
'X-RAY DIFFRACTION' 35 35 ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 107 through 215 )
;
'X-RAY DIFFRACTION' 36 36 ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 216 through 241 )
;
'X-RAY DIFFRACTION' 37 37 ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 242 through 302 )
;
'X-RAY DIFFRACTION' 38 38 ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 303 through 330 )
;
'X-RAY DIFFRACTION' 39 39 ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 331 through 349 )
;
'X-RAY DIFFRACTION' 40 40 ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 350 through 383 )
;
'X-RAY DIFFRACTION' 41 41 ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 384 through 416 )
;
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MAR345 'data collection' .                             ? 1 
PHASER phasing           .                             ? 2 
PHENIX refinement        '(phenix.refine: 1.8.3_1479)' ? 3 
XDS    'data reduction'  .                             ? 4 
XSCALE 'data scaling'    .                             ? 5 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 35  ? ? 77.84   170.00  
2  1 ASP A 88  ? ? -98.73  -89.38  
3  1 THR A 100 ? ? -105.22 -167.05 
4  1 GLN A 141 ? ? -119.96 58.52   
5  1 ASN A 159 ? ? 71.21   -0.27   
6  1 ASN A 248 ? ? 51.99   -112.44 
7  1 GLN A 352 ? ? -93.80  58.96   
8  1 ASP A 355 ? ? 3.69    -76.73  
9  1 ARG B 35  ? ? 77.74   169.49  
10 1 SER B 57  ? ? -56.91  -9.70   
11 1 GLN B 58  ? ? -63.53  -136.10 
12 1 HIS B 59  ? ? -93.58  40.16   
13 1 ASP B 88  ? ? -98.98  -93.95  
14 1 THR B 100 ? ? -107.89 -167.40 
15 1 GLN B 141 ? ? -119.80 58.51   
16 1 ASN B 248 ? ? 53.45   -112.50 
17 1 LYS B 323 ? ? -79.77  -159.53 
18 1 ILE B 324 ? ? 61.27   -34.06  
19 1 SER B 325 ? ? -41.88  109.13  
20 1 ASP B 355 ? ? -44.13  104.58  
21 1 ARG C 35  ? ? 77.09   171.08  
22 1 ASP C 88  ? ? -103.80 -100.50 
23 1 THR C 100 ? ? -107.55 -167.23 
24 1 GLN C 141 ? ? -117.50 57.17   
25 1 ASN C 248 ? ? 51.68   -109.88 
26 1 PRO C 254 ? ? -62.29  97.73   
27 1 SER C 325 ? ? -174.62 -87.73  
28 1 GLN C 352 ? ? -94.83  55.61   
29 1 LYS D 11  ? ? 55.08   112.91  
30 1 ARG D 35  ? ? 77.25   169.81  
31 1 SER D 57  ? ? -113.27 -152.37 
32 1 GLN D 58  ? ? -23.91  -110.10 
33 1 ASP D 88  ? ? -104.60 -91.72  
34 1 THR D 100 ? ? -106.28 -162.91 
35 1 GLN D 141 ? ? -116.14 56.07   
36 1 ASN D 159 ? ? 72.89   -2.06   
37 1 ASN D 248 ? ? 53.62   -112.89 
38 1 SER D 325 ? ? -74.47  24.27   
39 1 ASN D 338 ? ? 26.20   43.18   
40 1 ALA D 353 ? ? -82.07  -99.92  
41 1 ARG E 35  ? ? 78.97   169.82  
42 1 ASP E 88  ? ? -56.05  -92.84  
43 1 ASN E 248 ? ? 52.23   -113.36 
44 1 ARG E 322 ? ? -20.71  100.54  
45 1 LYS E 323 ? ? -21.91  -68.16  
46 1 ILE E 324 ? ? 124.36  -2.59   
47 1 SER E 325 ? ? -70.09  46.06   
48 1 ALA E 328 ? ? -53.71  108.08  
49 1 GLN E 352 ? ? -96.13  -64.90  
50 1 ALA E 353 ? ? 63.73   -11.47  
51 1 ASP E 355 ? ? -39.35  -78.14  
52 1 ARG F 35  ? ? 76.99   169.57  
53 1 ASP F 88  ? ? -102.25 -97.96  
54 1 THR F 100 ? ? -107.28 -165.58 
55 1 GLN F 141 ? ? -118.64 59.23   
56 1 ASP F 208 ? ? -113.44 65.20   
57 1 ASN F 212 ? ? -158.08 86.95   
58 1 ASN F 248 ? ? 50.37   -112.93 
59 1 LYS F 323 ? ? 168.13  -2.16   
60 1 ILE F 324 ? ? -45.18  -14.41  
61 1 ASN F 338 ? ? 53.59   18.84   
62 1 GLN F 352 ? ? -96.57  57.45   
63 1 ASP F 355 ? ? -53.23  80.72   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A LEU 1   ? A LEU 1   
2   1 Y 1 A TYR 2   ? A TYR 2   
3   1 Y 1 A HIS 3   ? A HIS 3   
4   1 Y 1 A ASN 4   ? A ASN 4   
5   1 Y 1 A SER 5   ? A SER 5   
6   1 Y 1 A GLN 6   ? A GLN 6   
7   1 Y 1 A PRO 7   ? A PRO 7   
8   1 Y 1 A THR 8   ? A THR 8   
9   1 Y 1 A SER 9   ? A SER 9   
10  1 Y 1 A SER 10  ? A SER 10  
11  1 Y 1 A LYS 256 ? A LYS 256 
12  1 Y 1 A ASN 257 ? A ASN 257 
13  1 Y 1 A PRO 258 ? A PRO 258 
14  1 Y 1 A PHE 259 ? A PHE 259 
15  1 Y 1 A ILE 260 ? A ILE 260 
16  1 Y 1 A SER 261 ? A SER 261 
17  1 Y 1 A PRO 262 ? A PRO 262 
18  1 Y 1 A SER 263 ? A SER 263 
19  1 Y 1 A SER 264 ? A SER 264 
20  1 Y 1 A THR 265 ? A THR 265 
21  1 Y 1 A SER 266 ? A SER 266 
22  1 Y 1 A TYR 267 ? A TYR 267 
23  1 Y 1 A HIS 268 ? A HIS 268 
24  1 Y 1 A GLY 269 ? A GLY 269 
25  1 Y 1 A SER 270 ? A SER 270 
26  1 Y 1 A GLY 271 ? A GLY 271 
27  1 Y 1 A PRO 417 ? A PRO 417 
28  1 Y 1 B LEU 1   ? B LEU 1   
29  1 Y 1 B TYR 2   ? B TYR 2   
30  1 Y 1 B HIS 3   ? B HIS 3   
31  1 Y 1 B ASN 4   ? B ASN 4   
32  1 Y 1 B SER 5   ? B SER 5   
33  1 Y 1 B GLN 6   ? B GLN 6   
34  1 Y 1 B PRO 7   ? B PRO 7   
35  1 Y 1 B THR 8   ? B THR 8   
36  1 Y 1 B SER 9   ? B SER 9   
37  1 Y 1 B SER 10  ? B SER 10  
38  1 Y 1 B LYS 256 ? B LYS 256 
39  1 Y 1 B ASN 257 ? B ASN 257 
40  1 Y 1 B PRO 258 ? B PRO 258 
41  1 Y 1 B PHE 259 ? B PHE 259 
42  1 Y 1 B ILE 260 ? B ILE 260 
43  1 Y 1 B SER 261 ? B SER 261 
44  1 Y 1 B PRO 262 ? B PRO 262 
45  1 Y 1 B SER 263 ? B SER 263 
46  1 Y 1 B SER 264 ? B SER 264 
47  1 Y 1 B THR 265 ? B THR 265 
48  1 Y 1 B SER 266 ? B SER 266 
49  1 Y 1 B TYR 267 ? B TYR 267 
50  1 Y 1 B HIS 268 ? B HIS 268 
51  1 Y 1 B GLY 269 ? B GLY 269 
52  1 Y 1 B SER 270 ? B SER 270 
53  1 Y 1 B PRO 417 ? B PRO 417 
54  1 Y 1 C LEU 1   ? C LEU 1   
55  1 Y 1 C TYR 2   ? C TYR 2   
56  1 Y 1 C HIS 3   ? C HIS 3   
57  1 Y 1 C ASN 4   ? C ASN 4   
58  1 Y 1 C SER 5   ? C SER 5   
59  1 Y 1 C GLN 6   ? C GLN 6   
60  1 Y 1 C PRO 7   ? C PRO 7   
61  1 Y 1 C THR 8   ? C THR 8   
62  1 Y 1 C SER 9   ? C SER 9   
63  1 Y 1 C SER 10  ? C SER 10  
64  1 Y 1 C LYS 256 ? C LYS 256 
65  1 Y 1 C ASN 257 ? C ASN 257 
66  1 Y 1 C PRO 258 ? C PRO 258 
67  1 Y 1 C PHE 259 ? C PHE 259 
68  1 Y 1 C ILE 260 ? C ILE 260 
69  1 Y 1 C SER 261 ? C SER 261 
70  1 Y 1 C PRO 262 ? C PRO 262 
71  1 Y 1 C SER 263 ? C SER 263 
72  1 Y 1 C SER 264 ? C SER 264 
73  1 Y 1 C THR 265 ? C THR 265 
74  1 Y 1 C SER 266 ? C SER 266 
75  1 Y 1 C TYR 267 ? C TYR 267 
76  1 Y 1 C HIS 268 ? C HIS 268 
77  1 Y 1 C GLY 269 ? C GLY 269 
78  1 Y 1 C SER 270 ? C SER 270 
79  1 Y 1 D LEU 1   ? D LEU 1   
80  1 Y 1 D TYR 2   ? D TYR 2   
81  1 Y 1 D HIS 3   ? D HIS 3   
82  1 Y 1 D ASN 4   ? D ASN 4   
83  1 Y 1 D SER 5   ? D SER 5   
84  1 Y 1 D GLN 6   ? D GLN 6   
85  1 Y 1 D PRO 7   ? D PRO 7   
86  1 Y 1 D THR 8   ? D THR 8   
87  1 Y 1 D SER 9   ? D SER 9   
88  1 Y 1 D LYS 256 ? D LYS 256 
89  1 Y 1 D ASN 257 ? D ASN 257 
90  1 Y 1 D PRO 258 ? D PRO 258 
91  1 Y 1 D PHE 259 ? D PHE 259 
92  1 Y 1 D ILE 260 ? D ILE 260 
93  1 Y 1 D SER 261 ? D SER 261 
94  1 Y 1 D PRO 262 ? D PRO 262 
95  1 Y 1 D SER 263 ? D SER 263 
96  1 Y 1 D SER 264 ? D SER 264 
97  1 Y 1 D THR 265 ? D THR 265 
98  1 Y 1 D SER 266 ? D SER 266 
99  1 Y 1 D TYR 267 ? D TYR 267 
100 1 Y 1 D HIS 268 ? D HIS 268 
101 1 Y 1 D GLY 269 ? D GLY 269 
102 1 Y 1 D SER 270 ? D SER 270 
103 1 Y 1 D GLY 271 ? D GLY 271 
104 1 Y 1 E LEU 1   ? E LEU 1   
105 1 Y 1 E TYR 2   ? E TYR 2   
106 1 Y 1 E HIS 3   ? E HIS 3   
107 1 Y 1 E ASN 4   ? E ASN 4   
108 1 Y 1 E SER 5   ? E SER 5   
109 1 Y 1 E GLN 6   ? E GLN 6   
110 1 Y 1 E PRO 7   ? E PRO 7   
111 1 Y 1 E THR 8   ? E THR 8   
112 1 Y 1 E SER 9   ? E SER 9   
113 1 Y 1 E SER 10  ? E SER 10  
114 1 Y 1 E LYS 256 ? E LYS 256 
115 1 Y 1 E ASN 257 ? E ASN 257 
116 1 Y 1 E PRO 258 ? E PRO 258 
117 1 Y 1 E PHE 259 ? E PHE 259 
118 1 Y 1 E ILE 260 ? E ILE 260 
119 1 Y 1 E SER 261 ? E SER 261 
120 1 Y 1 E PRO 262 ? E PRO 262 
121 1 Y 1 E SER 263 ? E SER 263 
122 1 Y 1 E SER 264 ? E SER 264 
123 1 Y 1 E THR 265 ? E THR 265 
124 1 Y 1 E SER 266 ? E SER 266 
125 1 Y 1 E TYR 267 ? E TYR 267 
126 1 Y 1 E HIS 268 ? E HIS 268 
127 1 Y 1 E GLY 269 ? E GLY 269 
128 1 Y 1 E SER 270 ? E SER 270 
129 1 Y 1 E PRO 417 ? E PRO 417 
130 1 Y 1 F LEU 1   ? F LEU 1   
131 1 Y 1 F TYR 2   ? F TYR 2   
132 1 Y 1 F HIS 3   ? F HIS 3   
133 1 Y 1 F ASN 4   ? F ASN 4   
134 1 Y 1 F SER 5   ? F SER 5   
135 1 Y 1 F GLN 6   ? F GLN 6   
136 1 Y 1 F PRO 7   ? F PRO 7   
137 1 Y 1 F THR 8   ? F THR 8   
138 1 Y 1 F SER 9   ? F SER 9   
139 1 Y 1 F LYS 256 ? F LYS 256 
140 1 Y 1 F ASN 257 ? F ASN 257 
141 1 Y 1 F PRO 258 ? F PRO 258 
142 1 Y 1 F PHE 259 ? F PHE 259 
143 1 Y 1 F ILE 260 ? F ILE 260 
144 1 Y 1 F SER 261 ? F SER 261 
145 1 Y 1 F PRO 262 ? F PRO 262 
146 1 Y 1 F SER 263 ? F SER 263 
147 1 Y 1 F SER 264 ? F SER 264 
148 1 Y 1 F THR 265 ? F THR 265 
149 1 Y 1 F SER 266 ? F SER 266 
150 1 Y 1 F TYR 267 ? F TYR 267 
151 1 Y 1 F HIS 268 ? F HIS 268 
152 1 Y 1 F GLY 269 ? F GLY 269 
153 1 Y 1 F SER 270 ? F SER 270 
154 1 Y 1 F PRO 417 ? F PRO 417 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 ALPHA-L-FUCOSE         FUC 
4 1,2-ETHANEDIOL         EDO 
5 water                  HOH 
# 
